Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (Scaffold attachment factor A) (SAF-A) (p120) (pp120)

 HNRPU_HUMAN             Reviewed;         825 AA.
Q00839; O75507; Q8N174; Q96HY9; Q9BQ09;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 6.
22-NOV-2017, entry version 201.
RecName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000303|PubMed:1628625};
Short=hnRNP U {ECO:0000303|PubMed:1628625};
AltName: Full=GRIP120 {ECO:0000303|PubMed:9353307};
AltName: Full=Nuclear p120 ribonucleoprotein {ECO:0000303|PubMed:7753047};
AltName: Full=Scaffold-attachment factor A {ECO:0000303|PubMed:1324173, ECO:0000303|Ref.3};
Short=SAF-A {ECO:0000303|PubMed:1324173, ECO:0000303|Ref.3};
AltName: Full=p120 {ECO:0000303|PubMed:7993898};
AltName: Full=pp120 {ECO:0000303|PubMed:7993898};
Name=HNRNPU {ECO:0000312|HGNC:HGNC:5048};
Synonyms=C1orf199 {ECO:0000312|HGNC:HGNC:5048},
HNRPU {ECO:0000312|HGNC:HGNC:5048}, SAFA, U21.1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SINGLE-STRANDED DNA- AND
RNA-BINDING, RNA-BINDING REGION, AND VARIANT LEU-712.
PubMed=1628625;
Kiledjian M., Dreyfuss G.;
"Primary structure and binding activity of the hnRNP U protein:
binding RNA through RGG box.";
EMBO J. 11:2655-2664(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=7509195; DOI=10.1016/0167-4781(94)90044-2;
Fackelmayer F.O., Richter A.;
"hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs
in human cells.";
Biochim. Biophys. Acta 1217:232-234(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-712.
Fackelmayer F.O.;
"A variant of human scaffold attachment factor A (SAF-A), also known
as heterogeneous nuclear ribonucleoprotein U (hnRNP-U).";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye, Lymph, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-7; 256-265 AND 463-476, PHOSPHORYLATION,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=7993898; DOI=10.1021/bi00253a007;
Jordan P., Heid H., Kinzel V., Kubler D.;
"Major cell surface-located protein substrates of an ecto-protein
kinase are homologs of known nuclear proteins.";
Biochemistry 33:14696-14706(1994).
[7]
PROTEIN SEQUENCE OF 2-9; 186-194; 319-330; 399-409; 423-432; 452-461;
464-475 AND 524-535, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 2-9; 13-21; 38-69; 187-204; 256-268; 306-324;
353-360; 424-433; 463-484; 495-510; 525-543; 552-558; 566-572;
576-590; 592-601; 627-635; 665-674 AND 734-755, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-739, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
DNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=1324173;
Romig H., Fackelmayer F.O., Renz A., Ramsperger U., Richter A.;
"Characterization of SAF-A, a novel nuclear DNA binding protein from
HeLa cells with high affinity for nuclear matrix/scaffold attachment
DNA elements.";
EMBO J. 11:3431-3440(1992).
[10]
DNA- AND RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=8068679; DOI=10.1021/bi00200a024;
Fackelmayer F.O., Richter A.;
"Purification of two isoforms of hnRNP-U and characterization of their
nucleic acid binding activity.";
Biochemistry 33:10416-10422(1994).
[11]
FUNCTION IN CHROMATIN STRUCTURE, DNA- AND RNA-BINDING, SUBCELLULAR
LOCATION, AND ASSOCIATION WITH HNRNP PARTICLES.
PubMed=8174554;
Fackelmayer F.O., Dahm K., Renz A., Ramsperger U., Richter A.;
"Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix
protein which binds DNA and RNA in vivo and in vitro.";
Eur. J. Biochem. 221:749-757(1994).
[12]
INTERACTION WITH CR2.
PubMed=7753047; DOI=10.1016/0161-5890(95)00005-Y;
Barel M., Balbo M., Gauffre A., Frade R.;
"Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21)
for its three intracellular ligands, the p53 anti-oncoprotein, the p68
calcium binding protein and the nuclear p120 ribonucleoprotein.";
Mol. Immunol. 32:389-397(1995).
[13]
DNA-BINDING, CHROMATIN-BINDING, AND ASSOCIATION WITH HNRNP PARTICLES.
PubMed=9204873; DOI=10.1021/bi970480f;
Goehring F., Fackelmayer F.O.;
"The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A)
is directly bound to chromosomal DNA in vivo: a chemical cross-linking
study.";
Biochemistry 36:8276-8283(1997).
[14]
INTERACTION WITH POU3F4.
PubMed=9105675;
Malik K.F., Jaffe H., Brady J., Young W.S. III;
"The class III POU factor Brn-4 interacts with other class III POU
factors and the heterogeneous nuclear ribonucleoprotein U.";
Brain Res. Mol. Brain Res. 45:99-107(1997).
[15]
CLEAVAGE BY CASPASES, DNA-BINDING, CHROMATIN-BINDING, SUBCELLULAR
LOCATION, ASSOCIATION WITH HNRNP PARTICLES, AND SAP DOMAIN.
