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ZN165_HUMAN
ID   ZN165_HUMAN             Reviewed;         485 AA.
AC   P49910;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Zinc finger protein 165;
DE   AltName: Full=Cancer/testis antigen 53;
DE            Short=CT53;
DE   AltName: Full=LD65;
DE   AltName: Full=Zinc finger and SCAN domain-containing protein 7;
GN   Name=ZNF165; Synonyms=ZPF165, ZSCAN7;
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=7490084; DOI=10.1006/geno.1995.1178;
RA   Tirosvoutis K.N., Divane A., Jones M., Affara N.A.;
RT   "Characterization of a novel zinc finger gene (ZNF165) mapping to 6p21 that
RT   is expressed specifically in testis.";
RL   Genomics 28:485-490(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9244436; DOI=10.1006/geno.1997.4806;
RA   Lee P.L., Gelbart T., West C., Adams M., Blackstone R., Beutler E.;
RT   "Three genes encoding zinc finger proteins on human chromosome 6p21.3:
RT   members of a new subclass of the Kruppel gene family containing the
RT   conserved SCAN box domain.";
RL   Genomics 43:191-201(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-162 AND LYS-195, 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.
CC   -!- INTERACTION:
CC       P49910; O43865: AHCYL1; NbExp=3; IntAct=EBI-741694, EBI-2371423;
CC       P49910; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-741694, EBI-3866279;
CC       P49910; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-741694, EBI-11977221;
CC       P49910; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-741694, EBI-739624;
CC       P49910; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-741694, EBI-3867333;
CC       P49910; G5E9A7: DMWD; NbExp=3; IntAct=EBI-741694, EBI-10976677;
CC       P49910; O14641: DVL2; NbExp=3; IntAct=EBI-741694, EBI-740850;
CC       P49910; Q92997: DVL3; NbExp=3; IntAct=EBI-741694, EBI-739789;
CC       P49910; P50402: EMD; NbExp=3; IntAct=EBI-741694, EBI-489887;
CC       P49910; Q01844: EWSR1; NbExp=2; IntAct=EBI-741694, EBI-739737;
CC       P49910; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-741694, EBI-5916454;
CC       P49910; Q14005-2: IL16; NbExp=3; IntAct=EBI-741694, EBI-17178971;
CC       P49910; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-741694, EBI-10171774;
CC       P49910; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-741694, EBI-10172052;
CC       P49910; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-741694, EBI-14065470;
CC       P49910; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-741694, EBI-10268010;
CC       P49910; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-741694, EBI-10172526;
CC       P49910; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-741694, EBI-741158;
CC       P49910; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-741694, EBI-79165;
CC       P49910; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-741694, EBI-742388;
CC       P49910; O60437: PPL; NbExp=3; IntAct=EBI-741694, EBI-368321;
CC       P49910; Q15287: RNPS1; NbExp=3; IntAct=EBI-741694, EBI-395959;
CC       P49910; P57086: SCAND1; NbExp=11; IntAct=EBI-741694, EBI-745846;
CC       P49910; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-741694, EBI-5235340;
CC       P49910; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-741694, EBI-725997;
CC       P49910; P13994: YJU2B; NbExp=6; IntAct=EBI-741694, EBI-716093;
CC       P49910; P17028: ZNF24; NbExp=3; IntAct=EBI-741694, EBI-707773;
CC       P49910; P15622-3: ZNF250; NbExp=3; IntAct=EBI-741694, EBI-10177272;
CC       P49910; O14978: ZNF263; NbExp=3; IntAct=EBI-741694, EBI-744493;
CC       P49910; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-741694, EBI-740727;
CC       P49910; Q9NWS9-2: ZNF446; NbExp=9; IntAct=EBI-741694, EBI-740232;
CC       P49910; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-741694, EBI-10172590;
CC       P49910; Q96K58-2: ZNF668; NbExp=3; IntAct=EBI-741694, EBI-12817597;
CC       P49910; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-741694, EBI-10251462;
CC       P49910; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-741694, EBI-11962574;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; X84801; CAA59268.1; -; mRNA.
DR   EMBL; U78722; AAC51658.1; -; mRNA.
DR   EMBL; U88086; AAD04755.1; -; Genomic_DNA.
DR   EMBL; U88084; AAD04755.1; JOINED; Genomic_DNA.
DR   EMBL; U88085; AAD04755.1; JOINED; Genomic_DNA.
DR   EMBL; AL121944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026092; AAH26092.1; -; mRNA.
DR   CCDS; CCDS4643.1; -.
