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 K (hnRNP K) (Transformation up-regulated nuclear protein) (TUNP)

 HNRPK_HUMAN             Reviewed;         463 AA.
P61978; Q07244; Q15671; Q59F98; Q5T6W4; Q60577; Q6IBN1; Q922Y7;
Q96J62;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
25-OCT-2017, entry version 174.
RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
Short=hnRNP K;
AltName: Full=Transformation up-regulated nuclear protein;
Short=TUNP;
Name=HNRNPK; Synonyms=HNRPK;
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 1), AND SUBCELLULAR LOCATION.
PubMed=1729596; DOI=10.1128/MCB.12.1.164;
Matunis M.J., Michael W.M., Dreyfuss G.;
"Characterization and primary structure of the poly(C)-binding
heterogeneous nuclear ribonucleoprotein complex K protein.";
Mol. Cell. Biol. 12:164-171(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
PubMed=8107114; DOI=10.1006/jmbi.1994.1116;
Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A.,
Gesser B., Nielsen H., Celis J.E.;
"Identification, molecular cloning, expression and chromosome mapping
of a family of transformation upregulated hnRNP-K proteins derived by
alternative splicing.";
J. Mol. Biol. 236:33-48(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Muscle;
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).
[10]
PROTEIN SEQUENCE OF 1-52; 70-103; 149-163; 192-201; 208-219; 317-325;
378-405 AND 423-456, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 38-46; 149-163; 208-219; 306-316 AND 378-396, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
INTERACTION WITH HCV CORE PROTEIN.
PubMed=9651361; DOI=10.1074/jbc.273.28.17651;
Hsieh T.-Y., Matsumoto M., Chou H.-C., Schneider R., Hwang S.B.,
Lee A.S., Lai M.M.C.;
"Hepatitis C virus core protein interacts with heterogeneous nuclear
ribonucleoprotein K.";
J. Biol. Chem. 273:17651-17659(1998).
[13]
INTERACTION WITH DDX1.
PubMed=12183465; DOI=10.1074/jbc.M206981200;
Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.;
"An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous
nuclear ribonucleoprotein K.";
J. Biol. Chem. 277:40403-40409(2002).
[14]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[15]
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).
[16]
FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION,
UBIQUITINATION, AND INDUCTION.
PubMed=16360036; DOI=10.1016/j.cell.2005.09.032;
Moumen A., Masterson P., O'Connor M.J., Jackson S.P.;
"hnRNP K: an HDM2 target and transcriptional coactivator of p53 in
response to DNA damage.";
Cell 123:1065-1078(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
[18]
INTERACTION WITH ANKRD28, AND PHOSPHORYLATION AT SER-284.
PubMed=16564677; DOI=10.1016/j.cellsig.2006.01.019;
Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
"PITK, a PP1 targeting subunit that modulates the phosphorylation of
the transcriptional regulator hnRNP K.";
Cell. Signal. 18:1769-1778(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-379, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[21]
INTERACTION WITH ASFV PROTEIN P30, AND SUBCELLULAR LOCATION.
PubMed=18775702; DOI=10.1016/j.febslet.2008.08.031;
Hernaez B., Escribano J.M., Alonso C.;
"African swine fever virus protein p30 interaction with heterogeneous
nuclear ribonucleoprotein K (hnRNP-K) during infection.";
FEBS Lett. 582:3275-3280(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND
SER-284, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND TYR-380, 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).
[26]
FUNCTION.
PubMed=20673990; DOI=10.1016/j.cell.2010.06.040;
Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J.,
Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M.,
Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.;
"A large intergenic noncoding RNA induced by p53 mediates global gene
repression in the p53 response.";
Cell 142:409-419(2010).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 AND
SER-379, 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).
[28]
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216; SER-284
AND SER-379, 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).
[30]
GLYCOSYLATION.
PubMed=22967762; DOI=10.1016/j.bbagen.2012.08.024;
Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F.,
Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.;
"Characterization of O-GlcNAc cycling and proteomic identification of
differentially O-GlcNAcylated proteins during G1/S transition.";
Biochim. Biophys. Acta 1820:1839-1848(2012).
[31]
SUBCELLULAR LOCATION.
PubMed=22721921; DOI=10.1016/j.ejcb.2012.05.005;
Cervero P., Himmel M., Kruger M., Linder S.;
"Proteomic analysis of podosome fractions from macrophages reveals
similarities to spreading initiation centres.";
Eur. J. Cell Biol. 91:908-922(2012).
