SP105_YEAST
ID SP105_YEAST Reviewed; 917 AA.
AC P53148; D6VU52;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Spindle pole body component SPC105;
DE AltName: Full=105 kDa spindle pole component protein;
GN Name=SPC105; OrderedLocusNames=YGL093W;
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=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9585415; DOI=10.1083/jcb.141.4.967;
RA Wigge P.A., Jensen O.N., Holmes S., Soues S., Mann M., Kilmartin J.V.;
RT "Analysis of the Saccharomyces spindle pole by matrix-assisted laser
RT desorption/ionization (MALDI) mass spectrometry.";
RL J. Cell Biol. 141:967-977(1998).
RN [5]
RP SUBUNIT, INTERACTION WITH KRE28, AND SUBCELLULAR LOCATION.
RX PubMed=14565975; DOI=10.1091/mbc.e03-06-0419;
RA Nekrasov V.S., Smith M.A., Peak-Chew S., Kilmartin J.V.;
RT "Interactions between centromere complexes in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:4931-4946(2003).
RN [6]
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 [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16715078; DOI=10.1038/ncb1414;
RA Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
RT "Molecular architecture of a kinetochore-microtubule attachment site.";
RL Nat. Cell Biol. 8:581-585(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-356 AND SER-380, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION BY
RP 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 [10]
RP INTERACTION WITH KRE28, AND FUNCTION.
RX PubMed=19893618; DOI=10.1371/journal.pone.0007640;
RA Pagliuca C., Draviam V.M., Marco E., Sorger P.K., De Wulf P.;
RT "Roles for the conserved spc105p/kre28p complex in kinetochore-microtubule
RT binding and the spindle assembly checkpoint.";
RL PLoS ONE 4:E7640-E7640(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-356 AND SER-380, 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: Forms a kinetochore complex with SPC105 which is required for
CC kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and
CC SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule
CC binding and the spindle assembly checkpoint.
CC {ECO:0000269|PubMed:19893618}.
CC -!- SUBUNIT: Component of the SPC105 complex composed of at least SPC105
CC and KRE28. The SPC105 complex interacts with the MIND and NDC80
CC complexes at the centromere. {ECO:0000269|PubMed:14565975,
CC ECO:0000269|PubMed:16715078, ECO:0000269|PubMed:19893618,
CC ECO:0000269|PubMed:9585415}.
CC -!- INTERACTION:
CC P53148; Q04431: KRE28; NbExp=3; IntAct=EBI-23870, EBI-32446;
CC P53148; P40460: NDC80; NbExp=2; IntAct=EBI-23870, EBI-25247;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Chromosome, centromere, kinetochore.
CC Note=Localizes to the nuclear side of the spindle pole body.
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DR EMBL; Z72615; CAA96799.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08013.1; -; Genomic_DNA.
DR PIR; S64100; S64100.
DR RefSeq; NP_011422.1; NM_001180958.1.
DR PDB; 4BL0; X-ray; 1.95 A; C/F=165-183.
DR PDBsum; 4BL0; -.
DR AlphaFoldDB; P53148; -.
DR SMR; P53148; -.
DR BioGRID; 33158; 424.
DR ComplexPortal; CPX-1899; Spc105 complex.
DR DIP; DIP-3019N; -.
DR IntAct; P53148; 10.
DR MINT; P53148; -.
DR STRING; 4932.YGL093W; -.
DR iPTMnet; P53148; -.
DR MaxQB; P53148; -.
DR PaxDb; P53148; -.
DR PRIDE; P53148; -.
DR EnsemblFungi; YGL093W_mRNA; YGL093W; YGL093W.
DR GeneID; 852787; -.
DR KEGG; sce:YGL093W; -.
DR SGD; S000003061; SPC105.
DR VEuPathDB; FungiDB:YGL093W; -.
DR eggNOG; ENOG502S20P; Eukaryota.
DR HOGENOM; CLU_012537_0_0_1; -.
DR InParanoid; P53148; -.
DR OMA; HSFDFVP; -.
DR BioCyc; YEAST:G3O-30593-MON; -.
DR PRO; PR:P53148; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53148; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0031617; C:NMS complex; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0051382; P:kinetochore assembly; IC:ComplexPortal.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR InterPro; IPR040850; Knl1_RWD_C.
DR InterPro; IPR033338; Spc105/Spc7.
DR InterPro; IPR013253; Spc7_domain.
DR PANTHER; PTHR28260; PTHR28260; 2.
DR Pfam; PF18210; Knl1_RWD_C; 1.
DR Pfam; PF08317; Spc7; 1.
DR SMART; SM00787; Spc7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..917
FT /note="Spindle pole body component SPC105"
FT /id="PRO_0000202755"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4BL0"
SQ SEQUENCE 917 AA; 104826 MW; 8B7ED1522916A319 CRC64;
MNVDERSRIG GREKDAGPGK GILKQNQSSQ MTSSFLENPG VRIPTRIITK KEVLDGSNTT
SRINTSNLQS MVKRRVSFAP DVTLHSFTFV PEQNNEIKEP RRRKTSTNSP TKISSQEEPL
VTSTQIDDAR TEEKTAAEED PDTSGMELTE PIVATPDSNK ASQHDPTSME MTEVFPRSIR
QKNPDVEGES IESSQQIDDV EAVREETMEL TAIHNVHDYD SISKDTVEGE PIDLTEYESK
PYVPNSVSRS TGKSSDYSVE RSNDKSDLSK SENKTNSSQP MEITDIFHAD PQNPMSLHSD
NNINNDGNEM ELTQIQTNFD RDNHHIDESP SEKHAFSSNK RRKLDTVSDY AASVTTPVKE
AKDTSGEDND GDLEMMEKMS PITFSDVDNK IGTRSNDVFT IEPGTEDTGM QTATDDEEDG
ENVDDNGNKI VEKTRLPEID KEGQSGIALP TQDYTLREFI NEVGVGFLDT KLIDDLDKKV
NFPLNSFNFV ENQRIDNVFS AFYIDIPILE VEAFRCKELW RSINESKDKF KDFEAQIDKS
HPPLLLQEYF SSDEKMKQLM RDQLQLVKGY SKLEAAMEWY EWRKKQLNGL ELILAENLNT
LKREYEKLNE EVEKVNSIRG KIRKLNEAIK EEIRSLKNLP SDSYKPTLMN RIKIEAFKQE
LMEHSISLSS SNDFTQEMRS LKLAIAKKSN DILTLRSEVA SIDKKIEKRK LFTRFDLPKL
RDTLKILESL TGVRFLKFSK ATLSIAFLQL DDLRVDINLA NFKNNPLSSM KVMNDSNNDD
MSYHLFTMLL KNVEAEHQDS MLSNLFFAMK KWRPLLKYIK LLKLLFPVKI TQTEEEEALL
QFKDYDRRNK TAFFYVISLV SFAQGVFSEN GQIPMKVHIS TQQDYSPSRE VLSDRITHKI
SGVLPSFTKS RIHLEFT