PubMed=9405365; DOI=10.1093/emboj/16.24.7361;
Goehring F., Schwab B.L., Nicotera P., Leist M., Fackelmayer F.O.;
"The novel SAR-binding domain of scaffold attachment factor A (SAF-A)
is a target in apoptotic nuclear breakdown.";
EMBO J. 16:7361-7371(1997).
[16]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH NR3C1,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9353307;
Eggert M., Michel J., Schneider S., Bornfleth H., Baniahmad A.,
Fackelmayer F.O., Schmidt S., Renkawitz R.;
"The glucocorticoid receptor is associated with the RNA-binding
nuclear matrix protein hnRNP U.";
J. Biol. Chem. 272:28471-28478(1997).
[17]
FUNCTION IN MRNA TRANSCRIPTION ELONGATION INHIBITION, ASSOCIATION WITH
RNA POLYMERASE II HOLOENZYME, AND ASSOCIATION WITH TFIIH BASAL
TRANSCRIPTION FACTOR.
PubMed=10490622;
Kim M.K., Nikodem V.M.;
"hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and
represses RNA polymerase II elongation.";
Mol. Cell. Biol. 19:6833-6844(1999).
[18]
CLEAVAGE SITE BY CASP3, DNA-BINDING, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ASP-100.
PubMed=10671544;
Kipp M., Schwab B.L., Przybylski M., Nicotera P., Fackelmayer F.O.;
"Apoptotic cleavage of scaffold attachment factor A (SAF-A) by
caspase-3 occurs at a noncanonical cleavage site.";
J. Biol. Chem. 275:5031-5036(2000).
[19]
DNA-BINDING, CHROMATIN-BINDING, SUBCELLULAR LOCATION, AND SAP DOMAIN.
PubMed=11003645;
Kipp M., Goehring F., Ostendorp T., van Drunen C.M., van Driel R.,
Przybylski M., Fackelmayer F.O.;
"SAF-Box, a conserved protein domain that specifically recognizes
scaffold attachment region DNA.";
Mol. Cell. Biol. 20:7480-7489(2000).
[20]
INTERACTION WITH EP300, ASSOCIATION WITH RNP PARTICLES, AND
CHROMATIN-BINDING.
PubMed=11909954;
Martens J.H., Verlaan M., Kalkhoven E., Dorsman J.C., Zantema A.;
"Scaffold/matrix attachment region elements interact with a p300-
scaffold attachment factor A complex and are bound by acetylated
nucleosomes.";
Mol. Cell. Biol. 22:2598-2606(2002).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[22]
SUBCELLULAR LOCATION, AND RNA-BINDING RGG-BOX REGION.
PubMed=14608463; DOI=10.1007/s00412-003-0258-0;
Helbig R., Fackelmayer F.O.;
"Scaffold attachment factor A (SAF-A) is concentrated in inactive X
chromosome territories through its RGG domain.";
Chromosoma 112:173-182(2003).
[23]
SUBCELLULAR LOCATION.
PubMed=15563465; DOI=10.1074/jbc.C400531200;
Fackelmayer F.O.;
"A stable proteinaceous structure in the territory of inactive X
chromosomes.";
J. Biol. Chem. 280:1720-1723(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[25]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH ACTIN,
ACTIN-BINDING REGION, AND MUTAGENESIS OF 616-ARG--LYS-620.
PubMed=15711563; DOI=10.1038/nsmb904;
Kukalev A., Nord Y., Palmberg C., Bergman T., Percipalle P.;
"Actin and hnRNP U cooperate for productive transcription by RNA
polymerase II.";
Nat. Struct. Mol. Biol. 12:238-244(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-271,
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
MUTAGENESIS OF SER-59.
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[27]
FUNCTION (MICROBIAL INFECTION).
PubMed=16916646; DOI=10.1016/j.molcel.2006.07.021;
Valente S.T., Goff S.P.;
"Inhibition of HIV-1 gene expression by a fragment of hnRNP U.";
Mol. Cell 23:597-605(2006).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[29]
FUNCTION IN MRNA STABILIZATION, AND MESSENGER RNA-BINDING.
PubMed=17174306; DOI=10.1016/j.febslet.2006.11.062;
Yugami M., Kabe Y., Yamaguchi Y., Wada T., Handa H.;
"hnRNP-U enhances the expression of specific genes by stabilizing
mRNA.";
FEBS Lett. 581:1-7(2007).
[30]
FUNCTION IN TELOMERE REGULATION, AND ASSOCIATION WITH TELOMERASE
HOLOENZYME COMPLEX.
PubMed=18082603; DOI=10.1016/j.molcel.2007.09.023;
Fu D., Collins K.;
"Purification of human telomerase complexes identifies factors
involved in telomerase biogenesis and telomere length regulation.";
Mol. Cell 28:773-785(2007).
[31]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-66, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH CBX5,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19617346; DOI=10.1074/jbc.M109.037929;
Ameyar-Zazoua M., Souidi M., Fritsch L., Robin P., Thomas A.,
Hamiche A., Percipalle P., Ait-Si-Ali S., Harel-Bellan A.;
"Physical and functional interaction between heterochromatin protein
1alpha and the RNA-binding protein heterogeneous nuclear
ribonucleoprotein U.";
J. Biol. Chem. 284:27974-27979(2009).
[36]
INTERACTION WITH HIV-1 VIRUS REV PROTEIN (MICROBIAL INFECTION).
