CDC3/YLR314C Protein Information

Standard Name	Cdc3p
Systematic Name	Ylr314cp
ORF Classification	Verified
Description	Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble with other septins into rod-like complexes that can associate with other rods to form filament polymers; septin rings at the mother-bud neck act as scaffolds for recruiting factors needed for cell division and as barriers to prevent diffusion of specific proteins between mother and daughter cells (1, 2, 3, 4, 5, 6)
Name Description	Cell Division Cycle 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	520
Molecular Weight (Da)	60,054
Isoelectric Point (pI)	5.14

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Cdc3p (InterPro)
Physical Interactions	There are 243 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000168B59 \| P32457 MIPS: YLR314C NCBI: 2507385 \| 295597 \| 330443676 \| 347595806 \| 662131 \| NP_013418.2 GenBank/EMBL/DDBJ: DAA09624.2 \| L16548 \| U20618

Amino Acid Sequence (or in FASTA format)
1 MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND 51 DSERFEAAES DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV 101 GFANLPKQWH RRSIKNGFSF NLLCVGPDGI GKTTLMKTLF NNDDIEANLV 151 KDYEEELAND QEEEEGQGEG HENQSQEQRH KVKIKSYESV IEENGVKLNL 201 NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI NRHSINDKRI 251 HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK 301 KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE 351 NYSGNQVRGR SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL 401 YENYRSSKLA KLGIKQDNSV FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT 451 VFQQKVSEKE KKLQKSETEL FARHKEMKEK LTKQLKALED KKKQLELSIN 501 SASPNVNHSP VPTKKKGFLR *

Amino Acid Sequence (or in FASTA format)

       1  MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND
      51  DSERFEAAES DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV
     101  GFANLPKQWH RRSIKNGFSF NLLCVGPDGI GKTTLMKTLF NNDDIEANLV
     151  KDYEEELAND QEEEEGQGEG HENQSQEQRH KVKIKSYESV IEENGVKLNL
     201  NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI NRHSINDKRI
     251  HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK
     301  KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE
     351  NYSGNQVRGR SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL
     401  YENYRSSKLA KLGIKQDNSV FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT
     451  VFQQKVSEKE KKLQKSETEL FARHKEMKEK LTKQLKALED KKKQLELSIN
     501  SASPNVNHSP VPTKKKGFLR *

external links for Cdc3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Cdc3p

1)	Takizawa PA, et al. (2000) Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290(5490):341-4
2)	Gladfelter AS, et al. (2001) The septin cortex at the yeast mother-bud neck. Curr Opin Microbiol 4(6):681-9
3)	Hanrahan J and Snyder M (2003) Cytoskeletal activation of a checkpoint kinase. Mol Cell 12(3):663-73
4)	Versele M, et al. (2004) Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol Biol Cell 15(10):4568-83
5)	Vrabioiu AM, et al. (2004) The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J Biol Chem 279(4):3111-8
6)	McMurray MA, et al. (2011) Septin filament formation is essential in budding yeast. Dev Cell 20(4):540-9
7)	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