[32]
FUNCTION, SUMOYLATION AT LYS-422, UBIQUITINATION, AND MUTAGENESIS OF
LYS-422 AND ASP-424.
PubMed=22825850; DOI=10.1074/jbc.M112.390120;
Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.;
"DNA damage-induced heterogeneous nuclear ribonucleoprotein K
SUMOylation regulates p53 transcriptional activation.";
J. Biol. Chem. 287:30789-30799(2012).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-75; SER-216;
SER-284; SER-379 AND SER-420, 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).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-116 AND SER-284,
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).
[36]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-316, 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).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-405 AND LYS-422, 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).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-163 AND LYS-422, 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).
[39]
INVOLVEMENT IN AUKS.
PubMed=26173930; DOI=10.1002/humu.22837;
Au P.Y., You J., Caluseriu O., Schwartzentruber J., Majewski J.,
Bernier F.P., Ferguson M., Valle D., Parboosingh J.S., Sobreira N.,
Innes A.M., Kline A.D.;
"GeneMatcher aids in the identification of a new malformation syndrome
with intellectual disability, unique facial dysmorphisms, and skeletal
and connective tissue abnormalities caused by de novo variants in
HNRNPK.";
Hum. Mutat. 36:1009-1014(2015).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-422, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-52; LYS-60; LYS-163;
LYS-219; LYS-405 AND LYS-422, 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).
[43]
STRUCTURE BY NMR OF 375-463.
PubMed=10369774; DOI=10.1006/jmbi.1999.2818;
Baber J.L., Libutti D., Levens D., Tjandra N.;
"High precision solution structure of the C-terminal KH domain of
heterogeneous nuclear ribonucleoprotein K, a c-myc transcription
factor.";
J. Mol. Biol. 289:949-962(1999).
[44]
STRUCTURE BY NMR OF 379-463 IN COMPLEX WITH SINGLE-STRANDED DNA.
PubMed=12093748; DOI=10.1093/emboj/cdf352;
Braddock D.T., Baber J.L., Levens D., Clore G.M.;
"Molecular basis of sequence-specific single-stranded DNA recognition
by KH domains: solution structure of a complex between hnRNP K KH3 and
single-stranded DNA.";
EMBO J. 21:3476-3485(2002).
-!- FUNCTION: One of the major pre-mRNA-binding proteins. Binds
tenaciously to poly(C) sequences. Likely to play a role in the
nuclear metabolism of hnRNAs, particularly for pre-mRNAs that
contain cytidine-rich sequences. Can also bind poly(C) single-
stranded DNA. Plays an important role in p53/TP53 response to DNA
damage, acting at the level of both transcription activation and
repression. When sumoylated, acts as a transcriptional coactivator
of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN
induction (By similarity). As far as transcription repression is
concerned, acts by interacting with long intergenic RNA p21
(lincRNA-p21), a non-coding RNA induced by p53/TP53. This
interaction is necessary for the induction of apoptosis, but not
cell cycle arrest. {ECO:0000250, ECO:0000269|PubMed:16360036,
ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22825850}.
-!- SUBUNIT: Interacts with RBM42 and ZIK1. Interacts with BRDT (By
similarity). Identified in the spliceosome C complex. Interacts
with ANKRD28. Interacts with HCV core protein. Interacts with ASFV
p30 protein. Interacts with DDX1. Interacts with MDM2; this
interaction leads to ubiquitination and proteasomal degradation.
