STU1_YEAST
ID STU1_YEAST Reviewed; 1513 AA.
AC P38198; D6VPW5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein STU1;
DE AltName: Full=Suppressor of tubulin 1;
GN Name=STU1; OrderedLocusNames=YBL034C; ORFNames=YBL0416;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7806575; DOI=10.1083/jcb.127.6.1973;
RA Pasqualone D., Huffaker T.C.;
RT "STU1, a suppressor of a beta-tubulin mutation, encodes a novel and
RT essential component of the yeast mitotic spindle.";
RL J. Cell Biol. 127:1973-1984(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091857; DOI=10.1002/yea.320100003;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8.8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae reveals four new open reading frames including
RT homologs of animal DNA polymerase alpha-primases and bacterial GTP
RT cyclohydrolase II.";
RL Yeast 10:S13-S24(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [6]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH TUB2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12058056; DOI=10.1091/mbc.01-09-0458;
RA Yin H., You L., Pasqualone D., Kopski K.M., Huffaker T.C.;
RT "Stu1p is physically associated with beta-tubulin and is required for
RT structural integrity of the mitotic spindle.";
RL Mol. Biol. Cell 13:1881-1892(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-997; SER-1018 AND SER-1167,
RP AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1047 AND SER-1167, 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: Microtubule binding protein that promotes the stabilization
CC of dynamic microtubules. Required for separation of the spindle poles
CC during mitotic spindle formation. May cross-link overlapping
CC antiparallel microtubules in the spindle midzone.
CC {ECO:0000269|PubMed:12058056, ECO:0000269|PubMed:7806575}.
CC -!- SUBUNIT: Self-associates. Interacts with microtubules via the TUB2
CC subunit. {ECO:0000269|PubMed:12058056}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasm, cytoskeleton. Chromosome, centromere, kinetochore.
CC Note=Localizes to kinetochore microtubules and to the overlapping
CC microtubules of the spindle midzone.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; Z35655; CAA84714.1; -; Genomic_DNA.
DR EMBL; Z35795; CAA84854.1; -; Genomic_DNA.
DR EMBL; X74738; CAA52760.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07085.1; -; Genomic_DNA.
DR PIR; S45768; S45768.
DR RefSeq; NP_009519.1; NM_001178274.1.
DR PDB; 6COK; X-ray; 1.89 A; A=249-567.
DR PDBsum; 6COK; -.
DR AlphaFoldDB; P38198; -.
DR SMR; P38198; -.
DR BioGRID; 32663; 793.
DR DIP; DIP-2633N; -.
DR IntAct; P38198; 9.
DR MINT; P38198; -.
DR STRING; 4932.YBL034C; -.
DR iPTMnet; P38198; -.
DR MaxQB; P38198; -.
DR PaxDb; P38198; -.
DR PRIDE; P38198; -.
DR EnsemblFungi; YBL034C_mRNA; YBL034C; YBL034C.
DR GeneID; 852246; -.
DR KEGG; sce:YBL034C; -.
DR SGD; S000000130; STU1.
DR VEuPathDB; FungiDB:YBL034C; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_256206_0_0_1; -.
DR InParanoid; P38198; -.
DR OMA; TFWYYYK; -.
DR BioCyc; YEAST:G3O-28936-MON; -.
DR PRO; PR:P38198; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38198; protein.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:SGD.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005827; C:polar microtubule; IDA:SGD.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:SGD.
DR GO; GO:0043515; F:kinetochore binding; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0060172; P:astral microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR Pfam; PF12348; CLASP_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1513
FT /note="Protein STU1"
FT /id="PRO_0000072294"
FT REGION 461..716
FT /note="Interaction with microtubules"
FT REGION 586..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1047
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:6COK"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6COK"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 387..404
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 466..483
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 506..517
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 522..538
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:6COK"
FT HELIX 553..560
FT /evidence="ECO:0007829|PDB:6COK"
SQ SEQUENCE 1513 AA; 174177 MW; E7F64B5A5D03588D CRC64;
MSSFNNETNN NSNTNTHPDD SFPLYTVFKD ESVPIEEKMA LLTRFKGHVK KELVNESSIQ
AYFAALLFIS GHYAYRSYPR LIFLSHSSLC YLIKRVAMQS PVQFNDTLVE QLLNHLIFEL
PNEKKFWLAS IKAIEAIYLV NPSKIQAILA NFLRRPSENQ NGDYLNRIKS TLLTIDELIQ
INEKNNSNHL QLLRFFMLSF TNLLNNNLNE HANDDNNNVI IELIFDIMYK YLKMDDENSQ
DLIDGFINDL EVEKFKQKFI SLAKSQDQHG SQEDKSTLFD EEYEFQLLLA EAKLPQLSNN
LSSKDPAMKK NYESLNQLQQ DLENLLAPFQ SVKETEQNWK LRQSNIIELD NIISGNIPKD
NPEEFVTVIK EVQLIELISR ATSSLRTTLS LTALLFLKRL IHILNDQLPL SILDQIFVIF
KNLLSSTKKI SSQTAFHCLI TLIIDINHFH NKLFQLSFLL INEKTVTPRF CSAILLRSFL
IKFNDSNLSL NNSNTTSPTS KLENNIIYIE EWLKKGISDS QTTVREAMRL TFWYFYKCYP
TNAKRLLSSS FSPQLKKATE LAIPAHLNIN YQVSRVSSTA SASSATSRLY SHSSNNSSRK
TSLLEQKRNY PSYAQPTQSS STSLLNAPAV TAGGSVIASK LSNKLKTNLR STSEYSSKEN
EKRARHHDSM NSVSNSNTKD NNNVTKRKVS APPSSTAATK VSENYTNFDD FPSNQIDLTD
ELSNSYSNPL IKKYMDKNDV SMSSSPISLK GSNKLGEYET LYKKFNDASF PAQIKDALQY
LQKELLLTSQ QSSSAPKFEF PMIMKKLRQI MIKSPNDFKP FLSIEKFTNG VPLNYLIELY
SINSFDYAEI LKNRMNPEKP YELTNLIITI ADLFNFLNAN NCPNDFKLYY MKYKTTFFNY
NFKLLLEIFR NLNIKHDNTL RSGTNDLMPK ISMILFQIYG KEFDYTCYFN LIFEIYKFDN
NRFNKLLADF DIVSTKMKIC HELEKKDANF KVEDIISRES SVSFTPIDNK KSEGDEESDD
AVDENDVKKC MEMTMINPFK NLETDKTLEL KNNVGKRTSS TDSVVIHDDN DKDKKLSEMT
KIVSVYQLDQ PNPAKEEDDI DMENSQKSDL NLSEIFQNSG ENTERKLKDD NEPTVKFSTD
PPKIINEPEK LIGNGNENEK PDLETMSPIK INGDENMGQK QRITVKRERD VALTEQDINS
KKMKLVNNKK SEKMHLLIMD NFPRDSLTVY EISHLLMVDS NGNTLMDFDV YFNHMSKAIN
RIKSGSFTMK HINYLIEPLI TCFQNQKMTD WLTNENGFDE LLDVAIMLLK STDDTPSIPS
KISSKSIILV HCLLVWKKFL NTLSENADDD GVSVRMCFEE VWEQILLMLN KFSDYGNEIY
KLAQEFRDSL MLSHFFKKHS ATRILSMLVT EIQPDTAGVK ETFLIETLWK MLQSPTICQQ
FKKSNISEII QTMSYFIMGT DNTSWNFTSA VVLARCLRVL QTTPDYTEQE TERLFDCLPK
NVFKMIMFIA SNE