Q08496 (DIA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein DIA2

Alternative name(s):
Digs into agar protein 2

Gene names

Name:	DIA2
Ordered Locus Names:	YOR080W
ORF Names:	YOR29-31

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	732 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins By similarity. The SCF(DIA2) complex is specifically involved in the pheromone induced degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA replication origins. Involved in DNA replication, genome stability, and the control of cell cycle, probably through its association to replication origins to facilitate the ubiquitination of another origin-binding protein. Required for invasive growth and growth under alkaline conditions. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Subunit structure	Component of the SCF(DIA2) complex containing CDC53, SKP1, RBX1 and DIA2. Interacts with SKP1. Ref.9
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the DIA2 family. Contains 1 F-box domain. Contains 7 LRR (leucine-rich) repeats. Contains 3 TPR repeats.
Sequence caution	The sequence CAA94565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA99273.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA99275.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Nucleus
Domain	Leucine-rich repeat Repeat TPR repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype. Source: SGD cell cycle Inferred from electronic annotation. Source: UniProtKB-KW invasive growth in response to glucose limitation Inferred from genetic interaction Ref.5. Source: SGD protein ubiquitination Inferred from direct assay. Source: GOC regulation of DNA replication Inferred from mutant phenotype Ref.11. Source: SGD
Cellular component	SCF ubiquitin ligase complex Inferred from direct assay Ref.9Ref.11. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	DNA replication origin binding Inferred from physical interaction Ref.11. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 732	732	Protein DIA2		PRO_0000233003
Regions
	Repeat	15 – 48	34	TPR 1
	Repeat	78 – 111	34	TPR 2
	Repeat	113 – 145	33	TPR 3
	Domain	204 – 251	48	F-box
	Repeat	425 – 449	25	LRR 1
	Repeat	480 – 505	26	LRR 2
	Repeat	509 – 532	24	LRR 3
	Repeat	550 – 574	25	LRR 4
	Repeat	579 – 602	24	LRR 5
	Repeat	616 – 637	22	LRR 6
	Repeat	645 – 669	25	LRR 7
Amino acid modifications
	Modified residue	393	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q08496 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 98B610994BA2F803	FASTA	732	85,070
	10 20 30 40 50 60 MSSPGNSGVA IDSTVLKAIE LGTRLFKSGE YLQAKRIFTN ALRVCDSYSQ EQIMRIRNAY 70 80 90 100 110 120 QLDTARPDNK RLYHPRYIKI LDNICACYEK LNDLKSCLDV SQRLLKLEPG NIKCYIRCTR 130 140 150 160 170 180 TLIKLKDWKR AYKTCSRGLQ LCNNDSNHLR QQKQFIKNNM VQKQDGKRSY IDPLEETKIA 190 200 210 220 230 240 KKKKNNNVLE SLPKKKIKGS TKKTDLVGNL PIEILPIIFQ RFTTKELVTL SLVCNKWRDK 250 260 270 280 290 300 ILYHLDCFQE FNLAPINFKN FVKFMDFLQQ NFTRTYRKYI LSQVKVSSRI TSEELRITQL 310 320 330 340 350 360 LFSKMPKCIN IERLILSMPT LTTTQIFKLM VRGGTDFFTR LLELSLMITY RPDKQHELEI 370 380 390 400 410 420 LQTCPLLKKI ELIFVNSLVP IFDGNNSVGR DGSFNVMARH TNMQISTADN DEQGIVEEKV 430 440 450 460 470 480 IYSELEKITL ICDKKKIKNF PLCRALLRGQ FPLLQKLTIT GVTFPMNNQD IMNFQWLLNF 490 500 510 520 530 540 PDLKELWIED NDNCELSKFL QLLKFSNVWK NLEKLTFREN KLYPIVNLDE DQPVTNDDEV 550 560 570 580 590 600 PSMLFYKENL QNLEKLDLMG TSISGSALTR LCEQEYLDGR KLRSLNIGNC PNIQFPNNHA 610 620 630 640 650 660 HTARMILDVN AVLKRLSKLE EINLSHLSSL NDSTMKSFII NVPFLENLKR LDISHNFEIT 670 680 690 700 710 720 GISIYEFLKK FQMDHDNEAG GQPLAYLNID GCSQVSHITV NMIRAQNLVT QVDCVYERDV 730 WRKFGINSYS YS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames." Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M. Yeast 13:379-390(1997) [PubMed: 9133743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis." Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A., Tyers M. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999) [PubMed: 10582239] [Abstract] Cited for: DOMAIN, FUNCTION.