PubMed=19808671; DOI=10.1074/jbc.M109.021659;
Hadian K., Vincendeau M., Maeusbacher N., Nagel D., Hauck S.M.,
Ueffing M., Loyter A., Werner T., Wolff H., Brack-Werner R.;
"Identification of a heterogeneous nuclear ribonucleoprotein-
recognition region in the HIV Rev protein.";
J. Biol. Chem. 284:33384-33391(2009).
[37]
FUNCTION IN MRNA STABILITY, COMPONENT OF THE CRD-MEDIATED MRNA
STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19029303; DOI=10.1261/rna.1175909;
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RNPs.";
RNA 15:104-115(2009).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-66 AND SER-271,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-352; LYS-516;
LYS-524; LYS-551; LYS-565; LYS-635 AND LYS-814, ACETYLATION [LARGE
SCALE ANALYSIS] AT LYS-215 (ISOFORM 2), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[40]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ERBB4.
PubMed=20858735; DOI=10.1158/1541-7786.MCR-10-0042;
Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
"Interactions of ErbB4 and Kap1 connect the growth factor and DNA
damage response pathways.";
Mol. Cancer Res. 8:1388-1398(2010).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-59; SER-66 AND SER-271, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[43]
FUNCTION IN MITOSIS, INTERACTION WITH AURKA; NCL AND TPX2, ASSOCIATION
WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=21242313; DOI=10.1242/jcs.063347;
Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
Fukui K.;
"The nuclear scaffold protein SAF-A is required for kinetochore-
microtubule attachment and contributes to the targeting of Aurora-A to
mitotic spindles.";
J. Cell Sci. 124:394-404(2011).
[44]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-59 AND SER-66, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[45]
FUNCTION IN PRE-MRNA ALTERNATIVE SPLICING, PRE-MRNA-BINDING, AND
SNRNA-BINDING.
PubMed=22325991; DOI=10.1016/j.molcel.2012.01.009;
Xiao R., Tang P., Yang B., Huang J., Zhou Y., Shao C., Li H., Sun H.,
Zhang Y., Fu X.D.;
"Nuclear matrix factor hnRNP U/SAF-A exerts a global control of
alternative splicing by regulating U2 snRNP maturation.";
Mol. Cell 45:656-668(2012).
[46]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[48]
FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH ACTIN, H19
RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23811339; DOI=10.1016/j.bbagen.2013.06.026;
Bi H.S., Yang X.Y., Yuan J.H., Yang F., Xu D., Guo Y.J., Zhang L.,
Zhou C.C., Wang F., Sun S.H.;
"H19 inhibits RNA polymerase II-mediated transcription by disrupting
the hnRNP U-actin complex.";
Biochim. Biophys. Acta 1830:4899-4906(2013).
[49]
INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
PubMed=23640942; DOI=10.1515/hsz-2013-0111;
Wachter K., Kohn M., Stohr N., Huttelmaier S.;
"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-
binding proteins) is modulated by distinct RNA-binding domains.";
Biol. Chem. 394:1077-1090(2013).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59; SER-66;
SER-267; SER-271; THR-532 AND THR-582, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-271 AND THR-286,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[52]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-702; ARG-733; ARG-739;
ARG-755 AND ARG-762, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-609 AND LYS-670,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[54]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[55]
INTERACTION WITH GEMIN5.
PubMed=25911097; DOI=10.1074/jbc.M115.646257;
Workman E., Kalda C., Patel A., Battle D.J.;
"Gemin5 binds to the survival motor neuron mRNA to regulate SMN
expression.";
J. Biol. Chem. 290:15662-15669(2015).
[56]
INTERACTION WITH UBQLN2.
PubMed=25616961; DOI=10.1093/hmg/ddv020;
Gilpin K.M., Chang L., Monteiro M.J.;
"ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction
between ubiquilin-2 and hnRNPA1.";
Hum. Mol. Genet. 24:2565-2577(2015).
[57]
FUNCTION IN MITOSIS, INTERACTION WITH AURKA; PLK1 AND TPX2,
PHOSPHORYLATION AT SER-59 BY PLK1, DEPHOSPHORYLATION BY PP2A,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-59.
PubMed=25986610; DOI=10.1128/MCB.01312-14;
Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
Lees-Miller S.P.;
"Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
required for mitosis.";
Mol. Cell. Biol. 35:2699-2713(2015).
[58]
XIST RNA-BINDING.
PubMed=26244333; DOI=10.1371/journal.pgen.1005430;
Yamada N., Hasegawa Y., Yue M., Hamada T., Nakagawa S., Ogawa Y.;
"Xist exon 7 contributes to the stable localization of Xist RNA on the
inactive X-chromosome.";
PLoS Genet. 11:E1005430-E1005430(2015).
[59]
FUNCTION IN CHROMATIN STRUCTURE, SUBUNIT, ATPASE DOMAIN, AND
RNA-BINDING RGG-BOX REGION.