Interacts with p53/TP53. {ECO:0000250,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12093748,
ECO:0000269|PubMed:12183465, ECO:0000269|PubMed:16360036,
ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:18775702,
ECO:0000269|PubMed:9651361}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-304185, EBI-304185;
P29846:- (xeno); NbExp=9; IntAct=EBI-304185, EBI-8847394;
Q8N9J2:-; NbExp=6; IntAct=EBI-304185, EBI-10268244;
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-304185, EBI-743598;
Q9NYB9-2:ABI2; NbExp=4; IntAct=EBI-7060731, EBI-11096309;
P55064:AQP5; NbExp=3; IntAct=EBI-304185, EBI-746103;
O14965:AURKA; NbExp=2; IntAct=EBI-304185, EBI-448680;
Q8V1E7:C'204L (xeno); NbExp=5; IntAct=EBI-304185, EBI-8068745;
Q5I0X4:C6orf226; NbExp=6; IntAct=EBI-304185, EBI-10244057;
Q14011:CIRBP; NbExp=8; IntAct=EBI-304185, EBI-538850;
Q5D0E6:DALRD3; NbExp=3; IntAct=EBI-304185, EBI-2871865;
Q92608:DOCK2; NbExp=6; IntAct=EBI-304185, EBI-448771;
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-304185, EBI-1185167;
Q96D16:FBXL18; NbExp=6; IntAct=EBI-304185, EBI-744419;
P62993:GRB2; NbExp=9; IntAct=EBI-304185, EBI-401755;
Q8WVV9:HNRNPLL; NbExp=8; IntAct=EBI-304185, EBI-535849;
Q6NYL1:LOC440157; NbExp=4; IntAct=EBI-7060731, EBI-14362198;
Q6IPE9:MARK4; NbExp=6; IntAct=EBI-304185, EBI-10250211;
P43243:MATR3; NbExp=4; IntAct=EBI-304185, EBI-352602;
Q00987:MDM2; NbExp=2; IntAct=EBI-304185, EBI-389668;
Q9Y5E9:PCDHB14; NbExp=6; IntAct=EBI-304185, EBI-10329013;
Q99873:PRMT1; NbExp=3; IntAct=EBI-304185, EBI-78738;
Q8WWY3:PRPF31; NbExp=7; IntAct=EBI-7060731, EBI-1567797;
P79522:PRR3; NbExp=6; IntAct=EBI-304185, EBI-2803328;
Q96PU8:QKI; NbExp=6; IntAct=EBI-304185, EBI-945792;
Q9Y272:RASD1; NbExp=6; IntAct=EBI-304185, EBI-740818;
P98179:RBM3; NbExp=6; IntAct=EBI-304185, EBI-2949699;
P38159:RBMX; NbExp=11; IntAct=EBI-304185, EBI-743526;
P0DJD3:RBMY1A1; NbExp=3; IntAct=EBI-304185, EBI-8638511;
Q15415:RBMY1J; NbExp=4; IntAct=EBI-7060731, EBI-8642021;
Q6ZRY4:RBPMS2; NbExp=4; IntAct=EBI-7060731, EBI-11987469;
Q14D33:RTP5; NbExp=4; IntAct=EBI-7060731, EBI-10217913;
P09012:SNRPA; NbExp=4; IntAct=EBI-304185, EBI-607085;
O60504:SORBS3; NbExp=4; IntAct=EBI-304185, EBI-741237;
Q9UQ90:SPG7; NbExp=6; IntAct=EBI-304185, EBI-717201;
P12931:SRC; NbExp=6; IntAct=EBI-304185, EBI-621482;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-304185, EBI-750109;
P04637:TP53; NbExp=2; IntAct=EBI-7060731, EBI-366083;
Q9H3D4:TP63; NbExp=2; IntAct=EBI-304185, EBI-2337775;
P29597:TYK2; NbExp=3; IntAct=EBI-304185, EBI-1383454;
Q01081:U2AF1; NbExp=3; IntAct=EBI-304185, EBI-632461;
Q96MU7:YTHDC1; NbExp=3; IntAct=EBI-304185, EBI-2849854;
G3V1X1:ZFC3H1; NbExp=3; IntAct=EBI-304185, EBI-6448783;
Q66K41:ZNF385C; NbExp=6; IntAct=EBI-304185, EBI-10219231;
Q9H9D4:ZNF408; NbExp=4; IntAct=EBI-7060731, EBI-347633;
Q86XF7:ZNF575; NbExp=4; IntAct=EBI-7060731, EBI-14069183;
Q3KQV3:ZNF792; NbExp=3; IntAct=EBI-304185, EBI-10240849;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1729596}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:16360036,
ECO:0000269|PubMed:1729596, ECO:0000269|PubMed:18775702,
ECO:0000269|PubMed:22721921}. Cell projection, podosome
{ECO:0000269|PubMed:22721921}. Note=Recruited to p53/TP53-
responsive promoters, in the presence of functional p53/TP53
(PubMed:16360036). In case of ASFV infection, there is a shift in
the localization which becomes predominantly nuclear
(PubMed:18775702).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P61978-1, Q07244-1;
Sequence=Displayed;
Name=2;
IsoId=P61978-2, Q07244-2;
Sequence=VSP_002822;
Name=3;
IsoId=P61978-3; Sequence=VSP_021669, VSP_002822;
Note=No experimental confirmation available.;
-!- INDUCTION: By DNA damage, including ionizing radiations and
phleomycin treatment or UV irradiation. This induction requires
ATM kinase activity (ionizing radiations and phleomycin) or ATR
activity (UV irradiation). Up-regulation is due to protein
stabilization. Constitutive protein levels are controlled by MDM2-
mediated ubiquitination and degradation via the proteasome
pathway. {ECO:0000269|PubMed:16360036}.
