P39717 (GPB2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit beta 2

Alternative name(s):
Gbeta mimic kelch protein 2

Gene names

Name:	GPB2
Synonyms:	KRH1
Ordered Locus Names:	YAL056W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Beta subunit of a guanine nucleotide-binding protein (G protein). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth. Ref.1 Ref.5 Ref.7
Subunit structure	G proteins are composed of 3 units, alpha, beta and gamma. GPB1 interacts with the alpha subunit GPA2. Ref.1
Subcellular location	Cytoplasm. Mitochondrion Ref.6.
Sequence similarities	Contains 4 Kelch repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Domain	Kelch repeat Repeat
Molecular function	Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ascospore formation Inferred from mutant phenotype. Source: SGD glucose mediated signaling pathway Inferred from mutant phenotype Ref.1. Source: SGD invasive growth in response to glucose limitation Inferred from mutant phenotype Ref.1. Source: SGD negative regulation of Ras protein signal transduction Inferred from genetic interaction. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD pseudohyphal growth Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	mitochondrion Inferred from direct assay Ref.6. Source: SGD plasma membrane Inferred from direct assay. Source: SGD
Molecular function	GTPase activating protein binding Inferred from physical interaction. Source: SGD cAMP-dependent protein kinase inhibitor activity Inferred from genetic interaction Ref.7. Source: SGD signal transducer activity Inferred from physical interaction Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 880	880	Guanine nucleotide-binding protein subunit beta 2		PRO_0000119071
Regions
	Repeat	291 – 339	49	Kelch 1
	Repeat	377 – 425	49	Kelch 2
	Repeat	501 – 552	52	Kelch 3
	Repeat	691 – 738	48	Kelch 4
Amino acid modifications
	Modified residue	24	1	Phosphoserine Ref.8
Natural variations
	Natural variant	215	1	Y → H in strain: Sigma 1278B.
	Natural variant	221	1	L → P in strain: Sigma 1278B.
	Natural variant	552	1	S → R in strain: Sigma 1278B.
	Natural variant	674	1	A → T in strain: Sigma 1278B.
	Natural variant	777	1	P → S in strain: Sigma 1278B.
Experimental info
	Sequence conflict	661	1	V → I in AAC04977. Ref.2
	Sequence conflict	802	1	C → F in AAC04977. Ref.2
	Sequence conflict	814 – 815	2	ED → AA in AAC04977. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39717 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 343627001C52020E	FASTA	880	98,656
	10 20 30 40 50 60 MEISSSPWND GGYSPYERNR VAVSPFSSAL EGEERIETSR SLGDHCFEPL PYVTNYLSIF 70 80 90 100 110 120 ALFGKEIFGD KGNVSSRNEY LLKKYYSLKK PFVLRHNGHA LKNPDMPLQR NDILQTNFMV 130 140 150 160 170 180 DKFLNRTVRS VNFNNFKIIS DMQSKSGRGT KSGTNQNQSA DAIQNICLPS IPSALPYFQY 190 200 210 220 230 240 YRKLLTVNTK EWDILKLHSL WVPKLRKDFK DFSLYGDKNS LKPIDSHYDE DNTMKKNLFF 250 260 270 280 290 300 ERSPSRQTLD GKGCASKGYD ISSGNMIIPS LFSEDKLPAL TYHCSVELNG NIYIFGGLMP 310 320 330 340 350 360 CYSYEEDAPM LNDFFVDGIK NLPPPLLPQV INNPSMVNNP HLYVASIPSC RFSKPKMGGY 370 380 390 400 410 420 IPPPLLCVQG SKLTDRHIFF YGGFEIRTET RGDENGKYHL KKRLYVNNTG YILDIMSFKF 430 440 450 460 470 480 TKIDIIVQPS KYNAYPTMSS RFGHLQISID NPNRRASVHS SSMNEIHKMG SASMKQGSSI 490 500 510 520 530 540 TSGRLEKAAV LSSLPHNTVH TVIIFGGYRQ TGDDRYEAMN DLWKIEIPVI RRGKKGYCKF 550 560 570 580 590 600 SETANAILLT PSEKDKSDWP EERAFSAFSV HGTSLMDRSS LDMRLLNNLK NHFVLKPSYI 610 620 630 640 650 660 SQDRVVSPKP VFPMMVHGTH QDLFNSGSAA QESPKAGASA SSASAASFDP DMDDNLENYI 670 680 690 700 710 720 VNPGRKSSSI PMTAIGRQRL ILSQEKPVGK TVVLHGGSNG LNVLDDMWLM DLECETWTPI 730 740 750 760 770 780 ETFAKADSSE DGDEKLDSVN VGLVGHRMES IGRICVCIGG MVQEDVDQFY SENDDEPPRK 790 800 810 820 830 840 RKVDTLPLGG NFLNTIDLST QCWEEHKITL SKKEDDEDRQ DSENEDTNSN IVVGVGGTSL 850 860 870 880 QCDKSIILIG GLISRRSNVK EIYLHGTITK SIFPSVNPSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Galpha protein Gpa2 controls yeast differentiation by interacting with kelch repeat proteins that mimic Gbeta subunits." Harashima T., Heitman J. Mol. Cell 10:163-173(2002) [PubMed: 12150916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH GPA2. Strain: Sigma 1278B.
[2]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed: 7731988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Fisk D., Cherry J.M. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[4]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 661; 802 AND 814-815. Strain: ATCC 204508 / S288c.
[5]	"Krh1p and Krh2p act downstream of the Gpa2p G(alpha) subunit to negatively regulate haploid invasive growth." Batlle M., Lu A., Green D.A., Xue Y., Hirsch J.P. J. Cell Sci. 116:701-710(2003) [PubMed: 12538771] [Abstract] Cited for: FUNCTION.
[6]	"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].
[7]	"Cyclic AMP-independent regulation of protein kinase A substrate phosphorylation by Kelch repeat proteins." Lu A., Hirsch J.P. Eukaryot. Cell 4:1794-1800(2005) [PubMed: 16278446] [Abstract] Cited for: FUNCTION.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB127946 Genomic DNA. Translation: BAD04042.1. AB127947 Genomic DNA. Translation: BAD04043.1. U12980 Genomic DNA. Translation: AAC04977.2. BK006935 Genomic DNA. Translation: DAA06932.2.
PIR	S51965.
RefSeq	NP_009345.3. NM_001178199.2.
3D structure databases
ProteinModelPortal	P39717.
SMR	P39717. Positions 692-720.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-7315N.
IntAct	P39717. 2 interactions.
MINT	MINT-630753.
STRING	P39717.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	851243.
KEGG	sce:YAL056W.
NMPDR	fig|4932.3.peg.20.
Organism-specific databases
CYGD	YAL056w.
SGD	S000000052. GPB2.
Phylogenomic databases
eggNOG	fuNOG08279.
GeneTree	EFGT00050000008624.
HOGENOM	HBG203613.
OMA	FGGYRQT.
OrthoDB	EOG473T17.
Gene expression databases
ArrayExpress	P39717.
Genevestigator	P39717.
GermOnline	YAL056W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011043. Gal_Oxase/kelch_b-propeller. IPR015915. Kelch-typ_b-propeller. [Graphical view]
Gene3D	G3DSA:2.120.10.80. Kelch-typ_b-propeller. 3 hits.
SUPFAM	SSF50965. Gal_oxid_central. 1 hit.
ProtoNet	Search...
Other
NextBio	968174.

Entry information

Entry name

GPB2_YEAST

Accession

Primary (citable) accession number: P39717
Secondary accession number(s): D6VPG2, P39716

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program