Reviewed, UniProtKB/Swiss-Prot P35197 (GCS1_YEAST)

Names and origin

Protein names

Recommended name:
    ADP-ribosylation factor GTPase-activating protein GCS1
      Short name=ARF GAP GCS1

Gene names

Name:	GCS1
Ordered Locus Names:	YDL226C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces. Ref.3 Ref.4 Ref.5
Subcellular location	Cytoplasm. Mitochondrion. Cytoplasm › perinuclear region. Golgi apparatus Probable. Note: Found also in the mitochondria and in the perinuclear region.
Miscellaneous	Present with 9560 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Contains 1 Arf-GAP domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus Mitochondrion
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ER to Golgi vesicle-mediated transport Ref.3 Inferred from genetic interaction. Source: SGD Golgi to plasma membrane protein transport Inferred from mutant phenotype. Source: SGD actin filament reorganization during cell cycle Inferred from genetic interaction. Source: SGD regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro retrograde vesicle-mediated transport, Golgi to ER Ref.3 Inferred from direct assay. Source: SGD
Cellular component	ER-Golgi intermediate compartment Ref.3 Inferred from physical interaction. Source: SGD cytoskeleton Inferred from mutant phenotype. Source: SGD endosome Inferred from direct assay. Source: SGD mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from direct assay. Source: SGD
Molecular function	ARF GTPase activator activity Inferred from direct assay. Source: SGD actin binding Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-7475,EBI-7475
DPM1	P14020	1	EBI-7475,EBI-6101
PIS1	P06197	1	EBI-7475,EBI-13458
SNA3	P14359	1	EBI-7475,EBI-26122
SNC2	P33328	1	EBI-7475,EBI-17512
SSU81	P40073	1	EBI-7475,EBI-18140
TVP38	P36164	1	EBI-7475,EBI-26527
VPS68	Q12016	1	EBI-7475,EBI-29309
YIP1	P53039	1	EBI-7475,EBI-25295
YIP4	P53093	1	EBI-7475,EBI-24124

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	ADP-ribosylation factor GTPase-activating protein GCS1		PRO_0000074224
Regions
	Domain	11 – 127	117	Arf-GAP
	Zinc finger	26 – 49	24	C4-type
Amino acid modifications
	Modified residue	67	1	Phosphothreonine Ref.10
	Modified residue	144	1	Phosphoserine Ref.10
	Modified residue	157	1	Phosphoserine Ref.10 Ref.8 Ref.9
	Modified residue	161	1	Phosphothreonine Ref.10 Ref.8 Ref.9
	Modified residue	168	1	Phosphoserine Ref.10
	Modified residue	170	1	Phosphothreonine Ref.10 Ref.9 Ref.6
	Modified residue	174	1	Phosphoserine Ref.9
	Modified residue	175	1	Phosphoserine Ref.9 Ref.6
	Modified residue	216	1	Phosphoserine Ref.10
	Modified residue	217	1	Phosphothreonine Ref.10
	Modified residue	229	1	Phosphoserine Ref.10
	Modified residue	230	1	Phosphoserine Ref.10
	Modified residue	232	1	Phosphothreonine Ref.10
	Modified residue	260	1	Phosphoserine Ref.10
Natural variations
	Natural variant	27	1	M → I
Experimental info
	Mutagenesis	29	1	C → Y in GCS1-1; severely affect the function.

Sequences

	Sequence		Length	Mass (Da)
	P35197-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 3215525F3EF9CF17	FASTA	352	39,296
	10 20 30 40 50 60 MSDWKVDPDT RRRLLQLQKI GANKKCMDCG APNPQWATPK FGAFICLECA GIHRGLGVHI 70 80 90 100 110 120 SFVRSITMDQ FKPEELLRME KGGNEPLTEW FKSHNIDLSL PQKVKYDNPV AEDYKEKLTC 130 140 150 160 170 180 LCEDRVFEER EHLDFDASKL SATSQTAASA TPGVAQSREG TPLENRRSAT PANSSNGANF 190 200 210 220 230 240 QKEKNEAYFA ELGKKNQSRP DHLPPSQGGK YQGFGSTPAK PPQERSAGSS NTLSLENFQA 250 260 270 280 290 300 DPLGTLSRGW GLFSSAVTKS FEDVNETVIK PHVQQWQSGE LSEETKRAAA QFGQKFQETS 310 320 330 340 350 SYGFQAFSNF TKNFNGNAED SSTAGNTTHT EYQKIDNNDK KNEQDEDKWD DF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A member of a novel family of yeast 'Zn-finger' proteins mediates the transition from stationary phase to cell proliferation." Ireland L.S., Johnston G.C., Drebot M.A., Dhillon N., Demaggio A.J., Hoekstra M.F., Singer R.A. EMBO J. 13:3812-3821(1994) [PubMed: 8070409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function." Poon P.P., Cassel D., Spang A., Rotman M., Pick E., Singer R.A., Johnston G.C. EMBO J. 18:555-564(1999) [PubMed: 9927415] [Abstract] Cited for: FUNCTION.
[4]	"The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network." Poon P.P., Nothwehr S.F., Singer R.A., Johnston G.C. J. Cell Biol. 155:1239-1250(2001) [PubMed: 11756474] [Abstract] Cited for: FUNCTION.
[5]	"The yeast ADP-ribosylation factor GAP, Gcs1p, is involved in maintenance of mitochondrial morphology." Huang C.F., Chen C.C., Tung L., Buu L.M., Lee F.J.-S. J. Cell Sci. 115:275-282(2002) [PubMed: 11839779] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-175, MASS SPECTROMETRY.
[7]	"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].
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND THR-161, MASS SPECTROMETRY.
[9]	"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-157; THR-161; THR-170; SER-174 AND SER-175, MASS SPECTROMETRY.
[10]	"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 THR-67; SER-144; SER-157; THR-161; SER-168; THR-170; SER-216; THR-217; SER-229; SER-230; THR-232 AND SER-260, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L24125 Genomic DNA. Translation: AAA50389.1. Z74274 Genomic DNA. Translation: CAA98805.1.
PIR	S47006.
RefSeq	NP_010055.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:809N.
IntAct	P35197. 22 interactions.
STRING	P35197.
Proteomic databases
PeptideAtlas	P35197.
Genome annotation databases
Ensembl	YDL226C; YDL226C; YDL226C; Saccharomyces cerevisiae. [Genome view]
GeneID	851372.
KEGG	sce:YDL226C.
NMPDR	fig|4932.3.peg.788.
Organism-specific databases
CYGD	YDL226c.
SGD	S000002385. GCS1.
Phylogenomic databases
HOGENOM	P35197.
OMA	CLECAGI
OrthoDB	EOG9FXSQZ
Gene expression databases
ArrayExpress	P35197.
Genevestigator	P35197.
GermOnline	YDL226C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001164. ArfGAP. [Graphical view]
Pfam	PF01412. ArfGap. 1 hit. [Graphical view]
PRINTS	PR00405. REVINTRACTNG.
SMART	SM00105. ArfGap. 1 hit. [Graphical view]
PROSITE	PS50115. ARFGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968495.

Entry information

Entry name

GCS1_YEAST

Accession

Primary (citable) accession number: P35197

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 24, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)