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Heterogeneous nuclear ribonucleoprotein U (hnRNP U) (SP120) (Scaffold-attachment factor A) (SAF-A)

 HNRPU_RAT               Reviewed;         798 AA.
Q6IMY8;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-MAR-2018, entry version 121.
RecName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000312|RGD:620372};
Short=hnRNP U {ECO:0000312|RGD:620372};
AltName: Full=SP120 {ECO:0000303|PubMed:8509422};
AltName: Full=Scaffold-attachment factor A {ECO:0000250|UniProtKB:Q00839};
Short=SAF-A {ECO:0000250|UniProtKB:Q00839};
Name=Hnrnpu {ECO:0000312|RGD:620372}; Synonyms=Hnrpu;
ORFNames=rCG_20317;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|EMBL:AAH72529.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[4]
DNA-BINDING.
PubMed=8509422;
Tsutsui K., Tsutsui K., Okada S., Watarai S., Seki S., Yasuda T.,
Shohmori T.;
"Identification and characterization of a nuclear scaffold protein
that binds the matrix attachment region DNA.";
J. Biol. Chem. 268:12886-12894(1993).
[5]
FUNCTION, INTERACTION WITH TOP2A, RNA-BINDING, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=20554522; DOI=10.1074/jbc.M110.112979;
Kawano S., Miyaji M., Ichiyasu S., Tsutsui K.M., Tsutsui K.;
"Regulation of DNA Topoisomerase IIbeta through RNA-dependent
association with heterogeneous nuclear ribonucleoprotein U (hnRNP
U).";
J. Biol. Chem. 285:26451-26460(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. 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. 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). Required for the topoisomerase TOP2A protein
stability and activity in a RNA-dependent manner
(PubMed:20554522). Plays a role as a RNA polymerase II (Pol II)
holoenzyme transcription regulator. 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. 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. Positively regulates CBX5-induced
transcriptional gene silencing and retention of CBX5 in the
nucleus. Negatively regulates glucocorticoid-mediated
transcriptional activation. Key regulator of transcription
initiation and elongation in embryonic stem cells upon leukemia
inhibitory factor (LIF) signaling. Involved in the long non-coding
RNA H19-mediated Pol II transcriptional repression. Participates
in the circadian regulation of the core clock component
ARNTL/BMAL1 transcription. Plays a role in the regulation of
telomere length. Plays a role as a global pre-mRNA alternative
splicing modulator by regulating U2 small nuclear
ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA
stability. Component of the CRD-mediated complex that promotes MYC
mRNA stabilization. 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).
Plays a role in mitotic cell cycle regulation. Involved in the
formation of stable mitotic spindle microtubules (MTs) attachment
to kinetochore, spindle organization and chromosome congression.
Phosphorylation at Ser-58 by PLK1 is required for chromosome
alignement and segregation and progression through mitosis.
Contributes also to the targeting of AURKA to mitotic spindle MTs
(By similarity). Binds to double- and single-stranded DNA and RNA,
poly(A), poly(C) and poly(G) oligoribonucleotides
(PubMed:20554522). Binds to chromatin-associated RNAs (caRNAs) (By
similarity). Associates with chromatin to scaffold/matrix
attachment region (S/MAR) elements in DNA (PubMed:8509422).
Associates with chromatin in a chromatin-associated RNAs (caRNAs)-
dependent manner. Binds to the Xist RNA. Binds the long non-coding
H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to
small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA.
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). Also negatively regulates embryonic
stem cell differentiation upon LIF signaling. Required for
embryonic development (By similarity).
{ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q8VEK3,
ECO:0000269|PubMed:20554522, ECO:0000269|PubMed:8509422}.
-!- 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. ATP hydrolysis is required
to cycle from an oligomeric to monomeric state to compact
chromatin. Component of the coding region determinant (CRD)-
mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and
YBX1. Identified in the spliceosome C complex. Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Associates with heterogeneous nuclear ribonucleoprotein
(hnRNP) particles. Associates (via middle region) with the C-
terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this
association occurs in a RNA-independent manner. 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.
Associates with the telomerase holoenzyme complex. Associates with
spindle microtubules (MTs) in a TPX2-dependent manner. 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.
Interacts with AURKA. Interacts (via C-terminus) with CBX5; this
interaction is, at least in part, RNA-dependent. Interacts with
CR2. Interacts with CRY1. Interacts (via C-terminus) with EP300;
this interaction enhances DNA-binding to nuclear scaffold/matrix
attachment region (S/MAR) elements. Interacts with ERBB4.
