MCPH1_GORGO
ID MCPH1_GORGO Reviewed; 835 AA.
AC P61591;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15056607; DOI=10.1093/hmg/ddh126;
RA Evans P.D., Anderson J.R., Vallender E.J., Choi S.S., Lahn B.T.;
RT "Reconstructing the evolutionary history of microcephalin, a gene
RT controlling human brain size.";
RL Hum. Mol. Genet. 13:1139-1145(2004).
CC -!- FUNCTION: Implicated in chromosome condensation and DNA damage induced
CC cellular responses. May play a role in neurogenesis and regulation of
CC the size of the cerebral cortex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC27 and maybe other components of the APC/C
CC complex. Interacts with histone variant H2AX under DNA damage
CC conditions (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}.
CC -!- DOMAIN: BRCT domain 1 is required to prevent abnormal chromosome
CC condensation. It binds directly to the SWI-SNF chromatin remodeling
CC complex (By similarity). {ECO:0000250}.
CC -!- DOMAIN: BRCT domains 2 and 3 recognize phosphoserine/phosphothreonine
CC marks on proteins with high selectivity, and mediate interaction with
CC phosphorylated CDC27. They also mediate the dual recognition of
CC phosphoserine and phosphotyrosine in the C-terminal tail of histone
CC H2AX (By similarity). {ECO:0000250}.
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DR EMBL; AY553009; AAS91382.1; -; Genomic_DNA.
DR EMBL; AY552996; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY552997; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY552998; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY552999; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553000; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553001; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553002; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553003; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553004; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553005; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553006; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553007; AAS91382.1; JOINED; Genomic_DNA.
DR EMBL; AY553008; AAS91382.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P61591; -.
DR SMR; P61591; -.
DR STRING; 9593.ENSGGOP00000017784; -.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; P61591; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0021987; P:cerebral cortex development; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.10190; -; 3.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR022047; Microcephalin-like.
DR InterPro; IPR029504; Microcephalin_mammal.
DR PANTHER; PTHR14625; PTHR14625; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF12258; Microcephalin; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 3.
DR SUPFAM; SSF52113; SSF52113; 3.
DR PROSITE; PS50172; BRCT; 3.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..835
FT /note="Microcephalin"
FT /id="PRO_0000096295"
FT DOMAIN 1..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 640..730
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 751..833
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..376
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT79"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
SQ SEQUENCE 835 AA; 92591 MW; D65C6D6C86230714 CRC64;
MAAPILKDVV AYVEVWSSNG TENYSKTFTT QLVDMGAKVS KTFNKQVTHV IFKDGYQSTW
DKAQKRGVKL VSVLWVEKCR TAGAHIDESL FPAANTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMAKELQR QKTSLDDDVP ILLFESNGSL IYTPTIEINS SHHSAMEKRL
QEMKEKRENL SPTSSQLIQQ SHDNPSNSLC EAPLNISRDT LCSDEYFAGG LHSSFDDLCG
NSGCGNQERK LEGSINDIKS DVCISSLVSK ANNIHSSPSF THLDKSSPQK FLSNLSKEEI
NLQRNIAGKI VTPDQKQAAG MSQETFEEKY RLSPTLSSIK GHLLIHSRPR SSSVKRKRVS
HGSHSPPKEK CKRKRSIRRS IMPRLQLCRS EGRLQHVAGP ALKALSCGES SYDDYFSPDN
LKERNSENLP PESQLPSSPA QFSCRSLSKK ERTSIFEMSD FSCVGKKTRT VDITNFTAKT
ISSPQKTGNG EGRATSSCVT SAPEEALRCC RQAGKEDGCP EGNGFSYTIE DPALPKGHDG
DLTALEGSLE EMKEAVGLKS TQNRGTTSKI SNSSEGEAQS EHEPCFIVDC NMETSTEEKE
NLPGGYSGSV KNRPTRHDVL DDSCDGFKDL IKPHEEMKKS GRGKKPTRTL VMTSMPSEKQ
NVVIQVVDKL KGFSIAPDVC ETTTHVLSGK PLRTLNVLLG IARGCWVLSY DWVLWSLELG
HWISEEPFEL SHHFPAAPLC RSECHLSAGP YRGTLFADQP VMFVSPASSP PVAKLCELVH
LCGGRVSQVP RQASIVIGPY SGKKKATVKY LSEKWVLDSI TQHKVCASEN YLLSQ
