UniProt: A0A0G2JZ52

Database: UniProt
Entry: A0A0G2JZ52_RAT

LinkDB:  A0A0G2JZ52_RAT 
Original site:  A0A0G2JZ52_RAT

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Ontology (50)   
   GO (50)   
Gene (4)   
   ENSEMBL-UP (3)   
   RGD (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (15)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (2)   
   PubMed (2)   
All databases (72)   

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ID   A0A0G2JZ52_RAT          Unreviewed;       803 AA.
AC   A0A0G2JZ52;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000313|Ensembl:ENSRNOP00000070912.1};
GN   Name=Hnrnpu {ECO:0000313|Ensembl:ENSRNOP00000070912.1,
GN   ECO:0000313|RGD:620372};
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:0000313|Ensembl:ENSRNOP00000070912.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000070912.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070912.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000070912.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070912.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_006250373.1; XM_006250311.3.
DR   AlphaFoldDB; A0A0G2JZ52; -.
DR   SMR; A0A0G2JZ52; -.
DR   Ensembl; ENSRNOT00000078061.2; ENSRNOP00000070912.1; ENSRNOG00000033790.5.
DR   RGD; 620372; Hnrnpu.
DR   GeneTree; ENSGT00940000156546; -.
DR   OMA; APKMETE; -.
DR   OrthoDB; 5402316at2759; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000033790; Expressed in thymus and 20 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JZ52; baseline and differential.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; IEA:Ensembl.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098577; C:inactive sex chromosome; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:1990498; C:mitotic spindle microtubule; IEA:Ensembl.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR   GO; GO:0008143; F:poly(A) binding; IEA:Ensembl.
DR   GO; GO:0017130; F:poly(C) RNA binding; IEA:Ensembl.
DR   GO; GO:0034046; F:poly(G) binding; IEA:Ensembl.
DR   GO; GO:0036002; F:pre-mRNA binding; IEA:Ensembl.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0017069; F:snRNA binding; IEA:Ensembl.
DR   GO; GO:0070034; F:telomerase RNA binding; IEA:Ensembl.
DR   GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR   GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:Ensembl.
DR   GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0034244; P:negative regulation of transcription elongation by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:Ensembl.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1902889; P:protein localization to spindle microtubule; IEA:Ensembl.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:1902275; P:regulation of chromatin organization; IEA:Ensembl.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR   CDD; cd12884; SPRY_hnRNP; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U; 1.
DR   PANTHER; PTHR12381; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U FAMILY MEMBER; 1.
DR   Pfam; PF13671; AAA_33; 1.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   803 AA;  87932 MW;  55C252B302951DC3 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
     GSVHVNVLCE EYRGPTKCVP VIP
//

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