CDC13/YDL220C Protein Information Help

Standard Name Cdc13p 1, 2
Systematic Name Ydl220cp
Alias Est4p 3
ORF Classification Verified
Description Single stranded DNA-binding protein found at TG1-3 telomere G-tails; regulates telomere replication through recruitment of specific sub-complexes, but the essential function is telomere capping; autophagy and proteasome are involved in Cdc13p degradation (4, 5)
Name Description Cell Division Cycle 6
Experimental Data
Molecules/cell 319 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 924
Molecular Weight (Da) 104,903
Isoelectric Point (pI) 6.55

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Cdc13p (InterPro)
Physical Interactions There are 94 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000012720F | P32797
MIPS: YDL220C
NCBI: 1431371 | 171181 | 20664217 | 21903395 | 307568372 | 307568373 | 307568374 | 307568375 | 307568376 | 310942887 | 310942888 | 428698268 | 428698269 | 48425547 | 6319981 | NP_010061.1
GenBank/EMBL/DDBJ: DAA11644.1 | M76550 | Z74269
Amino Acid Sequence (or in FASTA format)
 
       1  MDTLEEPECP PHKNRIFVSS SKDFEGYPSK AIVPVQFVAL LTSIHLTETK
      51  CLLGFSNFER RGDQSQEDQY LIKLKFKDRG SERLARITIS LLCQYFDIEL
     101  PDLDSDSGAS PTVILRDIHL ERLCFSSCKA LYVSKHGNYT LFLEDIKPLD
     151  LVSVISTIST KSTNSSKHSS SELISECDLN NSLVDIFNNL IEMNRDEKNR
     201  FKFVKLIHYD IELKKFVQDQ QKVLSQKSKA AAINPFFVPN RLGIPYIESQ
     251  NEFNSQLMTL NVDEPTTDIS NMGEEMHDSA DPIEDSDSST TSSTGKYFSS
     301  KSYIQSQTPE RKTSVPNNWH DDDSGSKRKR KLSFHSPNAS SIRKAISYEQ
     351  LSLASVGSVE RLEGKIVGMN PPQFASINEF KYCTLKLYFT QLLPNVPDKV
     401  LVPGVNCIEI VIPTRERICE LFGVLNCQSD KISDILLLEK PDRISVEVER
     451  ILWDNDKTAS PGMAVWSLKN ISTDTQAQAQ VQVPAQSSAS IDPSRTRMSK
     501  MARKDPTIEF CQLGLDTFET KYITMFGMLV SCSFDKPAFI SFVFSDFTKN
     551  DIVQNYLYDR YLIDYENKLE LNEGFKAIMY KNQFETFDSK LRKIFNNGLR
     601  DLQNGRDENL SQYGIVCKMN IKVKMYNGKL NAIVRECEPV PHSQISSIAS
     651  PSQCEHLRLF YQRAFKRIGE SAISRYFEEY RRFFPIHRNG SHLAKLRFDE
     701  VKHEPKKSPT TPALAEHIPD LNADVSSFDV KFTDISSLLD SSARLPRPQQ
     751  THKSNTLYSC EGRIIAIEYH ASDLCFHITN ELPLLQTRGL APERVLQLHI
     801  ITSKNFAYFF NRSSAYLQRQ PLEEKYTQLA QFLGHSFKFN ITSSLTLFPD
     851  TTVALQIWCP IECTFRELQQ QLAHPKVAAA PDSGSLDCAI NATVNPLRLL
     901  AAQNGVTVKK EEDNDDDAGA VPTS*

external links for Cdc13p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Cdc13p
1) Garvik B, et al.  (1995) Single-stranded DNA arising at telomeres in cdc13 mutants may constitute a specific signal for the RAD9 checkpoint. Mol Cell Biol 15(11):6128-38
2) Garvik, B. and Hartwell, L.  (1989) Personal Communication, Mortimer Map Edition 10
3) Lendvay TS, et al.  (1996) Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional EST genes. Genetics 144(4):1399-412
4) Lustig AJ  (2001) Cdc13 subcomplexes regulate multiple telomere functions. Nat Struct Biol 8(4):297-9
5) Baek GH, et al.  (2012) The Cdc48 protein and its cofactor Vms1 are involved in Cdc13 protein degradation. J Biol Chem 287(32):26788-95
6) Hartwell LH, et al.  (1970) Genetic control of the cell-division cycle in yeast. I. Detection of mutants. Proc Natl Acad Sci U S A 66(2):352-9
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41