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ZN276_MOUSE
ID   ZN276_MOUSE             Reviewed;         614 AA.
AC   Q8CE64; Q3TQL7; Q3V088; Q80ZN3; Q8C912; Q9ESV2;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Zinc finger protein 276;
DE            Short=Zfp-276;
GN   Name=Znf276; Synonyms=Zfp276;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, Skin, and Testis;
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 [MRNA] OF 149-614 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J;
RX   PubMed=10936049; DOI=10.1006/geno.2000.6252;
RA   Wong J.C., Alon N., Norga K., Kruyt F.A.E., Youssoufian H., Buchwald M.;
RT   "Cloning and analysis of the mouse Fanconi anemia group A cDNA and an
RT   overlapping penta zinc finger cDNA.";
RL   Genomics 67:273-283(2000).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, centromere,
CC       kinetochore {ECO:0000250|UniProtKB:Q8N554}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CE64-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CE64-2; Sequence=VSP_026106, VSP_026107;
CC   -!- TISSUE SPECIFICITY: Found in all the examined tissues, with highest
CC       levels in kidney, liver, lung, and spleen.
CC       {ECO:0000269|PubMed:10936049}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels in all stages of embryonic
CC       development examined. {ECO:0000269|PubMed:10936049}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG01634.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC31505.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK028939; BAC26204.1; -; mRNA.
DR   EMBL; AK043258; BAC31505.1; ALT_INIT; mRNA.
DR   EMBL; AK133363; BAE21616.1; -; mRNA.
DR   EMBL; AK163486; BAE37365.1; -; mRNA.
DR   EMBL; AF178935; AAG01634.1; ALT_INIT; mRNA.
DR   CCDS; CCDS52699.1; -. [Q8CE64-1]
DR   RefSeq; NP_065243.2; NM_020497.2. [Q8CE64-1]
DR   AlphaFoldDB; Q8CE64; -.
DR   SMR; Q8CE64; -.
DR   BioGRID; 208217; 17.
DR   IntAct; Q8CE64; 1.
DR   STRING; 10090.ENSMUSP00000001092; -.
DR   iPTMnet; Q8CE64; -.
DR   PhosphoSitePlus; Q8CE64; -.
DR   EPD; Q8CE64; -.
DR   MaxQB; Q8CE64; -.
DR   PaxDb; Q8CE64; -.
DR   PeptideAtlas; Q8CE64; -.
DR   PRIDE; Q8CE64; -.
DR   ProteomicsDB; 275069; -. [Q8CE64-1]
DR   ProteomicsDB; 275070; -. [Q8CE64-2]
DR   Antibodypedia; 17483; 132 antibodies from 19 providers.
DR   DNASU; 57247; -.
DR   Ensembl; ENSMUST00000001092; ENSMUSP00000001092; ENSMUSG00000001065. [Q8CE64-1]
DR   GeneID; 57247; -.
DR   KEGG; mmu:57247; -.
DR   UCSC; uc009nva.2; mouse. [Q8CE64-2]
DR   UCSC; uc009nvb.2; mouse. [Q8CE64-1]
DR   CTD; 57247; -.
DR   MGI; MGI:1888495; Zfp276.
DR   VEuPathDB; HostDB:ENSMUSG00000001065; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158841; -.
DR   HOGENOM; CLU_040755_0_0_1; -.
DR   InParanoid; Q8CE64; -.
DR   OMA; LAVKWAW; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q8CE64; -.
DR   TreeFam; TF332664; -.
DR   BioGRID-ORCS; 57247; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q8CE64; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8CE64; protein.
DR   Bgee; ENSMUSG00000001065; Expressed in granulocyte and 197 other tissues.
DR   ExpressionAtlas; Q8CE64; baseline and differential.
DR   Genevisible; Q8CE64; MM.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR012934; Znf_AD.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF07776; zf-AD; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS51915; ZAD; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Centromere; Chromosome; DNA-binding; Kinetochore;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..614
FT                   /note="Zinc finger protein 276"
FT                   /id="PRO_0000047324"
FT   DOMAIN          78..164
FT                   /note="ZAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT   ZN_FING         434..458
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         465..490
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         496..518
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         524..546
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         554..577
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT   VAR_SEQ         337..350
FT                   /note="QLGETQVPSSTSDD -> KQHLWLMLEQDSVF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026106"
FT   VAR_SEQ         351..614
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026107"
FT   CONFLICT        353
FT                   /note="K -> R (in Ref. 1; BAC26204)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509..510
FT                   /note="KH -> ND (in Ref. 2; AAG01634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="A -> G (in Ref. 2; AAG01634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="L -> W (in Ref. 2; AAG01634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   614 AA;  67339 MW;  1F5716CFADE16533 CRC64;
     MKRDRLGRFL SPGIARQRGG SGGGCGSGRT RGRPSRSGGT SADGAAAQLS WGSMTRSCGD
     TGDDGTDEAG AGRTLAMGHC RLCHGKFSSR SLRSISDRVP GETSERLSPG ERVFIRDFQR
     LLGVAVHQDP ALPQSVCKNC YTQFYQCHSL LRTFLQRVNV SPAGQRKPCT KVGVQPTTVA
     EEGACVADLI ASSPRCLHGL VGWVHEHAVS CGSLPSLQRT LSSEYCGIIQ AVWGCDQGHD
     FTMDTASSCR ALFLDSALAV KWAWGKDLSP RLAQNSESNP TGAASRLCQA RETQVGSETK
     TLPSVDVALL HSHGDSVGPG LGPCTQPHLA PSEAPGQLGE TQVPSSTSDD RVKDEFSDLS
     EGDFLSEDES DKKQTPQSSD ESFEPYPEKK VSGKKSEGRE AKRPEEPKIR KKPGPKPGWK
     KKLRCEREEL PTIYKCPYQG CTAVYRGADG MKKHIKEHHE EVRERPCPHP GCNKVFMIDR
     YLQRHVKLIH TEVRNYICDE CGQTFKQRKH LLVHQMRHSG AKPLQCEVCG FQCRQRASLK
     YHMTKHKAET ELDFACDQCG RRFEKAHNLN VHMSMVHPLT QAQDRALPLE AEPPPGPLSP
     SGTMEGQAVK PEPT
 
 
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