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P46675

- STU2_YEAST

UniProt

P46675 - STU2_YEAST

Protein

Protein STU2

Gene

STU2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body.

    GO - Molecular functioni

    1. microtubule binding Source: SGD
    2. structural constituent of cytoskeleton Source: SGD

    GO - Biological processi

    1. microtubule nucleation Source: SGD
    2. mitotic spindle organization in nucleus Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32201-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein STU2
    Alternative name(s):
    Suppressor of tubulin 2
    Gene namesi
    Name:STU2
    Ordered Locus Names:YLR045C
    ORF Names:L2108
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR045c.
    SGDiS000004035. STU2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body. Cytoplasmcytoskeletonspindle
    Note: Localizes primarily to the spindle pole body (SPB) and to a lesser extent along spindle microtubules.

    GO - Cellular componenti

    1. cell cortex Source: SGD
    2. condensed nuclear chromosome kinetochore Source: SGD
    3. kinetochore Source: SGD
    4. spindle microtubule Source: SGD
    5. spindle pole body Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 888888Protein STU2PRO_0000072295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphoserine1 Publication
    Modified residuei813 – 8131Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP46675.
    PaxDbiP46675.
    PeptideAtlasiP46675.

    Expressioni

    Gene expression databases

    GenevestigatoriP46675.

    Interactioni

    Subunit structurei

    Binds to microtubules. Interacts with SPC72.1 Publication

    Protein-protein interaction databases

    BioGridi31320. 113 interactions.
    DIPiDIP-2462N.
    IntActiP46675. 44 interactions.
    MINTiMINT-501107.
    STRINGi4932.YLR045C.

    Structurei

    Secondary structure

    1
    888
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 174
    Helixi23 – 3816
    Helixi58 – 636
    Helixi69 – 8315
    Helixi93 – 11018
    Helixi117 – 13216
    Beta strandi134 – 1374
    Helixi138 – 1447
    Helixi145 – 1495
    Helixi153 – 17018
    Turni171 – 1744
    Helixi177 – 1848
    Helixi185 – 1873
    Helixi188 – 1925
    Helixi197 – 21115
    Helixi231 – 24111
    Helixi256 – 26813
    Helixi325 – 3273
    Helixi332 – 3365
    Helixi341 – 35414
    Helixi356 – 3583
    Helixi370 – 38213
    Helixi386 – 40318
    Turni405 – 4073
    Helixi410 – 42213
    Helixi423 – 4253
    Helixi429 – 44517
    Helixi456 – 46510
    Helixi471 – 48717
    Helixi493 – 4997
    Turni500 – 5023
    Helixi503 – 5119
    Helixi516 – 53318
    Helixi536 – 5383
    Helixi539 – 5446
    Helixi547 – 55812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QK1X-ray1.70A317-560[»]
    4FFBX-ray2.88C1-272[»]
    ProteinModelPortaliP46675.
    SMRiP46675. Positions 11-272, 317-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46675.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati453 – 49038HEAT 1Add
    BLAST
    Repeati498 – 53538HEAT 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the TOG/XMAP215 family.Curated
    Contains 2 HEAT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG253097.
    GeneTreeiENSGT00390000014757.
    HOGENOMiHOG000216643.
    KOiK16803.
    OMAiPQIRMEC.
    OrthoDBiEOG7PK97G.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR021133. HEAT_type_2.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50077. HEAT_REPEAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46675-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGEEEVDYT TLPLEERLTY KLWKARLEAY KELNQLFRNS VGDISRDDNI    50
    QIYWRDPTLF AQYITDSNVV AQEQAIVALN SLIDAFASSS LKNAHNITLI 100
    STWTPLLVEK GLTSSRATTK TQSMSCILSL CGLDTSITQS VELVIPFFEK 150
    KLPKLIAAAA NCVYELMAAF GLTNVNVQTF LPELLKHVPQ LAGHGDRNVR 200
    SQTMNLIVEI YKVTGNNSDL LEEILFKKLK PIQVKDLHKL FAKVGDEPSS 250
    SKMLFEWEKR ELEKKRSQEE EARKRKSILS NDEGEYQIDK DGDTLMGMET 300
    DMPPSKQQSG VQIDTFSMLP EETILDKLPK DFQERITSSK WKDRVEALEE 350
    FWDSVLSQTK KLKSTSQNYS NLLGIYGHII QKDANIQAVA LAAQSVELIC 400
    DKLKTPGFSK DYVSLVFTPL LDRTKEKKPS VIEAIRKALL TICKYYDPLA 450
    SSGRNEDMLK DILEHMKHKT PQIRMECTQL FNASMKEEKD GYSTLQRYLK 500
    DEVVPIVIQI VNDTQPAIRT IGFESFAILI KIFGMNTFVK TLEHLDNLKR 550
    KKIEETVKTL PNFSIASGST HSTIETNKQT GPMENKFLLK KSSVLPSKRV 600
    ASSPLRNDNK SKVNPIGSVA SASKPSMVAA NNKSRVLLTS KSLATPKNVV 650
    ANSTDKNEKL IEEYKYRLQK LQNDEMIWTK ERQSLLEKMN NTENYKIEMI 700
    KENEMLREQL KEAQSKLNEK NIQLRSKEID VNKLSDRVLS LENELRNMEI 750
    ELDRNKKRND TNLQSMGTIS SYSIPSSTVS SNYGVKSLSS ALPFKEEEDV 800
    RRKEDVNYER RSSESIGDLP HRVNSLNIRP YRKNGTGVSS VSDDLDIDFN 850
    DSFASEESYK RAAAVTSTLK ARIEKMKAKS RREGTTRT 888
    Length:888
    Mass (Da):100,918
    Last modified:November 1, 1995 - v1
    Checksum:i7A49C3702E21C7BF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35247 Genomic DNA. Translation: AAA79057.1.
    X94607 Genomic DNA. Translation: CAA64292.1.
    Z73217 Genomic DNA. Translation: CAA97574.1.
    BK006945 Genomic DNA. Translation: DAA09363.1.
    PIRiS61619.
    RefSeqiNP_013146.1. NM_001181932.1.

