SP110_YEAST
ID SP110_YEAST Reviewed; 944 AA.
AC P32380; D6VSY5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Spindle pole body component 110;
DE AltName: Full=Extragenic suppressor of CMD1-1 mutant protein 1;
DE AltName: Full=Nuclear filament-related protein 1;
DE AltName: Full=Spindle pole body spacer protein SPC110;
GN Name=SPC110; Synonyms=NUF1, XCM1; OrderedLocusNames=YDR356W;
GN ORFNames=D9476.3;
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], SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1541631; DOI=10.1083/jcb.116.6.1319;
RA Mirzayan C., Copeland C.S., Snyder M.;
RT "The NUF1 gene encodes an essential coiled-coil related protein that is a
RT potential component of the yeast nucleoskeleton.";
RL J. Cell Biol. 116:1319-1332(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=7503995; DOI=10.1083/jcb.123.5.1175;
RA Kilmartin J.V., Dyos S.L., Kershaw D., Finch J.T.;
RT "A spacer protein in the Saccharomyces cerevisiae spindle poly body whose
RT transcript is cell cycle-regulated.";
RL J. Cell Biol. 123:1175-1184(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INTERACTION WITH CMD1, AND DOMAIN.
RX PubMed=8247006; DOI=10.1128/mcb.13.12.7913-7924.1993;
RA Geiser J.R., Sundberg H.A., Chang B.H., Muller E.G., Davis T.N.;
RT "The essential mitotic target of calmodulin is the 110-kilodalton component
RT of the spindle pole body in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:7913-7924(1993).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPC97 AND SPC98.
RX PubMed=9384578; DOI=10.1093/emboj/16.23.6985;
RA Knop M., Schiebel E.;
RT "Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to
RT the spindle pole body via their interaction with Spc110p.";
RL EMBO J. 16:6985-6995(1997).
RN [7]
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 [8]
RP PHOSPHORYLATION AT SER-60; THR-64 AND THR-68, AND FUNCTION.
RX PubMed=11278681; DOI=10.1074/jbc.m010461200;
RA Friedman D.B., Kern J.W., Huneycutt B.J., Vinh D.B., Crawford D.K.,
RA Steiner E., Scheiltz D., Yates J. III, Resing K.A., Ahn N.G., Winey M.,
RA Davis T.N.;
RT "Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-
RT terminal domain.";
RL J. Biol. Chem. 276:17958-17967(2001).
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 SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15872084; DOI=10.1091/mbc.e05-03-0214;
RA Muller E.G., Snydsman B.E., Novik I., Hailey D.W., Gestaut D.R.,
RA Niemann C.A., O'Toole E.T., Giddings T.H. Jr., Sundin B.A., Davis T.N.;
RT "The organization of the core proteins of the yeast spindle pole body.";
RL Mol. Biol. Cell 16:3341-3352(2005).
RN [11]
RP SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-91.
RX PubMed=17213332; DOI=10.1242/jcs.03342;
RA Huisman S.M., Smeets M.F., Segal M.;
RT "Phosphorylation of Spc110p by Cdc28p-Clb5p kinase contributes to correct
RT spindle morphogenesis in S. cerevisiae.";
RL J. Cell Sci. 120:435-446(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-529, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-60 AND SER-80, 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: Component of the spindle pole body (SPB) required for the
CC proper execution of spindle pole body (SPB) duplication. Potential role
CC in cross-linking filaments or anchoring other molecules. It is
CC essential for growth. {ECO:0000269|PubMed:10339566,
CC ECO:0000269|PubMed:11278681, ECO:0000269|PubMed:1541631,
CC ECO:0000269|PubMed:17213332, ECO:0000269|PubMed:7503995,
CC ECO:0000269|PubMed:9384578}.
CC -!- SUBUNIT: Homodimer. Component of the SPC110 complex containing at least
CC CMD1, SPC29 and SCP110. Interacts with SPC97 and SPC98.
CC {ECO:0000269|PubMed:10339566, ECO:0000269|PubMed:15872084,
CC ECO:0000269|PubMed:8247006, ECO:0000269|PubMed:9384578}.
CC -!- INTERACTION:
CC P32380; P06787: CMD1; NbExp=5; IntAct=EBI-12369, EBI-3976;
CC P32380; P40457: MLP2; NbExp=3; IntAct=EBI-12369, EBI-25261;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body. Note=Tightly associated with the
CC nucleus. It is present in a granular pattern that excludes the
CC nucleolus.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPC110 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z11582; CAA77668.1; -; Genomic_DNA.
DR EMBL; X73297; CAA51733.1; -; Genomic_DNA.
DR EMBL; U28372; AAB64791.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12195.1; -; Genomic_DNA.
DR PIR; S26710; S26710.
DR RefSeq; NP_010643.3; NM_001180664.3.
DR PDB; 4DS7; X-ray; 2.15 A; E/F/G/H=891-944.
DR PDB; 7M2W; EM; 3.00 A; K/U/X/Y=1-220.
DR PDB; 7M2X; EM; 3.60 A; U=1-220.
DR PDB; 7M2Y; EM; 4.03 A; U=1-220.
