SPC98_YEAST
ID SPC98_YEAST Reviewed; 846 AA.
AC P53540; D6W157;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Spindle pole body component SPC98;
GN Name=SPC98; OrderedLocusNames=YNL126W; ORFNames=N1222, N1879;
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=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=8670895; DOI=10.1002/j.1460-2075.1996.tb00764.x;
RA Geissler S., Pereira G., Spang A., Knop M., Soues S., Kilmartin J.V.,
RA Schiebel E.;
RT "The spindle pole body component Spc98p interacts with the gamma-tubulin-
RT like Tub4p of Saccharomyces cerevisiae at the sites of microtubule
RT attachment.";
RL EMBO J. 15:3899-3911(1996).
RN [6]
RP INTERACTION WITH SPC72.
RX PubMed=9670012; DOI=10.1093/emboj/17.14.3952;
RA Knop M., Schiebel E.;
RT "Receptors determine the cellular localization of a gamma-tubulin complex
RT and thereby the site of microtubule formation.";
RL EMBO J. 17:3952-3967(1998).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-136, 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).
CC -!- FUNCTION: Involved in microtubule organization by the microtubule
CC organizing center, the spindle pole body (SPB). Probably part of the
CC microtubule attachment site at the SPB.
CC -!- SUBUNIT: Interacts with TUB4, SPC72 and SPC97.
CC {ECO:0000269|PubMed:9670012}.
CC -!- INTERACTION:
CC P53540; P38863: SPC97; NbExp=7; IntAct=EBI-17794, EBI-17786;
CC P53540; P53378: TUB4; NbExp=4; IntAct=EBI-17794, EBI-19013;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body.
CC -!- MISCELLANEOUS: Present with 56 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
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DR EMBL; Z46843; CAA86899.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93378.1; -; Genomic_DNA.
DR EMBL; Z71402; CAA96007.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10423.1; -; Genomic_DNA.
DR PIR; S59262; S59262.
DR RefSeq; NP_014273.1; NM_001182964.1.
DR PDB; 5FLZ; EM; 6.90 A; B=1-846.
DR PDB; 5FM1; EM; 8.00 A; B=1-846.
DR PDB; 7M2W; EM; 3.00 A; F/H=1-846.
DR PDB; 7M2X; EM; 3.60 A; D=1-846.
DR PDB; 7M2Y; EM; 4.03 A; C=1-846.
DR PDB; 7M2Z; EM; 3.70 A; C=1-846.
DR PDBsum; 5FLZ; -.
DR PDBsum; 5FM1; -.
DR PDBsum; 7M2W; -.
DR PDBsum; 7M2X; -.
DR PDBsum; 7M2Y; -.
DR PDBsum; 7M2Z; -.
DR AlphaFoldDB; P53540; -.
DR SMR; P53540; -.
DR BioGRID; 35701; 111.
DR ComplexPortal; CPX-1198; Gamma tubulin small complex.
DR DIP; DIP-938N; -.
DR IntAct; P53540; 14.
DR MINT; P53540; -.
DR STRING; 4932.YNL126W; -.
DR iPTMnet; P53540; -.
DR MaxQB; P53540; -.
DR PaxDb; P53540; -.
DR PRIDE; P53540; -.
DR EnsemblFungi; YNL126W_mRNA; YNL126W; YNL126W.
DR GeneID; 855597; -.
DR KEGG; sce:YNL126W; -.
DR SGD; S000005070; SPC98.
DR VEuPathDB; FungiDB:YNL126W; -.
DR eggNOG; KOG2000; Eukaryota.
DR GeneTree; ENSGT00940000157872; -.
DR HOGENOM; CLU_333507_0_0_1; -.
DR InParanoid; P53540; -.
DR OMA; LWRIKKN; -.
DR BioCyc; YEAST:G3O-33147-MON; -.
DR PRO; PR:P53540; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53540; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IDA:SGD.
DR GO; GO:0005822; C:inner plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0005816; C:spindle pole body; IC:ComplexPortal.
DR GO; GO:0043015; F:gamma-tubulin binding; IMP:SGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IDA:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..846
FT /note="Spindle pole body component SPC98"
FT /id="PRO_0000078123"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 215..241
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 248..274
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 325..352
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 419..434
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 443..466
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 486..500
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 535..539
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 582..615
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 624..655
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 657..668
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 689..693
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 721..736
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 739..741
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 758..792
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 793..797
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 800..831
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 836..844
FT /evidence="ECO:0007829|PDB:7M2W"
SQ SEQUENCE 846 AA; 98227 MW; 803048B05D5E5105 CRC64;
MELEPTLFGI IEALAPQLLS QSHLQTFVSD VVNLLRSSTK SATQLGPLID FYKLQSLDSP
ETTIMWHKIE KFLDALFGIQ NTDDMVKYLS VFQSLLPSNY RAKIVQKSSG LNMENLANHE
HLLSPVRAPS IYTEASFENM DRFSERRSMV SSPNRYVPSS TYSSVTLRQL SNPYYVNTIP
EEDILKYVSY TLLATTSALF PFDHEQIQIP SKIPNFESGL LHLIFEAGLL YQSLGYKVEK
FRMLNISPMK KALIIEISEE LQNYTAFVNN LVSSGTVVSL KSLYREIYEN IIRLRIYCRF
TEHLEELSGD TFLIELNIFK SHGDLTIRKI ATNLFNSMIS LYYEYLMNWL TKGLLRATYG
EFFIAENTDT NGTDDDFIYH IPIEFNQERV PAFIPKELAY KIFMIGKSYI FLEKYCKEVQ
WTNEFSKKYH VLYQSNSYRG ISTNFFEIIN DQYSEIVNHT NQILNQKFHY RDVVFALKNI
LLMGKSDFMD ALIEKANDIL ATPSDSLPNY KLTRVLQEAV QLSSLRHLMN SPRNSSVING
LDARVLDLGH GSVGWDVFTL DYILYPPLSL VLNVNRPFGR KEYLRIFNFL WRFKKNNYFY
QKEMLKSNDI IRSFKKIRGY NPLIRDIINK LSRISILRTQ FQQFNSKMES YYLNCIIEEN
FKEMTRKLQR TENKSQNQFD LIRLNNGTIE LNGILTPKAE VLTKSSSSKP QKHAIEKTLN
IDELESVHNT FLTNILSHKL FATNTSEISV GDYSGQPYPT SLVLLLNSVY EFVKVYCNLN
DIGYEIFIKM NLNDHEASNG LLGKFNTNLK EIVSQYKNFK DRLYIFRADL KNDGDEELFL
LSKSLR
