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Protein

GTPase-interacting component 2

Gene

GIC2

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

Required for cell size and shape control, bud site selection, bud emergence, actin cytoskeletal organization, mitotic spindle orientation/positioning, and mating projection formation in response to mating pheromone.

GO - Molecular functioni

  • GTPase activator activity Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • Rho GTPase binding Source: SGD

GO - Biological processi

  • establishment of cell polarity Source: SGD
  • positive regulation of formin-nucleated actin cable assembly Source: SGD
  • regulation of cell shape Source: UniProtKB-KW
  • regulation of exit from mitosis Source: SGD
  • septin ring organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

BioCyciYEAST:G3O-29868-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase-interacting component 2
Gene namesi
Name:GIC2
Ordered Locus Names:YDR309C
ORF Names:D9740.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR309C.
SGDiS000002717. GIC2.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cellular bud neck Source: UniProtKB-SubCell
  • cellular bud tip Source: SGD
  • cytoskeleton Source: UniProtKB-SubCell
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 383383GTPase-interacting component 2PRO_0000212660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei254 – 2541PhosphoserineCombined sources
Modified residuei258 – 2581PhosphoserineCombined sources
Modified residuei337 – 3371PhosphoserineCombined sources
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei367 – 3671PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06648.

PTM databases

iPTMnetiQ06648.

Interactioni

Subunit structurei

Interacts with GTP-bound CDC42.

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC11P324582EBI-7585,EBI-4178
CDC12P324685EBI-7585,EBI-4182
CDC3P324573EBI-7585,EBI-4429

GO - Molecular functioni

  • Rho GTPase binding Source: SGD

Protein-protein interaction databases

BioGridi32362. 72 interactions.
DIPiDIP-2277N.
IntActiQ06648. 25 interactions.
MINTiMINT-558890.

Structurei

3D structure databases

ProteinModelPortaliQ06648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 14714CRIBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi74 – 10229Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the BORG/CEP family.Curated
Contains 1 CRIB domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000066862.
HOGENOMiHOG000000874.
InParanoidiQ06648.
OMAiQHISHAD.
OrthoDBiEOG7D5B1C.

Family and domain databases

InterProiIPR000095. CRIB_dom.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSASITNTG NETMNLPQMR SIWLDEDEEA EKLYGLQAQQ FMGSDDEENL
60 70 80 90 100
GITFINSDKP VLSNKKNIEL PPLSPNSHPS CHHRRSNSNS AKSKESSSSS
110 120 130 140 150
SSANKTNHKK VFLKLNLLKK KLLGAQPDIR GKGISTPFDF QHISHADTRN
160 170 180 190 200
GFQDEQLQEP SSLSTEIKDD YTSSSSKRDS KSLNKAFVTE RIPANRESKL
210 220 230 240 250
ISRSHENKTS RLSVARSISV TSSNYSKNTQ GNNHSINGRV VSTSTMATSI
260 270 280 290 300
FEYSPNASPK QFKNKSHALG HRYTNSTDSS ESSLDFLKNY NFPTLLEDKP
310 320 330 340 350
ILDFLPRSQR SSAYRSLLET PNSNKDSAKA FFPSRQSPLP KRRNSIATPS
360 370 380
PQSKFSYSDS PVNHRKSFDD VLYSFNQLEP LQT
Length:383
Mass (Da):42,852
Last modified:November 1, 1996 - v1
Checksum:iD1BE002BCD48EB03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64745.1.
AY557791 Genomic DNA. Translation: AAS56117.1.
BK006938 Genomic DNA. Translation: DAA12148.1.
PIRiS61195.
RefSeqiNP_010595.1. NM_001180617.1.

Genome annotation databases

EnsemblFungiiYDR309C; YDR309C; YDR309C.
GeneIDi851904.
KEGGisce:YDR309C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64745.1.
AY557791 Genomic DNA. Translation: AAS56117.1.
BK006938 Genomic DNA. Translation: DAA12148.1.
PIRiS61195.
RefSeqiNP_010595.1. NM_001180617.1.

3D structure databases

ProteinModelPortaliQ06648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32362. 72 interactions.
DIPiDIP-2277N.
IntActiQ06648. 25 interactions.
MINTiMINT-558890.

PTM databases

iPTMnetiQ06648.

Proteomic databases

MaxQBiQ06648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR309C; YDR309C; YDR309C.
GeneIDi851904.
KEGGisce:YDR309C.

Organism-specific databases

EuPathDBiFungiDB:YDR309C.
SGDiS000002717. GIC2.

Phylogenomic databases

GeneTreeiENSGT00530000066862.
HOGENOMiHOG000000874.
InParanoidiQ06648.
OMAiQHISHAD.
OrthoDBiEOG7D5B1C.

Enzyme and pathway databases

BioCyciYEAST:G3O-29868-MONOMER.

Miscellaneous databases

PROiQ06648.

Family and domain databases

InterProiIPR000095. CRIB_dom.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae."
    Chen G.C., Kim Y.J., Chan C.S.
    Genes Dev. 11:2958-2971(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast."
    Brown J.L., Jaquenoud M., Gulli M.P., Chant J., Peter M.
    Genes Dev. 11:2972-2982(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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-254; SER-258 AND SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGIC2_YEAST
AccessioniPrimary (citable) accession number: Q06648
Secondary accession number(s): D6VST8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1130 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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