HNRPU_RAT
ID HNRPU_RAT Reviewed; 798 AA.
AC Q6IMY8;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000312|RGD:620372};
DE Short=hnRNP U {ECO:0000312|RGD:620372};
DE AltName: Full=SP120 {ECO:0000303|PubMed:8509422};
DE AltName: Full=Scaffold-attachment factor A {ECO:0000250|UniProtKB:Q00839};
DE Short=SAF-A {ECO:0000250|UniProtKB:Q00839};
GN Name=Hnrnpu {ECO:0000312|RGD:620372}; Synonyms=Hnrpu; ORFNames=rCG_20317;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAH72529.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DNA-BINDING.
RX PubMed=8509422; DOI=10.1016/s0021-9258(18)31469-8;
RA Tsutsui K., Tsutsui K., Okada S., Watarai S., Seki S., Yasuda T.,
RA Shohmori T.;
RT "Identification and characterization of a nuclear scaffold protein that
RT binds the matrix attachment region DNA.";
RL J. Biol. Chem. 268:12886-12894(1993).
RN [5]
RP FUNCTION, INTERACTION WITH TOP2A, RNA-BINDING, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20554522; DOI=10.1074/jbc.m110.112979;
RA Kawano S., Miyaji M., Ichiyasu S., Tsutsui K.M., Tsutsui K.;
RT "Regulation of DNA Topoisomerase IIbeta through RNA-dependent association
RT with heterogeneous nuclear ribonucleoprotein U (hnRNP U).";
RL J. Biol. Chem. 285:26451-26460(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: DNA- and RNA-binding protein involved in several cellular
CC processes such as nuclear chromatin organization, telomere-length
CC regulation, transcription, mRNA alternative splicing and stability,
CC Xist-mediated transcriptional silencing and mitotic cell progression.
CC Plays a role in the regulation of interphase large-scale gene-rich
CC chromatin organization through chromatin-associated RNAs (caRNAs) in a
CC transcription-dependent manner, and thereby maintains genomic
CC stability. Required for the localization of the long non-coding Xist
CC RNA on the inactive chromosome X (Xi) and the subsequent initiation and
CC maintenance of X-linked transcriptional gene silencing during X-
CC inactivation (By similarity). Required for the topoisomerase TOP2A
CC protein stability and activity in a RNA-dependent manner
CC (PubMed:20554522). Plays a role as a RNA polymerase II (Pol II)
CC holoenzyme transcription regulator. Promotes transcription initiation
CC by direct association with the core-TFIIH basal transcription factor
CC complex for the assembly of a functional pre-initiation complex with
CC Pol II in a actin-dependent manner. Blocks Pol II transcription
CC elongation activity by inhibiting the C-terminal domain (CTD)
CC phosphorylation of Pol II and dissociates from Pol II pre-initiation
CC complex prior to productive transcription elongation. Positively
CC regulates CBX5-induced transcriptional gene silencing and retention of
CC CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated
CC transcriptional activation. Key regulator of transcription initiation
CC and elongation in embryonic stem cells upon leukemia inhibitory factor
CC (LIF) signaling. Involved in the long non-coding RNA H19-mediated Pol
CC II transcriptional repression. Participates in the circadian regulation
CC of the core clock component ARNTL/BMAL1 transcription. Plays a role in
CC the regulation of telomere length. Plays a role as a global pre-mRNA
CC alternative splicing modulator by regulating U2 small nuclear
CC ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability.
CC Component of the CRD-mediated complex that promotes MYC mRNA
CC stabilization. Enhances the expression of specific genes, such as tumor
CC necrosis factor TNFA, by regulating mRNA stability, possibly through
CC binding to the 3'-untranslated region (UTR). Plays a role in mitotic
CC cell cycle regulation. Involved in the formation of stable mitotic
CC spindle microtubules (MTs) attachment to kinetochore, spindle
CC organization and chromosome congression. Phosphorylation at Ser-58 by
CC PLK1 is required for chromosome alignement and segregation and
CC progression through mitosis. Contributes also to the targeting of AURKA
CC to mitotic spindle MTs (By similarity). Binds to double- and single-
CC stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides
CC (PubMed:20554522). Binds to chromatin-associated RNAs (caRNAs) (By
CC similarity). Associates with chromatin to scaffold/matrix attachment
CC region (S/MAR) elements in DNA (PubMed:8509422). Associates with
CC chromatin in a chromatin-associated RNAs (caRNAs)-dependent manner.