PubMed=28622508; DOI=10.1016/j.cell.2017.05.029;
Nozawa R.S., Boteva L., Soares D.C., Naughton C., Dun A.R., Buckle A.,
Ramsahoye B., Bruton P.C., Saleeb R.S., Arnedo M., Hill B.,
Duncan R.R., Maciver S.K., Gilbert N.;
"SAF-A regulates interphase chromosome structure through
oligomerization with chromatin-associated RNAs.";
Cell 169:1214-1227(2017).
[60]
ADP-RIBOSYLATION AT SER-187.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[61]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-495; LYS-516;
LYS-524; LYS-536; LYS-565; LYS-574; LYS-609; LYS-626; LYS-635;
LYS-664; LYS-670 AND LYS-814, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[62]
STRUCTURE BY NMR OF 23-42.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SAP domain of human E1B-55kDa-associated
protein 5 isoform C.";
Submitted (JAN-2008) to the PDB data bank.
[63]
INVOLVEMENT IN EIEE54, AND VARIANT EIEE54 805-TRP--TYR-825 DEL.
PubMed=23708187; DOI=10.1038/ng.2646;
Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J.,
Cook J., Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S.,
Wallace G., Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S.,
Mackay M.T., Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z.,
Zelnick N., Lerman-Sagie T., Lev D., Moeller R.S., Gill D.,
Andrade D.M., Freeman J.L., Sadleir L.G., Shendure J., Berkovic S.F.,
Scheffer I.E., Mefford H.C.;
"Targeted resequencing in epileptic encephalopathies identifies de
novo mutations in CHD2 and SYNGAP1.";
Nat. Genet. 45:825-830(2013).
[64]
VARIANT EIEE54 171-GLN--TYR-825 DEL.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
-!- FUNCTION: DNA- and RNA-binding protein involved in several
cellular processes such as nuclear chromatin organization,
telomere-length regulation, transcription, mRNA alternative
splicing and stability, Xist-mediated transcriptional silencing
and mitotic cell progression (PubMed:10490622, PubMed:18082603,
PubMed:19029303, PubMed:22325991, PubMed:25986610,
PubMed:28622508). Plays a role in the regulation of interphase
large-scale gene-rich chromatin organization through chromatin-
associated RNAs (caRNAs) in a transcription-dependent manner, and
thereby maintains genomic stability (PubMed:1324173,
PubMed:8174554, PubMed:28622508). Required for the localization of
the long non-coding Xist RNA on the inactive chromosome X (Xi) and
the subsequent initiation and maintenance of X-linked
transcriptional gene silencing during X-inactivation (By
similarity). Plays a role as a RNA polymerase II (Pol II)
holoenzyme transcription regulator (PubMed:8174554,
PubMed:9353307, PubMed:10490622, PubMed:15711563, PubMed:19617346,
PubMed:23811339). Promotes transcription initiation by direct
association with the core-TFIIH basal transcription factor complex
for the assembly of a functional pre-initiation complex with Pol
II in a actin-dependent manner (PubMed:10490622, PubMed:15711563).
Blocks Pol II transcription elongation activity by inhibiting the
C-terminal domain (CTD) phosphorylation of Pol II and dissociates
from Pol II pre-initiation complex prior to productive
transcription elongation (PubMed:10490622). Positively regulates
CBX5-induced transcriptional gene silencing and retention of CBX5
in the nucleus (PubMed:19617346). Negatively regulates
glucocorticoid-mediated transcriptional activation
(PubMed:9353307). Key regulator of transcription initiation and
elongation in embryonic stem cells upon leukemia inhibitory factor
(LIF) signaling (By similarity). Involved in the long non-coding
RNA H19-mediated Pol II transcriptional repression
(PubMed:23811339). Participates in the circadian regulation of the
core clock component ARNTL/BMAL1 transcription (By similarity).
Plays a role in the regulation of telomere length
(PubMed:18082603). Plays a role as a global pre-mRNA alternative
splicing modulator by regulating U2 small nuclear
ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a
role in mRNA stability (PubMed:17174306, PubMed:17289661,
PubMed:19029303). Component of the CRD-mediated complex that
promotes MYC mRNA stabilization (PubMed:19029303). Enhances the
expression of specific genes, such as tumor necrosis factor TNFA,
by regulating mRNA stability, possibly through binding to the 3'-
untranslated region (UTR) (PubMed:17174306). Plays a role in
mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610).
