ID   ZN302_HUMAN             Reviewed;         478 AA.
AC   Q9NR11; Q658J3; Q9BZD8; Q9P0J4;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Zinc finger protein 302;
DE   AltName: Full=Zinc finger protein 135-like;
DE   AltName: Full=Zinc finger protein 140-like;
DE   AltName: Full=Zinc finger protein 327;
GN   Name=ZNF302; Synonyms=ZNF135L, ZNF140L, ZNF327;
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).
RA   Mao Y.-M., Xie Y., Zhao W., Kang Y., Lin S.-R., Sun Z.-H., Zhou Z.;
RT   "Molecular cloning and characterization of a full-length cDNA encoding a
RT   novel KRAB type zinc finger protein.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Mao Y.-M., Xie Y., Wang Z., Ying K., Lin S.-R., Deng Y.-F., Sun Z.-H.;
RT   "A novel KRAB ZFP gene involved in hepatic cancer.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Adrenal gland;
RA   Gu J., Fu S., Ren S., Jin W., Gu Y., Huang Q., Dong H., Yu Y., Fu G.,
RA   Wang Y., Chen Z., Han Z.;
RT   "A novel gene expressed in human adrenal gland.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=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 MRNA] (ISOFORM 2).
RC   TISSUE=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   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-183, 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   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-183, AND IDENTIFICATION BY MASS
RP   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       Q9NR11; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-3916142, EBI-739624;
CC       Q9NR11-2; P14136: GFAP; NbExp=3; IntAct=EBI-12988373, EBI-744302;
CC       Q9NR11-2; P42858: HTT; NbExp=3; IntAct=EBI-12988373, EBI-466029;
CC       Q9NR11-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12988373, EBI-1055254;
CC       Q9NR11-2; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-12988373, EBI-12012928;
CC       Q9NR11-2; P07196: NEFL; NbExp=3; IntAct=EBI-12988373, EBI-475646;
CC       Q9NR11-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12988373, EBI-748974;
CC       Q9NR11-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12988373, EBI-396669;
CC       Q9NR11-2; O76024: WFS1; NbExp=3; IntAct=EBI-12988373, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NR11-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NR11-2; Sequence=VSP_006914;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF265236; AAF74775.1; -; mRNA.
DR   EMBL; AF326206; AAK11224.1; -; mRNA.
DR   EMBL; AF155656; AAF67475.1; -; mRNA.
DR   EMBL; AL834318; CAD38987.1; -; mRNA.
DR   EMBL; BC024176; AAH24176.1; -; mRNA.
DR   CCDS; CCDS46042.1; -. [Q9NR11-2]
DR   RefSeq; NP_001012320.1; NM_001012320.2. [Q9NR11-2]
DR   RefSeq; NP_001276110.1; NM_001289181.1.
DR   RefSeq; NP_001276111.1; NM_001289182.1.
DR   RefSeq; NP_001276112.1; NM_001289183.1. [Q9NR11-2]
DR   RefSeq; NP_001276113.1; NM_001289184.1.
DR   RefSeq; NP_001276114.1; NM_001289185.1.
DR   RefSeq; NP_001276115.1; NM_001289186.1. [Q9NR11-2]
DR   RefSeq; NP_001276116.1; NM_001289187.1. [Q9NR11-2]
DR   RefSeq; NP_001276117.1; NM_001289188.1.
DR   RefSeq; NP_001276118.1; NM_001289189.1.
DR   RefSeq; NP_001276119.1; NM_001289190.1.
DR   RefSeq; NP_001276120.1; NM_001289191.1.
DR   RefSeq; NP_001276121.1; NM_001289192.1.
DR   RefSeq; NP_060913.2; NM_018443.3. [Q9NR11-2]
DR   RefSeq; NP_061145.2; NM_018675.2.
DR   AlphaFoldDB; Q9NR11; -.
DR   SMR; Q9NR11; -.
DR   BioGRID; 120987; 21.
DR   IntAct; Q9NR11; 23.
DR   MINT; Q9NR11; -.
DR   iPTMnet; Q9NR11; -.
DR   PhosphoSitePlus; Q9NR11; -.
DR   BioMuta; ZNF302; -.
DR   DMDM; 23397010; -.
DR   EPD; Q9NR11; -.
DR   MassIVE; Q9NR11; -.
DR   MaxQB; Q9NR11; -.
DR   PeptideAtlas; Q9NR11; -.
DR   ProteomicsDB; 82242; -. [Q9NR11-1]
DR   ProteomicsDB; 82243; -. [Q9NR11-2]
DR   Pumba; Q9NR11; -.