CC Binds to the Xist RNA. Binds the long non-coding H19 RNA. Binds to
CC SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs
CC (snRNAs). Binds to the 3'-UTR of TNFA mRNA. Binds (via RNA-binding RGG-
CC box region) to the long non-coding Xist RNA; this binding is direct and
CC bridges the Xist RNA and the inactive chromosome X (Xi). Also
CC negatively regulates embryonic stem cell differentiation upon LIF
CC signaling. Required for embryonic development (By similarity). Binds to
CC brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of
CC Blnc1 by ZBTB7B required to drive brown and beige fat development and
CC thermogenesis (By similarity). {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:20554522,
CC ECO:0000269|PubMed:8509422}.
CC -!- SUBUNIT: Oligomer (via ATPase domain and RNA-binding RGG-box region);
CC oligomerization occurs upon ATP-binding in a chromatin-associated RNAs
CC (caRNAs)- and transcription-dependent manner and is required for
CC chromatin decompaction. ATP hydrolysis is required to cycle from an
CC oligomeric to monomeric state to compact chromatin. Component of the
CC coding region determinant (CRD)-mediated complex, composed of DHX9,
CC HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in the spliceosome C
CC complex. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Associates with heterogeneous nuclear
CC ribonucleoprotein (hnRNP) particles. Associates (via middle region)
CC with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme;
CC this association occurs in a RNA-independent manner. Associates (via
CC middle region) with the core-TFIIH basal transcription factor complex;
CC this association inhibits the CTD phosphorylation of RNA polymerase II
CC holoenzyme by down-regulating TFIIH kinase activity. Associates with
CC the telomerase holoenzyme complex. Associates with spindle microtubules
CC (MTs) in a TPX2-dependent manner. Interacts (via C-terminus) with
CC actin; this interaction is direct and mediates association with the
CC phosphorylated CTD of RNA polymerase II and is disrupted in presence of
CC the long non-coding H19 RNA. Interacts with AURKA. Interacts (via C-
CC terminus) with CBX5; this interaction is, at least in part, RNA-
CC dependent. Interacts with CR2. Interacts with CRY1. Interacts (via C-
CC terminus) with EP300; this interaction enhances DNA-binding to nuclear
CC scaffold/matrix attachment region (S/MAR) elements. Interacts with
CC ERBB4. Interacts with GEMIN5. Interacts with IGF2BP1. Interacts with
CC IGF2BP2 and IGF2BP3. Interacts with NCL; this interaction occurs during
CC mitosis. Interacts (via C-terminus) with NR3C1 (via C-terminus).
CC Interacts with PLK1; this interaction induces phosphorylation of HNRNPU
CC at Ser-58 in mitosis. Interacts with POU3F4. Interacts with SMARCA4;
CC this interaction occurs in embryonic stem cells and stimulates global
CC Pol II-mediated transcription (By similarity). Interacts (via C-
CC terminus) with TOP2A; this interaction protects the topoisomerase TOP2A
CC from degradation and positively regulates the relaxation of supercoiled
CC DNA by TOP2A in a RNA-dependent manner (PubMed:20554522). Interacts
CC with TPX2; this interaction recruits HNRNPU to spindle microtubules
CC (MTs). Interacts with UBQLN2 (By similarity). Interacts (via RNA-
CC binding RGG-box region) with ZBTB7B; the interaction facilitates the
CC recruitment of long non-coding RNA Blnc1 by ZBTB7B (By similarity).
CC Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:20554522}.
CC -!- INTERACTION:
CC Q6IMY8; D4A5I9: Myo6; NbExp=4; IntAct=EBI-931601, EBI-26553770;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00839}. Nucleus
CC matrix {ECO:0000250|UniProtKB:Q00839}. Chromosome
CC {ECO:0000250|UniProtKB:Q00839}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q00839}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q00839}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00839}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00839}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q00839}.
CC Midbody {ECO:0000250|UniProtKB:Q00839}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q00839}. Cell surface
CC {ECO:0000250|UniProtKB:Q00839}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q00839}. Note=Localizes at inactive X chromosome
CC (Xi) regions. Localizes in the nucleus during interphase. At metaphase,
CC localizes with mitotic spindle microtubules (MTs). At anaphase,
CC localizes in the mitotic spindle midzone. Localizes in spindle MTs
CC proximal to spindle poles in a TPX2- and AURKA-dependent manner. The
CC Ser-58 phosphorylated form localizes to centrosomes during prophase and
CC metaphase, to mitotic spindles in anaphase and to the midbody during
CC cytokinesis. Colocalizes with SMARCA4 in the nucleus (By similarity).
