P32797 (CDC13_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division control protein 13

Gene names

Name:	CDC13
Ordered Locus Names:	YDL220C

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

General annotation (Comments)

Function	Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG1-3] strand lengthening via interaction with EST1. Promotes [C1-3A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity. Ref.5 Ref.6 Ref.7
Subunit structure	Interacts with POL1, EST1, FUN12, STM1, STN1 and TEN1. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Chromosome › telomere.
Miscellaneous	Present with 319 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Contains 1 OB DNA-binding domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Chromosome Telomere
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW telomere capping Inferred from mutant phenotype Ref.1. Source: SGD telomere maintenance via telomerase Inferred from mutant phenotype. Source: SGD
Cellular component	nuclear telomere cap complex Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.7Ref.4. Source: IntAct single-stranded telomeric DNA binding Inferred from direct assay. Source: SGD telomerase inhibitor activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EST1	P17214	3	EBI-4187,EBI-6684
POL1	P13382	4	EBI-4187,EBI-6128
STN1	P38960	5	EBI-4187,EBI-18427

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 924

924

Cell division control protein 13

PRO_0000089441

Regions

DNA binding

500 – 686

187

OB Ref.13 Ref.14

Amino acid modifications

Modified residue

306

1

Phosphoserine Ref.11 Ref.12

Modified residue

308

1

Phosphothreonine Ref.11 Ref.12

Modified residue

333

1

Phosphoserine Ref.10

Modified residue

336

1

Phosphoserine Ref.10

Experimental info

Mutagenesis

50

1

K → Q: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. Ref.7

Mutagenesis

72

1

I → T: Disrupts interaction with POL1 and FUN12. Ref.7

Mutagenesis

124

1

C → R: Disrupts interaction with POL1 but not FUN12. Ref.7

Mutagenesis

149

1

L → S: Disrupts interaction with POL1 but not FUN12. Ref.7

Mutagenesis

228

1

S → P: Disrupts interaction with POL1 but not FUN12. Ref.7

Mutagenesis

243

1

G → R: Disrupts interaction with POL1 and FUN12. Ref.7

Mutagenesis

392

1

L → P: Disrupts interaction with POL1 but not FUN12. Ref.7

Mutagenesis

523

1

I → V: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. Ref.7

Sequence conflict

40

1

L → A in AAA99990. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

924

Helix Strand Turn

Details...

