MCPH1_MACFA
ID MCPH1_MACFA Reviewed; 842 AA.
AC Q5IFK1;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Microcephalin {ECO:0000250|UniProtKB:Q8NEM0};
GN Name=MCPH1 {ECO:0000250|UniProtKB:Q8NEM0};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(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; AY742816; AAW55574.1; -; mRNA.
DR RefSeq; NP_001306456.1; NM_001319527.1.
DR AlphaFoldDB; Q5IFK1; -.
DR SMR; Q5IFK1; -.
DR STRING; 9541.XP_005562588.1; -.
DR GeneID; 102144975; -.
DR CTD; 79648; -.
DR eggNOG; KOG4362; Eukaryota.
DR Proteomes; UP000233100; 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 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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..842
FT /note="Microcephalin"
FT /id="PRO_0000096298"
FT DOMAIN 1..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 647..737
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 758..840
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 346..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..607
FT /note="Basic and acidic 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 842 AA; 93530 MW; 8FEBA83F1A90B821 CRC64;
MAAPILKDVV AYVEVWSSNG TENYSKTFTT QLVDMGAKVS KTFNKQVTHV IFKDGYQSTW
DKARKRGVKL VSVLWVEKCR TAGAHIDESL FPAANTNEHL PSLIKKKRKC MQPKDFNFKT
PENDKRFQKK FEKMAKELQR QKTSLDDDVP ILLFESNGSL TYSPTIKINS SHHSAMEKRL
QEMKEKRENL SPTSSQMIQQ SHDNPSNSLC EAPLNISHDT LCSDESIAGG LHSSFDDLCG
NSECGNQERK LGGSINDTKS DMCISSLVLK TNNTHLSPSF AHLDKSSPQK FLSNLSKEEI
NLQRNIVGKI VTPDQKQAAG MSQETFEEKY RLSPTLSSTK GHLLIHSRPR SSSVKRKRVS
YGFHSPPKEK CKRKRSIRRS IMPRLQLCRS EGSLQCMAGP ALEALGCGES SYDDYFSPDN
LKERNSENLP PKSQLPSNPA QFSCRSLSKK ERTSIFEMSD FSCVGKKPRT VDITSFTAKT
ICSPQKTASG EGCATFSCVT SEESSAPEET LRYCRQAGPQ QKEDAWPEGN GFSYTIEDPS
LPKGHDGDLT PFEGILEEVK EAVGLKSTQD KGTTSKISNS SEGEAPSEHE PRSVVDCNVE
RSAEEKENLP GGYSGSVKNR PTRRDVLDGS CDSFKDLIKP HEELKKSGKG KKPTRTLVMT
SMPSEKQNVV IQVVDKLKGF SIARDVCETT THVLSGKPLR TLNVLLGIAR GCWVLSYDWV
LWSLESGQWI SEEPFELSNH FPAAPLCRRE CHLSAGPYRG TLFADQPVMF VSPASSPPVA
KLCELVHLCG GRVSQVPRQA SIVIGPYSGK KKATVKYLSE KWVLDSITQH KVCASENYLL
PQ
