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P46675

- STU2_YEAST

UniProt

P46675 - STU2_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 174Combined sources
Helixi23 – 3816Combined sources
Helixi58 – 636Combined sources
Helixi69 – 8315Combined sources
Helixi93 – 11018Combined sources
Helixi117 – 13216Combined sources
Beta strandi134 – 1374Combined sources
Helixi138 – 1447Combined sources
Helixi145 – 1495Combined sources
Helixi153 – 17018Combined sources
Turni171 – 1744Combined sources
Helixi177 – 1848Combined sources
Helixi185 – 1873Combined sources
Helixi188 – 1925Combined sources
Helixi197 – 21115Combined sources
Helixi231 – 24111Combined sources
Helixi256 – 26813Combined sources
Helixi325 – 3273Combined sources
Helixi332 – 3365Combined sources
Helixi341 – 35414Combined sources
Helixi356 – 3583Combined sources
Helixi370 – 38213Combined sources
Helixi386 – 40318Combined sources
Turni405 – 4073Combined sources
Helixi410 – 42213Combined sources
Helixi423 – 4253Combined sources
Helixi429 – 44517Combined sources
Helixi456 – 46510Combined sources
Helixi471 – 48717Combined sources
Helixi493 – 4997Combined sources
Turni500 – 5023Combined sources
Helixi503 – 5119Combined sources
Helixi516 – 53318Combined sources
Helixi536 – 5383Combined sources
Helixi539 – 5446Combined sources
Helixi547 – 55812Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QK1X-ray1.70A317-560[»]
4FFBX-ray2.88C1-272[»]
4U3JX-ray2.81C318-560[»]
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.
InParanoidiP46675.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGEEEVDYT TLPLEERLTY KLWKARLEAY KELNQLFRNS VGDISRDDNI
60 70 80 90 100
QIYWRDPTLF AQYITDSNVV AQEQAIVALN SLIDAFASSS LKNAHNITLI
110 120 130 140 150
STWTPLLVEK GLTSSRATTK TQSMSCILSL CGLDTSITQS VELVIPFFEK
160 170 180 190 200
KLPKLIAAAA NCVYELMAAF GLTNVNVQTF LPELLKHVPQ LAGHGDRNVR
210 220 230 240 250
SQTMNLIVEI YKVTGNNSDL LEEILFKKLK PIQVKDLHKL FAKVGDEPSS
260 270 280 290 300
SKMLFEWEKR ELEKKRSQEE EARKRKSILS NDEGEYQIDK DGDTLMGMET
310 320 330 340 350
DMPPSKQQSG VQIDTFSMLP EETILDKLPK DFQERITSSK WKDRVEALEE
360 370 380 390 400
FWDSVLSQTK KLKSTSQNYS NLLGIYGHII QKDANIQAVA LAAQSVELIC
410 420 430 440 450
DKLKTPGFSK DYVSLVFTPL LDRTKEKKPS VIEAIRKALL TICKYYDPLA
460 470 480 490 500
SSGRNEDMLK DILEHMKHKT PQIRMECTQL FNASMKEEKD GYSTLQRYLK
510 520 530 540 550
DEVVPIVIQI VNDTQPAIRT IGFESFAILI KIFGMNTFVK TLEHLDNLKR
560 570 580 590 600
KKIEETVKTL PNFSIASGST HSTIETNKQT GPMENKFLLK KSSVLPSKRV
610 620 630 640 650
ASSPLRNDNK SKVNPIGSVA SASKPSMVAA NNKSRVLLTS KSLATPKNVV
660 670 680 690 700
ANSTDKNEKL IEEYKYRLQK LQNDEMIWTK ERQSLLEKMN NTENYKIEMI
710 720 730 740 750
KENEMLREQL KEAQSKLNEK NIQLRSKEID VNKLSDRVLS LENELRNMEI
760 770 780 790 800
ELDRNKKRND TNLQSMGTIS SYSIPSSTVS SNYGVKSLSS ALPFKEEEDV
810 820 830 840 850
RRKEDVNYER RSSESIGDLP HRVNSLNIRP YRKNGTGVSS VSDDLDIDFN
860 870 880
DSFASEESYK RAAAVTSTLK ARIEKMKAKS RREGTTRT
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 [» ]
4U3J X-ray 2.81 C 318-560 [» ]
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.
InParanoidi P46675.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 123 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