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Protein

Cell division control protein 13

Gene

CDC13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi500 – 686187OBAdd
BLAST

GO - Molecular functioni

  • single-stranded telomeric DNA binding Source: SGD
  • telomerase inhibitor activity Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • negative regulation of telomerase activity Source: SGD
  • regulation of telomere maintenance via telomerase Source: SGD
  • ribonucleoprotein complex localization Source: SGD
  • telomere capping Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via telomerase Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29601-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 13
Gene namesi
Name:CDC13
Ordered Locus Names:YDL220C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL220C.
SGDiS000002379. CDC13.

Subcellular locationi

GO - Cellular componenti

  • CST complex Source: SGD
  • nuclear chromosome, telomeric region Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501K → Q: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. 1 Publication
Mutagenesisi72 – 721I → T: Disrupts interaction with POL1 and FUN12. 1 Publication
Mutagenesisi124 – 1241C → R: Disrupts interaction with POL1 but not FUN12. 1 Publication
Mutagenesisi149 – 1491L → S: Disrupts interaction with POL1 but not FUN12. 1 Publication
Mutagenesisi228 – 2281S → P: Disrupts interaction with POL1 but not FUN12. 1 Publication
Mutagenesisi243 – 2431G → R: Disrupts interaction with POL1 and FUN12. 1 Publication
Mutagenesisi392 – 3921L → P: Disrupts interaction with POL1 but not FUN12. 1 Publication
Mutagenesisi523 – 5231I → V: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 924924Cell division control protein 13PRO_0000089441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei306 – 3061PhosphoserineCombined sources
Modified residuei308 – 3081PhosphothreonineCombined sources
Modified residuei333 – 3331PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32797.
PeptideAtlasiP32797.

PTM databases

iPTMnetiP32797.

Interactioni

Subunit structurei

Interacts with POL1, EST1, FUN12, STM1, STN1 and TEN1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EST1P172143EBI-4187,EBI-6684
POL1P133824EBI-4187,EBI-6128
STN1P389605EBI-4187,EBI-18427

Protein-protein interaction databases

BioGridi31825. 579 interactions.
DIPiDIP-1229N.
IntActiP32797. 10 interactions.
MINTiMINT-402072.

Structurei

Secondary structure

1
924
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 255Combined sources
Beta strandi32 – 4615Combined sources
Beta strandi48 – 569Combined sources
Beta strandi62 – 643Combined sources
Beta strandi70 – 756Combined sources
Helixi79 – 9517Combined sources
Beta strandi113 – 1153Combined sources
Helixi118 – 1203Combined sources
Beta strandi125 – 13511Combined sources
Beta strandi138 – 14811Combined sources
Helixi151 – 16010Combined sources
Helixi178 – 19518Combined sources
Beta strandi197 – 2004Combined sources
Helixi203 – 2053Combined sources
Helixi211 – 22111Combined sources
Helixi348 – 3525Combined sources
Beta strandi359 – 37214Combined sources
Helixi377 – 3804Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi385 – 3906Combined sources
Beta strandi394 – 3963Combined sources
Turni403 – 4053Combined sources
Beta strandi406 – 4127Combined sources
Helixi415 – 4228Combined sources
Helixi424 – 4263Combined sources
Helixi429 – 4368Combined sources
Turni437 – 4393Combined sources
Beta strandi444 – 45310Combined sources
Beta strandi463 – 47210Combined sources
Turni510 – 5123Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi539 – 5446Combined sources
Beta strandi565 – 5673Combined sources
Turni571 – 5733Combined sources
Beta strandi575 – 5806Combined sources
Helixi581 – 59212Combined sources
Beta strandi595 – 5973Combined sources
Helixi599 – 6024Combined sources
Beta strandi617 – 6248Combined sources
Beta strandi626 – 6294Combined sources
Beta strandi631 – 6344Combined sources
Beta strandi642 – 6443Combined sources
Helixi645 – 6484Combined sources
Helixi653 – 66816Combined sources
Helixi670 – 6756Combined sources
Helixi677 – 6804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KXLNMR-A497-694[»]
1S40NMR-A497-694[»]
3NWSX-ray2.50A/B/C/D13-227[»]
3NWTX-ray2.70A13-227[»]
3OIPX-ray2.50A12-243[»]
3OIQX-ray2.40A12-243[»]
4HCEX-ray2.30A/B344-495[»]
ProteinModelPortaliP32797.
SMRiP32797. Positions 13-224, 346-475, 500-686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32797.

