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ZFP69_HUMAN
ID   ZFP69_HUMAN             Reviewed;         526 AA.
AC   Q49AA0; Q5SWM5; Q6ZWK8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Zinc finger protein 69 homolog {ECO:0000250|UniProtKB:A2A761};
DE   AltName: Full=Zinc finger protein 642;
GN   Name=ZFP69; Synonyms=ZNF642;
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].
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=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
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   [4]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19578398; DOI=10.1371/journal.pgen.1000541;
RA   Scherneck S., Nestler M., Vogel H., Blueher M., Block M.D.,
RA   Berriel Diaz M., Herzig S., Schulz N., Teichert M., Tischer S.,
RA   Al-Hasani H., Kluge R., Schuermann A., Joost H.G.;
RT   "Positional cloning of zinc finger domain transcription factor Zfp69, a
RT   candidate gene for obesity-associated diabetes contributed by mouse locus
RT   Nidd/SJL.";
RL   PLoS Genet. 5:E1000541-E1000541(2009).
CC   -!- FUNCTION: Putative transcription factor that appears to regulate lipid
CC       metabolism. {ECO:0000250|UniProtKB:A2A761}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A2A761}.
CC   -!- TISSUE SPECIFICITY: Expressed in visceral and subcutaneous adipose
CC       tissue. {ECO:0000269|PubMed:19578398}.
CC   -!- INDUCTION: Up-regulated in both visceral and subcutaneous adipose
CC       tissue of diabetic individuals. {ECO:0000269|PubMed:19578398}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC85492.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK122618; BAC85492.1; ALT_SEQ; mRNA.
DR   EMBL; AL603839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041873; AAH41873.1; -; mRNA.
DR   CCDS; CCDS30686.1; -.
DR   RefSeq; NP_001307107.1; NM_001320178.1.
DR   RefSeq; NP_001307108.1; NM_001320179.1.
DR   RefSeq; NP_940896.2; NM_198494.2.
DR   RefSeq; XP_006710669.1; XM_006710606.3.
DR   AlphaFoldDB; Q49AA0; -.
DR   SMR; Q49AA0; -.
DR   STRING; 9606.ENSP00000361791; -.
DR   iPTMnet; Q49AA0; -.
DR   PhosphoSitePlus; Q49AA0; -.
DR   BioMuta; ZFP69; -.
DR   DMDM; 115502934; -.
DR   jPOST; Q49AA0; -.
DR   MassIVE; Q49AA0; -.
DR   MaxQB; Q49AA0; -.
DR   PaxDb; Q49AA0; -.
DR   PeptideAtlas; Q49AA0; -.
DR   PRIDE; Q49AA0; -.
DR   ProteomicsDB; 62038; -.
DR   Antibodypedia; 32097; 41 antibodies from 16 providers.
DR   DNASU; 339559; -.
DR   Ensembl; ENST00000372705.3; ENSP00000361790.3; ENSG00000187815.10.
DR   Ensembl; ENST00000372706.6; ENSP00000361791.1; ENSG00000187815.10.
DR   GeneID; 339559; -.
DR   KEGG; hsa:339559; -.
DR   MANE-Select; ENST00000372706.6; ENSP00000361791.1; NM_001320179.2; NP_001307108.1.
DR   UCSC; uc001cfo.4; human.
DR   CTD; 339559; -.
DR   DisGeNET; 339559; -.
DR   GeneCards; ZFP69; -.
DR   HGNC; HGNC:24708; ZFP69.
DR   HPA; ENSG00000187815; Low tissue specificity.
DR   MIM; 617939; gene.
DR   neXtProt; NX_Q49AA0; -.
DR   OpenTargets; ENSG00000187815; -.
DR   PharmGKB; PA134917508; -.
DR   VEuPathDB; HostDB:ENSG00000187815; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162278; -.
DR   HOGENOM; CLU_002678_0_2_1; -.
DR   InParanoid; Q49AA0; -.
DR   OMA; QTILTHK; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q49AA0; -.
DR   TreeFam; TF337055; -.
DR   PathwayCommons; Q49AA0; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 339559; 25 hits in 1092 CRISPR screens.
DR   GenomeRNAi; 339559; -.
DR   Pharos; Q49AA0; Tdark.
DR   PRO; PR:Q49AA0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q49AA0; protein.
DR   Bgee; ENSG00000187815; Expressed in cortical plate and 127 other tissues.
DR   Genevisible; Q49AA0; HS.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
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; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
KW   DNA-binding; Lipid metabolism; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..526
FT                   /note="Zinc finger protein 69 homolog"
FT                   /id="PRO_0000252161"
FT   DOMAIN          1..39
FT                   /note="SCAN box"
FT   DOMAIN          76..147
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         467..489
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   VARIANT         113
FT                   /note="V -> L (in dbSNP:rs34752670)"
FT                   /id="VAR_033583"
FT   CONFLICT        159
FT                   /note="T -> A (in Ref. 3; AAH41873)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  61181 MW;  F0B624CF36BF4F36 CRC64;
     MPQQLLITLP TEASTWVKLQ HPKKAVEGAP LWEDVTKMFE GEALLSQDAE DVKTQRESLE
     DEVTPGLPTA ESQELLTFKD ISIDFTQEEW GQLAPAHQNL YREVMLENYS NLVSVGYQLS
     KPSVISQLEK GEEPWMAEKE GPGDPSSDLK SKIETIESTA KSTISQERLY HGIMMESFMR
     DDIIYSTLRK VSTYDDVLER HQETCMRDVR QAILTHKKRV QETNKFGENI IVHSNVIIEQ
     RHHKYDTPTK RNTYKLDLIN HPTSYIRTKT YECNICEKIF KQPIHLTEHM RIHTGEKPFR
     CKECGRAFSQ SASLSTHQRI HTGEKPFECE ECGKAFRHRS SLNQHHRTHT GEKPYVCDKC
     QKAFSQNISL VQHLRTHSGE KPFTCNECGK TFRQIRHLSE HIRIHTGEKP YACTACCKTF
     SHRAYLTHHQ RIHTGERPYK CKECGKAFRQ RIHLSNHKTV HTGVKAYECN RCGKAYRHDS
     SFKKHQRHHT GEKPYECNEC GKAFSYNSSL SRHHEIHRRN AFRNKV
 
 
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