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ZN860_HUMAN
ID   ZN860_HUMAN             Reviewed;         632 AA.
AC   A6NHJ4; B4DFA4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Zinc finger protein 860;
GN   Name=ZNF860;
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 [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220, 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. {ECO:0000250}.
CC   -!- INTERACTION:
CC       A6NHJ4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-17263060, EBI-739624;
CC       A6NHJ4; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-17263060, EBI-10172052;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK294003; BAG57365.1; -; mRNA.
DR   EMBL; AC108485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS46784.1; -.
DR   RefSeq; NP_001131146.2; NM_001137674.2.
DR   RefSeq; XP_016861788.1; XM_017006299.1.
DR   AlphaFoldDB; A6NHJ4; -.
DR   SMR; A6NHJ4; -.
DR   BioGRID; 131322; 5.
DR   IntAct; A6NHJ4; 2.
DR   STRING; 9606.ENSP00000373274; -.
DR   iPTMnet; A6NHJ4; -.
DR   PhosphoSitePlus; A6NHJ4; -.
DR   BioMuta; ZNF860; -.
DR   jPOST; A6NHJ4; -.
DR   MassIVE; A6NHJ4; -.
DR   MaxQB; A6NHJ4; -.
DR   PaxDb; A6NHJ4; -.
DR   PeptideAtlas; A6NHJ4; -.
DR   PRIDE; A6NHJ4; -.
DR   ProteomicsDB; 1202; -.
DR   Antibodypedia; 57012; 64 antibodies from 14 providers.
DR   DNASU; 344787; -.
DR   Ensembl; ENST00000360311.5; ENSP00000373274.3; ENSG00000197385.6.
DR   GeneID; 344787; -.
DR   KEGG; hsa:344787; -.
DR   MANE-Select; ENST00000360311.5; ENSP00000373274.3; NM_001137674.3; NP_001131146.2.
DR   UCSC; uc011axg.3; human.
DR   CTD; 344787; -.
DR   DisGeNET; 344787; -.
DR   GeneCards; ZNF860; -.
DR   HGNC; HGNC:34513; ZNF860.
DR   HPA; ENSG00000197385; Tissue enhanced (lymphoid).
DR   neXtProt; NX_A6NHJ4; -.
DR   OpenTargets; ENSG00000197385; -.
DR   PharmGKB; PA164727773; -.
DR   VEuPathDB; HostDB:ENSG00000197385; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000154397; -.
DR   HOGENOM; CLU_002678_44_5_1; -.
DR   InParanoid; A6NHJ4; -.
DR   OMA; NYRNLHS; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; A6NHJ4; -.
DR   TreeFam; TF341892; -.
DR   PathwayCommons; A6NHJ4; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; A6NHJ4; -.
DR   BioGRID-ORCS; 344787; 11 hits in 1040 CRISPR screens.
DR   GenomeRNAi; 344787; -.
DR   Pharos; A6NHJ4; Tdark.
DR   PRO; PR:A6NHJ4; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; A6NHJ4; protein.
DR   Bgee; ENSG00000197385; Expressed in cortical plate and 94 other tissues.
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   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; 10.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
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..632
FT                   /note="Zinc finger protein 860"
FT                   /id="PRO_0000350815"
FT   DOMAIN          24..99
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         230..252
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         258..280
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         286..308
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         314..336
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         342..364
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         370..392
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         398..420
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         426..448
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         454..476
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         482..504
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         510..532
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         538..560
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         566..588
FT                   /note="C2H2-type 13; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         594..616
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CONFLICT        547
FT                   /note="F -> Y (in Ref. 1; BAG57365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586
FT                   /note="R -> K (in Ref. 1; BAG57365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   632 AA;  73757 MW;  54F37E8AC0386171 CRC64;
     MLREEAAQKR KEKEPGMALP QGHLTFRDVA IEFSLEEWKC LDPTQRALYR AMMLENYRNL
     HSVDISSKCM MKKFSSTAQG NTEVDTGTLE RHESHHIGDF CFQKIGKDIH DFEFQWQEDK
     RNSHEATMTQ IKKLTGSTDR YDRRHPGNKP IKDQLGLSFH SHLPELHIFQ TKGKVGNQVE
     KSINDASSVL TSQRISSRPK IHISNNYENN FFHSSLLTLK QEVHIREKSF QCNESGKAFN
     CSSLLRKHQI IYLGGKQYKC DVCGKVFNQK RYLACHHRCH TGEKPYKCNE CGKVFNQQSN
     LASHHRLHTG EKPYKCEECD KVFSRKSNLE RHRRIHTGEK PYKCKVCEKA FRRDSHLTQH
     TRIHTGEKPY KCNECGKAFS GQSTLIHHQA IHGIGKLYKC NDCHKVFSNA TTIANHWRIH
     NEERSYKCNK CGKFFRRRSY LVVHWRTHTG EKPYKCNECG KTFHHNSALV IHKAIHTGEK
     PYKCNECGKT FRHNSALVIH KAIHTGEKPY KCNECGKVFN QQATLARHHR LHTGEKPYKC
     EECDTVFSRK SHHETHKRIH TGEKPYKCDD FDEAFSQASS YAKQRRIHMG EKHHKCDDCG
     KAFTSHSHRI RHQRIHTGQK SYKCHKRGKV FS
 
 
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