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MOB2_MOUSE
ID   MOB2_MOUSE              Reviewed;         235 AA.
AC   Q8VI63; Q3UXL5; Q9CZJ5;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=MOB kinase activator 2;
DE   AltName: Full=Mob2 homolog;
DE   AltName: Full=Mps one binder kinase activator-like 2;
DE   AltName: Full=Ovary-specific MOB-like protein;
GN   Name=Mob2; Synonyms=Mmh;
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] (ISOFORM 1).
RC   TISSUE=Ovary;
RA   Hennebold J.D., Tanaka M., Saito J., Hanson B.R., Adashi E.Y.;
RT   "Ovary-selective genes I: the generation and characterization of an ovary-
RT   selective cDNA library.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Muellerian duct;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, and Testis;
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: Stimulates the autophosphorylation and kinase activity of
CC       STK38 and STK38L. {ECO:0000250}.
CC   -!- SUBUNIT: Binds STK38 and STK38L. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC       region {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VI63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VI63-2; Sequence=VSP_012300;
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR   EMBL; AF228503; AAL55655.1; -; mRNA.
DR   EMBL; AK012535; BAB28303.1; -; mRNA.
DR   EMBL; AK135483; BAE22548.1; -; mRNA.
DR   EMBL; BC037588; AAH37588.1; -; mRNA.
DR   CCDS; CCDS40190.1; -. [Q8VI63-1]
DR   CCDS; CCDS85460.1; -. [Q8VI63-2]
DR   RefSeq; NP_001334489.1; NM_001347560.1. [Q8VI63-2]
DR   RefSeq; NP_082584.1; NM_028308.2. [Q8VI63-1]
DR   RefSeq; XP_017177396.1; XM_017321907.1.
DR   AlphaFoldDB; Q8VI63; -.
DR   SMR; Q8VI63; -.
DR   BioGRID; 221678; 1.
DR   STRING; 10090.ENSMUSP00000081455; -.
DR   iPTMnet; Q8VI63; -.
DR   PhosphoSitePlus; Q8VI63; -.
DR   CPTAC; non-CPTAC-3728; -.
DR   EPD; Q8VI63; -.
DR   MaxQB; Q8VI63; -.
DR   PaxDb; Q8VI63; -.
DR   PeptideAtlas; Q8VI63; -.
DR   PRIDE; Q8VI63; -.
DR   ProteomicsDB; 295650; -. [Q8VI63-1]
DR   ProteomicsDB; 295651; -. [Q8VI63-2]
DR   Antibodypedia; 22879; 151 antibodies from 28 providers.
DR   DNASU; 101513; -.
DR   Ensembl; ENSMUST00000084418; ENSMUSP00000081455; ENSMUSG00000025147. [Q8VI63-1]
DR   Ensembl; ENSMUST00000211000; ENSMUSP00000147643; ENSMUSG00000025147. [Q8VI63-2]
DR   Ensembl; ENSMUST00000211206; ENSMUSP00000147608; ENSMUSG00000025147. [Q8VI63-2]
DR   GeneID; 101513; -.
DR   KEGG; mmu:101513; -.
DR   UCSC; uc009kmk.1; mouse. [Q8VI63-1]
DR   CTD; 81532; -.
DR   MGI; MGI:1919891; Mob2.
DR   VEuPathDB; HostDB:ENSMUSG00000025147; -.
DR   eggNOG; KOG0440; Eukaryota.
DR   GeneTree; ENSGT01050000244956; -.
DR   HOGENOM; CLU_038321_1_0_1; -.
DR   InParanoid; Q8VI63; -.
DR   OMA; YHAHYPQ; -.
DR   PhylomeDB; Q8VI63; -.
DR   TreeFam; TF300789; -.
DR   BioGRID-ORCS; 101513; 3 hits in 38 CRISPR screens.
DR   ChiTaRS; Mob2; mouse.
DR   PRO; PR:Q8VI63; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8VI63; protein.
DR   Bgee; ENSMUSG00000025147; Expressed in hindlimb stylopod muscle and 223 other tissues.
DR   ExpressionAtlas; Q8VI63; baseline and differential.
DR   Genevisible; Q8VI63; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.140.30; -; 1.
DR   InterPro; IPR005301; MOB_kinase_act_fam.
DR   InterPro; IPR036703; MOB_kinase_act_sf.
DR   PANTHER; PTHR22599; PTHR22599; 1.
DR   Pfam; PF03637; Mob1_phocein; 1.
DR   SMART; SM01388; Mob1_phocein; 1.
DR   SUPFAM; SSF101152; SSF101152; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..235
FT                   /note="MOB kinase activator 2"
FT                   /id="PRO_0000193569"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..85
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012300"
SQ   SEQUENCE   235 AA;  26851 MW;  184610E54600F229 CRC64;
     MDWLMGKSKA KPNGKKPAAE EKKVYLEPEH TKSRITDFEF KELVVLPREI DLNEWLASNT
     TTFFHHINLQ YSTISEFCTG ETCQTMAVCN TQYYWYDERG KKVKCTAPQY VDFVMSSVQK
     LVTDEDVFPT KYGREFPSSF ESLVKKICKY LFHVLGHIYW AHFKETLALE LHGHLNTLYV
     HFILFAREFN LLDPKETAVM DDLTEVLCSS PGNSGATGDG ANSGASGAQN HVKER
 
 
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