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Q12280 (IQG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras GTPase-activating-like protein IQG1
Alternative name(s):
Cytokinesis protein 1
IQGAP-related protein 1
Gene names
Name:IQG1
Synonyms:CYK1
Ordered Locus Names:YPL242C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis. Seems to be involved in additional tasks during cell division like axial bud-site selection and targeted secretion by recruiting the spatial landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. May be regulated by calcium ions. Ref.4 Ref.5 Ref.6 Ref.13

Subunit structure

Interacts with AFR1, AKR1, activated CDC42, calmodulin (CMD1), myosin MYO1 and its light chain MLC1, BUD4, INN1, SEC3 and TEM1. Ref.1 Ref.6 Ref.7 Ref.8 Ref.13

Subcellular location

Bud neck. Note: Forms a ring at the bud neck in a MLC1-dependent manner, which contracts at the end of cytokinesis. Ref.5 Ref.9 Ref.13

Domain

The calponin homology (CH) domain binds to actin filaments and is required for their recruitment to the bud neck.

The IQ domains serve as interaction surface for the myosin light chain MLC1.

The Ras-GAP domain is required for contraction of the actomyosin ring and is needed for the interaction with TEM1. It probably does not stimulate GTPase activity.

Miscellaneous

Present with 279 molecules/cell in log phase SD medium. Ref.10

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 7 IQ domains.

Contains 1 Ras-GAP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUD4P471364EBI-35351,EBI-3848
MLC1P531417EBI-35351,EBI-10988

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14951495Ras GTPase-activating-like protein IQG1
PRO_0000056652

Regions

Domain108 – 217110CH
Domain447 – 46721IQ 1
Domain538 – 56730IQ 2
Domain568 – 59730IQ 3
Domain599 – 62830IQ 4
Domain629 – 65830IQ 5
Domain687 – 71630IQ 6
Domain717 – 74630IQ 7
Domain860 – 1071212Ras-GAP
Coiled coil759 – 79840 Potential
Compositional bias37 – 7640Ser-rich

Amino acid modifications

Modified residue3541Phosphoserine Ref.11 Ref.12
Modified residue3651Phosphoserine Ref.12

Experimental info

Mutagenesis4571L → P in IQG1-1; causes a defect in cytokinesis at 37 degrees Celsius. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q12280 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C0C7582808154DCC

FASTA1,495172,830
        10         20         30         40         50         60 
MTAYSGSPSK PGNNNSYLNR YVENLGTNVT PPLRPQSSSK INSSLNIASP SHLKTKTSAS 

        70         80         90        100        110        120 
NSSATILSKK VESSVSKLKP SLPNKLVGKY TVDLSNYSKI ELRYYEFLCR VSEVKIWIEA 

       130        140        150        160        170        180 
VIEEALPSEI ELCVGDSLRN GVFLAKLTQR INPDLTTVIF PAGDKLQFKH TQNINAFFGL 

       190        200        210        220        230        240 
VEHVGVPDSF RFELQDLYNK KNIPQVFETL HILISMINKK WPGKTPALTN VSGQISFTKE 

       250        260        270        280        290        300 
EIAACKKAWP RIRDFKSLGT NINTAPASPE EPKEKRSGLI KDFNKFERPN IPVEEILITP 

       310        320        330        340        350        360 
RKNITDANCS DFSNTPSPYN EAPKMSNLDV VVEKRKFTPI EPSLLGPTPS LEYSPIKNKS 

       370        380        390        400        410        420 
LSYYSPTISK YLTYDTEFYT RRSRAREEDL NYYQTFKYSP SHYSPMRRER MTEEQFLEKV 

       430        440        450        460        470        480 
VQLQNICRGV NTRFNLYIQK RLLNLFEQDI LRFQACLRGN KFRVLSSMYL PIRRAKIDVP 

       490        500        510        520        530        540 
HVEAIQSRIK GSRIRYKYDK LKFTLSRFSC TVELLQAYCR SKLLKTTVNT KLNDIEISHY 

       550        560        570        580        590        600 
PLTKLQSYMR ASYVRKKVMS LNTKLNDERE SIMKFSAIIR GNVVRCSEDA ILSAVHDVHK 

       610        620        630        640        650        660 
ENISKLQSLI RGIFTRSCLA SIIYSLGKEN CNIIQLSACI RGNAVRHKVQ SLFAPENNLS 

       670        680        690        700        710        720 
ETVHDLQGLV RGILVRYTLD LVDDIVEYNN LALFQAFSRG ALVRESLDQK SSFYKRNVRS 

       730        740        750        760        770        780 
VIMIQSWIRK SLQRSAYLEL LDCPNPSLWA VKKFVHLLNG TATIEEVQNQ LESCQASLDS 

       790        800        810        820        830        840 
ENMKKERLLK SIRQQLNING VLDKFGLLKD KDHELGISDS TIPKSKYQKY EKLFYMLQVD 

       850        860        870        880        890        900 
PSYWKLLYLK EPEFVAKNVY MTFGTVNQRM NDRERSYFTR FVCEMLQNAI NEAPSIESFL 

       910        920        930        940        950        960 
DNRSQFWQTI LQDFLRRESP EFFSIIVPVL DYLSDPVVDF ESDPYKIYQE IHGFSSPQHC 

       970        980        990       1000       1010       1020 
SPVDDASTKN KFIDNLRCLW HAIEMVAEIY TRKVHTIPVE IRYLCTKIFC YAADKNIEEI 

