MOB1_YEAST
ID MOB1_YEAST Reviewed; 314 AA.
AC P40484; D6VVI1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DBF2 kinase activator protein MOB1;
DE AltName: Full=MPS1 binder 1;
DE AltName: Full=Maintenance of ploidy protein MOB1;
GN Name=MOB1; OrderedLocusNames=YIL106W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 INTERACTION WITH DBF2.
RX PubMed=9528782; DOI=10.1128/mcb.18.4.2100;
RA Komarnitsky S.I., Chiang Y.-C., Luca F.C., Chen J., Toyn J.H., Winey M.,
RA Johnston L.H., Denis C.L.;
RT "DBF2 protein kinase binds to and acts through the cell cycle-regulated
RT MOB1 protein.";
RL Mol. Cell. Biol. 18:2100-2107(1998).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11434459; DOI=10.1266/ggs.76.141;
RA Yoshida S., Toh-e A.;
RT "Regulation of the localization of Dbf2 and Mob1 during cell division of
RT Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 76:141-147(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11564880; DOI=10.1128/mcb.21.20.6972-6983.2001;
RA Luca F.C., Mody M., Kurischko C., Roof D.M., Giddings T.H., Winey M.;
RT "Saccharomyces cerevisiae Mob1p is required for cytokinesis and mitotic
RT exit.";
RL Mol. Cell. Biol. 21:6972-6983(2001).
RN [7]
RP FUNCTION, INTERACTION WITH DBF2, AND PHOSPHORYLATION BY CDC15.
RX PubMed=11404483; DOI=10.1073/pnas.141098998;
RA Mah A.S., Jang J., Deshaies R.J.;
RT "Protein kinase Cdc15 activates the Dbf2-Mob1 kinase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7325-7330(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16176976; DOI=10.1091/mbc.e05-04-0337;
RA Stoepel J., Ottey M.A., Kurischko C., Hieter P., Luca F.C.;
RT "The mitotic exit network Mob1p-Dbf2p kinase complex localizes to the
RT nucleus and regulates passenger protein localization.";
RL Mol. Biol. Cell 16:5465-5479(2005).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36 AND SER-80, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36; SER-80 AND
RP SER-229, AND 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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 79-314, MUTAGENESIS OF THR-105 AND
RP SER-107, AND INTERACTION WITH MOB2.
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).
CC -!- FUNCTION: Functions as an activator subunit for the DBF2 protein
CC kinase. Binds to DBF2, which is required for the phosphorylation and
CC activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-
CC MOB1 is part of the mitotic exit network (MEN) signaling cascade, which
CC regulates release from the nucleus and activity of phosphatase CDC14.
CC Required for inactivation of mitotic cyclin-dependent kinase for exit
CC from mitosis, cytokinesis and G1 gene transcription.
CC {ECO:0000269|PubMed:11404483, ECO:0000269|PubMed:11564880,
CC ECO:0000269|PubMed:16176976}.
CC -!- SUBUNIT: Interacts with protein kinase DBF2 to form the MEN DBF2-MOB1
CC kinase complex. {ECO:0000269|PubMed:11404483,
CC ECO:0000269|PubMed:16934835, ECO:0000269|PubMed:9528782}.
CC -!- INTERACTION:
CC P40484; P22204: DBF2; NbExp=15; IntAct=EBI-11119, EBI-5569;
CC P40484; P32328: DBF20; NbExp=7; IntAct=EBI-11119, EBI-5588;
CC P40484; P39008: POP2; NbExp=2; IntAct=EBI-11119, EBI-13629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, spindle pole body. Bud neck. Chromosome,
CC centromere. Note=Localizes predominantly to the cytoplasmic surface of
CC the spindle pole body during anaphase and to a ring at the bud neck
CC during cytokinesis. Translocates to the nucleus during mitosis and
CC associates with centromere DNA.
CC -!- PTM: Phosphorylated by CDC15. {ECO:0000269|PubMed:11404483}.
CC -!- MISCELLANEOUS: Present with 5020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; Z38125; CAA86274.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08447.1; -; Genomic_DNA.
DR PIR; S48466; S48466.
DR RefSeq; NP_012160.2; NM_001179454.1.
DR PDB; 2HJN; X-ray; 2.00 A; A=79-314.
DR PDB; 5NCN; X-ray; 3.50 A; A=79-314.
DR PDBsum; 2HJN; -.
DR PDBsum; 5NCN; -.
DR AlphaFoldDB; P40484; -.
DR SMR; P40484; -.
DR BioGRID; 34885; 349.
DR ComplexPortal; CPX-1683; DBF2-MOB1 kinase complex.
DR ComplexPortal; CPX-5341; DBF20-MOB1 kinase complex.
DR DIP; DIP-2320N; -.
DR IntAct; P40484; 28.
DR MINT; P40484; -.
DR STRING; 4932.YIL106W; -.
DR iPTMnet; P40484; -.
DR MaxQB; P40484; -.
DR PaxDb; P40484; -.
DR PRIDE; P40484; -.
DR EnsemblFungi; YIL106W_mRNA; YIL106W; YIL106W.
DR GeneID; 854700; -.
DR KEGG; sce:YIL106W; -.
DR SGD; S000001368; MOB1.
DR VEuPathDB; FungiDB:YIL106W; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_4_2_1; -.
DR InParanoid; P40484; -.
DR OMA; PQSCPRM; -.
DR BioCyc; YEAST:G3O-31362-MON; -.
DR EvolutionaryTrace; P40484; -.
DR PRO; PR:P40484; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40484; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0034973; C:Sid2-Mob1 complex; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0019207; F:kinase regulator activity; IDA:SGD.
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:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0010458; P:exit from mitosis; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:ComplexPortal.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
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; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..314
FT /note="DBF2 kinase activator protein MOB1"
FT /id="PRO_0000193582"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 105
FT /note="T->A,D: No effect."
FT /evidence="ECO:0000269|PubMed:16934835"
FT MUTAGEN 107
FT /note="S->A,D: No effect."
FT /evidence="ECO:0000269|PubMed:16934835"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 153..175
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2HJN"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2HJN"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2HJN"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:2HJN"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 248..265
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:2HJN"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:2HJN"
SQ SEQUENCE 314 AA; 35882 MW; 0B50B1D18D7EF54A CRC64;
MSFLQNFHIS PGQTIRSTRG FKWNTANAAN NAGSVSPTKA TPHNNTINGN NNNANTINNR
ADFTNNPVNG YNESDHGRMS PVLTTPKRHA PPPEQLQNVT DFNYTPSHQK PFLQPQAGTT
VTTHQDIKQI VEMTLGSEGV LNQAVKLPRG EDENEWLAVH CVDFYNQINM LYGSITEFCS
PQTCPRMIAT NEYEYLWAFQ KGQPPVSVSA PKYVECLMRW CQDQFDDESL FPSKVTGTFP
EGFIQRVIQP ILRRLFRVYA HIYCHHFNEI LELNLQTVLN TSFRHFCLFA QEFELLRPAD
FGPLLELVME LRDR