Interacts with GEMIN5. Interacts with IGF2BP1. Interacts with
IGF2BP2 and IGF2BP3. Interacts with NCL; this interaction occurs
during mitosis. Interacts (via C-terminus) with NR3C1 (via C-
terminus). Interacts with PLK1; this interaction induces
phosphorylation of HNRNPU at Ser-58 in mitosis. Interacts with
POU3F4. Interacts with SMARCA4; this interaction occurs in
embryonic stem cells and stimulates global Pol II-mediated
transcription (By similarity). 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 (PubMed:20554522).
Interacts with TPX2; this interaction recruits HNRNPU to spindle
microtubules (MTs). Interacts with UBQLN2 (By similarity).
{ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q8VEK3,
ECO:0000269|PubMed:20554522}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00839}.
Nucleus matrix {ECO:0000250|UniProtKB:Q00839}. Chromosome
{ECO:0000250|UniProtKB:Q00839}. Nucleus speckle
{ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q00839}. Chromosome, centromere,
kinetochore {ECO:0000250|UniProtKB:Q00839}. Cytoplasm,
cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00839}. Cytoplasm,
cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00839}. Midbody
{ECO:0000250|UniProtKB:Q00839}. Cytoplasm
{ECO:0000250|UniProtKB:Q00839}. Cell surface
{ECO:0000250|UniProtKB:Q00839}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q00839}. Note=Localizes at inactive X
chromosome (Xi) regions. Localizes in the nucleus during
interphase. At metaphase, localizes with mitotic spindle
microtubules (MTs). At anaphase, localizes in the mitotic spindle
midzone. Localizes in spindle MTs proximal to spindle poles in a
TPX2- and AURKA-dependent manner. The Ser-58 phosphorylated form
localizes to centrosomes during prophase and metaphase, to mitotic
spindles in anaphase and to the midbody during cytokinesis.
Colocalizes with SMARCA4 in the nucleus (By similarity).
Colocalizes with CBX5 in the nucleus. Colocalizes with NR3C1 in
nuclear speckles. Localized in cytoplasmic ribonucleoprotein (RNP)
granules containing untranslated mRNAs.
{ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q8VEK3}.
-!- DOMAIN: The SAP domain is necessary for specific binding to
nuclear scaffold/matrix attachment region (S/MAR) elements in DNA.
The RNA-binding RGG-box region is necessary for its association
with inactive X chromosome (Xi) regions and to chromatin-
associated RNAs (caRNAs). Both the DNA-binding domain SAP and the
RNA-binding RGG-box region are necessary for the localization of
Xist RNA on the Xi. The ATPase and RNA-binding RGG-box regions are
necessary for oligomerization. {ECO:0000250|UniProtKB:Q00839,
ECO:0000250|UniProtKB:Q8VEK3}.
-!- PTM: Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting
in a loss of DNA- and chromatin-binding activities.
{ECO:0000250|UniProtKB:Q00839}.
-!- PTM: Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1
and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.
{ECO:0000250|UniProtKB:Q00839}.
-!- PTM: Arg-707 and Arg-713 are dimethylated, probably to asymmetric
dimethylarginine (By similarity). {ECO:0000250|UniProtKB:Q00839,
ECO:0000250|UniProtKB:Q8VEK3}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}.
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EMBL; AABR07021872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473985; EDL94801.1; -; Genomic_DNA.
EMBL; BC072529; AAH72529.1; -; mRNA.
RefSeq; NP_476480.2; NM_057139.2.
UniGene; Rn.4328; -.
IntAct; Q6IMY8; 3.
STRING; 10116.ENSRNOP00000046783; -.
PaxDb; Q6IMY8; -.
Ensembl; ENSRNOT00000044477; ENSRNOP00000046783; ENSRNOG00000033790.
GeneID; 117280; -.
KEGG; rno:117280; -.
CTD; 3192; -.
RGD; 620372; Hnrnpu.
eggNOG; KOG2242; Eukaryota.
eggNOG; ENOG4111X2K; LUCA.
GeneTree; ENSGT00390000020210; -.
HOVERGEN; HBG061101; -.
KO; K12888; -.
TreeFam; TF317301; -.
Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000033790; -.
ExpressionAtlas; Q6IMY8; baseline and differential.
GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISO:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0098577; C:inactive sex chromosome; ISO:RGD.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0032991; C:macromolecular complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; ISS:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; ISO:RGD.
GO; GO:0016363; C:nuclear matrix; ISO:RGD.
GO; GO:0016607; C:nuclear speck; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
GO; GO:0001047; F:core promoter binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0044877; F:macromolecular complex binding; ISO:RGD.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
GO; GO:0008143; F:poly(A) binding; ISO:RGD.
GO; GO:0017130; F:poly(C) RNA binding; ISO:RGD.
GO; GO:0034046; F:poly(G) binding; IDA:RGD.
GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
GO; GO:0003723; F:RNA binding; IDA:RGD.
GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISS:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
GO; GO:0003727; F:single-stranded RNA binding; ISO:RGD.
GO; GO:0017069; F:snRNA binding; ISO:RGD.
GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
GO; GO:0001097; F:TFIIH-class transcription factor binding; ISO:RGD.
GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:RGD.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISO:RGD.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:RGD.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISO:RGD.
GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; ISO:RGD.
GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IDA:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:1902889; P:protein localization to spindle microtubule; ISS:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
GO; GO:1990280; P:RNA localization to chromatin; ISO:RGD.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Acetylation; Activator; ADP-ribosylation; ATP-binding; Cell cycle;
Cell division; Centromere; Chromatin regulator; Chromosome;
Citrullination; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Differentiation; Isopeptide bond;
Kinetochore; Methylation; Mitosis; mRNA processing; mRNA splicing;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Ribonucleoprotein; Spliceosome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q00839}.
CHAIN 2 798 Heterogeneous nuclear ribonucleoprotein
U.
/FTId=PRO_0000442272.
DOMAIN 8 42 SAP. {ECO:0000250|UniProtKB:Q00839,
ECO:0000255|PROSITE-ProRule:PRU00186}.
DOMAIN 242 438 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
NP_BIND 478 485 ATP. {ECO:0000255}.
REGION 462 646 ATPase domain.
{ECO:0000250|UniProtKB:Q00839}.
REGION 585 600 Actin-binding.
{ECO:0000250|UniProtKB:Q00839}.
REGION 688 713 RNA-binding RGG-box.
{ECO:0000250|UniProtKB:Q8VEK3}.
COILED 624 651 {ECO:0000255}.
COMPBIAS 2 154 Asp/Glu-rich (acidic).
COMPBIAS 85 88 Poly-Glu. {ECO:0000255}.
COMPBIAS 116 119 Poly-Glu. {ECO:0000255}.
COMPBIAS 677 767 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
SITE 94 95 Cleavage; by CASP3.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 180 180 ADP-ribosylserine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 229 229 Citrulline.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 239 239 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 240 240 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 260 260 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 326 326 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 490 490 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 498 498 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 506 506 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 525 525 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 539 539 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 609 609 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 676 676 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 689 689 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 694 694 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 701 701 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 707 707 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 707 707 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q8VEK3}.
MOD_RES 707 707 Omega-N-methylated arginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 713 713 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 713 713 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 713 713 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 713 713 Omega-N-methylated arginine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 728 728 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 735 735 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q00839}.
MOD_RES 787 787 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 498 498 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 510 510 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 539 539 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 600 600 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 638 638 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 644 644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q00839}.
CROSSLNK 787 787 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q00839}.
SEQUENCE 798 AA; 87732 MW; 638C059C3D602DE5 CRC64;
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP AMEPGNGSLD
LGGDAAGRSG AGLEQEAAAG AEDDEEEEGI AALDGDQMEL GEENGAAGAA DAGAMEEEEA
ASEDENGDDQ GFQEGEDELG DEEEGAGDEN GHGEQQSQPP AAAQQASQQR GPGKEAAGKS
SGPTSLFAVT VAPPGARQGQ QQAGGDGKTE QKAGDKKRGV KRPREDHGRG YFEYIEENKY
SRAKSPQPPV EEEDEHFDDT VVCLDTYNCD LHFKISRDRL SASSLTMESF AFLWAGGRAS
YGVSKGKVCF EMKVTEKIPV RHLYTKDIDI HEVRIGWSLT TSGMLLGEEE FSYGYSLKGI
KTCNCETEDY GEKFDENDVI TCFANFETDE VELSYAKNGQ DLGVAFKISK EVLADRPLFP
HVLCHNCAVE FNFGQKEKPY FPIPEDCTFI QNVPLEDRVR GPKGPEEKKD CEVVMMIGLP
GAGKTTWVTK HAAENPGKYN ILGTNTIMDK MMVAGFKKQM ADTGKLNTLL QRAPQCLGKF
IEIAARKKRN FILDQTNVSA AAQRRKMCLF AGFQRKAVVV CPKDEDYKQR TQKKAEVEGK
DLPEHAVLKM KGNFTLPEVA ECFDEITYVE LQKEEAQKLL EQYKEESKKA LPPEKKQNTG
SKKSNKNKSG KNQFNRGGGH RGRGGFNMRG GNFRGGAPGN RGGYNRRGNM PQRGGGGGSG
GIGYPYPRGP VFPGRGGYSN RGNYNRGGMP NRGNYNQNFR GRGNNRGYKN QSQGYNQWQQ
GQFWGQKPWS QHYHQGYY


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