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ZN787_MOUSE
ID   ZN787_MOUSE             Reviewed;         381 AA.
AC   Q8BIF9; B9EHE2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Zinc finger protein 787;
GN   Name=Znf787; Synonyms=Zfp787;
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=C57BL/6J;
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
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=BAC36810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK077458; BAC36810.1; ALT_FRAME; mRNA.
DR   EMBL; CH466627; EDL31307.1; -; Genomic_DNA.
DR   EMBL; BC137753; AAI37754.1; -; mRNA.
DR   CCDS; CCDS20769.1; -.
DR   RefSeq; NP_001013030.1; NM_001013012.1.
DR   RefSeq; XP_006540376.1; XM_006540313.3.
DR   AlphaFoldDB; Q8BIF9; -.
DR   SMR; Q8BIF9; -.
DR   BioGRID; 211946; 26.
DR   IntAct; Q8BIF9; 1.
DR   STRING; 10090.ENSMUSP00000092468; -.
DR   iPTMnet; Q8BIF9; -.
DR   PhosphoSitePlus; Q8BIF9; -.
DR   EPD; Q8BIF9; -.
DR   MaxQB; Q8BIF9; -.
DR   PaxDb; Q8BIF9; -.
DR   PeptideAtlas; Q8BIF9; -.
DR   PRIDE; Q8BIF9; -.
DR   ProteomicsDB; 299602; -.
DR   Antibodypedia; 33179; 88 antibodies from 16 providers.
DR   DNASU; 67109; -.
DR   Ensembl; ENSMUST00000094870; ENSMUSP00000092468; ENSMUSG00000046792.
DR   GeneID; 67109; -.
DR   KEGG; mmu:67109; -.
DR   UCSC; uc009fap.1; mouse.
DR   CTD; 67109; -.
DR   MGI; MGI:1914359; Zfp787.
DR   VEuPathDB; HostDB:ENSMUSG00000046792; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163064; -.
DR   HOGENOM; CLU_002678_19_0_1; -.
DR   InParanoid; Q8BIF9; -.
DR   OMA; PKPYVCM; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q8BIF9; -.
DR   TreeFam; TF337689; -.
DR   BioGRID-ORCS; 67109; 6 hits in 72 CRISPR screens.
DR   ChiTaRS; Zfp787; mouse.
DR   PRO; PR:Q8BIF9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BIF9; protein.
DR   Bgee; ENSMUSG00000046792; Expressed in retinal neural layer and 249 other tissues.
DR   ExpressionAtlas; Q8BIF9; baseline and differential.
DR   Genevisible; Q8BIF9; MM.
DR   GO; GO:0005634; C:nucleus; 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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
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; 5.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..381
FT                   /note="Zinc finger protein 787"
FT                   /id="PRO_0000287607"
FT   ZN_FING         66..88
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         94..116
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         122..144
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         150..172
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         178..200
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         280..303
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         317..339
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..65
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD87"
FT   MOD_RES         122
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD87"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD87"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD87"
FT   CROSSLNK        211
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6DD87"
FT   CONFLICT        193
FT                   /note="L -> M (in Ref. 1; BAC36810)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  40477 MW;  06F4C15E90FF8F0F CRC64;
     MELREEAWSP GPLDSEDQQM ASHENPVDIL IMDDDDVPSW PPTKLSPPQS APPPGPPPRP
     RPPAPYICTE CGKSFSHWSK LTRHQRTHTG ERPNACTDCG KTFSQSSHLV QHRRIHTGEK
     PYACSECGKR FSWSSNLMQH QRIHTGEKPY TCPDCGRSFT QSKSLAKHRR SHSGLKPFVC
     PRCGRGFSQP KSLARHLRLH PELSGPGVAA KVLAASVRRA KAPEEATAAD GEIAIPVGDG
     EGIIVVGPPG DGAAAAAALA GVGTRATGTR SRRAPAPKPY VCMECGKGFG HGAGLLAHQR
     AQHGDGLGVA VGEEPAHICV ECGEGFVQGA ALRRHKKIHA VGAPSVCSSC GQSFYRAGGE
     DDGEDQSAGA RCAECRGGEA R
 
 
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