MCPH1_HYLLA
ID MCPH1_HYLLA Reviewed; 840 AA.
AC P61592;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
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; AH013764; AAS91380.1; -; Genomic_DNA.
DR AlphaFoldDB; P61592; -.
DR SMR; P61592; -.
DR PRIDE; P61592; -.
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; 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..840
FT /note="Microcephalin"
FT /id="PRO_0000096297"
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 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..586
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 316..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..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"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
SQ SEQUENCE 840 AA; 92887 MW; 51265B4274C8CB87 CRC64;
MAAHILKDVV AYVEVWSSNG TENYSKTFTT QLVDMGAKVS KTFNKQVTHV IFKDGYQSTW
DKAQKRGVKL VSVLWVEKCR TAGAHIDESL FPAINTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMAKELQR QKTSLDDDVP ILLFESSGSL TYSPTIKINS SHHSAMEKRL
QEMKEKRENL SPSSSQMIQQ SHDNPSNSLC EAPLNISRDT LCSDESFAGG VHSSFDDLCG
NSGCGNQERK LGGSINDIES DMCISSLVLK ANNIHSSPSF THLDKSSPQK FLSNLSKEEI
NLQRNIAGKI VTPDQKQAAG MSQETFEEKY RLSPTLSSTK GHLLIRSRPS SSSVKRQRVS
HGSHSPSKGK SKRKRSIRRS IMPRLQLCRS EGSLQHVAGP ALKALSCGES SYDDYFSPDN
LKERNSENLP PTSQLPSSLA QFSCRSLSKK ERTSIFEMSD FSCIGKKTRT VDITSFTAKT
ISSPQKTANG EGRATLSCVT SEESSAPGET LRCCRQAGKE DACPEGNGFS YTIEDPPFPK
GHDGDLTPLE GSLEEVKEAV GLKSTQNKGT TSKISNSSEG EAQSEHEPCF IVDCNMETST
EEKENLPGGY GGSVKNRPTR HDLLDDSCDS FKDLIKPHEE LKKSGRGKKP TRTLVMTSMP
SEKQNVVIQV VDKLKGFSIA PDVCETTTHV LSGKPLRTLN VLLGIARGCW VLSYDWVLWS
LELGHWISEE PFELSNHFPA APLCRSECHL SAGPYRGTLF ADQPVMFVSP ASSPPVAKLC
ELVHLCGGRV SQVPRQASIV IGPYSGKKKA TVKYLSEKWV LDSIIQHKVC ASENYLLPQR
