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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
 
 
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