ID   MS18A_OTOGA             Reviewed;         232 AA.
AC   B5SNH4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein Mis18-alpha;
GN   Name=MIS18A;
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii(Bushbaby).";
RL   Submitted (MAR-2011) 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; DP000874; ACH99683.1; -; Genomic_DNA.
DR   RefSeq; XP_003797117.1; XM_003797069.2.
DR   AlphaFoldDB; B5SNH4; -.
DR   STRING; 30611.ENSOGAP00000015351; -.
DR   Ensembl; ENSOGAT00000017142; ENSOGAP00000015351; ENSOGAG00000017137.
DR   GeneID; 100948126; -.
DR   KEGG; oga:100948126; -.
DR   CTD; 54069; -.
DR   eggNOG; ENOG502S9R8; Eukaryota.
DR   GeneTree; ENSGT00940000154267; -.
DR   HOGENOM; CLU_101031_0_0_1; -.
DR   InParanoid; B5SNH4; -.
DR   OMA; EMKMLVM; -.
DR   OrthoDB; 1453138at2759; -.
DR   TreeFam; TF333200; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cell cycle; Cell division; Centromere; Chromosome; Isopeptide bond;
KW   Metal-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..232
FT                   /note="Protein Mis18-alpha"
FT                   /id="PRO_0000359881"
FT   DOMAIN          79..177
FT                   /note="Mis18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
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         140
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   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   MOD_RES         39
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         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
FT   CROSSLNK        161
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYP9"
SQ   SEQUENCE   232 AA;  25942 MW;  844DCCD211740F26 CRC64;
     MAGAWSSNCC RGSSTGCMCC NKGKRNDSLL LGKRLSEDSS RQQLLQKWES MWSSTSGDAS
     EGDTEKERLE EAAVAEEKPL VFLCSGCRRP LGDSLSWVTN QEDTNCILLR SVSCNVSVDK
     EQKLSKREKE NGCILETLYC AGCSLNLGYV YRCTPRDLDS KRDLFCLSVE AIESYILGSA
     EKQIVSEDKE LFNLESRVEI EKSLKQMEDV LKALHMKLWE VESKLSFAGS KS