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ZN875_HUMAN
ID   ZN875_HUMAN             Reviewed;         659 AA.
AC   P10072; A8MRS7; Q6PJD0; Q9BSW9; Q9UM09;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 4.
DT   03-AUG-2022, entry version 199.
DE   RecName: Full=Zinc finger protein 875 {ECO:0000305};
DE   AltName: Full=Krueppel-related zinc finger protein 1;
DE   AltName: Full=Protein HKR1;
GN   Name=ZNF875 {ECO:0000312|HGNC:HGNC:4928};
GN   Synonyms=HKR1 {ECO:0000312|HGNC:HGNC:4928};
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), AND VARIANT ILE-513.
RX   PubMed=9813242; DOI=10.1016/s0378-1119(98)00464-8;
RA   Oguri T., Katoh O., Takahashi T., Isobe T., Kuramoto K., Hirata S.,
RA   Yamakido M., Watanabe H.;
RT   "The Kruppel-type zinc finger family gene, HKR1, is induced in lung cancer
RT   by exposure to platinum drugs.";
RL   Gene 222:61-67(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-513.
RC   TISSUE=Ovary;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-499.
RX   PubMed=2850480; DOI=10.1128/mcb.8.8.3104-3113.1988;
RA   Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T., Law M.L.,
RA   Seuanez H.N., O'Brien S.J., Vogelstein B.;
RT   "The GLI-Kruppel family of human genes.";
RL   Mol. Cell. Biol. 8:3104-3113(1988).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P10072-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P10072-2; Sequence=VSP_035755;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86058.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB013897; BAA86058.1; ALT_INIT; mRNA.
DR   EMBL; AC016590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471126; EAW56722.1; -; Genomic_DNA.
DR   EMBL; BC004513; AAH04513.2; -; mRNA.
DR   EMBL; BC017256; AAH17256.1; -; mRNA.
DR   EMBL; M20675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS12502.1; -. [P10072-1]
DR   CCDS; CCDS82338.1; -. [P10072-2]
DR   PIR; C31201; C31201.
DR   RefSeq; NP_001316692.1; NM_001329763.1. [P10072-2]
DR   RefSeq; NP_001316693.1; NM_001329764.1. [P10072-2]
DR   RefSeq; NP_861451.1; NM_181786.3. [P10072-1]
DR   RefSeq; XP_016882167.1; XM_017026678.1.
DR   AlphaFoldDB; P10072; -.
DR   SMR; P10072; -.
DR   BioGRID; 129883; 3.
DR   IntAct; P10072; 1.
DR   STRING; 9606.ENSP00000315505; -.
DR   iPTMnet; P10072; -.
DR   PhosphoSitePlus; P10072; -.
DR   BioMuta; HKR1; -.
DR   DMDM; 215274257; -.
DR   MassIVE; P10072; -.
DR   PaxDb; P10072; -.
DR   PeptideAtlas; P10072; -.
DR   PRIDE; P10072; -.
DR   ProteomicsDB; 52558; -. [P10072-1]
DR   ProteomicsDB; 52559; -. [P10072-2]
DR   Antibodypedia; 29891; 188 antibodies from 24 providers.
DR   DNASU; 284459; -.
DR   Ensembl; ENST00000324411.8; ENSP00000315505.3; ENSG00000181666.19. [P10072-1]
DR   Ensembl; ENST00000392153.8; ENSP00000375994.3; ENSG00000181666.19. [P10072-2]
DR   GeneID; 284459; -.
DR   KEGG; hsa:284459; -.
DR   MANE-Select; ENST00000392153.8; ENSP00000375994.3; NM_001353803.2; NP_001340732.1. [P10072-2]
DR   UCSC; uc002ogb.5; human. [P10072-1]
DR   CTD; 284459; -.
DR   DisGeNET; 284459; -.
DR   GeneCards; ZNF875; -.
DR   HGNC; HGNC:4928; ZNF875.
DR   HPA; ENSG00000181666; Tissue enhanced (retina).
DR   MIM; 165250; gene.
DR   neXtProt; NX_P10072; -.
DR   OpenTargets; ENSG00000181666; -.
DR   PharmGKB; PA29306; -.
DR   VEuPathDB; HostDB:ENSG00000181666; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163548; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; P10072; -.
DR   OMA; FGAIKYE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P10072; -.
DR   TreeFam; TF338096; -.
DR   PathwayCommons; P10072; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P10072; -.
DR   BioGRID-ORCS; 284459; 13 hits in 1100 CRISPR screens.
DR   ChiTaRS; HKR1; human.
DR   GeneWiki; HKR1; -.
DR   GenomeRNAi; 284459; -.
DR   Pharos; P10072; Tbio.
DR   PRO; PR:P10072; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P10072; protein.
DR   Bgee; ENSG00000181666; Expressed in pancreatic ductal cell and 173 other tissues.
DR   ExpressionAtlas; P10072; baseline and differential.
DR   Genevisible; P10072; 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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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   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; 12.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..659
FT                   /note="Zinc finger protein 875"
FT                   /id="PRO_0000047270"
FT   DOMAIN          33..104
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         301..323
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         329..351
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         357..379
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         385..407
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         413..435
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         441..463
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         469..491
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         497..519
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         525..547
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         553..575
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         579..601
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         607..629
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         635..657
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          191..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..30
FT                   /note="MRVNHTVSTMLPTCMVHRQTMSCSGAGGIT -> MATGLLRAKKE (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035755"
FT   VARIANT         448
FT                   /note="R -> H (in dbSNP:rs2921563)"
FT                   /id="VAR_047404"
FT   VARIANT         513
FT                   /note="S -> I (in dbSNP:rs3745765)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9813242"
FT                   /id="VAR_047405"
FT   VARIANT         628
FT                   /note="T -> I (in dbSNP:rs3745764)"
FT                   /id="VAR_047406"
SQ   SEQUENCE   659 AA;  75128 MW;  36D48F8EA3A6D80A CRC64;
     MRVNHTVSTM LPTCMVHRQT MSCSGAGGIT AFVAFRDVAV YFTQEEWRLL SPAQRTLHRE
     VMLETYNHLV SLEIPSSKPK LIAQLERGEA PWREERKCPL DLCPESKPEI QLSPSCPLIF
     SSQQALSQHV WLSHLSQLFS SLWAGNPLHL GKHYPEDQKQ QQDPFCFSGK AEWIQEGEDS
     RLLFGRVSKN GTSKALSSPP EEQQPAQSKE DNTVVDIGSS PERRADLEET DKVLHGLEVS
     GFGEIKYEEF GPGFIKESNL LSLQKTQTGE TPYMYTEWGD SFGSMSVLIK NPRTHSGGKP
     YVCRECGRGF TWKSNLITHQ RTHSGEKPYV CKDCGRGFTW KSNLFTHQRT HSGLKPYVCK
     ECGQSFSLKS NLITHQRAHT GEKPYVCREC GRGFRQHSHL VRHKRTHSGE KPYICRECEQ
     GFSQKSHLIR HLRTHTGEKP YVCTECGRHF SWKSNLKTHQ RTHSGVKPYV CLECGQCFSL
     KSNLNKHQRS HTGEKPFVCT ECGRGFTRKS TLSTHQRTHS GEKPFVCAEC GRGFNDKSTL
     ISHQRTHSGE KPFMCRECGR RFRQKPNLFR HKRAHSGAFV CRECGQGFCA KLTLIKHQRA
     HAGGKPHVCR ECGQGFSRQS HLIRHQRTHS GEKPYICRKC GRGFSRKSNL IRHQRTHSG
 
 
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