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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)DescriptionActionsGraphical viewLength
DNA bindingi500 – 686OBAdd BLAST187

GO - Molecular functioni

  • G-rich strand telomeric DNA binding Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi50K → Q: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. 1 Publication1
Mutagenesisi72I → T: Disrupts interaction with POL1 and FUN12. 1 Publication1
Mutagenesisi124C → R: Disrupts interaction with POL1 but not FUN12. 1 Publication1
Mutagenesisi149L → S: Disrupts interaction with POL1 but not FUN12. 1 Publication1
Mutagenesisi228S → P: Disrupts interaction with POL1 but not FUN12. 1 Publication1
Mutagenesisi243G → R: Disrupts interaction with POL1 and FUN12. 1 Publication1
Mutagenesisi392L → P: Disrupts interaction with POL1 but not FUN12. 1 Publication1
Mutagenesisi523I → V: Increase in length of X' and Y' telomeres. Disrupts interaction with POL1 but not FUN12. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000894411 – 924Cell division control protein 13Add BLAST924

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei306PhosphoserineCombined sources1
Modified residuei308PhosphothreonineCombined sources1
Modified residuei333PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32797.
PRIDEiP32797.

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 interactors.
DIPiDIP-1229N.
IntActiP32797. 10 interactors.
MINTiMINT-402072.

Structurei

Secondary structure

1924
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 25Combined sources5
Beta strandi32 – 46Combined sources15
Beta strandi48 – 56Combined sources9
Beta strandi62 – 64Combined sources3
Beta strandi70 – 75Combined sources6
Helixi79 – 95Combined sources17
Beta strandi113 – 115Combined sources3
Helixi118 – 120Combined sources3
Beta strandi125 – 135Combined sources11
Beta strandi138 – 148Combined sources11
Helixi151 – 160Combined sources10
Helixi178 – 195Combined sources18
Beta strandi197 – 200Combined sources4
Helixi203 – 205Combined sources3
Helixi211 – 221Combined sources11
Helixi348 – 352Combined sources5
Beta strandi359 – 372Combined sources14
Helixi377 – 380Combined sources4
Beta strandi381 – 383Combined sources3
Beta strandi385 – 390Combined sources6
Beta strandi394 – 396Combined sources3
Turni403 – 405Combined sources3
Beta strandi406 – 412Combined sources7
Helixi415 – 422Combined sources8
Helixi424 – 426Combined sources3
Helixi429 – 436Combined sources8
Turni437 – 439Combined sources3
Beta strandi444 – 453Combined sources10
Beta strandi463 – 472Combined sources10
Turni510 – 512Combined sources3
Beta strandi521 – 525Combined sources5
Beta strandi531 – 533Combined sources3
Beta strandi539 – 544Combined sources6
Beta strandi565 – 567Combined sources3
Turni571 – 573Combined sources3
Beta strandi575 – 580Combined sources6
Helixi581 – 592Combined sources12
Beta strandi595 – 597Combined sources3
Helixi599 – 602Combined sources4
Beta strandi617 – 624Combined sources8
Beta strandi626 – 629Combined sources4
Beta strandi631 – 634Combined sources4
Beta strandi642 – 644Combined sources3
Helixi645 – 648Combined sources4
Helixi653 – 668Combined sources16
Helixi670 – 675Combined sources6
Helixi677 – 680Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32797.

Family & Domainsi

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

InParanoidiP32797.
KOiK11115.
OMAiTRERICE.
OrthoDBiEOG092C0UX4.

Family and domain databases

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)DescriptionActionsGraphical viewLength
Sequence conflicti40L → A in AAA99990 (PubMed:7565765).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP32797.

Proteomic databases

MaxQBiP32797.
PRIDEiP32797.

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.
OrthoDBiEOG092C0UX4.

Enzyme and pathway databases

BioCyciYEAST:G3O-29601-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32797.
PROiP32797.

Family and domain databases

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...

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: November 2, 2016
This is version 147 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.