ZN638_HUMAN
ID ZN638_HUMAN Reviewed; 1978 AA.
AC Q14966; A0A096LPH6; B5MDV1; B7ZLD1; Q53R34; Q5XJ05; Q68DP3; Q6P2H2; Q7Z3T7;
AC Q8NF92; Q8TCA1; Q9H2G1; Q9NP37;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Zinc finger protein 638;
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen se33-1 {ECO:0000303|PubMed:11149944};
DE Short=CTCL-associated antigen se33-1 {ECO:0000303|PubMed:11149944};
DE AltName: Full=Nuclear protein 220 {ECO:0000303|PubMed:8647861};
DE AltName: Full=Zinc finger matrin-like protein;
GN Name=ZNF638; Synonyms=NP220 {ECO:0000303|PubMed:8647861}, ZFML;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RC TISSUE=Epithelium;
RX PubMed=8647861; DOI=10.1074/jbc.271.21.12525;
RA Inagaki H., Matsushima Y., Nakamura K., Ohshima M., Kadowaki T.,
RA Kitagawa Y.;
RT "A large DNA-binding nuclear protein with RNA recognition motif and
RT serine/arginine-rich domain.";
RL J. Biol. Chem. 271:12525-12531(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), IDENTIFICATION AS TUMOR-ASSOCIATED
RP ANTIGEN, AND VARIANTS SER-980 AND VAL-1912.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RA Chan C.W., Tsui S.K.W., Fung K.P., Lee C.Y., Waye M.M.Y.;
RT "Identification of a variant splice form of human nuclear protein NP220
RT mRNA encoding an isoform with truncated carboxyl-terminal.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-110
RP AND MET-1726.
RC TISSUE=Cervix, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Cerebellum, Skin, and Testis;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FHL2.
RX PubMed=11813260; DOI=10.1002/jcb.10041.abs;
RA Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y.,
RA Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P.;
RT "Interaction of the heart-specific LIM domain protein, FHL2, with DNA-
RT binding nuclear protein, hNP220.";
RL J. Cell. Biochem. 84:556-566(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-383; SER-420;
RP SER-614; SER-1401 AND SER-1882, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-1100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-383; SER-552 AND
RP SER-1667, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
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., Buerckstuemmer 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1401, AND IDENTIFICATION BY
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-289; SER-299;
RP SER-369; SER-383; SER-420; SER-552; SER-605; SER-636; SER-1100; SER-1667
RP AND SER-1882, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [21]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-47; ARG-49 AND ARG-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-292; LYS-775; LYS-1676 AND
RP LYS-1820, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-913 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
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).
RN [23]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH MPHOSPH8; TASOR; SETDB1; HDAC1
RP AND HDAC4.
RX PubMed=30487602; DOI=10.1038/s41586-018-0750-6;
RA Zhu Y., Wang G.Z., Cingoez O., Goff S.P.;
RT "NP220 mediates silencing of unintegrated retroviral DNA.";
RL Nature 564:278-282(2018).
CC -!- FUNCTION: Transcription factor that binds to cytidine clusters in
CC double-stranded DNA (PubMed:8647861, PubMed:30487602). Plays a key role
CC in the silencing of unintegrated retroviral DNA: some part of the
CC retroviral DNA formed immediately after infection remains unintegrated
CC in the host genome and is transcriptionally repressed
CC (PubMed:30487602). Mediates transcriptional repression of unintegrated
CC viral DNA by specifically binding to the cytidine clusters of
CC retroviral DNA and mediating the recruitment of chromatin silencers,
CC such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and
CC HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by
CC acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or
CC CEBPG), controlling the expression of PPARG and probably of other
CC proadipogenic genes, such as SREBF1 (By similarity). May also regulate
CC alternative splicing of target genes during adipogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q61464,
CC ECO:0000269|PubMed:30487602, ECO:0000269|PubMed:8647861}.
CC -!- SUBUNIT: Interacts with FHL2 (PubMed:11813260). Interacts with CEBPA,
CC CEBPD and CEBPG (By similarity). Interacts with MPHOSPH8 and TASOR
CC components of the HUSH complex; leading to recruitment of the HUSH
CC complex (PubMed:30487602). Interacts with SETDB1 (PubMed:30487602).
CC Interacts with HDAC1 (PubMed:30487602). Interacts with HDAC4
CC (PubMed:30487602). {ECO:0000250|UniProtKB:Q61464,
CC ECO:0000269|PubMed:11813260, ECO:0000269|PubMed:30487602}.