-!- PTM: Arg-296 and Arg-299 are dimethylated, probably to asymmetric
dimethylarginine.
-!- PTM: Sumoylated by CBX4. Sumoylation is increased upon DNA damage,
such as that produced by doxorubicin, etoposide, UV light and
camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under
these conditions. {ECO:0000269|PubMed:16564677,
ECO:0000269|PubMed:22825850, ECO:0000269|PubMed:8107114}.
-!- PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect
monoubiquitination, but slightly decreases HNRNPK poly-
ubiquitination. {ECO:0000269|PubMed:16360036,
ECO:0000269|PubMed:22825850}.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner. {ECO:0000269|PubMed:22967762}.
-!- MASS SPECTROMETRY: Mass=50976.25; Method=MALDI; Range=1-463
(P61978-1); Evidence={ECO:0000269|PubMed:11840567};
-!- DISEASE: Au-Kline syndrome (AUKS) [MIM:616580]: A disorder
characterized by intellectual disability, facial dysmorphism,
cardiac defects, and connective tissue and skeletal abnormalities.
Dysmorphic features include long palpebral fissures, ptosis, a
broad prominent nasal bridge, hypoplastic alae nasi, an open
downturned mouth, ears with underdeveloped and thick helices, high
palate, and a unique tongue with a prominent median crease.
Hypotonia, hyporeflexia, and high pain tolerance are additional
features. {ECO:0000269|PubMed:26173930}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAD92799.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HNRNPKID44314ch9q21.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S74678; AAB20770.1; -; mRNA.
EMBL; X72727; CAA51267.1; -; mRNA.
EMBL; CR456771; CAG33052.1; -; mRNA.
EMBL; AB209562; BAD92799.1; ALT_INIT; mRNA.
EMBL; AK291336; BAF84025.1; -; mRNA.
EMBL; AB451263; BAG70077.1; -; mRNA.
EMBL; AB451390; BAG70204.1; -; mRNA.
EMBL; AL354733; CAI16020.1; -; Genomic_DNA.
EMBL; CH471089; EAW62675.1; -; Genomic_DNA.
EMBL; CH471089; EAW62677.1; -; Genomic_DNA.
EMBL; BC000355; AAH00355.1; -; mRNA.
EMBL; BC014980; AAH14980.1; -; mRNA.
CCDS; CCDS6667.1; -.
CCDS; CCDS6668.1; -. [P61978-2]
PIR; S43363; S43363.
RefSeq; NP_001305115.1; NM_001318186.1.
RefSeq; NP_001305116.1; NM_001318187.1. [P61978-3]
RefSeq; NP_001305117.1; NM_001318188.1. [P61978-1]
RefSeq; NP_002131.2; NM_002140.4. [P61978-2]
RefSeq; NP_112552.1; NM_031262.3. [P61978-1]
RefSeq; NP_112553.1; NM_031263.3. [P61978-2]
RefSeq; XP_005252017.1; XM_005251960.2. [P61978-2]
RefSeq; XP_005252020.1; XM_005251963.3. [P61978-3]
RefSeq; XP_005252022.1; XM_005251965.2. [P61978-3]
RefSeq; XP_016870157.1; XM_017014668.1. [P61978-1]
UniGene; Hs.522257; -.
PDB; 1J5K; NMR; -; A=379-463.
PDB; 1KHM; NMR; -; A=379-463.
PDB; 1ZZI; X-ray; 1.80 A; A/B=385-463.
PDB; 1ZZJ; X-ray; 2.30 A; A/B/C=385-463.
PDB; 1ZZK; X-ray; 0.95 A; A=385-463.
PDBsum; 1J5K; -.
PDBsum; 1KHM; -.
