P54786 (ZDS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein ZDS2

Gene names

Name:	ZDS2
Synonyms:	MCS1
Ordered Locus Names:	YML109W
ORF Names:	YM8339.10

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a negative regulator of polarized growth via an alternative mechanism to ZDS1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways. Ref.5 Ref.7
Subunit structure	Interacts with SKG6. Ref.4
Miscellaneous	'ZDS' means 'zillion different screens' as both ZDS1 and ZDS2 have been found by a wide variety of genetic screens. Present with 105 molecules/cell in log phase SD medium.
Sequence similarities	To yeast ZDS1/NRC1/CES1.

Ontologies

Keywords
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell aging Inferred from mutant phenotype PubMed 10662670. Source: SGD cell shape checkpoint Inferred from genetic interaction PubMed 20980617. Source: SGD chromatin silencing at rDNA Inferred from mutant phenotype PubMed 10662670. Source: SGD establishment of cell polarity Inferred from genetic interaction PubMed 8816439. Source: SGD positive regulation of G2/M transition of mitotic cell cycle Inferred from mutant phenotype PubMed 21536748. Source: SGD regulation of protein localization Inferred from genetic interaction PubMed 18762578. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay PubMed 21536748. Source: SGD cellular bud tip Inferred from direct assay PubMed 20980617. Source: SGD cytoplasm Inferred from direct assay PubMed 21536748. Source: SGD nucleus Inferred from physical interaction PubMed 10662670. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-29637,EBI-29637
CDC55	Q00362	9	EBI-29637,EBI-1942

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 942	942	Protein ZDS2		PRO_0000066570
Amino acid modifications
	Modified residue	50	1	Phosphoserine Ref.8
	Modified residue	167	1	Phosphoserine Ref.10
	Modified residue	172	1	Phosphoserine Ref.10
	Modified residue	716	1	Phosphoserine Ref.9 Ref.10
Experimental info
	Sequence conflict	7	1	M → V in AAB37541. Ref.1
	Sequence conflict	23	1	T → S in AAB37541. Ref.1
	Sequence conflict	530	1	A → P in AAB37541. Ref.1
	Sequence conflict	546	1	A → G in AAB37541. Ref.1
	Sequence conflict	633	1	V → A in AAB37541. Ref.1
	Sequence conflict	668	1	N → S in AAB37541. Ref.1
	Sequence conflict	711	1	V → VNC in AAB37541. Ref.1
	Sequence conflict	723	1	Missing in AAB37541. Ref.1
	Sequence conflict	729	1	A → E in AAB37541. Ref.1
	Sequence conflict	833	1	S → P in AAB37541. Ref.1
	Sequence conflict	914 – 942	29	TGDIA…LIPDI → HWRYSLQW in AAB37541. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54786 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A1C9DD9A539E4291	FASTA	942	105,496
	10 20 30 40 50 60 MVLMEDMQNK DGHNTVENSS GGTDSNNNIQ MRRMRKTQLS KKELFEKRKS DVLIAAKSLD 70 80 90 100 110 120 TEIQNVKNLK RLSIGSMDLV IDPELEFKVN SRNSYSSDSS KESLQESLHE ENIIRSEQKE 130 140 150 160 170 180 EQGSEDNDAY EEGDATNVDD SIDITQTEYL HDEETLEKEK IIRNASSSTS SSARVTSRNR 190 200 210 220 230 240 RLSGVKTLAH DVVLDVENDH DSKMVDLTQN LLWVPADQHP NVKPENYLEL IQDTLQNIQI 250 260 270 280 290 300 STNQDIDENK LELGNNHVIS NRKRTGSVVR RPSRLKTSYT KFDDEPPLAD KPQEGEIQVD 310 320 330 340 350 360 KRISSSDIKT IRSVSLKEIT EELTKISNNA GLTDSDAVTL ARSLSMSGSF TNESLHLNGN 370 380 390 400 410 420 HTENDNEFAS NMFNETGLTI PERSSLRRSK FNTYKIRLEG SSLPQAVKLN SLMNIQTNDN 430 440 450 460 470 480 RRSASSPASY TQVPQEQASL NDFHEIFDHY RRTSTDWSTE NEKYVDSTNY YSDEEDLTHA 490 500 510 520 530 540 SISQESSLLS TDSSNNSVLI KPHNTGSMIS EKLDQHVSSS EKSNTNNSEA NHGWSWLNSS 550 560 570 580 590 600 NGSLNANEQT YQQLTDDEDD EECVDNEKAD FVNLSVSRRA KSTKRASERI NHSKNRHSPI 610 620 630 640 650 660 FQIHSEEAKS VVITPSVVSS SESQPSKPTA PAVVEKKVEL PTDTQASTHK KNSLEKRLAK 670 680 690 700 710 720 LFKRKQHNGT CKSDVKVIKK SVKKELKKKA SHSSLSKFRK SPKKKPQEAE VERPSSPTKT 730 740 750 760 770 780 ITTEDIDTAS VIEPEVRSSN ASTLLPDSHT SHSSEFVVET ISELDGDDSF DISGGDVNYD 790 800 810 820 830 840 VEVHSSISRD TTAGLEEDIG AEREDNTSPT APQISTLPPR KLTFEDVVKP DYSNAPIKFT 850 860 870 880 890 900 DSAFGFPLPM ITNSTVIMFD HRLGINVERA IYRLSHLKLS DPGRELRQQV LLSNFMYSYL 910 920 930 940 NLVNHTLYME QVGTGDIAFN GDSALGMMDK NDSDGTILIP DI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in the homologous ZDS1 and ZDS2 genes affect cell cycle progression." Yu Y., Jiang Y.W., Wellinger R.J., Carlson K., Roberts J.M., Stillman D.J. Mol. Cell. Biol. 16:5254-5263(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [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]	"A protein interaction map for cell polarity development." Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W., Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R., McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P., Boone C. , Pringle J.R., Davis T.N., Fields S., Drubin D.G. J. Cell Biol. 154:549-571(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SKG6.
[5]	"Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3 phosphorylation of a cAMP-dependent protein kinase regulatory subunit." Griffioen G., Swinnen S., Thevelein J.M. J. Biol. Chem. 278:23460-23471(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant." Zanelli C.F., Valentini S.R. Genetics 171:1571-1581(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, MASS SPECTROMETRY. Strain: ADR376.
[9]	"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-716, MASS SPECTROMETRY.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-172 AND SER-716, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U32938 Genomic DNA. Translation: AAB37541.1. Z49210 Genomic DNA. Translation: CAA89109.1. BK006946 Genomic DNA. Translation: DAA09789.1.
PIR	S53963.
RefSeq	NP_013598.1. NM_001182471.1.
3D structure databases
ProteinModelPortal	P54786.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1517N.
IntAct	P54786. 52 interactions.
MINT	MINT-411150.
Proteomic databases
PaxDb	P54786.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML109W; YML109W; YML109W.
GeneID	854931.
KEGG	sce:YML109W.
Organism-specific databases
CYGD	YML109w.
SGD	S000004577. ZDS2.
Phylogenomic databases
eggNOG	NOG68442.
GeneTree	ENSGT00530000067622.
HOGENOM	HOG000144432.
OMA	RRSKFNT.
OrthoDB	EOG4V72RV.
Gene expression databases
ArrayExpress	P54786.
Genevestigator	P54786.
GermOnline	YML109W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013941. ZDS1_C. [Graphical view]
Pfam	PF08632. Zds_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977962.

Entry information

Entry name

ZDS2_YEAST

Accession

Primary (citable) accession number: P54786
Secondary accession number(s): D6W0H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program