DR   PIR; S52411; S52411.
DR   RefSeq; NP_003438.1; NM_003447.3.
DR   RefSeq; XP_016866747.1; XM_017011258.1.
DR   RefSeq; XP_016866748.1; XM_017011259.1.
DR   RefSeq; XP_016866749.1; XM_017011260.1.
DR   AlphaFoldDB; P49910; -.
DR   SMR; P49910; -.
DR   BioGRID; 113511; 48.
DR   IntAct; P49910; 43.
DR   MINT; P49910; -.
DR   STRING; 9606.ENSP00000366542; -.
DR   iPTMnet; P49910; -.
DR   PhosphoSitePlus; P49910; -.
DR   BioMuta; ZNF165; -.
DR   DMDM; 1731420; -.
DR   jPOST; P49910; -.
DR   MassIVE; P49910; -.
DR   PaxDb; P49910; -.
DR   PeptideAtlas; P49910; -.
DR   PRIDE; P49910; -.
DR   ProteomicsDB; 56177; -.
DR   ABCD; P49910; 9 sequenced antibodies.
DR   Antibodypedia; 25827; 205 antibodies from 22 providers.
DR   DNASU; 7718; -.
DR   Ensembl; ENST00000377325.2; ENSP00000366542.1; ENSG00000197279.5.
DR   Ensembl; ENST00000683778.1; ENSP00000507525.1; ENSG00000197279.5.
DR   GeneID; 7718; -.
DR   KEGG; hsa:7718; -.
DR   MANE-Select; ENST00000683778.1; ENSP00000507525.1; NM_001376491.1; NP_001363420.1.
DR   CTD; 7718; -.
DR   DisGeNET; 7718; -.
DR   GeneCards; ZNF165; -.
DR   HGNC; HGNC:12953; ZNF165.
DR   HPA; ENSG00000197279; Tissue enhanced (testis).
DR   MIM; 600834; gene.
DR   neXtProt; NX_P49910; -.
DR   OpenTargets; ENSG00000197279; -.
DR   PharmGKB; PA37535; -.
DR   VEuPathDB; HostDB:ENSG00000197279; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163388; -.
DR   HOGENOM; CLU_002678_49_3_1; -.
DR   InParanoid; P49910; -.
DR   OMA; VKRQWEK; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P49910; -.
DR   TreeFam; TF338304; -.
DR   PathwayCommons; P49910; -.
DR   SignaLink; P49910; -.
DR   SIGNOR; P49910; -.
DR   BioGRID-ORCS; 7718; 13 hits in 1098 CRISPR screens.
DR   ChiTaRS; ZNF165; human.
DR   GeneWiki; Zinc_finger_protein_165; -.
DR   GenomeRNAi; 7718; -.
DR   Pharos; P49910; Tbio.
DR   PRO; PR:P49910; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P49910; protein.
DR   Bgee; ENSG00000197279; Expressed in sperm and 130 other tissues.
DR   ExpressionAtlas; P49910; baseline and differential.
DR   Genevisible; P49910; 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: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; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
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..485
FT                   /note="Zinc finger protein 165"
FT                   /id="PRO_0000047436"
FT   DOMAIN          62..127
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         290..314
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         344..366
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         372..394
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         400..422
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         428..450
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         456..478
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        23
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        162
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        195
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   485 AA;  55771 MW;  1265D859D1713AE8 CRC64;
     MATEPKKAAA QNSPEDEGLL IVKIEEEEFI HGQDTCLQRS ELLKQELCRQ LFRQFCYQDS
     PGPREALSRL RELCCQWLKP EIHTKEQILE LLVLEQFLTI LPGDLQAWVH EHYPESGEEA
     VTILEDLERG TDEAVLQVQA HEHGQEIFQK KVSPPGPALN VKLQPVETKA HFDSSEPQLL
     WDCDNESENS RSMPKLEIFE KIESQRIISG RISGYISEAS GESQDICKSA GRVKRQWEKE
     SGESQRLSSA QDEGFGKILT HKNTVRGEII SHDGCERRLN LNSNEFTHQK SCKHGTCDQS
     FKWNSDFINH QIIYAGEKNH QYGKSFKSPK LAKHAAVFSG DKTHQCNECG KAFRHSSKLA
     RHQRIHTGER CYECNECGKS FAESSDLTRH RRIHTGERPF GCKECGRAFN LNSHLIRHQR
     IHTREKPYEC SECGKTFRVS SHLIRHFRIH TGEKPYECSE CGRAFSQSSN LSQHQRIHMR
     ENLLM
 
 
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