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ZN654_MOUSE
ID   ZN654_MOUSE             Reviewed;        1112 AA.
AC   Q9DAU9; A0A140LI34; Q8K390;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 3.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Zinc finger protein 654 {ECO:0000305};
GN   Name=Znf654 {ECO:0000250|UniProtKB:Q8IZM8}; Synonyms=Zfp654;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-1112.
RC   STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-1112.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1111, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1111, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27760.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH68018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB24088.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CT030641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027760; AAH27760.1; ALT_INIT; mRNA.
DR   EMBL; BC068018; AAH68018.1; ALT_INIT; mRNA.
DR   EMBL; AK005508; BAB24088.2; ALT_INIT; mRNA.
DR   CCDS; CCDS84250.1; -.
DR   RefSeq; NP_001334174.1; NM_001347245.1.
DR   RefSeq; NP_082335.1; NM_028059.2.
DR   AlphaFoldDB; Q9DAU9; -.
DR   STRING; 10090.ENSMUSP00000052946; -.
DR   iPTMnet; Q9DAU9; -.
DR   PhosphoSitePlus; Q9DAU9; -.
DR   EPD; Q9DAU9; -.
DR   MaxQB; Q9DAU9; -.
DR   PaxDb; Q9DAU9; -.
DR   PeptideAtlas; Q9DAU9; -.
DR   PRIDE; Q9DAU9; -.
DR   ProteomicsDB; 314788; -.
DR   Antibodypedia; 32053; 130 antibodies from 23 providers.
DR   DNASU; 72020; -.
DR   Ensembl; ENSMUST00000207826; ENSMUSP00000146656; ENSMUSG00000047141.
DR   GeneID; 72020; -.
DR   KEGG; mmu:72020; -.
DR   UCSC; uc007zqd.1; mouse.
DR   CTD; 72020; -.
DR   MGI; MGI:1919270; Zfp654.
DR   VEuPathDB; HostDB:ENSMUSG00000047141; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00950000183034; -.
DR   HOGENOM; CLU_026570_1_0_1; -.
DR   InParanoid; Q9DAU9; -.
DR   OMA; TFKCPAN; -.
DR   OrthoDB; 355592at2759; -.
DR   PhylomeDB; Q9DAU9; -.
DR   TreeFam; TF326007; -.
DR   BioGRID-ORCS; 72020; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Zfp654; mouse.
DR   PRO; PR:Q9DAU9; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9DAU9; protein.
DR   Bgee; ENSMUSG00000047141; Expressed in spermatid and 245 other tissues.
DR   ExpressionAtlas; Q9DAU9; baseline and differential.
DR   Genevisible; Q9DAU9; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; 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: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; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1112
FT                   /note="Zinc finger protein 654"
FT                   /id="PRO_0000311947"
FT   ZN_FING         566..588
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         738..763
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         779..801
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         807..831
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         836..860
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          482..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1112 AA;  126445 MW;  BA59294CDC9BF871 CRC64;
     MAEEESDQEA ERLGEELVAI VESPPGPVGL LAAGDGRGGA GGGGCGGGVG ISSRDYCRRF
     CQVVEDYAGR WQVPLPQLQV LQTALCCFTS ASASFPDECE HVQYVLSSLA VSFFELLLFF
     GRDEFYEEPL KDILGSFQEC QNHLRRYGNV NLELVTRIIK DGGPWEDPVL QAVLKAQPAS
     QEIVNKYLSS ENPLFFELRA RYLIACERIP EAMALIKSCI NHPEISKDLY FHQALFTCLF
     MSPVEDQLFR EHLLKTDCKS GIDIICNTEK EGKTLLALQL CESFLIPQLQ NGDMYYIWEL
     IFLWSKLQLK SNPSKQVFVD QCYQLLRTAT NVRVIFPFMK IIKDEVEEEG LQICVEICGC
     ALQLDLHDDP ETKCLIYKTI AHFLPNDLEI VRVCALSVFF LERSLDAYHT VEELYRRPDE
     EYSEGMSTVQ NRVRFELLPI LKKGLFFDPE FWNFVMIKKN CVALLRDKSA VKLLNENTLE
     NPSSSLKKRV DQQSVEEDQS TGETDPDDAS VVQPKGQVNV KRSLSALNTS KVDHSVPRHR
     CMLCNKEFLG GHIVRHAQAH QKKGSFACVI CGRKFRNRGL MQKHLKNHVK KIQRQQIATA
     QQDDPEVITL EEINGSKSLI SFENGNSNTK GLEIETLTAS SERNKEVIRE HMAEFIKIPI
     AIPENAIENI IENGKPDASF NNISESLPQC DDDYEEEENE DDYEDDYDLN QETSVLHKIN
     GTVCHPKDVY ATDQEGNFKC PALGCVRIFK RIGFLNMHAR TVHPTDLNVR QTVMKWSKGK
     CKFCQRQFED SQHFIDHLNR HSYPNVYFCL HFNCNESFKL PFQLAQHTKS HRIFQAQCSF
     PECHELFEDL PLLYEHEAQH YLSKTPESSA QLSEVVPNHQ EIDPFSNENQ TIHHPVSTSK
     SRKYSTEPKT YIDTMEKKTD SLVHNGNEHS DDTVSNISLI DQKMPAIEPN PENTHSTTDL
     VNGHSEIEQT PLVTSDPTLK IDINRNRTEN GSILPSVESQ EHSALSVSQA PSKPNLTSEQ
     TSYGLIVTKP FVRPLPPSYL DERYLSMPKR RKFLTDIVDA CSDQDNMYKK PVKRLRCGKC
     LTTYCNAEAL EAHLAQKKCQ TLFGFDSDDE SA
 
 
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