Involved in the formation of stable mitotic spindle microtubules
(MTs) attachment to kinetochore, spindle organization and
chromosome congression (PubMed:21242313). Phosphorylation at Ser-
59 by PLK1 is required for chromosome alignement and segregation
and progression through mitosis (PubMed:25986610). Contributes
also to the targeting of AURKA to mitotic spindle MTs
(PubMed:21242313). Binds to double- and single-stranded DNA and
RNA, poly(A), poly(C) and poly(G) oligoribonucleotides
(PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873,
PubMed:9405365). Binds to chromatin-associated RNAs (caRNAs)
(PubMed:28622508). Associates with chromatin to scaffold/matrix
attachment region (S/MAR) elements in a chromatin-associated RNAs
(caRNAs)-dependent manner (PubMed:7509195, PubMed:1324173,
PubMed:9204873, PubMed:9405365, PubMed:10671544, PubMed:11003645,
PubMed:11909954, PubMed:28622508). Binds to the Xist RNA
(PubMed:26244333). Binds the long non-coding H19 RNA
(PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions
(PubMed:22325991). Binds to small nuclear RNAs (snRNAs)
(PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA
(PubMed:17174306). Binds (via RNA-binding RGG-box region) to the
long non-coding Xist RNA; this binding is direct and bridges the
Xist RNA and the inactive chromosome X (Xi) (By similarity). Also
negatively regulates embryonic stem cell differentiation upon LIF
signaling (By similarity). Required for embryonic development (By
similarity). {ECO:0000250|UniProtKB:Q8VEK3,
ECO:0000269|PubMed:10490622, ECO:0000269|PubMed:10671544,
ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:11909954,
ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:15711563,
ECO:0000269|PubMed:1628625, ECO:0000269|PubMed:17174306,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18082603,
ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19617346,
ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:22325991,
ECO:0000269|PubMed:23811339, ECO:0000269|PubMed:25986610,
ECO:0000269|PubMed:26244333, ECO:0000269|PubMed:28622508,
ECO:0000269|PubMed:7509195, ECO:0000269|PubMed:8068679,
ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9204873,
ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.
-!- FUNCTION: (Microbial infection) Negatively regulates
immunodeficiency virus type 1 (HIV-1) replication by preventing
the accumulation of viral mRNA transcripts in the cytoplasm.
{ECO:0000269|PubMed:16916646}.
-!- SUBUNIT: Oligomer (via ATPase domain and RNA-binding RGG-box
region); oligomerization occurs upon ATP-binding in a chromatin-
associated RNAs (caRNAs)- and transcription-dependent manner and
is required for chromatin decompaction (PubMed:28622508). ATP
hydrolysis is required to cycle from an oligomeric to monomeric
state to compact chromatin (PubMed:28622508). Component of the
coding region determinant (CRD)-mediated complex, composed of
DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303).
Identified in the spliceosome C complex (PubMed:11991638).
Identified in a IGF2BP1-dependent mRNP granule complex containing
untranslated mRNAs (PubMed:17289661, PubMed:19029303). Associates
with heterogeneous nuclear ribonucleoprotein (hnRNP) particles
(PubMed:8174554, PubMed:9204873, PubMed:9405365, PubMed:11909954).
Associates (via middle region) with the C-terminal domain (CTD)
RNA polymerase II (Pol II) holoenzyme; this association occurs in
a RNA-independent manner (PubMed:10490622). Associates (via middle
region) with the core-TFIIH basal transcription factor complex;
this association inhibits the CTD phosphorylation of RNA
polymerase II holoenzyme by downregulating TFIIH kinase activity
(PubMed:10490622). Associates with the telomerase holoenzyme
complex (PubMed:18082603). Associates with spindle microtubules
(MTs) in a TPX2-dependent manner (PubMed:21242313). Interacts (via
C-terminus) with actin; this interaction is direct and mediates
association with the phosphorylated CTD of RNA polymerase II and
is disrupted in presence of the long non-coding H19 RNA
(PubMed:15711563, PubMed:23811339). Interacts with AURKA
(PubMed:21242313, PubMed:25986610). Interacts (via C-terminus)
with CBX5; this interaction is, at least in part, RNA-dependent
(PubMed:19617346). Interacts with CR2 (PubMed:7753047). Interacts
with CRY1 (By similarity). Interacts (via C-terminus) with EP300;
this interaction enhances DNA-binding to nuclear scaffold/matrix
attachment region (S/MAR) elements (PubMed:11909954). Interacts
with ERBB4 (PubMed:20858735). Interacts with GEMIN5
(PubMed:25911097). Interacts with IGF2BP1 (PubMed:17289661,
PubMed:23640942). Interacts with IGF2BP2 and IGF2BP3
(PubMed:23640942). Interacts with NCL; this interaction occurs
during mitosis (PubMed:21242313). Interacts (via C-terminus) with
NR3C1 (via C-terminus) (PubMed:9353307). Interacts with PLK1; this
interaction induces phosphorylation of HNRNPU at Ser-59 in mitosis
(PubMed:25986610). Interacts with POU3F4 (PubMed:9105675).
Interacts with SMARCA4; this interaction occurs in embryonic stem
cells and stimulates global Pol II-mediated transcription.
Interacts (via C-terminus) with TOP2A; this interaction protects
the topoisomerase TOP2A from degradation and positively regulates
the relaxation of supercoiled DNA by TOP2A in a RNA-dependent
manner (By similarity). Interacts with TPX2; this interaction
recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313,
PubMed:25986610). Interacts with UBQLN2 (PubMed:25616961).
{ECO:0000250|UniProtKB:Q6IMY8, ECO:0000250|UniProtKB:Q8VEK3,
ECO:0000269|PubMed:10490622, ECO:0000269|PubMed:11909954,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15711563,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18082603,
ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19617346,
ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:21242313,
ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:23811339,
ECO:0000269|PubMed:25616961, ECO:0000269|PubMed:25911097,
ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:28622508,
ECO:0000269|PubMed:7753047, ECO:0000269|PubMed:8174554,
ECO:0000269|PubMed:9105675, ECO:0000269|PubMed:9204873,
ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein Rev.