CC -!- INTERACTION:
CC Q14966-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-25845021, EBI-10968534;
CC Q14966-2; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-25845021, EBI-11110431;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00130, ECO:0000269|PubMed:11813260,
CC ECO:0000269|PubMed:8647861}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q14966-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14966-2; Sequence=VSP_014802, VSP_014803;
CC Name=3;
CC IsoId=Q14966-3; Sequence=VSP_014806;
CC Name=4;
CC IsoId=Q14966-4; Sequence=VSP_014804, VSP_014805;
CC Name=5;
CC IsoId=Q14966-5; Sequence=VSP_014801;
CC Name=6;
CC IsoId=Q14966-6; Sequence=VSP_059342, VSP_059343;
CC -!- DOMAIN: The matrin-type zinc finger domain is required for localization
CC to nuclear speckles. {ECO:0000250|UniProtKB:Q61464}.
CC -!- MISCELLANEOUS: [Isoform 5]: Tumor-associated antigen found in several
CC cutaneous T-cell lymphoma (CTCL), and in particular in mycosis
CC fungoides patients and in Sezary syndrome patients.
CC {ECO:0000305|PubMed:11149944}.
CC -!- MISCELLANEOUS: [Isoform 5]: Broadly expressed. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64530.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; D83032; BAA11748.1; -; mRNA.
DR EMBL; AF273049; AAG34909.1; -; mRNA.
DR EMBL; AF534078; AAM97681.1; -; mRNA.
DR EMBL; BX537425; CAD97667.1; -; mRNA.
DR EMBL; CR749322; CAH18177.1; -; mRNA.
DR EMBL; AC007878; AAF66079.1; -; Genomic_DNA.
DR EMBL; AC096569; AAY14979.1; -; Genomic_DNA.
DR EMBL; AC104084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024000; AAH24000.1; -; mRNA.
DR EMBL; BC064530; AAH64530.1; ALT_SEQ; mRNA.
DR EMBL; BC083513; AAH83513.1; -; mRNA.
DR EMBL; BC143728; AAI43729.1; -; mRNA.
DR CCDS; CCDS1917.1; -. [Q14966-1]
DR PIR; JU0239; JU0239.
DR PIR; JU0240; JU0240.
DR RefSeq; NP_001014972.1; NM_001014972.2. [Q14966-1]
DR RefSeq; NP_001239541.1; NM_001252612.1. [Q14966-1]
DR RefSeq; NP_001239542.1; NM_001252613.1. [Q14966-3]
DR RefSeq; NP_055312.2; NM_014497.4. [Q14966-1]
DR PDB; 6SXW; X-ray; 2.75 A; A=676-749.
DR PDBsum; 6SXW; -.
DR AlphaFoldDB; Q14966; -.
DR SMR; Q14966; -.
DR BioGRID; 118145; 241.
DR DIP; DIP-42386N; -.
DR IntAct; Q14966; 69.
DR MINT; Q14966; -.
DR STRING; 9606.ENSP00000386433; -.
DR GlyGen; Q14966; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14966; -.
DR PhosphoSitePlus; Q14966; -.
DR BioMuta; ZNF638; -.
DR DMDM; 71153483; -.
DR CPTAC; CPTAC-1371; -.
DR EPD; Q14966; -.
DR jPOST; Q14966; -.
DR MassIVE; Q14966; -.
DR MaxQB; Q14966; -.
DR PaxDb; Q14966; -.
DR PeptideAtlas; Q14966; -.
DR PRIDE; Q14966; -.
DR ProteomicsDB; 60262; -. [Q14966-1]
DR ProteomicsDB; 60263; -. [Q14966-2]
DR ProteomicsDB; 60264; -. [Q14966-3]
DR ProteomicsDB; 60265; -. [Q14966-4]
DR ProteomicsDB; 60266; -. [Q14966-5]
DR Antibodypedia; 31207; 103 antibodies from 22 providers.
DR DNASU; 27332; -.
DR Ensembl; ENST00000264447.9; ENSP00000264447.4; ENSG00000075292.19. [Q14966-1]
DR Ensembl; ENST00000409544.5; ENSP00000386433.1; ENSG00000075292.19. [Q14966-1]
DR Ensembl; ENST00000410075.5; ENSP00000485608.1; ENSG00000075292.19. [Q14966-6]
DR GeneID; 27332; -.
DR KEGG; hsa:27332; -.
DR MANE-Select; ENST00000264447.9; ENSP00000264447.4; NM_014497.5; NP_055312.2.
DR UCSC; uc002shx.4; human. [Q14966-1]
DR CTD; 27332; -.
DR DisGeNET; 27332; -.
DR GeneCards; ZNF638; -.
DR HGNC; HGNC:17894; ZNF638.
DR HPA; ENSG00000075292; Low tissue specificity.
DR MIM; 614349; gene.
DR neXtProt; NX_Q14966; -.
DR OpenTargets; ENSG00000075292; -.
DR PharmGKB; PA134983478; -.
DR VEuPathDB; HostDB:ENSG00000075292; -.