CC Colocalizes with CBX5 in the nucleus. Colocalizes with NR3C1 in nuclear
CC speckles. Localized in cytoplasmic ribonucleoprotein (RNP) granules
CC containing untranslated mRNAs. {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000250|UniProtKB:Q8VEK3}.
CC -!- DOMAIN: The SAP domain is necessary for specific binding to nuclear
CC scaffold/matrix attachment region (S/MAR) elements in DNA. The RNA-
CC binding RGG-box region is necessary for its association with inactive X
CC chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs). Both
CC the DNA-binding domain SAP and the RNA-binding RGG-box region are
CC necessary for the localization of Xist RNA on the Xi. The ATPase and
CC RNA-binding RGG-box regions are necessary for oligomerization.
CC {ECO:0000250|UniProtKB:Q00839, ECO:0000250|UniProtKB:Q8VEK3}.
CC -!- PTM: Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a
CC loss of DNA- and chromatin-binding activities.
CC {ECO:0000250|UniProtKB:Q00839}.
CC -!- PTM: Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and
CC dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.
CC {ECO:0000250|UniProtKB:Q00839}.
CC -!- PTM: Arg-707 and Arg-713 are dimethylated, probably to asymmetric
CC dimethylarginine (By similarity). {ECO:0000250|UniProtKB:Q00839,
CC ECO:0000250|UniProtKB:Q8VEK3}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}.
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DR EMBL; AABR07021872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473985; EDL94801.1; -; Genomic_DNA.
DR EMBL; BC072529; AAH72529.1; -; mRNA.
DR RefSeq; NP_476480.2; NM_057139.2.
DR AlphaFoldDB; Q6IMY8; -.
DR SMR; Q6IMY8; -.
DR CORUM; Q6IMY8; -.
DR IntAct; Q6IMY8; 8.
DR MINT; Q6IMY8; -.
DR STRING; 10116.ENSRNOP00000046783; -.
DR iPTMnet; Q6IMY8; -.
DR jPOST; Q6IMY8; -.
DR PaxDb; Q6IMY8; -.
DR PRIDE; Q6IMY8; -.
DR Ensembl; ENSRNOT00000044477; ENSRNOP00000046783; ENSRNOG00000033790.
DR GeneID; 117280; -.
DR KEGG; rno:117280; -.
DR CTD; 3192; -.
DR RGD; 620372; Hnrnpu.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000156546; -.
DR HOGENOM; CLU_012140_1_0_1; -.
DR InParanoid; Q6IMY8; -.
DR PhylomeDB; Q6IMY8; -.
DR TreeFam; TF317301; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q6IMY8; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000033790; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q6IMY8; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISO:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0098577; C:inactive sex chromosome; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0008143; F:poly(A) binding; ISO:RGD.
DR GO; GO:0017130; F:poly(C) RNA binding; ISO:RGD.
DR GO; GO:0034046; F:poly(G) binding; IDA:RGD.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:RGD.
DR GO; GO:0017069; F:snRNA binding; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:RGD.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISO:RGD.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:RGD.
DR GO; GO:0016071; P:mRNA metabolic process; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:RGD.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IDA:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1902889; P:protein localization to spindle microtubule; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:1990280; P:RNA localization to chromatin; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12884; SPRY_hnRNP; 1.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR026745; hnRNP_U.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035778; SPRY_hnRNP_U.
DR PANTHER; PTHR12381:SF11; PTHR12381:SF11; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ADP-ribosylation; ATP-binding; Cell cycle;
KW Cell division; Centromere; Chromatin regulator; Chromosome; Citrullination;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Isopeptide bond; Kinetochore; Methylation; Mitosis;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW Spliceosome; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CHAIN 2..798
FT /note="Heterogeneous nuclear ribonucleoprotein U"
FT /id="PRO_0000442272"
FT DOMAIN 8..42
FT /note="SAP"
FT /evidence="ECO:0000250|UniProtKB:Q00839,
FT ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 242..438
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 41..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..646
FT /note="ATPase domain"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT REGION 585..600
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT REGION 645..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..713
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT REGION 743..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 624..651
FT /evidence="ECO:0000255"
FT COMPBIAS 78..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 94..95
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 180
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 229
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 490
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 498
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 506
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 525
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 539
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 609
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 676
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 689
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 694
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 701
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 707
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 707
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 713
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 713
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 728
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 735
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT MOD_RES 787
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 644
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00839"
SQ 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
