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MS18A_RAT
ID   MS18A_RAT               Reviewed;         223 AA.
AC   B2RZC4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein Mis18-alpha;
GN   Name=Mis18a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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: Required for recruitment of CENPA to centromeres and normal
CC       chromosome segregation during mitosis. {ECO:0000250|UniProtKB:Q9NYP9}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with OIP5/MIS18B. Identified in a
CC       complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7 and RBBP4.
CC       {ECO:0000250|UniProtKB:Q9NYP9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NYP9}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9NYP9}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q9NYP9}. Note=Associated with centromeres in
CC       interphase cells, from late anaphase to the G1 phase. Not detected on
CC       centromeres during earlier phases of mitosis. Associated with
CC       chromatin. {ECO:0000250|UniProtKB:Q9NYP9}.
CC   -!- SIMILARITY: Belongs to the mis18 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01129}.
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DR   EMBL; BC167102; AAI67102.1; -; mRNA.
DR   RefSeq; NP_001120995.2; NM_001127523.2.
DR   AlphaFoldDB; B2RZC4; -.
DR   STRING; 10116.ENSRNOP00000037080; -.
DR   PhosphoSitePlus; B2RZC4; -.
DR   PaxDb; B2RZC4; -.
DR   Ensembl; ENSRNOT00000037444; ENSRNOP00000037080; ENSRNOG00000021555.
DR   GeneID; 288272; -.
DR   KEGG; rno:288272; -.
DR   UCSC; RGD:1310778; rat.
DR   CTD; 54069; -.
DR   RGD; 1310778; Mis18a.
DR   eggNOG; ENOG502S3DZ; Eukaryota.
DR   GeneTree; ENSGT00940000154267; -.
DR   HOGENOM; CLU_101031_0_0_1; -.
DR   InParanoid; B2RZC4; -.
DR   OrthoDB; 1453138at2759; -.
DR   PhylomeDB; B2RZC4; -.
DR   TreeFam; TF333200; -.
DR   Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   PRO; PR:B2RZC4; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Genevisible; B2RZC4; RN.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; ISO:RGD.
DR   GO; GO:0007059; P:chromosome segregation; ISO:RGD.
DR   GO; GO:0044030; P:regulation of DNA methylation; ISO:RGD.
DR   InterPro; IPR034752; Mis18.
DR   InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR   Pfam; PF03226; Yippee-Mis18; 1.
DR   PROSITE; PS51793; MIS18; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Isopeptide bond;
KW   Metal-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..223
FT                   /note="Protein Mis18-alpha"
FT                   /id="PRO_0000359882"
FT   DOMAIN          71..169
FT                   /note="Mis18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   CROSSLNK        153
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
SQ   SEQUENCE   223 AA;  25216 MW;  D7CFCC75AEFF990E CRC64;
     MAGTFSLEPC STSSSCNHQG KRSESSLLEK RLSEDSSRHW RLQKWASMSS ADASRTLLER
     REEKAAAAEN PLVFLCTRCR RPLGDSLTWV ASQEDTNCIL LRSVSSNVSV DKEQKLSKCR
     DEDGCILETL YCSGCSLSLG YVYRCTPKNL DYKRNLFCLS VEAVESYTLG SSEQQIVSEE
     EFFNLESRVE IEKSIKQMED VLTVMQAKLW EVESKLSKAG RYS
 
 
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