[5]	"Genetic analysis reveals that FLO11 upregulation and cell polarization independently regulate invasive growth in Saccharomyces cerevisiae." Palecek S.P., Parikh A.S., Kron S.J. Genetics 156:1005-1023(2000) [PubMed: 11063681] [Abstract] Cited for: FUNCTION.
[6]	"Pheromone-dependent destruction of the Tec1 transcription factor is required for MAP kinase signaling specificity in yeast." Bao M.Z., Schwartz M.A., Cantin G.T., Yates J.R. III, Madhani H.D. Cell 119:991-1000(2004) [PubMed: 15620357] [Abstract] Cited for: FUNCTION.
[7]	"Uncovering novel cell cycle players through the inactivation of securin in budding yeast." Sarin S., Ross K.E., Boucher L., Green Y., Tyers M., Cohen-Fix O. Genetics 168:1763-1771(2004) [PubMed: 15579722] [Abstract] Cited for: FUNCTION.
[8]	"Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment." Serrano R., Bernal D., Simon E., Arino J. J. Biol. Chem. 279:19698-19704(2004) [PubMed: 14993228] [Abstract] Cited for: FUNCTION.
[9]	"Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro." Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M. Proteins 54:455-467(2004) [PubMed: 14747994] [Abstract] Cited for: INTERACTION WITH SKP1, RECONSTITUTION OF THE SCF(DIA2) COMPLEX.
[10]	"A DNA integrity network in the yeast Saccharomyces cerevisiae." Pan X., Ye P., Yuan D.S., Wang X., Bader J.S., Boeke J.D. Cell 124:1069-1081(2006) [PubMed: 16487579] [Abstract] Cited for: FUNCTION.
[11]	"The F-box protein Dia2 regulates DNA replication." Koepp D.M., Kile A.C., Swaminathan S., Rodriguez-Rivera V. Mol. Biol. Cell 17:1540-1548(2006) [PubMed: 16421250] [Abstract] Cited for: IDENTIFICATION IN THE SCF(DIA2) COMPLEX, FUNCTION OF THE SCF(DIA2) COMPLEX.
[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-393, MASS SPECTROMETRY.
[13]	"The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome progression complex." Morohashi H., Maculins T., Labib K. Curr. Biol. 19:1943-1949(2009) [PubMed: 19913425] [Abstract] Cited for: IDENTIFICATION OF INITIATION SITE. Strain: ATCC 208353 / W303-1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z70678 Genomic DNA. Translation: CAA94565.1. Different initiation. Z74988 Genomic DNA. Translation: CAA99273.1. Different initiation. Z74989 Genomic DNA. Translation: CAA99275.1. Different initiation. BK006948 Genomic DNA. Translation: DAA10859.2.
PIR	S66963.
RefSeq	NP_014723.2. NM_001183499.1.
3D structure databases
ProteinModelPortal	Q08496.
SMR	Q08496. Positions 79-141, 613-661.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6496N.
IntAct	Q08496. 34 interactions.
MINT	MINT-672797.
STRING	Q08496.
Proteomic databases
PeptideAtlas	Q08496.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR080W; YOR080W; YOR080W.
GeneID	854247.
KEGG	sce:YOR080W.
NMPDR	fig|4932.3.peg.5826.
Organism-specific databases
CYGD	YOR080w.
SGD	S000005606. DIA2.
Phylogenomic databases
eggNOG	fuNOG10072.
HOGENOM	HBG202835.
OrthoDB	EOG4ZSDC8.
Gene expression databases
ArrayExpress	Q08496.
Genevestigator	Q08496.
GermOnline	YOR080W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001810. F-box_dom_cyclin-like. IPR001611. Leu-rich_rpt. IPR013026. TPR-contain. IPR011990. TPR-like_helical. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
KO	K15068.
Pfam	PF00646. F-box. 1 hit. [Graphical view]
SMART	SM00256. FBOX. 1 hit. [Graphical view]
PROSITE	PS50181. FBOX. 1 hit. PS51450. LRR. 4 hits. PS50005. TPR. False negative. PS50293. TPR_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	976159.

Entry information

Entry name

DIA2_YEAST

Accession

Primary (citable) accession number: Q08496
Secondary accession number(s): D6W2E3, O00034, Q7LGN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	October 5, 2010
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program