Family & Domainsi

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

InParanoidiP32797.
KOiK11115.
OMAiTRERICE.
OrthoDBiEOG76QFT2.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR031749. Cdc13_N.
IPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERiPTHR14513. PTHR14513. 1 hit.
PfamiPF16853. CDC13_N. 1 hit.
PF02765. POT1. 1 hit.
[Graphical view]
SMARTiSM00976. Telo_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

P32797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTLEEPECP PHKNRIFVSS SKDFEGYPSK AIVPVQFVAL LTSIHLTETK
60 70 80 90 100
CLLGFSNFER RGDQSQEDQY LIKLKFKDRG SERLARITIS LLCQYFDIEL
110 120 130 140 150
PDLDSDSGAS PTVILRDIHL ERLCFSSCKA LYVSKHGNYT LFLEDIKPLD
160 170 180 190 200
LVSVISTIST KSTNSSKHSS SELISECDLN NSLVDIFNNL IEMNRDEKNR
210 220 230 240 250
FKFVKLIHYD IELKKFVQDQ QKVLSQKSKA AAINPFFVPN RLGIPYIESQ
260 270 280 290 300
NEFNSQLMTL NVDEPTTDIS NMGEEMHDSA DPIEDSDSST TSSTGKYFSS
310 320 330 340 350
KSYIQSQTPE RKTSVPNNWH DDDSGSKRKR KLSFHSPNAS SIRKAISYEQ
360 370 380 390 400
LSLASVGSVE RLEGKIVGMN PPQFASINEF KYCTLKLYFT QLLPNVPDKV
410 420 430 440 450
LVPGVNCIEI VIPTRERICE LFGVLNCQSD KISDILLLEK PDRISVEVER
460 470 480 490 500
ILWDNDKTAS PGMAVWSLKN ISTDTQAQAQ VQVPAQSSAS IDPSRTRMSK
510 520 530 540 550
MARKDPTIEF CQLGLDTFET KYITMFGMLV SCSFDKPAFI SFVFSDFTKN
560 570 580 590 600
DIVQNYLYDR YLIDYENKLE LNEGFKAIMY KNQFETFDSK LRKIFNNGLR
610 620 630 640 650
DLQNGRDENL SQYGIVCKMN IKVKMYNGKL NAIVRECEPV PHSQISSIAS
660 670 680 690 700
PSQCEHLRLF YQRAFKRIGE SAISRYFEEY RRFFPIHRNG SHLAKLRFDE
710 720 730 740 750
VKHEPKKSPT TPALAEHIPD LNADVSSFDV KFTDISSLLD SSARLPRPQQ
760 770 780 790 800
THKSNTLYSC EGRIIAIEYH ASDLCFHITN ELPLLQTRGL APERVLQLHI
810 820 830 840 850
ITSKNFAYFF NRSSAYLQRQ PLEEKYTQLA QFLGHSFKFN ITSSLTLFPD
860 870 880 890 900
TTVALQIWCP IECTFRELQQ QLAHPKVAAA PDSGSLDCAI NATVNPLRLL
910 920
AAQNGVTVKK EEDNDDDAGA VPTS
Length:924
Mass (Da):104,904
Last modified:July 11, 2002 - v2
Checksum:i9FE0AD08520A6F8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401L → A in AAA99990 (PubMed:7565765).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76550 Genomic DNA. Translation: AAA99990.1.
Z74269 Genomic DNA. Translation: CAA98800.1.
BK006938 Genomic DNA. Translation: DAA11644.1.
PIRiS67783. S27421.
RefSeqiNP_010061.1. NM_001180280.1.

Genome annotation databases

EnsemblFungiiYDL220C; YDL220C; YDL220C.
GeneIDi851306.
KEGGisce:YDL220C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76550 Genomic DNA. Translation: AAA99990.1.
Z74269 Genomic DNA. Translation: CAA98800.1.
BK006938 Genomic DNA. Translation: DAA11644.1.
PIRiS67783. S27421.
RefSeqiNP_010061.1. NM_001180280.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KXLNMR-A497-694[»]
1S40NMR-A497-694[»]
3NWSX-ray2.50A/B/C/D13-227[»]
3NWTX-ray2.70A13-227[»]
3OIPX-ray2.50A12-243[»]
3OIQX-ray2.40A12-243[»]
4HCEX-ray2.30A/B344-495[»]
ProteinModelPortaliP32797.
SMRiP32797. Positions 13-224, 346-475, 500-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31825. 579 interactions.
DIPiDIP-1229N.
IntActiP32797. 10 interactions.
MINTiMINT-402072.

PTM databases

iPTMnetiP32797.

Proteomic databases

MaxQBiP32797.
PeptideAtlasiP32797.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL220C; YDL220C; YDL220C.
GeneIDi851306.
KEGGisce:YDL220C.

Organism-specific databases

EuPathDBiFungiDB:YDL220C.
SGDiS000002379. CDC13.

Phylogenomic databases

InParanoidiP32797.
KOiK11115.
OMAiTRERICE.
OrthoDBiEOG76QFT2.

Enzyme and pathway databases

BioCyciYEAST:G3O-29601-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32797.
NextBioi968319.
PROiP32797.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR031749. Cdc13_N.
IPR012340. NA-bd_OB-fold.
IPR028389. POT1.
IPR011564. Telomer_end-bd_POT1/Cdc13.
[Graphical view]
PANTHERiPTHR14513. PTHR14513. 1 hit.
PfamiPF16853. CDC13_N. 1 hit.
PF02765. POT1. 1 hit.
[Graphical view]
SMARTiSM00976. Telo_bind. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STM1.
  9. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND THR-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.
  13. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.

Entry informationi

Entry nameiCDC13_YEAST
AccessioniPrimary (citable) accession number: P32797
Secondary accession number(s): D6VRD4, Q07650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 11, 2002
Last modified: May 11, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 319 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.