DR eggNOG; ENOG502QVQ7; Eukaryota.
DR GeneTree; ENSGT00940000153322; -.
DR HOGENOM; CLU_002180_0_0_1; -.
DR InParanoid; Q14966; -.
DR OMA; GQTNKPD; -.
DR OrthoDB; 301913at2759; -.
DR PhylomeDB; Q14966; -.
DR TreeFam; TF333921; -.
DR PathwayCommons; Q14966; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q14966; -.
DR BioGRID-ORCS; 27332; 56 hits in 1083 CRISPR screens.
DR ChiTaRS; ZNF638; human.
DR GeneWiki; ZNF638; -.
DR GenomeRNAi; 27332; -.
DR Pharos; Q14966; Tbio.
DR PRO; PR:Q14966; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q14966; protein.
DR Bgee; ENSG00000075292; Expressed in calcaneal tendon and 207 other tissues.
DR ExpressionAtlas; Q14966; baseline and differential.
DR Genevisible; Q14966; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033096; ZNF638.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15592:SF1; PTHR15592:SF1; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1978
FT /note="Zinc finger protein 638"
FT /id="PRO_0000082011"
FT DOMAIN 676..751
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 905..979
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DNA_BIND 1353..1477
FT /evidence="ECO:0000269|PubMed:8647861"
FT ZN_FING 1928..1958
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..571
FT /note="Involved in localization to nuclear speckles"
FT /evidence="ECO:0000250|UniProtKB:Q61464"
FT REGION 835..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1946..1978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..543
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 49
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 54
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61464"
FT MOD_RES 1667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1820
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..903
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11149944"
FT /id="VSP_014801"
FT VAR_SEQ 793..918
FT /note="AKTGQAKASVAKVNKSTGKSASSVKSVVTVAVKGNKASIKTAKSGGKKSLEA
FT KKTGNVKNKDSNKPVTIPENSEIKTSIEVKATENCAKEAISDAALEATENEPLNKETEE
FT MCVMLVSNLPNKGYS -> ESVDQTQQLVPLVRNTARDHDGTPENEGEETVQSALFGFQ
FT YDASDHTMAWLGPNTVPEVKEMILQDPQLQTTQLPQTTQAPDITWGMLKKTTYKAEQIL
FT LQTQKPFTPDNLFLALLSGDAKPEYEQ (in isoform 6)"
FT /id="VSP_059342"
FT VAR_SEQ 793..814
FT /note="AKTGQAKASVAKVNKSTGKSAS -> GLLPTGGGNNYPQIVLAPGLCH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014802"
FT VAR_SEQ 815..1978
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014803"
FT VAR_SEQ 919..1978
FT /note="Missing (in isoform 6)"
FT /id="VSP_059343"
FT VAR_SEQ 1100..1139
FT /note="SPGLKNSPIDESEVQTATDSPSVKPNELEEESTPSIQTET -> RLWLSKTL
FT RILKALLVEVPNLKRSHYFHLIWMNLLLWMRL (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014804"
FT VAR_SEQ 1140..1978
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014805"
FT VAR_SEQ 1918..1938
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014806"
FT VARIANT 110
FT /note="I -> V (in dbSNP:rs12612365)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_023069"
FT VARIANT 980
FT /note="N -> S (in dbSNP:rs3732235)"
FT /evidence="ECO:0000269|PubMed:11149944"
FT /id="VAR_023070"
FT VARIANT 1462
FT /note="S -> N (in dbSNP:rs10427371)"
FT /id="VAR_052238"
FT VARIANT 1726
FT /note="V -> M (in dbSNP:rs1804020)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_023071"
FT VARIANT 1912
FT /note="A -> V (in dbSNP:rs11542286)"
FT /evidence="ECO:0000269|PubMed:11149944"
FT /id="VAR_023072"
FT CONFLICT 58
