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Protein

Protein STU2

Gene

STU2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in anaphase. Has microtubule polymerase activity by accelerating microtubule growth and inhibiting catastrophe. The polymerase activity is proposed to involve a tethering mechanism at the microtubule plus end: a curved, longitudinally microtubule lattice-associated tubulin heterodimer (that cannot be incorporated into the microtubule lattice) is bound via one TOG domain while the other TOG domain binds to an unpolymerized tubulin heterodimer leading to lateral association of these tubulin heterdimers; polymerization-induced straightening of the tubulin heterodimer releases the polymerase (PubMed:11309422, PubMed:25172511, PubMed:16567500, PubMed:25097237). Is involved in regulation of kinetochore-microtubule attachments in a tension-dependent manner involving its association with the NDC80 complex; the function may be independent of its microtubule polymerase activity. Can either stabilize or destabilize kinetochore attachments, depending on the level of kinetochore tension and whether the microtubule tip is assembling or disassembling (PubMed:27156448).1 Publication4 Publications

GO - Molecular functioni

  • microtubule binding Source: SGD
  • microtubule plus-end binding Source: GO_Central
  • structural constituent of cytoskeleton Source: SGD

GO - Biological processi

  • establishment or maintenance of microtubule cytoskeleton polarity Source: GO_Central
  • microtubule nucleation Source: SGD
  • mitotic spindle organization in nucleus Source: SGD
  • spindle organization Source: GO_Central
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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR045C.
SGDiS000004035. STU2.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: SGD
  • condensed nuclear chromosome kinetochore Source: SGD
  • kinetochore Source: SGD
  • spindle microtubule Source: SGD
  • spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23W → A: Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. 2 Publications1
Mutagenesisi69V → D: Impairs polymerase activity under microtubule stress. 1 Publication1
Mutagenesisi116R → A: Decreases interaction with tubulin heterodimer. 1 Publication1
Mutagenesisi151K → A: Disrupts interaction with tubulin heterodimer. 1 Publication1
Mutagenesisi200R → A: No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. 2 Publications1
Mutagenesisi341W → A: Disrupts interaction with tubulin heterodimer. Impairs polymerase activity under microtubule stress. 2 Publications1
Mutagenesisi519R → A: Disrupts interaction with tubulin heterodimer. No effect on polymerase activity under normal conditions but impairs polymerase activity under microtubule stress. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000722951 – 888Protein STU2Add BLAST888

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineCombined sources1
Modified residuei277PhosphoserineCombined sources1
Modified residuei813PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46675.
PRIDEiP46675.
TopDownProteomicsiP46675.

PTM databases

iPTMnetiP46675.

Interactioni

Subunit structurei

Binds to microtubules. Homodimer; each monomer can bind via its TOG domains to two alpha/beta-tubulin heterodimers. Interacts with SPC72. Associates with the NDC80 complex.5 Publications

GO - Molecular functioni

  • microtubule binding Source: SGD
  • microtubule plus-end binding Source: GO_Central

Protein-protein interaction databases

BioGridi31320. 118 interactors.
DIPiDIP-2462N.
IntActiP46675. 45 interactors.
MINTiMINT-501107.

Structurei

Secondary structure

1888
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 17Combined sources4
Helixi23 – 38Combined sources16
Helixi58 – 63Combined sources6
Helixi69 – 83Combined sources15
Helixi93 – 110Combined sources18
Helixi117 – 132Combined sources16
Beta strandi134 – 137Combined sources4
Helixi138 – 144Combined sources7
Helixi145 – 149Combined sources5
Helixi153 – 170Combined sources18
Turni171 – 174Combined sources4
Helixi177 – 184Combined sources8
Helixi185 – 187Combined sources3
Helixi188 – 192Combined sources5
Helixi197 – 211Combined sources15
Helixi231 – 241Combined sources11
Helixi256 – 268Combined sources13
Helixi325 – 327Combined sources3
Helixi332 – 336Combined sources5
Helixi341 – 354Combined sources14
Helixi356 – 358Combined sources3
Helixi370 – 382Combined sources13
Helixi386 – 403Combined sources18
Turni405 – 407Combined sources3
Helixi410 – 422Combined sources13
Helixi423 – 425Combined sources3
Helixi429 – 445Combined sources17
Helixi456 – 465Combined sources10
Helixi471 – 487Combined sources17
Helixi493 – 499Combined sources7
Turni500 – 502Combined sources3
Helixi503 – 511Combined sources9
Helixi516 – 533Combined sources18
Helixi536 – 538Combined sources3
Helixi539 – 544Combined sources6
Helixi547 – 558Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QK1X-ray1.70A317-560[»]
4FFBX-ray2.88C1-272[»]
4U3JX-ray2.81C318-560[»]
ProteinModelPortaliP46675.
SMRiP46675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati51 – 88HEAT 1Sequence analysisAdd BLAST38
Repeati175 – 216HEAT 2Sequence analysisAdd BLAST42
Repeati411 – 448HEAT 3Sequence analysisAdd BLAST38
Repeati453 – 490HEAT 4Sequence analysisAdd BLAST38
Repeati503 – 541HEAT 5PROSITE-ProRule annotationAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 280TOG 11 PublicationAdd BLAST273
Regioni326 – 550TOG 11 PublicationAdd BLAST225

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili654 – 762Sequence analysisAdd BLAST109

Domaini

The coiled coil domain mediates homodimerization.1 Publication
The TOG (tumor overexpressed gene) domains are composed of six (for the most part non-canonical) HEAT repeats each. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. Two sets of TOG domains may wrap around a single free tubulin heterodimer accompanied by a open-to-closed conformational change of the STU2 homodimer. Both, TOG 1 and TOG 2 bind curved alpha/beta-tubulin with comparable affinity; the two TOG domains bind noncooperatively to two tubulin heterodimers. Free unpolymerized tubulin-binding is predominantly mediated by TOG 1, association with the microtubules plus ends is mediated by TOG 2 in cooperation with a C-terminal basic domain.2 Publications1 Publication

Sequence similaritiesi

Belongs to the TOG/XMAP215 family.Curated
Contains 5 HEAT repeats.Sequence analysis

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00390000014757.
HOGENOMiHOG000216643.
InParanoidiP46675.
KOiK16803.
OMAiQIRMECT.
OrthoDBiEOG092C0GZL.

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

        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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QK1X-ray1.70A317-560[»]
4FFBX-ray2.88C1-272[»]
4U3JX-ray2.81C318-560[»]
ProteinModelPortaliP46675.
SMRiP46675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31320. 118 interactors.
DIPiDIP-2462N.
IntActiP46675. 45 interactors.
MINTiMINT-501107.

PTM databases

iPTMnetiP46675.

Proteomic databases

MaxQBiP46675.
PRIDEiP46675.
TopDownProteomicsiP46675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR045C.
SGDiS000004035. STU2.

Phylogenomic databases

GeneTreeiENSGT00390000014757.
HOGENOMiHOG000216643.
InParanoidiP46675.
KOiK16803.
OMAiQIRMECT.
OrthoDBiEOG092C0GZL.

Enzyme and pathway databases

BioCyciYEAST:G3O-32201-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP46675.
PROiP46675.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.