DR PDB; 7M3P; X-ray; 2.00 A; A/B=164-207.
DR PDBsum; 4DS7; -.
DR PDBsum; 7M2W; -.
DR PDBsum; 7M2X; -.
DR PDBsum; 7M2Y; -.
DR PDBsum; 7M3P; -.
DR AlphaFoldDB; P32380; -.
DR SMR; P32380; -.
DR BioGRID; 32412; 304.
DR ComplexPortal; CPX-1419; Spindle pole body central plaque complex.
DR DIP; DIP-702N; -.
DR IntAct; P32380; 31.
DR MINT; P32380; -.
DR STRING; 4932.YDR356W; -.
DR iPTMnet; P32380; -.
DR MaxQB; P32380; -.
DR PaxDb; P32380; -.
DR PRIDE; P32380; -.
DR EnsemblFungi; YDR356W_mRNA; YDR356W; YDR356W.
DR GeneID; 851957; -.
DR KEGG; sce:YDR356W; -.
DR SGD; S000002764; SPC110.
DR VEuPathDB; FungiDB:YDR356W; -.
DR eggNOG; ENOG502QUTQ; Eukaryota.
DR HOGENOM; CLU_329279_0_0_1; -.
DR InParanoid; P32380; -.
DR OMA; EISMYQE; -.
DR BioCyc; YEAST:G3O-29907-MON; -.
DR PRO; PR:P32380; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32380; 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:0005822; C:inner plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:SGD.
DR GO; GO:0110120; P:gamma-tubulin complex localization to nuclear side of mitotic spindle pole body; IDA:SGD.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:SGD.
DR GO; GO:1902440; P:protein localization to mitotic spindle pole body; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR InterPro; IPR040593; Spc110_C.
DR Pfam; PF18520; Spc110_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..944
FT /note="Spindle pole body component 110"
FT /id="PRO_0000057993"
FT REGION 23..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..927
FT /note="Calmodulin-binding"
FT COILED 164..791
FT MOTIF 54..59
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 726..731
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 742..747
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 60
FT /note="Phosphoserine; by MPS1"
FT /evidence="ECO:0000269|PubMed:11278681,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphothreonine; by MPS1"
FT /evidence="ECO:0000269|PubMed:11278681"
FT MOD_RES 68
FT /note="Phosphothreonine; by MPS1"
FT /evidence="ECO:0000269|PubMed:11278681"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 91
FT /note="S->A: Leads to a mild increase in the proportion of
FT preanaphase spindles at the expense of elongated spindles."
FT /evidence="ECO:0000269|PubMed:17213332"
FT HELIX 120..141
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 164..203
FT /evidence="ECO:0007829|PDB:7M3P"
FT HELIX 901..933
FT /evidence="ECO:0007829|PDB:4DS7"
SQ SEQUENCE 944 AA; 111782 MW; 04FAA074BB8A0BC8 CRC64;
MDEASHLPNG SLKNMEFTPV GFIKSKRNTT QTQVVSPTKV PNANNGDENE GPVKKRQRRS
IDDTIDSTRL FSEASQFDDS FPEIKANIPP SPRSGNVDKS RKRNLIDDLK KDVPMSQPLK
EQEVREHQMK KERFDRALES KLLGKRHITY ANSDISNKEL YINEIKSLKH EIKELRKEKN
DTLNNYDTLE EETDDLKNRL QALEKELDAK NKIVNSRKVD DHSGCIEERE QMERKLAELE
RKLKTVKDQV LELENNSDVQ SLKLRSKEDE LKNLMNELNE LKSNAEEKDT QLEFKKNELR
KRTNELNELK IKSDEMDLQL KQKQNESKRL KDELNELETK FSENGSQSSA KENELKMLKN
KIAELEEEIS TKNSQLIAKE GKLASLMAQL TQLESKLNQR DSQLGSREEE LKKTNDKLQK
DIRIAREETV SKDERIIDLQ KKVKQLENDL FVIKKTHSES KTITDNELES KDKLIKILEN
DLKVAQEKYS KMEKELKERE FNYKISESKL EDEKTTLNEK ISNLAAENSQ LKNKIEDNST
ATHHMKENYE KQLESLRKDI EEYKESAKDS EDKIEELKIR IAENSAKVSE KRSKDIKQKD
EQISDLTQNL KLQEDEISSL KSIIDRYKKD FNQLKSEQSN IQHDLNLQIL NLENKLIESE
DELKSLRDSQ KIEIENWKRK YNNLSLENDR LLTEKESASD KEREISILNR KLDEMDKEKW
NLQESKEKYK RELQKVITAN DRLRREKEEL NENSNNIRIM EDKMTRIKKN YLSEITSLQE
ENRRLEERLI LNERRKDNDS TMQLNDIISY YKLKYHSEVR HNNDLKVIND YLNKVLALGT
RRLRLDTRKG EHSLNISLPD DDELDRDYYN SHVYTRYHDY EYPLRFNLNR RGPYFERRLS
FKTVALLVLA CVRMKRIAFY RRSDDNRLRI LRDRIESSSG RISW
