SPC42_YEAST
ID SPC42_YEAST Reviewed; 363 AA.
AC P36094; D6VXP4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Spindle pole body component SPC42;
GN Name=SPC42; OrderedLocusNames=YKL042W; ORFNames=YKL255;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154189; DOI=10.1002/yea.320091212;
RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome
RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a
RT new gene encoding a putative histone and seven new open reading frames.";
RL Yeast 9:1379-1384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=8603920; DOI=10.1083/jcb.132.5.887;
RA Donaldson A.D., Kilmartin J.V.;
RT "Spc42p: a phosphorylated component of the S. cerevisiae spindle pole body
RT (SPD) with an essential function during SPB duplication.";
RL J. Cell Biol. 132:887-901(1996).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SPC110 COMPLEX.
RX PubMed=10339566; DOI=10.1073/pnas.96.11.6205;
RA Elliott S., Knop M., Schlenstedt G., Schiebel E.;
RT "Spc29p is a component of the Spc110p subcomplex and is essential for
RT spindle pole body duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6205-6210(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-217, AND
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-217; SER-284 AND
RP SER-329, 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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 65-138.
RX PubMed=18850724; DOI=10.1021/bi801378z;
RA Zizlsperger N., Malashkevich V.N., Pillay S., Keating A.E.;
RT "Analysis of coiled-coil interactions between core proteins of the spindle
RT pole body.";
RL Biochemistry 47:11858-11868(2008).
CC -!- FUNCTION: Forms a polymeric layer at the periphery of the spindle pole
CC body (SPB) central plaque which has an essential function during SPB
CC duplication and may facilitate attachment of the SPB to the nuclear
CC membrane. {ECO:0000269|PubMed:10339566}.
CC -!- SUBUNIT: Component of the SPC110 complex containing at least CMD1,
CC SPC29, SPC42 and SCP110. {ECO:0000269|PubMed:10339566}.
CC -!- INTERACTION:
CC P36094; P53865: CNM67; NbExp=3; IntAct=EBI-17777, EBI-29172;
CC P36094; P40457: MLP2; NbExp=3; IntAct=EBI-17777, EBI-25261;
CC P36094; P32908: SMC1; NbExp=3; IntAct=EBI-17777, EBI-17402;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10339566}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:10339566}.
CC -!- SIMILARITY: Belongs to the SPC42 family. {ECO:0000305}.
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DR EMBL; X71621; CAA50630.1; -; Genomic_DNA.
DR EMBL; Z28042; CAA81877.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09114.1; -; Genomic_DNA.
DR PIR; S37863; S37863.
DR RefSeq; NP_012882.3; NM_001179608.3.
DR PDB; 2Q6Q; X-ray; 1.97 A; A/B=65-138.
DR PDB; 6OD2; X-ray; 2.44 A; A=246-298.
DR PDB; 6OEC; X-ray; 2.51 A; A/B/C/D/E/F/G/H/I/J/K/L=181-204.
DR PDB; 6OEI; X-ray; 2.58 A; A=11-130.
DR PDBsum; 2Q6Q; -.
DR PDBsum; 6OD2; -.
DR PDBsum; 6OEC; -.
DR PDBsum; 6OEI; -.
DR AlphaFoldDB; P36094; -.
DR SMR; P36094; -.
DR BioGRID; 34090; 321.
DR ComplexPortal; CPX-1419; Spindle pole body central plaque complex.
DR ComplexPortal; CPX-1420; Spindle pole body intermediate layer 2 complex.
DR DIP; DIP-2446N; -.
DR IntAct; P36094; 32.
DR MINT; P36094; -.
DR STRING; 4932.YKL042W; -.
DR iPTMnet; P36094; -.
DR MaxQB; P36094; -.
DR PaxDb; P36094; -.
DR PRIDE; P36094; -.
DR EnsemblFungi; YKL042W_mRNA; YKL042W; YKL042W.
DR GeneID; 853824; -.
DR KEGG; sce:YKL042W; -.
DR SGD; S000001525; SPC42.
DR VEuPathDB; FungiDB:YKL042W; -.
DR eggNOG; ENOG502RYX7; Eukaryota.
DR HOGENOM; CLU_056211_1_0_1; -.
DR InParanoid; P36094; -.
DR OMA; HNHATHR; -.
DR BioCyc; YEAST:G3O-31843-MON; -.
DR EvolutionaryTrace; P36094; -.
DR PRO; PR:P36094; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36094; protein.
DR GO; GO:0005823; C:central plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005821; C:intermediate layer of spindle pole body; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR InterPro; IPR021611; Spc42.
DR Pfam; PF11544; Spc42p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..363
FT /note="Spindle pole body component SPC42"
FT /id="PRO_0000072109"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..137
FT /evidence="ECO:0000255"
FT COILED 249..298
FT /evidence="ECO:0000255"
FT COMPBIAS 168..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 68..124
FT /evidence="ECO:0007829|PDB:2Q6Q"
FT HELIX 183..201
FT /evidence="ECO:0007829|PDB:6OEC"
SQ SEQUENCE 363 AA; 42271 MW; E3B56573FF516CE2 CRC64;
MNGSPTPKRY SSKSSRLYDD YYNIPYQYSN PTPMNRDYND VGSRINADKL VPEEYKRNTE
FINKAVQQNK ELNFKLREKQ NEIFELKKIA ETLRSKLEKY VDITKKLEDQ NLNLQIKISD
LEKKLSDANS TFKEMRFPKV KDPMVDDDPV SENYDQINVP KHRAPDATGN PRTTNKVSNT
SDQDSRLKAI ERTLSVLTNY VMRSEDGNND RMSPLPSPLN TILPINNRLN FQEPKRYNPT
VKVNPSDDDI MMYESAELKR VEEEIEELKR KILVRKKHDL RKLSLNNQLQ ELQSMMDGDD
NIKLDNVSKH NHATHRHSSQ SSRDYSPSSD ACLECSNDLY EKNRVKPENN MSETFATPTP
NNR