FT /note="H -> L (in Ref. 1; BAA11748)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="I -> V (in Ref. 3; AAM97681)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="M -> I (in Ref. 4; CAD97667)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="A -> V (in Ref. 4; CAH18177)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="S -> C (in Ref. 1; BAA11748)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="A -> D (in Ref. 4; CAD97667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="F -> L (in Ref. 4; CAD97667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="S -> P (in Ref. 4; CAD97667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336
FT /note="G -> S (in Ref. 4; CAH18177)"
FT /evidence="ECO:0000305"
FT CONFLICT 1404
FT /note="A -> T (in Ref. 4; CAD97667)"
FT /evidence="ECO:0000305"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:6SXW"
FT HELIX 690..697
FT /evidence="ECO:0007829|PDB:6SXW"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:6SXW"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:6SXW"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:6SXW"
FT STRAND 714..722
FT /evidence="ECO:0007829|PDB:6SXW"
FT HELIX 723..732
FT /evidence="ECO:0007829|PDB:6SXW"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:6SXW"
FT CROSSLNK Q14966-6:913
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1978 AA; 220625 MW; FC006A4BA4885455 CRC64;
MSRPRFNPRG DFPLQRPRAP NPSGMRPPGP FMRPGSMGLP RFYPAGRARG IPHRFAGHES
YQNMGPQRMN VQVTQHRTDP RLTKEKLDFH EAQQKKGKPH GSRWDDEPHI SASVAVKQSS
VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR
KMGRRLPNLP SQSRNKETLG SEAVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVEN
EFQSQQNISA SVPNPNVICN SMFPVEDVFR QMDFPGESSN NRSFFSVESG TKMSGLHISG
GQSVLEPIKS VNQSINQTVS QTMSQSLIPP SMNQQPFSSE LISSVSQQER IPHEPVINSS
NVHVGSRGSK KNYQSQADIP IRSPFGIVKA SWLPKFSHAD AQKMKRLPTP SMMNDYYAAS
PRIFPHLCSL CNVECSHLKD WIQHQNTSTH IESCRQLRQQ YPDWNPEILP SRRNEGNRKE
NETPRRRSHS PSPRRSRRSS SSHRFRRSRS PMHYMYRPRS RSPRICHRFI SRYRSRSRSR
SPYRIRNPFR GSPKCFRSVS PERMSRRSVR SSDRKKALED VVQRSGHGTE FNKQKHLEAA
DKGHSPAQKP KTSSGTKPSV KPTSATKSDS NLGGHSIRCK SKNLEDDTLS ECKQVSDKAV
SLQRKLRKEQ SLHYGSVLLI TELPEDGCTE EDVRKLFQPF GKVNDVLIVP YRKEAYLEME
FKEAITAIMK YIETTPLTIK GKSVKICVPG KKKAQNKEVK KKTLESKKVS ASTLKRDADA
SKAVEIVTST SAAKTGQAKA SVAKVNKSTG KSASSVKSVV TVAVKGNKAS IKTAKSGGKK
SLEAKKTGNV KNKDSNKPVT IPENSEIKTS IEVKATENCA KEAISDAALE ATENEPLNKE
TEEMCVMLVS NLPNKGYSVE EVYDLAKPFG GLKDILILSS HKKAYIEINR KAAESMVKFY
TCFPVLMDGN QLSISMAPEN MNIKDEEAIF ITLVKENDPE ANIDTIYDRF VHLDNLPEDG
LQCVLCVGLQ FGKVDHHVFI SNRNKAILQL DSPESAQSMY SFLKQNPQNI GDHMLTCSLS
PKIDLPEVQI EHDPELEKES PGLKNSPIDE SEVQTATDSP SVKPNELEEE STPSIQTETL
VQQEEPCEEE AEKATCDSDF AVETLELETQ GEEVKEEIPL VASASVSIEQ FTENAEECAL
NQQMFNSDLE KKGAEIINPK TALLPSDSVF AEERNLKGIL EESPSEAEDF ISGITQTMVE
AVAEVEKNET VSEILPSTCI VTLVPGIPTG DEKTVDKKNI SEKKGNMDEK EEKEFNTKET
RMDLQIGTEK AEKNEGRMDA EKVEKMAAMK EKPAENTLFK AYPNKGVGQA NKPDETSKTS
ILAVSDVSSS KPSIKAVIVS SPKAKATVSK TENQKSFPKS VPRDQINAEK KLSAKEFGLL
KPTSARSGLA ESSSKFKPTQ SSLTRGGSGR ISALQGKLSK LDYRDITKQS QETEARPSIM
KRDDSNNKTL AEQNTKNPKS TTGRSSKSKE EPLFPFNLDE FVTVDEVIEE VNPSQAKQNP
LKGKRKETLK NVPFSELNLK KKKGKTSTPR GVEGELSFVT LDEIGEEEDA AAHLAQALVT
VDEVIDEEEL NMEEMVKNSN SLFTLDELID QDDCISHSEP KDVTVLSVAE EQDLLKQERL
VTVDEIGEVE ELPLNESADI TFATLNTKGN EGDTVRDSIG FISSQVPEDP STLVTVDEIQ
DDSSDLHLVT LDEVTEEDED SLADFNNLKE ELNFVTVDEV GEEEDGDNDL KVELAQSKND
HPTDKKGNRK KRAVDTKKTK LESLSQVGPV NENVMEEDLK TMIERHLTAK TPTKRVRIGK
TLPSEKAVVT EPAKGEEAFQ MSEVDEESGL KDSEPERKRK KTEDSSSGKS VASDVPEELD
FLVPKAGFFC PICSLFYSGE KAMTNHCKST RHKQNTEKFM AKQRKEKEQN EAEERSSR