Turn

510 – 512

3

Beta strand

521 – 525

5

Beta strand

531 – 533

3

Beta strand

539 – 544

6

Beta strand

565 – 567

3

Turn

571 – 573

3

Beta strand

575 – 580

6

Helix

581 – 592

12

Beta strand

595 – 597

3

Helix

599 – 602

4

Beta strand

617 – 624

8

Beta strand

626 – 629

4

Beta strand

631 – 634

4

Beta strand

642 – 644

3

Helix

645 – 648

4

Helix

653 – 668

16

Helix

670 – 675

6

Helix

677 – 680

4

Sequences

	Sequence		Length	Mass (Da)
	P32797 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 9FE0AD08520A6F8A	FASTA	924	104,904
	10 20 30 40 50 60 MDTLEEPECP PHKNRIFVSS SKDFEGYPSK AIVPVQFVAL LTSIHLTETK CLLGFSNFER 70 80 90 100 110 120 RGDQSQEDQY LIKLKFKDRG SERLARITIS LLCQYFDIEL PDLDSDSGAS PTVILRDIHL 130 140 150 160 170 180 ERLCFSSCKA LYVSKHGNYT LFLEDIKPLD LVSVISTIST KSTNSSKHSS SELISECDLN 190 200 210 220 230 240 NSLVDIFNNL IEMNRDEKNR FKFVKLIHYD IELKKFVQDQ QKVLSQKSKA AAINPFFVPN 250 260 270 280 290 300 RLGIPYIESQ NEFNSQLMTL NVDEPTTDIS NMGEEMHDSA DPIEDSDSST TSSTGKYFSS 310 320 330 340 350 360 KSYIQSQTPE RKTSVPNNWH DDDSGSKRKR KLSFHSPNAS SIRKAISYEQ LSLASVGSVE 370 380 390 400 410 420 RLEGKIVGMN PPQFASINEF KYCTLKLYFT QLLPNVPDKV LVPGVNCIEI VIPTRERICE 430 440 450 460 470 480 LFGVLNCQSD KISDILLLEK PDRISVEVER ILWDNDKTAS PGMAVWSLKN ISTDTQAQAQ 490 500 510 520 530 540 VQVPAQSSAS IDPSRTRMSK MARKDPTIEF CQLGLDTFET KYITMFGMLV SCSFDKPAFI 550 560 570 580 590 600 SFVFSDFTKN DIVQNYLYDR YLIDYENKLE LNEGFKAIMY KNQFETFDSK LRKIFNNGLR 610 620 630 640 650 660 DLQNGRDENL SQYGIVCKMN IKVKMYNGKL NAIVRECEPV PHSQISSIAS PSQCEHLRLF 670 680 690 700 710 720 YQRAFKRIGE SAISRYFEEY RRFFPIHRNG SHLAKLRFDE VKHEPKKSPT TPALAEHIPD 730 740 750 760 770 780 LNADVSSFDV KFTDISSLLD SSARLPRPQQ THKSNTLYSC EGRIIAIEYH ASDLCFHITN 790 800 810 820 830 840 ELPLLQTRGL APERVLQLHI ITSKNFAYFF NRSSAYLQRQ PLEEKYTQLA QFLGHSFKFN 850 860 870 880 890 900 ITSSLTLFPD TTVALQIWCP IECTFRELQQ QLAHPKVAAA PDSGSLDCAI NATVNPLRLL 910 920 AAQNGVTVKK EEDNDDDAGA VPTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Single-stranded DNA arising at telomeres in cdc13 mutants may constitute a specific signal for the RAD9 checkpoint." Garvik B., Carson M., Hartwell L. Mol. Cell. Biol. 15:6128-6138(1995) [PubMed: 7565765] [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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Ten1 functions in telomere end protection and length regulation in association with Stn1 and Cdc13." Grandin N., Damon C., Charbonneau M. EMBO J. 20:1173-1183(2001) [PubMed: 11230140] [Abstract] Cited for: INTERACTION WITH TEN1.
[5]	"Cdc13 both positively and negatively regulates telomere replication." Chandra A., Hughes T.R., Nugent C.I., Lundblad V. Genes Dev. 15:404-414(2001) [PubMed: 11230149] [Abstract] Cited for: FUNCTION, INTERACTION WITH STN1.
[6]	"New function of CDC13 in positive telomere length regulation." Meier B., Driller L., Jaklin S., Feldmann H.M. Mol. Cell. Biol. 21:4233-4245(2001) [PubMed: 11390652] [Abstract] Cited for: FUNCTION, INTERACTION WITH EST1.
[7]	"The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein." Qi H., Zakian V.A. Genes Dev. 14:1777-1788(2000) [PubMed: 10898792] [Abstract] Cited for: FUNCTION, INTERACTION WITH EST1; FUN12 AND POL1, MUTAGENESIS OF LYS-50; ILE-72; CYS-124; LEU-149; SER-228; GLY-243; LEU-392 AND ILE-523.
[8]	"STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae." Hayashi N., Murakami S. Mol. Genet. Genomics 267:806-813(2002) [PubMed: 12207228] [Abstract] Cited for: INTERACTION WITH STM1.
[9]	"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].
[10]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-336, MASS SPECTROMETRY.
[11]	"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-306 AND THR-308, MASS SPECTROMETRY.
[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-306 AND THR-308, MASS SPECTROMETRY.
[13]	"Conserved structure for single-stranded telomeric DNA recognition." Mitton-Fry R.M., Anderson E.M., Hughes T.R., Lundblad V., Wuttke D.S. Science 296:145-147(2002) [PubMed: 11935027] [Abstract] Cited for: STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.
[14]	"Structural basis for telomeric single-stranded DNA recognition by yeast Cdc13." Mitton-Fry R.M., Anderson E.M., Theobald D.L., Glustrom L.W., Wuttke D.S. J. Mol. Biol. 338:241-255(2004) [PubMed: 15066429] [Abstract] Cited for: STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M76550 Genomic DNA. Translation: AAA99990.1.
Z74269 Genomic DNA. Translation: CAA98800.1.
BK006938 Genomic DNA. Translation: DAA11644.1.

PIR

S27421. S67783.

RefSeq

NP_010061.1. NM_001180280.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KXL	NMR	-	A	497-694	[»]
1S40	NMR	-	A	497-694	[»]
3NWS	X-ray	2.50	A/B/C/D	13-227	[»]
3NWT	X-ray	2.70	A	13-227	[»]
3OIP	X-ray	2.50	A	12-243	[»]
3OIQ	X-ray	2.40	A	12-243	[»]

ProteinModelPortal

P32797.

SMR

P32797. Positions 13-224, 500-686.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1229N.

IntAct

P32797. 12 interactions.

MINT

MINT-402072.

STRING

P32797.

Proteomic databases

PeptideAtlas

P32797.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDL220C; YDL220C; YDL220C.

GeneID

851306.

KEGG

sce:YDL220C.

NMPDR

fig|4932.3.peg.794.

Organism-specific databases

CYGD

YDL220c.

SGD

S000002379. CDC13.

Phylogenomic databases

eggNOG

fuNOG11718.

OMA

EYKLLKP.

OrthoDB

EOG49PF81.

Gene expression databases

ArrayExpress

P32797.

Genevestigator

P32797.

GermOnline

YDL220C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR011564. Telomer_end-bd.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.

KO

K11115.

Pfam

PF02765. Telo_bind. 1 hit.
[Graphical view]

SMART

SM00976. Telo_bind. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

ProtoNet

Search...

Other

NextBio

968319.

Entry information

Entry name

CDC13_YEAST

Accession

Primary (citable) accession number: P32797
Secondary accession number(s): D6VRD4, Q07650

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	July 11, 2002
Last modified:	December 14, 2011
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program