MOB2_YEAST
ID MOB2_YEAST Reviewed; 287 AA.
AC P43563; D6VTJ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=CBK1 kinase activator protein MOB2;
DE AltName: Full=MPS1 binder 2;
DE AltName: Full=Maintenance of ploidy protein MOB2;
GN Name=MOB2; OrderedLocusNames=YFL034C-B; ORFNames=YFL035C, YFL035C-A;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION OF INTRON.
RX PubMed=9436989; DOI=10.1091/mbc.9.1.29;
RA Luca F.C., Winey M.;
RT "MOB1, an essential yeast gene required for completion of mitosis and
RT maintenance of ploidy.";
RL Mol. Biol. Cell 9:29-46(1998).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11747810; DOI=10.1016/s0092-8674(01)00596-7;
RA Colman-Lerner A., Chin T.E., Brent R.;
RT "Yeast Cbk1 and Mob2 activate daughter-specific genetic programs to induce
RT asymmetric cell fates.";
RL Cell 107:739-750(2001).
RN [5]
RP FUNCTION, INTERACTION WITH CBK1, AND SUBCELLULAR LOCATION.
RX PubMed=12196508; DOI=10.1083/jcb.200203094;
RA Weiss E.L., Kurischko C., Zhang C., Shokat K., Drubin D.G., Luca F.C.;
RT "The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes polarized
RT growth and acts with the mitotic exit network to facilitate daughter cell-
RT specific localization of Ace2p transcription factor.";
RL J. Cell Biol. 158:885-900(2002).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INTERACTION WITH MOB1.
RX PubMed=16934835; DOI=10.1016/j.jmb.2006.07.007;
RA Mrkobrada S., Boucher L., Ceccarelli D.F.J., Tyers M., Sicheri F.;
RT "Structural and functional analysis of Saccharomyces cerevisiae Mob1.";
RL J. Mol. Biol. 362:430-440(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-33; SER-59 AND THR-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Functions as an activator subunit for the CBK1 protein
CC kinase. Part of the regulation of ACE2 activity and cellular
CC morphogenesis (RAM) signaling network. Required for coordinating
CC polarized cell growth during interphase with the onset of mitosis.
CC Required for mother/daughter cell separation after cytokinesis. Also
CC has a role in the prevention of nuclear export of ACE2 from the
CC daughter cell nucleus after mitotic exit. It coordinates ACE2-dependent
CC transcription with mitotic exit network activation.
CC {ECO:0000269|PubMed:11747810, ECO:0000269|PubMed:12196508}.
CC -!- SUBUNIT: Interacts with protein kinase CBK1 to form the RAM CBK1-MOB2
CC kinase complex. {ECO:0000269|PubMed:12196508,
CC ECO:0000269|PubMed:16934835}.
CC -!- INTERACTION:
CC P43563; P53894: CBK1; NbExp=7; IntAct=EBI-11125, EBI-4110;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes to the bud
CC cortex during polarized growth and to the bud neck and daughter cell
CC nucleus during late mitosis.
CC -!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D50617; BAA09204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006940; DAA12405.1; -; Genomic_DNA.
DR PIR; S58648; S58648.
DR RefSeq; NP_116618.1; NM_001179931.1.
DR PDB; 4LQP; X-ray; 4.50 A; B=46-287.
DR PDB; 4LQQ; X-ray; 3.60 A; B/E=46-287.
DR PDB; 4LQS; X-ray; 3.30 A; B=46-287.
DR PDB; 5NCL; X-ray; 3.15 A; B=46-287.
DR PDB; 5NCM; X-ray; 2.80 A; A=44-287.
DR PDBsum; 4LQP; -.
DR PDBsum; 4LQQ; -.
DR PDBsum; 4LQS; -.
DR PDBsum; 5NCL; -.
DR PDBsum; 5NCM; -.
DR AlphaFoldDB; P43563; -.
DR SMR; P43563; -.
DR BioGRID; 31111; 1747.
DR ComplexPortal; CPX-1684; CBK1-MOB2 kinase complex.
DR DIP; DIP-1449N; -.
DR IntAct; P43563; 18.
DR MINT; P43563; -.
DR STRING; 4932.YFL034C-B; -.
DR iPTMnet; P43563; -.
DR MaxQB; P43563; -.
DR PaxDb; P43563; -.
DR PRIDE; P43563; -.
DR EnsemblFungi; YFL034C-B_mRNA; YFL034C-B; YFL034C-B.
DR GeneID; 850508; -.
DR KEGG; sce:YFL034C-B; -.
DR SGD; S000001859; MOB2.
DR VEuPathDB; FungiDB:YFL034C-B; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244956; -.
DR HOGENOM; CLU_038321_2_1_1; -.
DR InParanoid; P43563; -.
DR OMA; FRVYSHM; -.
DR BioCyc; YEAST:G3O-30427-MON; -.
DR PRO; PR:P43563; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43563; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:ComplexPortal.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IDA:ComplexPortal.
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 3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..287
FT /note="CBK1 kinase activator protein MOB2"
FT /id="PRO_0000193583"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 122..144
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:5NCM"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5NCM"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:5NCM"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5NCM"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:5NCL"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:5NCM"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:5NCM"
SQ SEQUENCE 287 AA; 33276 MW; CFBA15FF83BFAA33 CRC64;
MSFFNFKAFG RNSKKNKNQP LNVAQPPAMN TIYSSPHSSN SRLSLRNKHH SPKRHSQTSF
PAQKSTPQSQ QLTSTTPQSQ QQEASERSES QQIMFLSEPF VRTALVKGSF KTIVQLPKYV
DLGEWIALNV FEFFTNLNQF YGVVAEYVTP DAYPTMNAGP HTDYLWLDAN NRQVSLPASQ
YIDLALTWIN NKVNDKNLFP TKNGLPFPQQ FSRDVQRIMV QMFRIFAHIY HHHFDKIVHL
SLEAHWNSFF SHFISFAKEF KIIDRKEMAP LLPLIESFEK QGKIIYN
