MCPH1_COLGU
ID MCPH1_COLGU Reviewed; 841 AA.
AC P61590;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=33548;
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; AY553051; AAS91381.1; -; Genomic_DNA.
DR EMBL; AY553038; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553039; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553040; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553041; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553042; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553043; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553044; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553045; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553046; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553047; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553048; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553049; AAS91381.1; JOINED; Genomic_DNA.
DR EMBL; AY553050; AAS91381.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P61590; -.
DR SMR; P61590; -.
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 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; Repeat.
FT CHAIN 1..841
FT /note="Microcephalin"
FT /id="PRO_0000096294"
FT DOMAIN 1..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 646..736
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 757..839
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 340..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT79"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
SQ SEQUENCE 841 AA; 93039 MW; BEEF28759E584CB6 CRC64;
MAAPILKDVV AYVEVWSSNG TENYSKTFTT QLVDMGAKVS KTFNKQVTHV IFKDGYQSTW
DKAQKRGVKL VSVLWVEKCR TAGAHIDESL FPAANTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMANELQR QKTSLDGDVP ILLFESNGSL TYSPIIKINS SHHSAMEKRL
QEMKEKRENL SPTSSQMIQQ SHDNPSNSLC EAPLNISHDT LCSDESIAGL HSSFDDLCGY
SGCGNQERKL GGSINDTKSA MCVSSLVLKT NHIHSSPSFA HLDKSSPQKF LSNLSKEEIN
LPRNIVGKIV TPDQKQAAGT SQETFEEKYR LSPTFSSTKG HLLIHSRPRS SSVKRKRVSY
GFHSPPKEKC KRKRSIRRSI MPRLQLCSSE GSRQHMAGPA LEALSCAESS YDDYFSPDNL
KERNSENLPP ESQLPSSPAQ FSCRSLSKKE RTSMFEMSDF SCIGKKTRTV DMTSFTAKTI
SSPQKTANGE GRATLSGVTS EESSAPEETL RCCRQAGPQQ KEGACPEGNG FSYTIEDPAL
PKGHDGDLTP LEGILEEVKE AVGLKSTQDK GTTSKISNSS EGEASSEHEP RSVVDCNVER
SAEEKENLLG GYSGSVKNRP TRHDVLDGSC DSFKDLIKPH EELKKSGKGK KPTRTLVMTS
MPSEKQNIVI QVVDKLKGFS IAPDVCETTT HVLSGKPLRT LNVLLGIARG CWVLSYDWVL
WSLESGHWIS EESFELSNHF PAAPLCRREC HLSAGPYRGT LFADQPVMFV SPASSPPVAK
LCELVHLCGG RVSQVPRQAS IVIGPYSGKK KATVKYLSEK WVLDSITQHK VCASENYLLP
Q