PDBsum; 1ZZI; -.
PDBsum; 1ZZJ; -.
PDBsum; 1ZZK; -.
ProteinModelPortal; P61978; -.
SMR; P61978; -.
BioGrid; 109431; 274.
CORUM; P61978; -.
DIP; DIP-31805N; -.
IntAct; P61978; 171.
MINT; MINT-225422; -.
STRING; 9606.ENSP00000365439; -.
iPTMnet; P61978; -.
PhosphoSitePlus; P61978; -.
SwissPalm; P61978; -.
BioMuta; HNRNPK; -.
DMDM; 48429103; -.
SWISS-2DPAGE; P61978; -.
MaxQB; P61978; -.
PaxDb; P61978; -.
PeptideAtlas; P61978; -.
PRIDE; P61978; -.
TopDownProteomics; P61978-1; -. [P61978-1]
DNASU; 3190; -.
Ensembl; ENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
Ensembl; ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
Ensembl; ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
Ensembl; ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
GeneID; 3190; -.
KEGG; hsa:3190; -.
UCSC; uc004ang.5; human.
CTD; 3190; -.
DisGeNET; 3190; -.
EuPathDB; HostDB:ENSG00000165119.18; -.
GeneCards; HNRNPK; -.
HGNC; HGNC:5044; HNRNPK.
HPA; CAB004435; -.
HPA; CAB016225; -.
HPA; HPA007644; -.
HPA; HPA044105; -.
MalaCards; HNRNPK; -.
MIM; 600712; gene.
MIM; 616580; phenotype.
neXtProt; NX_P61978; -.
OpenTargets; ENSG00000165119; -.
PharmGKB; PA162391350; -.
eggNOG; KOG2192; Eukaryota.
eggNOG; ENOG4111GSB; LUCA.
GeneTree; ENSGT00760000119144; -.
HOVERGEN; HBG051916; -.
InParanoid; P61978; -.
KO; K12886; -.
OMA; INPWANG; -.
OrthoDB; EOG091G0DHI; -.
PhylomeDB; P61978; -.
TreeFam; TF316335; -.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
SIGNOR; P61978; -.
ChiTaRS; HNRNPK; human.
EvolutionaryTrace; P61978; -.
GeneWiki; HNRPK; -.
GenomeRNAi; 3190; -.
PMAP-CutDB; P61978; -.
PRO; PR:P61978; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165119; -.
CleanEx; HS_HNRNPK; -.
ExpressionAtlas; P61978; baseline and differential.
Genevisible; P61978; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IMP:BHF-UCL.
GO; GO:0003697; F:single-stranded DNA binding; TAS:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0045716; P:positive regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:1902165; P:regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0072369; P:regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 3.
InterPro; IPR033090; hnRNP_K.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR012987; ROK_N.
PANTHER; PTHR10288:SF221; PTHR10288:SF221; 1.
Pfam; PF00013; KH_1; 3.
Pfam; PF08067; ROKNT; 1.
SMART; SM00322; KH; 3.
SUPFAM; SSF54791; SSF54791; 3.
PROSITE; PS50084; KH_TYPE_1; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Cell junction; Cell projection; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Glycoprotein;
Host-virus interaction; Isopeptide bond; Mental retardation;
Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
Spliceosome; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 463 Heterogeneous nuclear ribonucleoprotein
K.
/FTId=PRO_0000050096.
DOMAIN 42 104 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 54 76 1-1.
REPEAT 59 62 3-1.
DOMAIN 144 209 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 245 250 2-1.
REPEAT 257 260 3-2.
REPEAT 267 270 3-3.
REPEAT 295 298 3-4.
REPEAT 324 329 2-2.
DOMAIN 387 451 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REPEAT 399 421 1-2.
REPEAT 404 407 3-5.
REGION 1 276 Necessary for interaction with DDX1.
{ECO:0000269|PubMed:12183465}.
REGION 35 197 Interaction with ASFV p30.
REGION 54 421 2 X 22 AA approximate repeats.
REGION 59 407 5 X 4 AA repeats of G-X-G-G.
REGION 209 337 Interaction with ZIK1. {ECO:0000250}.
REGION 236 273 RNA-binding RGG-box.
REGION 245 329 2 X 6 AA approximate repeats.
COMPBIAS 289 294 Poly-Pro.
COMPBIAS 310 315 Poly-Pro.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.10}.
