MCPH1_PANTR
ID MCPH1_PANTR Reviewed; 835 AA.
AC P61593;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; AY552995; AAS91378.1; -; Genomic_DNA.
DR EMBL; AY552982; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552983; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552984; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552985; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552986; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552987; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552988; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552989; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552990; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552991; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552992; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552993; AAS91378.1; JOINED; Genomic_DNA.
DR EMBL; AY552994; AAS91378.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P61593; -.
DR SMR; P61593; -.
DR STRING; 9598.ENSPTRP00000034175; -.
DR PaxDb; P61593; -.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; P61593; -.
DR Proteomes; UP000002277; 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_0000096300"
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 332..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
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; 92584 MW; AB06B22E5C422CEC CRC64;
MAAPILKDVV AYVEVWSSNG TENYSKTFTT QLVEMGAKVS KTFNKQVTHV IFKDGYQSTW
DKAQKRGVKL VSVLWVEKCR TAGAHIDESL FPAANTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMAKELQR QKTNLDDDVP ILLFESNGSL IYTPTIEINS SHHSAMEKRL
QEMKEKRENL SPTSSQMIQQ SHDNPSNSLC EAPLNISRDT LCSDECFAGG LHSSFDDLCG
NSGCGNQERK LEGSINDIKS DVCISSLVLK ANNIHSSPSF THLDKSSPQK FLSNLSKEEI
NLQRNIAGKI VTPDQKQAAG VSQETFEEKY RLSPTLSSTK GHLLIHSRPR SSSVKRKRVS
HGSHSPPKEK CKRKRSIRRS IMPRLQLCRS EGRLQHVAGP ALEALSCGES SYDDYFSPDN
LKERNSENLP PESQLPSSPA QFSCRSLSKK ERTSIFEMSD FSCVGKKTRT VDITNFTAKT
ISSPQKTGNG EGRATSSCVT SAPEEALRCC GQAGKEDACP EGNGFSYTIE DPALPKGHDD
DLTPLEGSLE EMKEAVDLKS TQNKGTTSKI SNSSEGEAQS EHEPCFIVDC NMETSTEEKE
NLPGGYSGSV KNRPTRHDVL DDSCDGFKDL IKPHEELKKS GRGKKPTRTL VMTSMPSEKQ
NVVIQVVDKL KGFSIAPDVC ETTTHVLSGK PLRTLNVLLG IARGCWVLSY DWVLWSLELG
HWISEEPFEL SHHFPAAPLC RSECHLSAGP YRGTLFADQP VMFVSPASSP PVAKLCELVH
LCGGRVSQVP RQASIVIGPY SGKKKATVKY LSEKWVLDSI TQHKVCASEN YLLSQ
