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ZN865_MOUSE
ID   ZN865_MOUSE             Reviewed;        1058 AA.
AC   Q3U3I9; D3Z3M5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Zinc finger protein 865;
GN   Name=Znf865; Synonyms=Zfp865;
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 MRNA].
RC   STRAIN=NOD;
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   [2]
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).
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
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; AK154737; BAE32797.1; -; mRNA.
DR   EMBL; AC157563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS20753.1; -.
DR   RefSeq; NP_001028555.1; NM_001033383.2.
DR   RefSeq; XP_006540122.1; XM_006540059.2.
DR   RefSeq; XP_006540123.1; XM_006540060.1.
DR   AlphaFoldDB; Q3U3I9; -.
DR   SMR; Q3U3I9; -.
DR   STRING; 10090.ENSMUSP00000075601; -.
DR   iPTMnet; Q3U3I9; -.
DR   PhosphoSitePlus; Q3U3I9; -.
DR   EPD; Q3U3I9; -.
DR   jPOST; Q3U3I9; -.
DR   MaxQB; Q3U3I9; -.
DR   PaxDb; Q3U3I9; -.
DR   PeptideAtlas; Q3U3I9; -.
DR   PRIDE; Q3U3I9; -.
DR   ProteomicsDB; 302146; -.
DR   Antibodypedia; 69405; 41 antibodies from 12 providers.
DR   Ensembl; ENSMUST00000076251; ENSMUSP00000075601; ENSMUSG00000074405.
DR   GeneID; 319748; -.
DR   KEGG; mmu:319748; -.
DR   UCSC; uc009ezk.1; mouse.
DR   CTD; 319748; -.
DR   MGI; MGI:2442656; Zfp865.
DR   VEuPathDB; HostDB:ENSMUSG00000074405; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00530000064557; -.
DR   HOGENOM; CLU_010472_0_0_1; -.
DR   InParanoid; Q3U3I9; -.
DR   OMA; PTPQWGI; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q3U3I9; -.
DR   TreeFam; TF350857; -.
DR   BioGRID-ORCS; 319748; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Zfp865; mouse.
DR   PRO; PR:Q3U3I9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3U3I9; protein.
DR   Bgee; ENSMUSG00000074405; Expressed in embryonic brain and 93 other tissues.
DR   ExpressionAtlas; Q3U3I9; baseline and differential.
DR   Genevisible; Q3U3I9; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; 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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00355; ZnF_C2H2; 20.
DR   SUPFAM; SSF57667; SSF57667; 11.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 20.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
PE   2: Evidence at transcript 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..1058
FT                   /note="Zinc finger protein 865"
FT                   /id="PRO_0000404595"
FT   ZN_FING         220..242
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         248..270
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         350..372
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         378..400
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         407..429
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         546..568
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         574..596
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         602..624
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         664..686
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         692..714
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         791..813
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         819..841
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         847..869
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         875..897
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         903..925
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         931..953
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         959..981
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         988..1010
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1016..1038
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..81
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        801
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CJ78"
FT   CROSSLNK        1039
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P0CJ78"
SQ   SEQUENCE   1058 AA;  111676 MW;  4A9158A4AFD3AC71 CRC64;
     MEANQAGSGA GGGGSSGIGG EDGVHFQSYP FDFLEFLNHQ RFEPMELYGE HAKAVAALPC
     TPGPPPQPPP QPPPPQYDYP PQSSFKPKAE APSSSSSSSS SSSSSSSSSS SSSQAKKMDP
     PLPPTFGAPP PPLFDAAFPA PQWGIVDLSG HQHLFGNLKR GGPTPGPGVA SGLGTPTGTP
     GPLTTPSQTP PGPAVGAACD PTKDDKGYFR RLKYLMERRF PCGVCQKSFK QSSHLVQHML
     VHSGERPYEC GICGRTYNHV SSLIRHRRCH KDVPPTPTGG TPQPGPALPS LGLPVSTASA
     TASSDPAAVS SGPSATPATP ATSTDGNTTP AAPPGVAMPP SATTGGDGPF ACSLCWKVFK
     KPSHLHQHQI IHTGEKPFSC SVCSKSFNRR ESLKRHVKTH SADLLRLPCG ICGKVFRDAS
     YLLKHQAAHA AAGTPRPVYP CDLCGKTYSA PQSLLRHKAA HAPPVATEPA KDGAASVPQP
     PPPFPPGPYL LPADPSTTDE KATAAAAAVV YGAVPVPLLS AHPLLLGGAG NGGAGGPGAG
     GPSKTFCCGI CGRAFGRRET LKRHERIHTG EKPHQCPVCG KRFRESFHLS KHHVVHTRER
     PYKCELCGKV FGYPQSLTRH RQVHRLQLPC ALAGATGLAT GQGTTGACGP GAAGTSGGPA
     DLSYACSDCG EHFPDLFHVM SHKEAHMSEK PYGCDACGKT FGFIENLMWH KLVHQAAPER
     LLAPTPSGPQ SSDGGSSGGG TDASSVLDNG LAGEVGTAVA ALAGVSGGSE DAGGATVAGS
     GGGTSSGAER FSCATCGQSF KHFLGLVTHK YVHLVRRTLG CGLCGQSFAG AYDLLLHRRS
     HRQKRGFRCP VCGKRFWEAA LLMRHQRCHT EQRPYRCGVC GRGFLRSWYL RQHRVVHTGE
     RAFKCGVCAK HFAQSSSLAE HRRLHAVARP QRCGACGKTF RYRSNLLEHQ RLHLGERAYR
     CEHCGKGFFY LSSVLRHQRA HEPPRPELRC PACLKAFKDP GYFRKHLAAH QGGRPFRCSS
     CGEGFANTYG LKKHRLMHKA EGLGMPGTGG SALAGKDP
 
 
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