MCPH1_PONPY
ID MCPH1_PONPY Reviewed; 839 AA.
AC P61594;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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; AY553023; AAS91379.1; -; Genomic_DNA.
DR EMBL; AY553010; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553011; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553012; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553013; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553014; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553015; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553016; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553017; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553018; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553019; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553020; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553021; AAS91379.1; JOINED; Genomic_DNA.
DR EMBL; AY553022; AAS91379.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; P61594; -.
DR SMR; P61594; -.
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..839
FT /note="Microcephalin"
FT /id="PRO_0000096301"
FT DOMAIN 1..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 644..734
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 755..837
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 337..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 564..586
FT /note="Disordered"
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 564..583
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"
SQ SEQUENCE 839 AA; 92643 MW; 3B34840518493C9C CRC64;
MAAPILKDVV AYVEVWSSNG TENYSKTFTT QLVDMGAKVS KTFNKQVTHV IFKDGYQSTW
DKAQKRGVKL VSVLWVEKCR TAGAHIDESL FPAANTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMAKELQR QKTSLDGGVP ILLFESNGSL IYSPTIEINS SHHSAMENRL
QEMKEKRENL SPTSSQMIQQ SHDNPSNSLC EAPLNISHDT LCSGESFAGG LHSSFDDLCG
NSGCGNQERK LGGSINDIKS DMCISSLVLK ANNTHSSPSF THLDKSSPQK FLSNLSKEEI
NLQRNIAGKI VTPDQKQAAG MSQETFEEKY RLSPTLSSTK GHLLIHSRPR SSSVKRKRVS
HGSHSPPKEK CKRKRSIRRS IMPRLQLCRS EGSLQHVAGP ALQALSCGES SYDDYFSPDN
LKERNSENLP PESQLPSSPA QFSCRSLSKK ERTSIFEMSD FSCVGKKTRT VDIISFTAKT
ISSPQKTGNG EGLATLSCVT SEESSAPEEA LRCCRQAGKE DACPEGNGFS YTIEDPVLPK
GHDGDLTPLE GNLEEVKEAV GLKSTQNKGT TSKISNSSEG EAQSEHEPCF IGDCNMETST
EEKENLPGGY SGSVKNRPTR HDVLDDSCDG FKDLIKPHEE LKKSERGKKP TRTLVMTSMP
SEKQNVIIQV VDKLKGFSIA PDVCETTTHV LSGKPLRTLN VLLGIARGCW VLSYDWVLWS
LELGHWISEE PFELSNHFPA APLCRSECHL SAGPYRGTLF ADQPVMFVSP ASSPPVAKLC
ELVHLCGGRV SQVPRQASIV IGPYSGKKKA TVKYLSEKWV LDSITQHKVC ASENYLLSQ