DR   Antibodypedia; 29194; 119 antibodies from 17 providers.
DR   DNASU; 55900; -.
DR   Ensembl; ENST00000423823.6; ENSP00000405219.2; ENSG00000089335.22. [Q9NR11-2]
DR   Ensembl; ENST00000457781.6; ENSP00000391067.2; ENSG00000089335.22. [Q9NR11-2]
DR   Ensembl; ENST00000505242.6; ENSP00000421028.1; ENSG00000089335.22. [Q9NR11-2]
DR   GeneID; 55900; -.
DR   KEGG; hsa:55900; -.
DR   MANE-Select; ENST00000505242.6; ENSP00000421028.1; NM_001289187.2; NP_001276116.1. [Q9NR11-2]
DR   UCSC; uc002nvp.3; human. [Q9NR11-1]
DR   AGR; HGNC:13848; -.
DR   CTD; 55900; -.
DR   DisGeNET; 55900; -.
DR   GeneCards; ZNF302; -.
DR   HGNC; HGNC:13848; ZNF302.
DR   HPA; ENSG00000089335; Low tissue specificity.
DR   neXtProt; NX_Q9NR11; -.
DR   OpenTargets; ENSG00000089335; -.
DR   PharmGKB; PA37820; -.
DR   VEuPathDB; HostDB:ENSG00000089335; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161431; -.
DR   InParanoid; Q9NR11; -.
DR   OMA; VSNCTAH; -.
DR   OrthoDB; 3120634at2759; -.
DR   PhylomeDB; Q9NR11; -.
DR   TreeFam; TF337055; -.
DR   PathwayCommons; Q9NR11; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9NR11; -.
DR   BioGRID-ORCS; 55900; 12 hits in 1080 CRISPR screens.
DR   ChiTaRS; ZNF302; human.
DR   GenomeRNAi; 55900; -.
DR   Pharos; Q9NR11; Tdark.
DR   PRO; PR:Q9NR11; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9NR11; Protein.
DR   Bgee; ENSG00000089335; Expressed in endothelial cell and 199 other cell types or tissues.
DR   ExpressionAtlas; Q9NR11; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor 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   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
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:SF138; ZINC FINGER PROTEIN 589; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; Q9NR11; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..478
FT                   /note="Zinc finger protein 302"
FT                   /id="PRO_0000047522"
FT   DOMAIN          4..75
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         280..302
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         308..330
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         336..358
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         364..386
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..414
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         420..442
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         448..470
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        183
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   VAR_SEQ         72..169
FT                   /note="AYPFPLSHSVPASVNFGFSALFEHCSEVTEIFELSELCVFWVLHFLSNSPNS
FT                   TVEAFSRSKKKKKKKKKRQCFAFLIYFRLGIKMGKQGIINKEGYLY -> DWESRWENK
FT                   ELSTKKDIYD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_006914"
FT   CONFLICT        451
FT                   /note="N -> H (in Ref. 3; AAF67475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="V -> G (in Ref. 3; AAF67475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="V -> G (in Ref. 3; AAF67475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        472
FT                   /note="E -> G (in Ref. 3; AAF67475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476..478
FT                   /note="FEV -> LKFRNAGNPSTSLNH (in Ref. 3; AAF67475)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  54814 MW;  C7492069228F55A6 CRC64;
     MSQVTFSDVA IDFSHEEWAC LDSAQRDLYK DVMVQNYENL VSVGLSVTKP YVIMLLEDGK
     EPWMMEKKLS KAYPFPLSHS VPASVNFGFS ALFEHCSEVT EIFELSELCV FWVLHFLSNS
     PNSTVEAFSR SKKKKKKKKK RQCFAFLIYF RLGIKMGKQG IINKEGYLYE DSPQPVTMEK
     VVKQSYEFSN SNKNLEYTEC DTFRSTFHSK STLSEPQNNS AEGNSHKYDI LKKNLSKKSV
     IKSERINGGK KLLNSNKSGA AFNQSKSLTL PQTCNREKIY TCSECGKAFG KQSILSRHWR
     IHTGEKPYEC RECGKTFSHG SSLTRHQISH SGEKPYKCIE CGKAFSHGSS LTNHQSTHTG
     EKPYECMNCG KSFSRVSLLI QHLRIHTQEK RYECRICGKA FIHSSSLIHH QKSHTGEKPY
     ECRECGKAFC CSSHLTQHQR IHSMKKKYEC NKCLKVFSSF SFLVQHQSIH TEEKPFEV
//