{ECO:0000269|PubMed:19808671}.
-!- INTERACTION:
P42771:CDKN2A; NbExp=2; IntAct=EBI-351126, EBI-375053;
Q9UHD9:UBQLN2; NbExp=3; IntAct=EBI-351126, EBI-947187;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10671544,
ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:1324173,
ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465,
ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313,
ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9353307,
ECO:0000269|PubMed:9405365}. Nucleus matrix
{ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:14608463,
ECO:0000269|PubMed:8174554}. Chromosome
{ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:14608463,
ECO:0000269|PubMed:15563465}. Nucleus speckle
{ECO:0000269|PubMed:9353307}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:25986610}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21242313}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21242313,
ECO:0000269|PubMed:25986610}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:21242313}. Midbody
{ECO:0000269|PubMed:25986610}. Cytoplasm
{ECO:0000269|PubMed:19029303}. Cell surface
{ECO:0000269|PubMed:7993898}. Cytoplasmic granule
{ECO:0000269|PubMed:17289661}. Note=Localizes at inactive X
chromosome (Xi) regions (PubMed:11003645, PubMed:14608463,
PubMed:15563465). Localizes in the nucleus during interphase
(PubMed:21242313). At metaphase, localizes with mitotic spindle
microtubules (MTs) (PubMed:21242313). At anaphase, localizes in
the mitotic spindle midzone (PubMed:21242313). Localizes in
spindle MTs proximal to spindle poles in a TPX2- and AURKA-
dependent manner (PubMed:21242313). The Ser-59 phosphorylated form
localizes to centrosomes during prophase and metaphase, to mitotic
spindles in anaphase and to the midbody during cytokinesis
(PubMed:25986610). Colocalizes with SMARCA4 in the nucleus (By
similarity). Colocalizes with CBX5 in the nucleus
(PubMed:19617346). Colocalizes with NR3C1 in nuclear speckles
(PubMed:9353307). Localized in cytoplasmic ribonucleoprotein (RNP)
granules containing untranslated mRNAs (PubMed:17289661).
{ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:11003645,
ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19617346,
ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610,
ECO:0000269|PubMed:9353307}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q00839-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q00839-2; Sequence=VSP_005846;
Note=Contains a N6-acetyllysine at position 215.
{ECO:0000244|PubMed:19608861};
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:7509195}.
-!- DOMAIN: The SAP domain is necessary for specific binding to
nuclear scaffold/matrix attachment region (S/MAR) elements in DNA
(PubMed:9405365, PubMed:11003645). The RNA-binding RGG-box region
is necessary for its association with inactive X chromosome (Xi)
regions and to chromatin-associated RNAs (caRNAs)
(PubMed:14608463, PubMed:28622508). Both the DNA-binding domain
SAP and the RNA-binding RGG-box region are necessary for the
localization of Xist RNA on the Xi (By similarity). The ATPase and
RNA-binding RGG-box regions are necessary for oligomerization
(PubMed:28622508). {ECO:0000250|UniProtKB:Q8VEK3,
ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:14608463,
ECO:0000269|PubMed:28622508, ECO:0000269|PubMed:9405365}.
-!- PTM: Cleaved at Asp-100 by CASP3 during T-cell apoptosis,
resulting in a loss of DNA- and chromatin-binding activities
(PubMed:9405365, PubMed:10671544). {ECO:0000269|PubMed:10671544,
ECO:0000269|PubMed:9405365}.
-!- PTM: Extensively phosphorylated (PubMed:7993898). Phosphorylated
on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A
(PP2A) in mitosis (PubMed:25986610). {ECO:0000269|PubMed:25986610,
ECO:0000269|PubMed:7993898}.
-!- PTM: Arg-739 is dimethylated, probably to asymmetric
dimethylarginine (Ref.8). Arg-733 is dimethylated, probably to
asymmetric dimethylarginine (By similarity).
{ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|Ref.8}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}.
-!- DISEASE: Epileptic encephalopathy, early infantile, 54 (EIEE54)
[MIM:617391]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent.
{ECO:0000269|PubMed:23708187, ECO:0000269|PubMed:25356899}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAC19382.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X65488; CAA46472.1; -; mRNA.
EMBL; AF068846; AAC19382.1; ALT_SEQ; mRNA.
EMBL; BX323046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003367; AAH03367.1; -; mRNA.
EMBL; BC003621; AAH03621.1; -; mRNA.
EMBL; BC007950; AAH07950.2; -; mRNA.
EMBL; BC024767; AAH24767.1; -; mRNA.
EMBL; BC034925; AAH34925.1; -; mRNA.
CCDS; CCDS31081.1; -. [Q00839-2]
CCDS; CCDS41479.1; -. [Q00839-1]
PIR; S22765; S22765.
RefSeq; NP_004492.2; NM_004501.3. [Q00839-2]
RefSeq; NP_114032.2; NM_031844.2. [Q00839-1]
RefSeq; XP_016856604.1; XM_017001115.1. [Q00839-1]
RefSeq; XP_016856605.1; XM_017001116.1. [Q00839-1]
RefSeq; XP_016856606.1; XM_017001117.1. [Q00839-2]
UniGene; Hs.106212; -.
