ZN629_HUMAN
ID ZN629_HUMAN Reviewed; 869 AA.
AC Q9UEG4; Q15938;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Zinc finger protein 629;
DE AltName: Full=Zinc finger protein 65;
GN Name=ZNF629; Synonyms=KIAA0326, ZNF65;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-255.
RC TISSUE=Placenta;
RX PubMed=1946370; DOI=10.1073/pnas.88.21.9563;
RA Bray P.L., Lichter P., Thiesen H.-J., Ward D.C., Dawid I.B.;
RT "Characterization and mapping of human genes encoding zinc finger
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9563-9567(1991).
RN [3]
RP IDENTIFICATION.
RX PubMed=1505991; DOI=10.1016/0888-7543(92)90013-i;
RA Lichter P., Bray P., Ried T., Dawid I.B., Ward D.C.;
RT "Clustering of C2-H2 zinc finger motif sequences within telomeric and
RT fragile site regions of human chromosomes.";
RL Genomics 13:999-1007(1992).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-616, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-688 AND LYS-840, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-251; LYS-688; LYS-750 AND
RP LYS-840, AND 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9UEG4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-9977294, EBI-10175300;
CC Q9UEG4; Q86X02: CDR2L; NbExp=3; IntAct=EBI-9977294, EBI-11063830;
CC Q9UEG4; O95995: GAS8; NbExp=3; IntAct=EBI-9977294, EBI-1052570;
CC Q9UEG4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-9977294, EBI-5916454;
CC Q9UEG4; Q14541-2: HNF4G; NbExp=3; IntAct=EBI-9977294, EBI-18543805;
CC Q9UEG4; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-9977294, EBI-18398632;
CC Q9UEG4; O75564-2: JRK; NbExp=3; IntAct=EBI-9977294, EBI-17181882;
CC Q9UEG4; O95751: LDOC1; NbExp=3; IntAct=EBI-9977294, EBI-740738;
CC Q9UEG4; P36873: PPP1CC; NbExp=3; IntAct=EBI-9977294, EBI-356283;
CC Q9UEG4; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-9977294, EBI-748350;
CC Q9UEG4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-9977294, EBI-358489;
CC Q9UEG4; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9977294, EBI-742688;
CC Q9UEG4; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-9977294, EBI-11139477;
CC Q9UEG4; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-9977294, EBI-725997;
CC Q9UEG4; P13994: YJU2B; NbExp=3; IntAct=EBI-9977294, EBI-716093;
CC Q9UEG4; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-9977294, EBI-11962468;
CC Q9UEG4; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-9977294, EBI-5667516;
CC Q9UEG4; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-9977294, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002324; BAA20784.1; ALT_INIT; mRNA.
DR EMBL; M88374; AAA61332.1; -; Genomic_DNA.
DR CCDS; CCDS45463.1; -.
DR PIR; H45193; H45193.
DR RefSeq; NP_001073886.1; NM_001080417.2.
DR RefSeq; NP_001332899.1; NM_001345970.1.
DR AlphaFoldDB; Q9UEG4; -.
DR SMR; Q9UEG4; -.
DR BioGRID; 116942; 116.
DR IntAct; Q9UEG4; 30.
DR MINT; Q9UEG4; -.
DR STRING; 9606.ENSP00000262525; -.
DR iPTMnet; Q9UEG4; -.
DR PhosphoSitePlus; Q9UEG4; -.
DR BioMuta; ZNF629; -.
DR DMDM; 134035371; -.
DR EPD; Q9UEG4; -.
DR jPOST; Q9UEG4; -.
DR MassIVE; Q9UEG4; -.
DR MaxQB; Q9UEG4; -.
DR PaxDb; Q9UEG4; -.
DR PeptideAtlas; Q9UEG4; -.
DR PRIDE; Q9UEG4; -.
DR ProteomicsDB; 84146; -.
DR Antibodypedia; 7095; 12 antibodies from 7 providers.
DR DNASU; 23361; -.
DR Ensembl; ENST00000262525.6; ENSP00000262525.4; ENSG00000102870.6.
DR GeneID; 23361; -.
DR KEGG; hsa:23361; -.
DR MANE-Select; ENST00000262525.6; ENSP00000262525.4; NM_001080417.3; NP_001073886.1.
DR UCSC; uc002dzs.1; human.
DR CTD; 23361; -.
DR DisGeNET; 23361; -.
DR GeneCards; ZNF629; -.
DR HGNC; HGNC:29008; ZNF629.
DR HPA; ENSG00000102870; Low tissue specificity.
DR MIM; 619587; gene.
DR neXtProt; NX_Q9UEG4; -.
DR OpenTargets; ENSG00000102870; -.
DR PharmGKB; PA134930939; -.
DR VEuPathDB; HostDB:ENSG00000102870; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161909; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q9UEG4; -.
DR OMA; FKMPEGQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9UEG4; -.
DR TreeFam; TF350847; -.
DR PathwayCommons; Q9UEG4; -.
DR SignaLink; Q9UEG4; -.
DR BioGRID-ORCS; 23361; 52 hits in 1100 CRISPR screens.
DR ChiTaRS; ZNF629; human.
DR GenomeRNAi; 23361; -.
DR Pharos; Q9UEG4; Tdark.
DR PRO; PR:Q9UEG4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UEG4; protein.
DR Bgee; ENSG00000102870; Expressed in tendon of biceps brachii and 195 other tissues.
DR Genevisible; Q9UEG4; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF57667; SSF57667; 13.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..869
FT /note="Zinc finger protein 629"
FT /id="PRO_0000280426"
FT ZN_FING 150..172
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 178..200
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..228
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..284
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 318..340
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 346..368
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 402..424
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..536
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 569..591
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 714..736
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 768..790
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 842..864
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 840
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 707
FT /note="P -> A (in dbSNP:rs8050758)"
FT /id="VAR_052883"
SQ SEQUENCE 869 AA; 96620 MW; A3C1B86589BD57F5 CRC64;
MEPETALWGP DLQGPEQSPN DAHRGAESEN EEESPRQESS GEEIIMGDPA QSPESKDSTE
MSLERSSQDP SVPQNPPTPL GHSNPLDHQI PLDPPAPEVV PTPSDWTKAC EASWQWGALT
TWNSPPVVPA NEPSLRELVQ GRPAGAEKPY ICNECGKSFS QWSKLLRHQR IHTGERPNTC
SECGKSFTQS SHLVQHQRTH TGEKPYKCPD CGKCFSWSSN LVQHQRTHTG EKPYKCTECE
KAFTQSTNLI KHQRSHTGEK PYKCGECRRA FYRSSDLIQH QATHTGEKPY KCPECGKRFG
QNHNLLKHQK IHAGEKPYRC TECGKSFIQS SELTQHQRTH TGEKPYECLE CGKSFGHSST
LIKHQRTHLR EDPFKCPVCG KTFTLSATLL RHQRTHTGER PYKCPECGKS FSVSSNLINH
QRIHRGERPY ICADCGKSFI MSSTLIRHQR IHTGEKPYKC SDCGKSFIRS SHLIQHRRTH
TGEKPYKCPE CGKSFSQSSN LITHVRTHMD ENLFVCSDCG KAFLEAHELE QHRVIHERGK
TPARRAQGDS LLGLGDPSLL TPPPGAKPHK CLVCGKGFND EGIFMQHQRI HIGENPYKNA
DGLIAHAAPK PPQLRSPRLP FRGNSYPGAA EGRAEAPGQP LKPPEGQEGF SQRRGLLSSK
TYICSHCGES FLDRSVLLQH QLTHGNEKPF LFPDYRIGLG EGAGPSPFLS GKPFKCPECK
QSFGLSSELL LHQKVHAGGK SSQKSPELGK SSSVLLEHLR SPLGARPYRC SDCRASFLDR
VALTRHQETH TQEKPPNPED PPPEAVTLST DQEGEGETPT PTESSSHGEG QNPKTLVEEK
PYLCPECGAG FTEVAALLLH RSCHPGVSL
