ID   ZN331_HUMAN             Reviewed;         463 AA.
AC   Q9NQX6; Q96GJ4;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Zinc finger protein 331;
DE   AltName: Full=C2H2-like zinc finger protein rearranged in thyroid adenomas;
DE   AltName: Full=Zinc finger protein 361;
DE   AltName: Full=Zinc finger protein 463;
GN   Name=ZNF331; Synonyms=RITA, ZNF361, ZNF463;
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].
RC   TISSUE=Testis;
RX   PubMed=10502321;
RX   DOI=10.1002/(sici)1098-2264(199911)26:3<229::aid-gcc7>3.3.co;2-a;
RA   Rippe V., Belge G., Meiboom M., Kazmierczak B., Fusco A., Bullerdiek J.;
RT   "A KRAB zinc finger protein gene is the potential target of 19q13
RT   translocation in benign thyroid tumors.";
RL   Genes Chromosomes Cancer 26:229-236(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=11267678; DOI=10.1016/s0167-4781(01)00172-5;
RA   Wu H., Zhang S., Qiu W., Zhang G., Xia Q., Xiao C., Huang X., Huang M.,
RA   Agen P., Fan T., Yang J., Milunsky A.;
RT   "Isolation, characterization, and mapping of a novel human KRAB zinc finger
RT   protein encoding gene ZNF463.";
RL   Biochim. Biophys. Acta 1518:190-193(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-400, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109 AND LYS-400, 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).
CC   -!- FUNCTION: May be involved in transcriptional regulation. May play a
CC       role in spermatogenesis.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF272148; AAF78075.1; -; mRNA.
DR   EMBL; AF251515; AAF70179.2; -; mRNA.
DR   EMBL; BC009433; AAH09433.1; -; mRNA.
DR   CCDS; CCDS33102.1; -.
DR   RefSeq; NP_001073375.1; NM_001079906.1.
DR   RefSeq; NP_001073376.1; NM_001079907.1.
DR   RefSeq; NP_001240727.1; NM_001253798.1.
DR   RefSeq; NP_001240728.1; NM_001253799.1.
DR   RefSeq; NP_001240729.1; NM_001253800.1.
DR   RefSeq; NP_001240730.1; NM_001253801.2.
DR   RefSeq; NP_001304042.1; NM_001317113.1.
DR   RefSeq; NP_001304043.1; NM_001317114.1.
DR   RefSeq; NP_001304044.1; NM_001317115.1.
DR   RefSeq; NP_001304045.1; NM_001317116.1.
DR   RefSeq; NP_001304046.1; NM_001317117.1.
DR   RefSeq; NP_001304047.1; NM_001317118.1.
DR   RefSeq; NP_001304048.1; NM_001317119.1.
DR   RefSeq; NP_001304049.1; NM_001317120.1.
DR   RefSeq; NP_001304050.1; NM_001317121.1.
DR   RefSeq; NP_061025.5; NM_018555.5.
DR   RefSeq; XP_011525378.1; XM_011527076.2.
DR   RefSeq; XP_011525380.1; XM_011527078.2.
DR   RefSeq; XP_016882425.1; XM_017026936.1.
DR   RefSeq; XP_016882426.1; XM_017026937.1.
DR   RefSeq; XP_016882427.1; XM_017026938.1.
DR   RefSeq; XP_016882428.1; XM_017026939.1.
DR   RefSeq; XP_016882429.1; XM_017026940.1.
DR   AlphaFoldDB; Q9NQX6; -.
DR   SMR; Q9NQX6; -.
DR   BioGRID; 120663; 61.
DR   IntAct; Q9NQX6; 60.
DR   MINT; Q9NQX6; -.
DR   STRING; 9606.ENSP00000253144; -.
DR   iPTMnet; Q9NQX6; -.
DR   PhosphoSitePlus; Q9NQX6; -.
DR   BioMuta; ZNF331; -.
DR   DMDM; 34925661; -.
DR   EPD; Q9NQX6; -.
DR   jPOST; Q9NQX6; -.
DR   MassIVE; Q9NQX6; -.
DR   PaxDb; 9606-ENSP00000253144; -.
DR   PeptideAtlas; Q9NQX6; -.
DR   ProteomicsDB; 82225; -.
DR   Pumba; Q9NQX6; -.
DR   Antibodypedia; 32728; 128 antibodies from 19 providers.
DR   DNASU; 55422; -.
DR   Ensembl; ENST00000253144.13; ENSP00000253144.9; ENSG00000130844.19.
DR   Ensembl; ENST00000449416.6; ENSP00000393817.1; ENSG00000130844.19.
DR   Ensembl; ENST00000504493.6; ENSP00000425517.2; ENSG00000130844.19.
DR   Ensembl; ENST00000511154.5; ENSP00000421014.1; ENSG00000130844.19.
DR   Ensembl; ENST00000511593.6; ENSP00000427439.1; ENSG00000130844.19.
DR   Ensembl; ENST00000512387.6; ENSP00000421728.1; ENSG00000130844.19.
DR   Ensembl; ENST00000513999.5; ENSP00000423156.1; ENSG00000130844.19.
DR   Ensembl; ENST00000648122.1; ENSP00000496977.1; ENSG00000130844.19.
DR   Ensembl; ENST00000648236.1; ENSP00000497263.1; ENSG00000130844.19.
DR   Ensembl; ENST00000648397.1; ENSP00000497726.1; ENSG00000130844.19.
DR   Ensembl; ENST00000648511.1; ENSP00000497652.1; ENSG00000130844.19.
DR   Ensembl; ENST00000649326.1; ENSP00000498006.1; ENSG00000130844.19.
DR   GeneID; 55422; -.
DR   KEGG; hsa:55422; -.
DR   MANE-Select; ENST00000449416.6; ENSP00000393817.1; NM_001079906.2; NP_001073375.1.
DR   UCSC; uc002qbx.2; human.
DR   AGR; HGNC:15489; -.
DR   CTD; 55422; -.
DR   DisGeNET; 55422; -.
DR   GeneCards; ZNF331; -.
DR   HGNC; HGNC:15489; ZNF331.
DR   HPA; ENSG00000130844; Tissue enhanced (adrenal).
DR   MIM; 606043; gene.
DR   neXtProt; NX_Q9NQX6; -.
DR   OpenTargets; ENSG00000130844; -.
DR   PharmGKB; PA134866703; -.
DR   VEuPathDB; HostDB:ENSG00000130844; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161267; -.
DR   HOGENOM; CLU_002678_44_0_1; -.
DR   InParanoid; Q9NQX6; -.
DR   OMA; LDWMCEG; -.
DR   OrthoDB; 3120634at2759; -.
DR   PhylomeDB; Q9NQX6; -.
DR   TreeFam; TF341817; -.
DR   PathwayCommons; Q9NQX6; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9NQX6; -.
DR   BioGRID-ORCS; 55422; 12 hits in 1162 CRISPR screens.
DR   ChiTaRS; ZNF331; human.
DR   GeneWiki; ZNF331; -.
DR   GenomeRNAi; 55422; -.
DR   Pharos; Q9NQX6; Tbio.
DR   PRO; PR:Q9NQX6; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9NQX6; Protein.
DR   Bgee; ENSG00000130844; Expressed in lower lobe of lung and 207 other cell types or tissues.
DR   ExpressionAtlas; Q9NQX6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 12.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF147; KRAB DOMAIN-CONTAINING PROTEIN 5-RELATED; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   Pfam; PF13912; zf-C2H2_6; 2.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
DR   Genevisible; Q9NQX6; HS.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..463
FT                   /note="Zinc finger protein 331"
FT                   /id="PRO_0000047535"
FT   DOMAIN          6..78
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         131..153
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         159..181
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         187..209
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         215..237
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         243..265
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        400
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CONFLICT        59
FT                   /note="E -> K (in Ref. 3; AAH09433)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  53739 MW;  A9DB42D0870A7767 CRC64;
     MAQGLVTFAD VAIDFSQEEW ACLNSAQRDL YWDVMLENYS NLVSLDLESA YENKSLPTEK
     NIHEIRASKR NSDRRSKSLG RNWICEGTLE RPQRSRGRYV NQMIINYVKR PATREGTPPR
     THQRHHKENS FECKDCGKAF SRGYQLSQHQ KIHTGEKPYE CKECKKAFRW GNQLTQHQKI
     HTGEKPYECK DCGKAFRWGS SLVIHKRIHT GEKPYECKDC GKAFRRGDEL TQHQRFHTGE
     KDYECKDCGK TFSRVYKLIQ HKRIHSGEKP YECKDCGKAF ICGSSLIQHK RIHTGEKPYE
     CQECGKAFTR VNYLTQHQKI HTGEKPHECK ECGKAFRWGS SLVKHERIHT GEKPYKCTEC
     GKAFNCGYHL TQHERIHTGE TPYKCKECGK AFIYGSSLVK HERIHTGVKP YGCTECGKSF
     SHGHQLTQHQ KTHSGAKSYE CKECGKACNH LNHLREHQRI HNS
//