MCPH1_MOUSE
ID MCPH1_MOUSE Reviewed; 822 AA.
AC Q7TT79; Q8BNI9; Q8C9I7;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Microcephalin {ECO:0000303|PubMed:12046007};
GN Name=Mcph1 {ECO:0000312|MGI:MGI:2443308};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J X CBA/J;
RX PubMed=12046007; DOI=10.1086/341283;
RA Jackson A.P., Eastwood H., Bell S.M., Toomes C., Adu J., Carr I.M.,
RA Roberts E., Hampshire D.J., Crow Y.J., Mighell A.J., Karbani G., Jafri H.,
RA Rashid Y., Mueller R.F., Markham A.F., Woods C.G.;
RT "Identification of microcephalin, a protein implicated in determining the
RT size of the human brain.";
RL Am. J. Hum. Genet. 71:136-142(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-742.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: High levels of expression are found in the
CC developing forebrain and, in particular, in the walls of the lateral
CC ventricles. {ECO:0000269|PubMed:12046007}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY070216; AAL50216.1; -; mRNA.
DR EMBL; BC056924; AAH56924.1; -; mRNA.
DR EMBL; AK042026; BAC31136.1; ALT_INIT; mRNA.
DR EMBL; AK083572; BAC38955.2; -; mRNA.
DR CCDS; CCDS22124.1; -.
DR RefSeq; NP_775281.2; NM_173189.2.
DR RefSeq; XP_017168280.1; XM_017312791.1.
DR AlphaFoldDB; Q7TT79; -.
DR SMR; Q7TT79; -.
DR BioGRID; 232635; 3.
DR STRING; 10090.ENSMUSP00000037000; -.
DR iPTMnet; Q7TT79; -.
DR PhosphoSitePlus; Q7TT79; -.
DR jPOST; Q7TT79; -.
DR MaxQB; Q7TT79; -.
DR PaxDb; Q7TT79; -.
DR PRIDE; Q7TT79; -.
DR ProteomicsDB; 292195; -.
DR Antibodypedia; 2158; 379 antibodies from 32 providers.
DR Ensembl; ENSMUST00000039412; ENSMUSP00000037000; ENSMUSG00000039842.
DR GeneID; 244329; -.
DR KEGG; mmu:244329; -.
DR UCSC; uc009kzt.1; mouse.
DR CTD; 79648; -.
DR MGI; MGI:2443308; Mcph1.
DR VEuPathDB; HostDB:ENSMUSG00000039842; -.
DR eggNOG; KOG4362; Eukaryota.
DR GeneTree; ENSGT00390000018842; -.
DR HOGENOM; CLU_022062_0_0_1; -.
DR InParanoid; Q7TT79; -.
DR OMA; ESGHWIS; -.
DR OrthoDB; 1589580at2759; -.
DR PhylomeDB; Q7TT79; -.
DR TreeFam; TF332942; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR BioGRID-ORCS; 244329; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Mcph1; mouse.
DR PRO; PR:Q7TT79; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q7TT79; protein.
DR Bgee; ENSMUSG00000039842; Expressed in animal zygote and 194 other tissues.
DR ExpressionAtlas; Q7TT79; baseline and differential.
DR Genevisible; Q7TT79; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0046605; P:regulation of centrosome cycle; IMP:MGI.
DR GO; GO:0060623; P:regulation of chromosome condensation; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0043549; P:regulation of kinase activity; IMP:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..822
FT /note="Microcephalin"
FT /id="PRO_0000096299"
FT DOMAIN 10..99
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 627..717
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 738..820
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM0"
FT CONFLICT 726..742
FT /note="ICRLERHLSTQQYQGTL -> KYLSVSGQSDKVTWVLV (in Ref. 3;
FT BAC31136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 90373 MW; A2D92930A69968BE CRC64;
MEASGGVGGA FLKDVVAYVE VWSSKGTENY SRTFAKQLED MGATVSKTLN KQVTHVIFKD
GYQSTWDKAQ KTGAKLVSVL WVEKCRMAGA LVDESLFPAV NTDEHLPNLS RKKHKCMQPK
DFILKTPEND KRLQKKFEKM AEELQRQKAA LDDDVPVLLF ESPRSLVYSS PVNVMKRRLQ
DMKEKRENLS PTSSQMLEQS QQNPCVSLFE TSLNISHQPL SSDESFASGS HSSFGDSCGD
QERKLGRSAN EMTTVTCPSS PVLRASSFYG SASPNHLRQP RPQKAPDSPS KESINCQKDA
TGAVADSERK QAAGVSQGVP DEKLCLSPTM SIIEEHQVRL GPKNSSAKRK RAADLGSSPK
GKLKKRYKRK SALAIQLFKS DQSPPSTIRL IPGTPDVEAS SYEDYFSPDN LKERNSERLP
PEAQQLASPS LFHCRGLSKW ERRNMLEMCD FTCIGEKHRS ISSISDLISK SASSLEKPVK
EEVNTASTCL LLVETSANDS PGLCSQPGPQ LRDDTGPEGS SHPDTLSSSA HHITPLKGNS
TETRDPGDGK GSPKEGSTPP ASASPEDEVH ICNLSLGEDC NVEKSVEEKE NIATGYSESV
KNGPGRPDPS DSSCTGLVRP QQKPKKSEKE EKPTRTLVMT SMPSEKQTLI IQVVSTLKGF
SFAPEVCETT THVLVGKSAR TLNVLMGIAR GCWILSYEWV LLSLELGHWI SEEPFELSET
FPAAPICRLE RHLSTQQYQG TLFANQPKMF IAPASSPPRA KLCELVLLCG GQVSPAPQLA
SLIIGPYKGK KKARIQYLSE KWVLDSITQH KICDFNNYQL LQ