UniGene; Hs.411490; -.
UniGene; Hs.743421; -.
PDB; 1ZRJ; NMR; -; A=23-42.
PDBsum; 1ZRJ; -.
ProteinModelPortal; Q00839; -.
SMR; Q00839; -.
BioGrid; 109433; 524.
CORUM; Q00839; -.
DIP; DIP-684N; -.
IntAct; Q00839; 319.
MINT; MINT-1654412; -.
STRING; 9606.ENSP00000283179; -.
iPTMnet; Q00839; -.
PhosphoSitePlus; Q00839; -.
SwissPalm; Q00839; -.
BioMuta; HNRNPU; -.
DMDM; 254763463; -.
EPD; Q00839; -.
MaxQB; Q00839; -.
PaxDb; Q00839; -.
PeptideAtlas; Q00839; -.
PRIDE; Q00839; -.
DNASU; 3192; -.
Ensembl; ENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2]
Ensembl; ENST00000640218; ENSP00000491215; ENSG00000153187. [Q00839-1]
GeneID; 3192; -.
KEGG; hsa:3192; -.
UCSC; uc001iaz.2; human. [Q00839-1]
CTD; 3192; -.
DisGeNET; 3192; -.
EuPathDB; HostDB:ENSG00000153187.16; -.
GeneCards; HNRNPU; -.
HGNC; HGNC:5048; HNRNPU.
HPA; CAB011532; -.
HPA; HPA041057; -.
HPA; HPA058707; -.
MIM; 602869; gene.
MIM; 617391; phenotype.
neXtProt; NX_Q00839; -.
OpenTargets; ENSG00000153187; -.
PharmGKB; PA162391486; -.
eggNOG; ENOG410IR1W; Eukaryota.
eggNOG; ENOG410Y1WQ; LUCA.
GeneTree; ENSGT00390000020210; -.
HOGENOM; HOG000253920; -.
HOVERGEN; HBG061101; -.
InParanoid; Q00839; -.
KO; K12888; -.
OMA; QAFNQSW; -.
OrthoDB; EOG091G041T; -.
PhylomeDB; Q00839; -.
TreeFam; TF317301; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
SIGNOR; Q00839; -.
ChiTaRS; HNRNPU; human.
EvolutionaryTrace; Q00839; -.
GeneWiki; HNRPU; -.
GenomeRNAi; 3192; -.
PRO; PR:Q00839; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000153187; -.
CleanEx; HS_HNRNPU; -.
ExpressionAtlas; Q00839; baseline and differential.
Genevisible; Q00839; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0098577; C:inactive sex chromosome; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0032991; C:macromolecular complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0035326; F:enhancer binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0044877; F:macromolecular complex binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0017130; F:poly(C) RNA binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISS:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
GO; GO:0001097; F:TFIIH-class transcription factor binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
GO; GO:0033673; P:negative regulation of kinase activity; IMP:UniProtKB.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1902889; P:protein localization to spindle microtubule; IMP:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:1990280; P:RNA localization to chromatin; ISS:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
CDD; cd12884; SPRY_hnRNP; 1.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR026745; hnRNP_U.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR035778; SPRY_hnRNP_U.
PANTHER; PTHR12381:SF11; PTHR12381:SF11; 1.
Pfam; PF02037; SAP; 1.
Pfam; PF00622; SPRY; 1.
SMART; SM00513; SAP; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; ADP-ribosylation;
Alternative splicing; ATP-binding; Biological rhythms; Cell cycle;
Cell division; Centromere; Chromatin regulator; Chromosome;
Citrullination; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Direct protein sequencing;
Disease mutation; DNA-binding; Epilepsy; Isopeptide bond; Kinetochore;
Methylation; Mitosis; mRNA processing; mRNA splicing;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
Spliceosome; Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:7993898,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
CHAIN 2 825 Heterogeneous nuclear ribonucleoprotein
U.
/FTId=PRO_0000081872.
DOMAIN 8 42 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186,
ECO:0000269|PubMed:11003645,
ECO:0000269|PubMed:9405365}.
DOMAIN 267 464 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
NP_BIND 504 511 ATP. {ECO:0000255}.
REGION 488 672 ATPase domain.
{ECO:0000269|PubMed:28622508}.
REGION 611 626 Actin-binding.
{ECO:0000269|PubMed:15711563}.
REGION 714 739 RNA-binding RGG-box.
{ECO:0000269|PubMed:14608463,
ECO:0000269|PubMed:1628625}.
COMPBIAS 2 160 Asp/Glu-rich (acidic).
COMPBIAS 84 94 Poly-Glu.
COMPBIAS 161 209 Gln-rich.
COMPBIAS 703 825 Gly-rich.
COMPBIAS 740 750 Poly-Gly.
SITE 100 100 Cleavage; by CASP3.
{ECO:0000269|PubMed:10671544,
ECO:0000269|PubMed:9405365}.
