ID   MS18A_BOVIN             Reviewed;         235 AA.
AC   A5D7N9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protein Mis18-alpha;
GN   Name=MIS18A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; BC140629; AAI40630.1; -; mRNA.
DR   RefSeq; NP_001091479.1; NM_001098010.2.
DR   AlphaFoldDB; A5D7N9; -.
DR   STRING; 9913.ENSBTAP00000022106; -.
DR   PaxDb; A5D7N9; -.
DR   PRIDE; A5D7N9; -.
DR   Ensembl; ENSBTAT00000022106; ENSBTAP00000022106; ENSBTAG00000016619.
DR   GeneID; 510809; -.
DR   KEGG; bta:510809; -.
DR   CTD; 54069; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016619; -.
DR   VGNC; VGNC:31485; MIS18A.
DR   eggNOG; ENOG502S3DZ; Eukaryota.
DR   GeneTree; ENSGT00940000154267; -.
DR   HOGENOM; CLU_101031_0_0_1; -.
DR   InParanoid; A5D7N9; -.
DR   OMA; EMKMLVM; -.
DR   OrthoDB; 1453138at2759; -.
DR   TreeFam; TF333200; -.
DR   Reactome; R-BTA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000016619; Expressed in oocyte and 78 other tissues.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0000775; C:chromosome, centromeric region; IBA:GO_Central.
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; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
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..235
FT                   /note="Protein Mis18-alpha"
FT                   /id="PRO_0000359879"
FT   DOMAIN          82..180
FT                   /note="Mis18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   CROSSLNK        164
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
SQ   SEQUENCE   235 AA;  26318 MW;  D3DFA283E6097BB8 CRC64;
     MAGAWSSDCC EGCSSTNCTC GHKSKWGDSS LLGRRLSEDS SRHQLLQKWA SMWSSVSGDA
     SAACPERKRR EEAAEPAEED RPLVFLCSSC RRPLGDSLSW VASQEDTNCI LLRCVTCNVS
     VNEEQILSKR KNENGCILET LYCTGCSLNL GYLYRCTPKD LDYKRDLFCL SVGAIESYVL
     GSSERQIVSE DKELFNLESR VEIEKSLKQM EDVLKALQTK LWEVESKLSF TSCKS