MOB2_SCHPO
ID MOB2_SCHPO Reviewed; 244 AA.
AC O74558;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Maintenance of ploidy protein mob2;
GN Name=mob2; ORFNames=SPCC970.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH ORB6, AND SUBCELLULAR LOCATION.
RX PubMed=12456722; DOI=10.1242/jcs.00206;
RA Hou M.-C., Wiley D.J., Verde F., McCollum D.;
RT "Mob2p interacts with the protein kinase Orb6p to promote coordination of
RT cell polarity with cell cycle progression.";
RL J. Cell Sci. 116:125-135(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for coordinating polarized cell growth during
CC interphase with the onset of mitosis. {ECO:0000269|PubMed:12456722}.
CC -!- SUBUNIT: Interacts with orb6. {ECO:0000269|PubMed:12456722}.
CC -!- INTERACTION:
CC O74558; O13310: orb6; NbExp=4; IntAct=EBI-1563284, EBI-1563264;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12456722}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:12456722}. Note=Localizes to
CC the cell periphery and to the division site during septation and
CC cytokinesis.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20697.1; -; Genomic_DNA.
DR PIR; T41676; T41676.
DR RefSeq; NP_587851.1; NM_001022844.2.
DR AlphaFoldDB; O74558; -.
DR SMR; O74558; -.
DR BioGRID; 275589; 8.
DR IntAct; O74558; 1.
DR STRING; 4896.SPCC970.04c.1; -.
DR iPTMnet; O74558; -.
DR MaxQB; O74558; -.
DR PaxDb; O74558; -.
DR PRIDE; O74558; -.
DR EnsemblFungi; SPCC970.04c.1; SPCC970.04c.1:pep; SPCC970.04c.
DR GeneID; 2539016; -.
DR KEGG; spo:SPCC970.04c; -.
DR PomBase; SPCC970.04c; mob2.
DR VEuPathDB; FungiDB:SPCC970.04c; -.
DR eggNOG; KOG0440; Eukaryota.
DR HOGENOM; CLU_038321_2_0_1; -.
DR InParanoid; O74558; -.
DR OMA; FRVYSHM; -.
DR PhylomeDB; O74558; -.
DR PRO; PR:O74558; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0062200; P:RAM/MOR signaling pathway; IMP:PomBase.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
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 Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..244
FT /note="Maintenance of ploidy protein mob2"
FT /id="PRO_0000193581"
FT REGION 14..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 244 AA; 28109 MW; 62630694D7BA2608 CRC64;
MFLLNSLSRI TRGNRSKRHQ NLSDASSSSG SFSKKSSTSQ LVRTGSPSVE PTALYLQQPF
VRTHLVKGNF STIVSLPRFV DLDEWVALNV YELFTYLNHF YDVFATFCTV KTCPVMSAAA
NFDYTWLDNN RKPVHLPAPQ YIEYVLAWIE NRLHDQNVFP TKAGLPFPSN FLVIVKAIYK
QMFRIFAHMY YAHYAEILHL SLEAHWNSFF AHFIAFGKEF QLLDKRDTAP LKDLIVVLEN
QGNI
