GenomeNet

Database: UniProt
Entry: C9JQE8
LinkDB: C9JQE8
Original site: C9JQE8 
ID   C9JQE8_HUMAN            Unreviewed;      1451 AA.
AC   C9JQE8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   29-SEP-2021, entry version 91.
DE   SubName: Full=Nuclear receptor corepressor 2 {ECO:0000313|Ensembl:ENSP00000402808};
DE   Flags: Fragment;
GN   Name=NCOR2 {ECO:0000313|Ensembl:ENSP00000402808};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000402808, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0007829|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000402808, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RG   Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A., null.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3] {ECO:0007829|PubMed:18220336}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [4] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5] {ECO:0007829|PubMed:19413330}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6] {ECO:0007829|PubMed:19690332}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7] {ECO:0007829|PubMed:19608861}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10] {ECO:0007829|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [11] {ECO:0000313|Ensembl:ENSP00000402808}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [12] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14] {ECO:0007829|PubMed:28112733}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC       {ECO:0000256|ARBA:ARBA00010097}.
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DR   EMBL; AC069261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; C9JQE8; -.
DR   EPD; C9JQE8; -.
DR   MaxQB; C9JQE8; -.
DR   PeptideAtlas; C9JQE8; -.
DR   ProteomicsDB; 11234; -.
DR   Antibodypedia; 1103; 270 antibodies.
DR   Ensembl; ENST00000458234; ENSP00000402808; ENSG00000196498.
DR   UCSC; uc058uxg.1; human.
DR   HGNC; HGNC:7673; NCOR2.
DR   OpenTargets; ENSG00000196498; -.
DR   VEuPathDB; HostDB:ENSG00000196498; -.
DR   GeneTree; ENSGT00940000159022; -.
DR   HOGENOM; CLU_004689_0_0_1; -.
DR   ChiTaRS; NCOR2; human.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000196498; Expressed in sural nerve and 247 other tissues.
DR   ExpressionAtlas; C9JQE8; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR031557; N-CoR_GPS2_interact.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF15784; GPS2_interact; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
DR   PROSITE; PS51293; SANT; 2.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Proteomics identification {ECO:0007829|EPD:C9JQE8,
KW   ECO:0007829|MaxQB:C9JQE8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          427..478
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          610..661
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          613..657
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   DOMAIN          614..661
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51294"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..1033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1296..1315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1430..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          299..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        190..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..794
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..821
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1008
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1451
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000402808"
SQ   SEQUENCE   1451 AA;  160396 MW;  52D25D314CEF61F8 CRC64;
     MSGSTQPVAQ TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA SHLSPGSIIQ
     PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM EFIESKRPRL ELLPDPLLRP
     SPLLATGQPA GSEDLTKDRS LTGKLEPVSP PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD
     REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA
     AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ
     RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG
     LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMADPM
     KVYKDRQVMN MWSEQEKETF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK
     SLVRRSYRRR GKSQQQQQQQ QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN
     DKEDLLKEKT DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ
     SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK NFYFNYKKRQ
     NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV EDEEMEASGV SGNEEEMVEE
     AEALHASGNE VPRGECSGPA TVNNSSDTES IPSPHTEAAK DTGQNGPKPP ATLGADGPPP
     GPPTPPPEDI PAPTEPTPAS EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG
     EEQKPPAAEE LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS
     GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD PRANASPQKP
     LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP PPQNLQPESD APQQPGSSPR
     GKSRSPAPPA DKEAEKPVFF PAFAAEAQKL PGDPPCWTSG LPFPVPPREV IKASPHAPDP
     SAFSYAPPGH PLPLGLHDTA RPVLPRPPTI SNPPPLISSA KHPSVLERQI GAISQGMSVQ
     LHVPYSEHAK APVGPVTMGL PLPMDPKKLA PFSGVKQEQL SPRGQAGPPE SLGVPTAQEA
     SVLRGTALGS VPGGSITKGI PSTRVPSDSA ITYRGSITHG TPADVLYKGT ITRIIGEDSP
     SRLDRGREDS LPKGHVIYEG KKGHVLSYEG GMSVTQCSKE DGRSSSGPPH ETAAPKRTYD
     MMEGRVGRAI SSASIEGLMG RAIPPERHSP HHLKEQHHIR GSITQGIPRS YVEAQEDYLR
     REAKLLKREG TPPPPPPSRD LTEAYKTQAL GPLKLKPAHE GLVATVKEAG RSIHEIPREE
     LRHTPELPLA P
//
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