    Genome annotation databases

    EnsemblFungiiYLR045C; YLR045C; YLR045C.
    GeneIDi850734.
    KEGGisce:YLR045C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35247 Genomic DNA. Translation: AAA79057.1 .
    X94607 Genomic DNA. Translation: CAA64292.1 .
    Z73217 Genomic DNA. Translation: CAA97574.1 .
    BK006945 Genomic DNA. Translation: DAA09363.1 .
    PIRi S61619.
    RefSeqi NP_013146.1. NM_001181932.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QK1 X-ray 1.70 A 317-560 [» ]
    4FFB X-ray 2.88 C 1-272 [» ]
    ProteinModelPortali P46675.
    SMRi P46675. Positions 11-272, 317-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31320. 113 interactions.
    DIPi DIP-2462N.
    IntActi P46675. 44 interactions.
    MINTi MINT-501107.
    STRINGi 4932.YLR045C.

    Proteomic databases

    MaxQBi P46675.
    PaxDbi P46675.
    PeptideAtlasi P46675.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR045C ; YLR045C ; YLR045C .
    GeneIDi 850734.
    KEGGi sce:YLR045C.

    Organism-specific databases

    CYGDi YLR045c.
    SGDi S000004035. STU2.

    Phylogenomic databases

    eggNOGi NOG253097.
    GeneTreei ENSGT00390000014757.
    HOGENOMi HOG000216643.
    KOi K16803.
    OMAi PQIRMEC.
    OrthoDBi EOG7PK97G.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32201-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P46675.
    NextBioi 966834.
    PROi P46675.

    Gene expression databases

    Genevestigatori P46675.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR021133. HEAT_type_2.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50077. HEAT_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body."
      Wang P.J., Huffaker T.C.
      J. Cell Biol. 139:1271-1280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CUY696.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly."
      Chen X.P., Yin H., Huffaker T.C.
      J. Cell Biol. 141:1169-1179(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPC72.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-813, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTU2_YEAST
    AccessioniPrimary (citable) accession number: P46675
    Secondary accession number(s): D6VY47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mutations in STU2 suppress a cold-sensitive mutation in TUB2.
    Present with 1660 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3