Reviewed, UniProtKB/Swiss-Prot Q00684 (CDC14_YEAST)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein phosphatase CDC14
    EC=3.1.3.48

Gene names

Name:	CDC14
Synonyms:	OAF3
Ordered Locus Names:	YFR028C

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

General annotation (Comments)

Function	Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Required also for mitotic exit, where it is required for the termination of M phase. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus. Ref.2 Ref.6 Ref.7
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Component of the RENT (regulator of nucleolar silencing and telophase) complex which is composed of at least NET1, CDC14 and SIR2. Ref.6
Subcellular location	Nucleus › nucleolus. Cytoplasm. Ref.7
Miscellaneous	Present with 8550 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Sequence caution	The sequence AAA34477.1 differs from that shown. Reason: Frameshift at positions 116 and 190. The sequence CAA52971.1 differs from that shown. Reason: Frameshift at position 117.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mitotic cell cycle Inferred from mutant phenotype. Source: SGD nucleolus organization Inferred from genetic interaction. Source: SGD protein amino acid dephosphorylation Inferred from direct assay. Source: SGD regulation of exit from mitosis Inferred from genetic interaction. Source: SGD
Cellular component	RENT complex Inferred from direct assay. Source: SGD spindle pole body Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC5	P32562	2	EBI-4192,EBI-4440
GIC1	P38785	1	EBI-4192,EBI-7575
NET1	P47035	8	EBI-4192,EBI-25953
SIC1	P38634	1	EBI-4192,EBI-17127
SWI5	P08153	1	EBI-4192,EBI-18633
TOF2	Q02208	2	EBI-4192,EBI-27048
UTP7	P40055	1	EBI-4192,EBI-22597

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 551	551	Tyrosine-protein phosphatase CDC14		PRO_0000094875
Sites
	Active site	283	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	271	1	Phosphothreonine Ref.10
	Modified residue	467	1	Phosphoserine Ref.9 Ref.11
Experimental info
	Sequence conflict	118	1	A → P in BAA09533. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q00684-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 4EB3985DFA3FD823	FASTA	551	61,907
	10 20 30 40 50 60 MRRSVYLDNT IEFLRGRVYL GAYDYTPEDT DELVFFTVED AIFYNSFHLD FGPMNIGHLY 70 80 90 100 110 120 RFAVIFHEIL NDPENANKAV VFYSSASTRQ RANAACMLCC YMILVQAWTP HQVLQPLAQV 130 140 150 160 170 180 DPPFMPFRDA GYSNADFEIT IQDVVYGVWR AKEKGLIDLH SFNLESYEKY EHVEFGDFNV 190 200 210 220 230 240 LTPDFIAFAS PQEDHPKGYL ATKSSHLNQP FKSVLNFFAN NNVQLVVRLN SHLYNKKHFE 250 260 270 280 290 300 DIGIQHLDLI FEDGTCPDLS IVKNFVGAAE TIIKRGGKIA VHCKAGLGRT GCLIGAHLIY 310 320 330 340 350 360 TYGFTANECI GFLRFIRPGM VVGPQQHWLY LHQNDFREWK YTTRISLKPS EAIGGLYPLI 370 380 390 400 410 420 SLEEYRLQKK KLKDDKRVAQ NNIEGELRDL TMTPPSNGHG ALSARNSSQP STANNGSNSF 430 440 450 460 470 480 KSSAVPQTSP GQPRKGQNGS NTIEDINNNR NPTSHANRKV VIESNNSDDE SMQDTNGTSN 490 500 510 520 530 540 HYPKVSRKKN DISSASSSRM EDNEPSATNI NNAADDTILR QLLPKNRRVT SGRRTTSAAG 550 GIRKISGSIK K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and transcription during the cell cycle." Wan J., Xu H., Grunstein M. J. Biol. Chem. 267:11274-11280(1992) [PubMed: 1597462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Dominant mutant alleles of yeast protein kinase gene CDC15 suppress the lte1 defect in termination of M phase and genetically interact with CDC14." Shirayama M., Matsui Y., Toh-e A. Mol. Gen. Genet. 251:176-185(1996) [PubMed: 8668128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae." Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., Hanaoka F., Murakami Y. Yeast 12:177-190(1996) [PubMed: 8686381] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Mai B., Lipp M. Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-421.
[6]	"Net1 stimulates RNA polymerase I transcription and regulates nucleolar structure independently of controlling mitotic exit." Shou W., Sakamoto K.M., Keener J., Morimoto K.W., Traverso E.E., Azzam R., Hoppe G.J., Feldman R.M.R., DeModena J., Moazed D., Charbonneau H., Nomura M., Deshaies R.J. Mol. Cell 8:45-55(2001) [PubMed: 11511359] [Abstract] Cited for: FUNCTION, SUBUNIT.
[7]	"The Cdc14 phosphatase and the FEAR network control meiotic spindle disassembly and chromosome segregation." Marston A.L., Lee B.H., Amon A. Dev. Cell 4:711-726(2003) [PubMed: 12737806] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"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].
[9]	"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-467, 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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, MASS SPECTROMETRY.
[11]	"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-467, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M61194 Genomic DNA. Translation: AAA34477.1. Frameshift. D55715 Genomic DNA. Translation: BAA09533.1. D50617 Genomic DNA. Translation: BAA09267.1. X75077 Genomic DNA. Translation: CAA52971.1. Frameshift.
PIR	S56283.
RefSeq	NP_116684.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5116N.
IntAct	Q00684. 53 interactions.
STRING	Q00684.
Proteomic databases
PeptideAtlas	Q00684.
PRIDE	Q00684.
Genome annotation databases
Ensembl	YFR028C; YFR028C; YFR028C; Saccharomyces cerevisiae. [Genome view]
GeneID	850585.
GenomeReviews	Gene locus YFR028C in contig D50617_GR.
KEGG	sce:YFR028C.
NMPDR	fig|4932.3.peg.2317.
Organism-specific databases
CYGD	YFR028c.
SGD	S000001924. CDC14.
Phylogenomic databases
HOGENOM	Q00684.
OMA	DFEITIQ.
Enzyme and pathway databases
BRENDA	3.1.3.48. 250.
Gene expression databases
ArrayExpress	Q00684.
Genevestigator	Q00684.
GermOnline	YFR028C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000387. Dual-sp/Tyr_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR016130. Tyr_Pase_AS. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	966423.

Entry information

Entry name

CDC14_YEAST

Accession

Primary (citable) accession number: Q00684
Secondary accession number(s): Q05180, Q05673

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)