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ZN282_HUMAN
ID   ZN282_HUMAN             Reviewed;         671 AA.
AC   Q9UDV7; B4DRI5; O43691; Q6DKK0;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Zinc finger protein 282;
DE   AltName: Full=HTLV-I U5RE-binding protein 1;
DE            Short=HUB-1;
GN   Name=ZNF282; Synonyms=HUB1;
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).
RX   PubMed=9396811; DOI=10.1093/nar/25.24.5025;
RA   Okumura K., Sakaguchi G., Naito K., Tamura T., Igarashi H.;
RT   "HUB1, a novel Kruppel type zinc finger protein, represses the human T cell
RT   leukemia virus type I long terminal repeat-mediated expression.";
RL   Nucleic Acids Res. 25:5025-5032(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-293, 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: Binds to the U5 repressive element (U5RE) of the human T cell
CC       leukemia virus type I long terminal repeat. It recognizes the 5'-
CC       TCCACCCC-3' sequence as a core motif and exerts a strong repressive
CC       effect on HTLV-I LTR-mediated expression.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UDV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UDV7-2; Sequence=VSP_056545, VSP_056546;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA24380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D30612; BAA24380.1; ALT_INIT; mRNA.
DR   EMBL; AK299280; BAG61297.1; -; mRNA.
DR   EMBL; AK316282; BAH14653.1; -; mRNA.
DR   EMBL; AC004890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC073805; AAH73805.1; -; mRNA.
DR   CCDS; CCDS5895.1; -. [Q9UDV7-1]
DR   CCDS; CCDS78284.1; -. [Q9UDV7-2]
DR   RefSeq; NP_001290410.1; NM_001303481.1. [Q9UDV7-2]
DR   RefSeq; NP_003566.1; NM_003575.3. [Q9UDV7-1]
DR   AlphaFoldDB; Q9UDV7; -.
DR   SMR; Q9UDV7; -.
DR   BioGRID; 114010; 22.
DR   IntAct; Q9UDV7; 10.
DR   MINT; Q9UDV7; -.
DR   STRING; 9606.ENSP00000477841; -.
DR   iPTMnet; Q9UDV7; -.
DR   PhosphoSitePlus; Q9UDV7; -.
DR   BioMuta; ZNF282; -.
DR   DMDM; 116242858; -.
DR   jPOST; Q9UDV7; -.
DR   MassIVE; Q9UDV7; -.
DR   MaxQB; Q9UDV7; -.
DR   PaxDb; Q9UDV7; -.
DR   PeptideAtlas; Q9UDV7; -.
DR   PRIDE; Q9UDV7; -.
DR   ProteomicsDB; 4954; -.
DR   ProteomicsDB; 84119; -. [Q9UDV7-1]
DR   Antibodypedia; 18575; 88 antibodies from 18 providers.
DR   DNASU; 8427; -.
DR   Ensembl; ENST00000479907.1; ENSP00000418840.1; ENSG00000170265.12. [Q9UDV7-2]
DR   Ensembl; ENST00000610704.5; ENSP00000477841.1; ENSG00000170265.12. [Q9UDV7-1]
DR   GeneID; 8427; -.
DR   KEGG; hsa:8427; -.
DR   MANE-Select; ENST00000610704.5; ENSP00000477841.1; NM_003575.4; NP_003566.1.
DR   UCSC; uc011kun.2; human. [Q9UDV7-1]
DR   CTD; 8427; -.
DR   DisGeNET; 8427; -.
DR   GeneCards; ZNF282; -.
DR   HGNC; HGNC:13076; ZNF282.
DR   HPA; ENSG00000170265; Low tissue specificity.
DR   MIM; 603397; gene.
DR   neXtProt; NX_Q9UDV7; -.
DR   OpenTargets; ENSG00000170265; -.
DR   PharmGKB; PA37652; -.
DR   VEuPathDB; HostDB:ENSG00000170265; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161885; -.
DR   HOGENOM; CLU_002678_76_0_1; -.
DR   InParanoid; Q9UDV7; -.
DR   OMA; QEEPQCV; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9UDV7; -.
DR   TreeFam; TF337777; -.
DR   PathwayCommons; Q9UDV7; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; Q9UDV7; -.
DR   BioGRID-ORCS; 8427; 17 hits in 1101 CRISPR screens.
DR   ChiTaRS; ZNF282; human.
DR   GenomeRNAi; 8427; -.
DR   Pharos; Q9UDV7; Tdark.
DR   PRO; PR:Q9UDV7; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9UDV7; protein.
DR   Bgee; ENSG00000170265; Expressed in sural nerve and 121 other tissues.
DR   ExpressionAtlas; Q9UDV7; baseline and differential.
DR   Genevisible; Q9UDV7; 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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
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; 4.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..671
FT                   /note="Zinc finger protein 282"
FT                   /id="PRO_0000047506"
FT   DOMAIN          198..271
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         518..540
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         546..568
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         574..596
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         602..624
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         630..652
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          239..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..426
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         454..463
FT                   /note="VLPGERGSGE -> PHQGAALRVR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056545"
FT   VAR_SEQ         464..671
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056546"
FT   VARIANT         273
FT                   /note="M -> V (in dbSNP:rs1202418)"
FT                   /id="VAR_052805"
FT   CONFLICT        35
FT                   /note="E -> Q (in Ref. 1; BAA24380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="P -> R (in Ref. 1; BAA24380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   671 AA;  74295 MW;  FBD6001DC12CB26E CRC64;
     MQFVSTRPQP QQLGIQGLGL DSGSWSWAQA LPPEEVCHQE PALRGEMAEG MPPMQAQEWD
     MDARRPMPFQ FPPFPDRAPV FPDRMMREPQ LPTAEISLWT VVAAIQAVER KVDAQASQLL
     NLEGRTGTAE KKLADCEKTA VEFGNHMESK WAVLGTLLQE YGLLQRRLEN LENLLRNRNF
     WVLRLPPGSK GEAPKVPVTF VDIAVYFSED EWKNLDEWQK ELYNNLVKEN YKTLMSLDAE
     GSVPKPDAPV QAEPREEPCV WEQRHPEERE IPMDPEAGAE PLVPAQDASS QVKREDTLCV
     RGQRGLEERA IPTESITDSP ISAQDLLSRI KQEEHQCVWD QQDLADRDIP TDPNSESLIS
     AHDILSWIKQ EEQPYPWGPR DSMDGELGLD SGPSDSLLMV KNPPPAPPQP QPQPQPPQPQ
     LQSQPQPQSL PPIAVAENPG GPPSRGLLDD GFQVLPGERG SGEAPPGGDR STGGGGGDGG
     GGGGGAEAGT GAGGGCGSCC PGGLRRSLLL HGARSKPYSC PECGKSFGVR KSLIIHHRSH
     TKERPYECAE CEKSFNCHSG LIRHQMTHRG ERPYKCSECE KTYSRKEHLQ NHQRLHTGER
     PFQCALCGKS FIRKQNLLKH QRIHTGERPY TCGECGKSFR YKESLKDHLR VHSGGPGPGA
     PRQLPPPPER D
 
 
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