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ZN692_RAT
ID   ZN692_RAT               Reviewed;         533 AA.
AC   F6WEQ6; B2GUW5;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Zinc finger protein 692 {ECO:0000305};
DE   AltName: Full=AICAR responsive element binding protein {ECO:0000250|UniProtKB:Q9BU19};
GN   Name=Znf692 {ECO:0000250|UniProtKB:Q9BU19};
GN   Synonyms=Arebp {ECO:0000250|UniProtKB:Q9BU19},
GN   Zfp692 {ECO:0000312|RGD:1306740};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [3]
RP   FUNCTION.
RX   PubMed=17097062; DOI=10.1016/j.bbrc.2006.10.124;
RA   Inoue E., Yamauchi J.;
RT   "AMP-activated protein kinase regulates PEPCK gene expression by direct
RT   phosphorylation of a novel zinc finger transcription factor.";
RL   Biochem. Biophys. Res. Commun. 351:793-799(2006).
CC   -!- FUNCTION: May act as an transcriptional repressor for PCK1 gene
CC       expression, in turns may participate in the hepatic gluconeogenesis
CC       regulation through the activated AMPK signaling pathway.
CC       {ECO:0000269|PubMed:17097062}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BU19}.
CC   -!- PTM: Phosphorylation at Ser-471 results in loss of DNA-binding
CC       activity. {ECO:0000250|UniProtKB:Q9BU19}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AC097876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC166433; AAI66433.1; -; mRNA.
DR   RefSeq; XP_006246445.1; XM_006246383.3.
DR   RefSeq; XP_006246446.1; XM_006246384.3.
DR   RefSeq; XP_006246447.1; XM_006246385.3.
DR   RefSeq; XP_006246448.1; XM_006246386.3.
DR   AlphaFoldDB; F6WEQ6; -.
DR   SMR; F6WEQ6; -.
DR   STRING; 10116.ENSRNOP00000031984; -.
DR   Ensembl; ENSRNOT00000038123; ENSRNOP00000031984; ENSRNOG00000002682.
DR   GeneID; 303164; -.
DR   UCSC; RGD:1306740; rat.
DR   CTD; 103836; -.
DR   RGD; 1306740; Zfp692.
DR   GeneTree; ENSGT00940000161175; -.
DR   HOGENOM; CLU_045687_1_0_1; -.
DR   InParanoid; F6WEQ6; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; F6WEQ6; -.
DR   TreeFam; TF332664; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   ExpressionAtlas; F6WEQ6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..533
FT                   /note="Zinc finger protein 692"
FT                   /id="PRO_0000452720"
FT   ZN_FING         329..354
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         360..384
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         390..412
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         418..440
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         449..472
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          124..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..209
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..251
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU19"
FT   MOD_RES         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU19"
SQ   SEQUENCE   533 AA;  59219 MW;  28738E43C9B38FEB CRC64;
     MASPVADASR RRREKRRQLD ARRSKCRIRL GGHMEQWCLL KERLGFSLHS QLAKFLLDRY
     TSSGCVLCAG PEPVPQKGLQ YLVLLSHTHS RECSLVPGLR GPGGGEGELV WECSAGHTFS
     WEPSLIPTPS EVPKQAPLTH TTERTWCSEA RRKQEAEGLE CEHRERTQET RLSRRVEPPL
     ETDPSVGEDQ VVEEEEEEEE EEEEEELLSD ASPWTYSSSP DDSEPDVPRP PPSPVTHTPK
     EGEIPPVPAT LPTPCAVLAS LGSTAALTSD TEVQMELSRT SQVPAELQMT ESLDSPGSQA
     QSAPNPTCDE DTAQIGLRRI RKAAKRELMP CDFPGCGRIF SNRQYLNHHK KYQHIHQKSF
     CCPEPACGKS FNFKKHLKEH VKLHSDARDY ICEFCARSFR TSSNLVIHRR IHTGEKPLQC
     EICGFTCRQK ASLNWHRRKH AETAAALRFP CEFCGKRFEK PDSVVAHCSK SHPALLPVQE
     SPGSLGSSPS ISAPEPLQSP EGTSFSTSYD SNPAPSTSIS SPGVPAPRNT EKS
 
 
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