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ZXDB_MOUSE
ID   ZXDB_MOUSE              Reviewed;         873 AA.
AC   A2CE44; Q3V1M7; Q8CEQ1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Zinc finger X-linked protein ZXDB;
GN   Name=Zxdb;
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 252-873.
RC   STRAIN=C57BL/6J; TISSUE=Head, 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   [3]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-89, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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: Cooperates with CIITA to promote transcription of MHC class I
CC       and MHC class II genes. {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates. Interacts with ZXDC and CIITA (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ZXD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR293526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK016708; BAC25496.1; ALT_FRAME; mRNA.
DR   EMBL; AK132358; BAE21123.1; -; mRNA.
DR   CCDS; CCDS41065.1; -.
DR   RefSeq; NP_001074942.1; NM_001081473.1.
DR   AlphaFoldDB; A2CE44; -.
DR   SMR; A2CE44; -.
DR   STRING; 10090.ENSMUSP00000100524; -.
DR   iPTMnet; A2CE44; -.
DR   PhosphoSitePlus; A2CE44; -.
DR   MaxQB; A2CE44; -.
DR   PaxDb; A2CE44; -.
DR   PeptideAtlas; A2CE44; -.
DR   PRIDE; A2CE44; -.
DR   ProteomicsDB; 275249; -.
DR   Ensembl; ENSMUST00000101388; ENSMUSP00000100524; ENSMUSG00000073062.
DR   GeneID; 668166; -.
DR   KEGG; mmu:668166; -.
DR   UCSC; uc009ttq.1; mouse.
DR   CTD; 158586; -.
DR   MGI; MGI:3694898; Zxdb.
DR   VEuPathDB; HostDB:ENSMUSG00000073062; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162988; -.
DR   HOGENOM; CLU_007312_0_0_1; -.
DR   InParanoid; A2CE44; -.
DR   OMA; KVEWNVH; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; A2CE44; -.
DR   TreeFam; TF330996; -.
DR   BioGRID-ORCS; 668166; 5 hits in 69 CRISPR screens.
DR   PRO; PR:A2CE44; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2CE44; protein.
DR   Bgee; ENSMUSG00000073062; Expressed in caudate-putamen and 218 other tissues.
DR   Genevisible; A2CE44; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; 5.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   1: Evidence at protein level;
KW   Activator; Metal-binding; Methylation; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..873
FT                   /note="Zinc finger X-linked protein ZXDB"
FT                   /id="PRO_0000292802"
FT   ZN_FING         340..364
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         373..397
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         403..427
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         433..455
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         462..486
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         493..517
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         523..547
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         553..577
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         583..607
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         616..641
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..646
FT                   /note="Required for interaction with ZXDC"
FT                   /evidence="ECO:0000250"
FT   REGION          645..776
FT                   /note="Required for transcriptional activation"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        240..258
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         89
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   CONFLICT        271..280
FT                   /note="AAAAAAAAAA -> VAGGVVFFVG (in Ref. 2; BAE21123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="P -> R (in Ref. 2; BAC25496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="H -> P (in Ref. 2; BAC25496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        643
FT                   /note="L -> F (in Ref. 2; BAC25496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="L -> I (in Ref. 2; BAC25496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="A -> T (in Ref. 2; BAC25496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   873 AA;  90376 MW;  77E31C72C7098264 CRC64;
     MEIPRLLPAR GTPQGAGGGG CPAGGGGVHR APASLACQAP TRRLLLLRGA QDGGPGPRSA
     EAQRASRGLG PSLNRLAPRP DHRSSGGGRG GGAGGGGGGS GGGGGGGGGG GGGGGGGGSR
     GGSDDFFLLL LDPVGGDVET VGTEQAGAPV RREEAGAGPR PERRQSAGPP AGRPEPGPRC
     LSAVPAASPL PAAGPGPAAA AAAAAAAAFA GTITIHNQDL LLRFENGVLT LTTPPLPAWE
     PGVAPFPQPQ PPPQPGALIA PQAAAAGFPP AAAAAAAAAA AGAQLGDCPE LPPDLLLAEP
     AEPAACPAPP EEEAEAPAAA AAQSPRGPAG PGPGPGVVLY LCPEAQCGQT FAKKHQLKVH
     LLTHSSSQGQ RPFKCPLSGC GWTFTTSYKL KRHLQSHDKL RPFGCPVQGC GKSFTTVYNL
     KAHMKGHEQE NSFKCEVCEE SFPTQAKLST HQRSHFEPER PYQCAFSGCK KTFITVSALF
     SHNRAHFREQ ELFACSFPGC SKQYDKACRL KIHLRSHTGE RPFLCDFDGC GWNFTSMSKL
     LRHKRKHEDD RRFTCPVEGC GKSFTRAEHL KGHSITHLGT KPFVCPVEGC CARFSARSSL
     YIHSKKHLQD VGAWKSRCPV PTCNKLFTSK HSMKTHMTKR HNLSQDLLAQ LEAANSLTPS
     SELTSPGQSD LSGAELVSLF SDVPGHGSAA VLDTALVNSG ILTIDVASVN SSLAGSLPAD
     NNSNNHSLGQ AAEPRALRGA PSDLPQSLDT SLFFGTSVAG YQHSPLDMDD VSAGNVGLFG
     SLALKNSSLE PQALTPSNKL TVDTEALTPS STLCENSVSE LLTPAKAEWN VHPESDFFGH
     EEETQFGFSH PTGSHGSQKD TDLITVTGTP FLV
 
 
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