MOD_RES 34 34 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 198 198 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16564677}.
MOD_RES 316 316 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 377 377 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 380 380 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 405 405 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P61979}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 34 34 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 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 60 60 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 405 405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 111 134 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_021669.
VAR_SEQ 459 463 SGKFF -> ADVEGF (in isoform 2 and isoform
3). {ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_002822.
MUTAGEN 422 422 K->R: Loss of sumoylation. Loss of TP53
transcriptional stimulation.
{ECO:0000269|PubMed:22825850}.
MUTAGEN 424 424 D->A: Loss of sumoylation.
{ECO:0000269|PubMed:22825850}.
CONFLICT 32 32 A -> D (in Ref. 2; CAA51267).
{ECO:0000305}.
HELIX 381 384 {ECO:0000244|PDB:1KHM}.
STRAND 388 395 {ECO:0000244|PDB:1ZZK}.
TURN 396 398 {ECO:0000244|PDB:1ZZK}.
HELIX 399 402 {ECO:0000244|PDB:1ZZK}.
HELIX 405 407 {ECO:0000244|PDB:1ZZK}.
HELIX 408 417 {ECO:0000244|PDB:1ZZK}.
STRAND 420 423 {ECO:0000244|PDB:1ZZK}.
STRAND 430 439 {ECO:0000244|PDB:1ZZK}.
HELIX 441 459 {ECO:0000244|PDB:1ZZK}.
SEQUENCE 463 AA; 50976 MW; 0F70EE169B2A064A CRC64;
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL
FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF


Related products :

Catalog number Product name Quantity
18-003-43579 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.1 mg Protein A
18-003-43580 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.05 mg Aff Pur
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
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
29-401 HNRPUL1 is a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important ro 0.1 mg
29-500 HNRPUL1 is a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important ro 0.05 mg
EIAAB33407 Heterogeneous nuclear ribonucleoprotein A1-like 2,hnRNP A1-like 2,hnRNP core protein A1-like 2,HNRNPA1L,HNRNPA1L2,Homo sapiens,Human
EIAAB35657 HDP,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Rat,Rattus norvegicus,Single-strand RNA-binding protein
EIAAB35655 Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Homo sapiens,Human,Single-strand RNA-binding protein
EIAAB35658 Bos taurus,Bovine,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Single-strand RNA-binding protein,Unwinding protein 1,UP1
EIAAB35656 Fli-2,HDP-1,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Mouse,Mus musculus,Single-strand-binding protein,Tis,Topoisomerase-inhi
20-373-85044 Heterogeneous nuclear ribonucleoprotein F - hnRNP F; Nucleolin-like protein mcs94-1 Monoclonal 0.05 ml
18-003-43603 Heterogeneous nuclear ribonucleoprotein F - hnRNP F; Nucleolin-like protein mcs94-1 Polyclonal 0.1 mg Protein A
20-373-85015 Heterogeneous nuclear ribonucleoprotein F - hnRNP F; Nucleolin-like protein mcs94-1 Monoclonal 0.1 ml
18-003-43633 Heterogeneous nuclear ribonucleoprotein H3 - hnRNP H3; hnRNP 2H9 Polyclonal 0.1 mg Protein A
18-003-44203 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 mg Protein A
18-003-44204 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 mg Protein A
20-373-85047 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.05 ml
20-373-85018 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 ml
EIAAB32932 Heterogeneous nuclear ribonucleoprotein I,hnRNP I,Pig,Polypyrimidine tract-binding protein 1,PTB,PTB,PTBP1,Sus scrofa
EIAAB33722 Autoantigen p542,Heterogeneous nuclear ribonucleoprotein C-like 2,hnRNP associated with lethal yellow protein homolog,hnRNP core protein C-like 2,HNRPCL2,Homo sapiens,Human,P542,RALY,RNA-binding prote
EIAAB32929 Heterogeneous nuclear ribonucleoprotein I,hnRNP I,Mouse,Mus musculus,Polypyrimidine tract-binding protein 1,PTB,Ptb,Ptbp1
EIAAB30030 Alpha-CP1,Heterogeneous nuclear ribonucleoprotein E1,hnRNP E1,Mouse,Mus musculus,Pcbp1,Poly(rC)-binding protein 1
20-373-85045 Heterogeneous nuclear ribonucleoprotein H - hnRNP H 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