      1030       1040       1050       1060       1070       1080 
DSLRAISSIL VNVFVSEYLV NREYYGYKDS NVQKNNQKID ILMKSLATVF EIKNFDGFLD 

      1090       1100       1110       1120       1130       1140 
PLNQYANEIK PHIKDVLYNV LVDPEYEQEG DRLIYLDMVS PSPKLELLTE KVLEISGKFE 

      1150       1160       1170       1180       1190       1200 
EYLNEFPEAD ILHDILEKNL DNSSFPRSGR VTLELDASAY RFLVSDDKMR KIYDQVKRAF 

      1210       1220       1230       1240       1250       1260 
VYMMQIEDVD TNLYDLSIST ILPQDEPNFA NFLEQNPKIR DDPMIQKLKP LKYFTLKNVT 

      1270       1280       1290       1300       1310       1320 
LKKIHELEST GTFCSSDNKL QNFLNDIANT IKNPNYAIDY VTQEIYITKE TLTKISEMNH 

      1330       1340       1350       1360       1370       1380 
SLDIELSRLK KHVDHTIKDF QKAKDFSPVH KSKFGNFKNA VKKVQGRERS ELQGMKFKWN 

      1390       1400       1410       1420       1430       1440 
TKQLYERGVL KTIRGEKLAE LTVKVFGSSG PKFPDIIFKI STSDGSRFGI QMIDKRKGPD 

      1450       1460       1470       1480       1490 
KRYSDDVDSF SFKDLIKTQV EPKIETWKLF HSNVVVNNSQ LLHLIVSFFY KRNAL 

« Hide

References

« Hide 'large scale' references
[1]"Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p effects on the actin cytoskeleton."
Osman M.A., Cerione R.A.
J. Cell Biol. 142:443-455(1998) [PubMed: 9679143] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH AFR1; AKR1 AND CDC42.
Strain: CUY30.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast."
Epp J.A., Chant J.
Curr. Biol. 7:921-929(1997) [PubMed: 9382845] [Abstract]
Cited for: FUNCTION.
[5]"Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis."
Lippincott J., Li R.
J. Cell Biol. 140:355-366(1998) [PubMed: 9442111] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"The multiple roles of Cyk1p in the assembly and function of the actomyosin ring in budding yeast."
Shannon K.B., Li R.
Mol. Biol. Cell 10:283-296(1999) [PubMed: 9950677] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CMD1 AND TEM1.
[7]"Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis."
Boyne J.R., Yosuf H.M., Bieganowski P., Brenner C., Price C.
J. Cell Sci. 113:4533-4543(2000) [PubMed: 11082046] [Abstract]
Cited for: INTERACTION WITH MLC1 AND MYO1, MUTAGENESIS OF LEU-457.
[8]"Iqg1p links spatial and secretion landmarks to polarity and cytokinesis."
Osman M.A., Konopka J.B., Cerione R.A.
J. Cell Biol. 159:601-611(2002) [PubMed: 12446742] [Abstract]
Cited for: INTERACTION WITH BUD4 AND SEC3.
[9]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, MASS SPECTROMETRY.
[12]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-365, MASS SPECTROMETRY.
[13]"Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast."
Sanchez-Diaz A., Marchesi V., Murray S., Jones R., Pereira G., Edmondson R., Allen T., Labib K.
Nat. Cell Biol. 10:395-406(2008) [PubMed: 18344988] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH INN1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019644 Genomic DNA. Translation: AAB70827.1.
Z73598 Genomic DNA. Translation: CAA97963.1.
Z67751 Genomic DNA. Translation: CAA91603.1.
BK006949 Genomic DNA. Translation: DAA11195.1.
PIRS61023.
RefSeqNP_015082.1. NM_001184056.1.

3D structure databases

ProteinModelPortalQ12280.
SMRQ12280. Positions 99-258, 1369-1494.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1144N.
IntActQ12280. 12 interactions.
MINTMINT-1578204.
STRINGQ12280.

Proteomic databases

PeptideAtlasQ12280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL242C; YPL242C; YPL242C.
GeneID855834.
KEGGsce:YPL242C.
NMPDRfig|4932.3.peg.6209.

Organism-specific databases

CYGDYPL242c.
SGDS000006163. IQG1.

Phylogenomic databases

eggNOGfuNOG04232.
GeneTreeEFGT00050000002498.
HOGENOMHBG204004.
OMAPSLWAVK.
OrthoDBEOG4XH378.

Gene expression databases

ArrayExpressQ12280.
GenevestigatorQ12280.
GermOnlineYPL242C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001715. CH-domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR001936. RasGAP.
IPR000593. RasGAP_C.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 1 hit.
G3DSA:1.10.506.10. RasGAP. 1 hit.
KOK05767.
PfamPF00307. CH. 1 hit.
PF00612. IQ. 1 hit.
PF00616. RasGAP. 1 hit.
PF03836. RasGAP_C. 1 hit.
[Graphical view]
SMARTSM00033. CH. 1 hit.
SM00015. IQ. 3 hits.
[Graphical view]
SUPFAMSSF47576. Calponin-homology. 1 hit.
SSF48350. Rho_GAP. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS50096. IQ. False negative.
PS00509. RAS_GTPASE_ACTIV_1. False negative.
PS50018. RAS_GTPASE_ACTIV_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio980401.

Entry information

Entry nameIQG1_YEAST
AccessionPrimary (citable) accession number: Q12280
Secondary accession number(s): D6W3C9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families