MOD_RES 2 2 N-acetylserine; partial.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 59 59 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:25986610}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 186 186 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 187 187 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 255 255 Citrulline.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 265 265 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 266 266 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 516 516 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 524 524 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 532 532 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 551 551 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 565 565 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 582 582 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 635 635 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 702 702 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 715 715 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 720 720 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 727 727 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 733 733 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 733 733 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 739 739 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 739 739 Dimethylated arginine; in A2780 ovarian
carcinoma cell line. {ECO:0000269|Ref.8}.
MOD_RES 739 739 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 755 755 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 762 762 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 814 814 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 495 495 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 516 516 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 524 524 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 565 565 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 574 574 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 626 626 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 635 635 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 664 664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 814 814 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 213 231 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1628625,
ECO:0000303|PubMed:7509195}.
/FTId=VSP_005846.
VARIANT 171 825 Missing (in EIEE54).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078622.
VARIANT 712 712 F -> L (in dbSNP:rs1052660).
{ECO:0000269|PubMed:1628625,
ECO:0000269|Ref.3}.
/FTId=VAR_014712.
VARIANT 805 825 Missing (in EIEE54; unknown pathological
significance).
{ECO:0000269|PubMed:23708187}.
/FTId=VAR_078623.
MUTAGEN 59 59 S->A: No change in interaction with
AURKA, PLK1 and TPX2. Increases mitotic
chromosome misalignment and chromosome
segregation defects and time required to
progress through mitosis.
{ECO:0000269|PubMed:17081983}.
MUTAGEN 59 59 S->E: Increases mitotic chromosome
misalignment and chromosome segregation
defects and decreases time required to
progress through mitosis.
{ECO:0000269|PubMed:17081983}.
MUTAGEN 100 100 D->A: No cleavage by caspases during
apoptosis. Inhibits CASP3-induced
cleavage in vitro.
{ECO:0000269|PubMed:10671544}.
MUTAGEN 616 620 RTQKK->ATQAA: Loss of actin-binding.
{ECO:0000269|PubMed:15711563}.
CONFLICT 603 603 A -> V (in Ref. 5; AAH07950).
{ECO:0000305}.
SEQUENCE 825 AA; 90584 MW; 5D4EC4188436831F CRC64;
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR PAMEPGNGSL
DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD GDQMELGEEN GAAGAADSGP
MEEEEAASED ENGDDQGFQE GEDELGDEEE GAGDENGHGE QQPQPPATQQ QQPQQQRGAA
KEAAGKSSGP TSLFAVTVAP PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG
DKKRGVKRPR EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK
ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY TKDIDIHEVR
IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF DENDVITCFA NFESDEVELS
YAKNGQDLGV AFKISKEVLA GRPLFPHVLC HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP
LEDRVRGPKG PEEKKDCEVV MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA
GFKKQMADTG KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ
RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD EITYVELQKE
EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF NRGGGHRGRG GFNMRGGNFR
GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG
NYNQNFRGRG NNRGYKNQSQ GYNQWQQGQF WGQKPWSQHY HQGYY


Related products :

Catalog number Product name Quantity
201-20-6834 HNRNPU{heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)}mouse.mAb 0.2ml
HNRNPUL2 HNRNPU Gene heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)
201-20-2589 HNRNPU{heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A)}rabbit.pAb 0.2ml
GS-0995a heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) primary antibody, Host: Rabbit 200ul
CSB-EL010615MO Mouse heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) (HNRNPU) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL010615HU Human heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) (HNRNPU) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-PA010615GA01HU Rabbit anti-human heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA010615GA01HU Rabbit anti-human heterogeneous nuclear ribonucleoprotein U (scaffold attachment factor A) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
29-230 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.1 mg
29-274 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.1 mg
29-275 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.05 mg
18-003-43633 Heterogeneous nuclear ribonucleoprotein H3 - hnRNP H3; hnRNP 2H9 Polyclonal 0.1 mg Protein A
EIAAB33407 Heterogeneous nuclear ribonucleoprotein A1-like 2,hnRNP A1-like 2,hnRNP core protein A1-like 2,HNRNPA1L,HNRNPA1L2,Homo sapiens,Human
EIAAB35667 CArG-binding factor-A,CBF-A,Cbf-a,Cgbfa,Heterogeneous nuclear ribonucleoprotein A_B,hnRNP A_B,Hnrnpab,Hnrpab,Mouse,Mus musculus
18-003-43580 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.05 mg Aff Pur
18-003-43579 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.1 mg Protein A
20-373-85045 Heterogeneous nuclear ribonucleoprotein H - hnRNP H Monoclonal 0.05 ml
RH004* Rat heterogeneous nuclear ribonucleoprotein P2,hnRNP P2 ELISA Kit 96T
18-003-43575 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Polyclonal 0.05 mg Aff Pur
18-003-43574 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Polyclonal 0.1 mg Protein A
20-373-85016 Heterogeneous nuclear ribonucleoprotein H - hnRNP H Monoclonal 0.1 ml
20-373-85019 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Monoclonal 0.1 ml
E02H0091 Rat Heterogeneous Nuclear Ribonucleoprotein A1 ELISA , hnRNP
E02H0260 Rat Heterogeneous nuclear ribonucleoprotein A2 ELISA, hnRNP A2
20-373-85048 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Monoclonal 0.05 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur