ZN331_HUMAN
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 03-AUG-2022, entry version 176.
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>3.0.co;2-j;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 60.
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; Q9NQX6; -.
DR PeptideAtlas; Q9NQX6; -.
DR PRIDE; Q9NQX6; -.
DR ProteomicsDB; 82225; -.
DR Antibodypedia; 32728; 122 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 CTD; 55422; -.
DR DisGeNET; 55422; -.
DR GeneCards; ZNF331; -.
DR HGNC; HGNC:15489; ZNF331.
DR HPA; ENSG00000130844; Low tissue specificity.
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; WACLDST; -.
DR OrthoDB; 1318335at2759; -.
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 1084 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 205 other tissues.
DR ExpressionAtlas; Q9NQX6; baseline and differential.
DR Genevisible; Q9NQX6; HS.
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 transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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
