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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
 
 
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