Reviewed, UniProtKB/Swiss-Prot P07834 (CDC4_YEAST)

Names and origin

Protein names

Recommended name:
    Cell division control protein 4
Alternative name(s):
    F-box protein CDC4
    E3 ubiquitin ligase complex SCF subunit CDC4

Gene names

Name:	CDC4
Ordered Locus Names:	YFL009W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	779 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. Required for HTA1-HTB1 locus transcription activation. Required for G1/S and G2/M transition.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with DCD53 and SKP1. Component of the SCF(CDC4) complex containing CDC53, SKP1, RBX1 and CDC4. CDC34. Interacts with CDC6 and CIC1. Interacts with SIC1; the interaction involves a SIC1 double phosphorylated motif (degron). Homodimerizes; the dimerization increases SIC1 ubiquitination in vitro.
Subcellular location	Nucleus.
Sequence similarities	Contains 1 F-box domain. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Sporulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Ref.13 Inferred from mutant phenotype. Source: SGD G2/M transition of mitotic cell cycle Ref.13 Inferred from genetic interaction. Source: SGD SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Ref.6 Ref.7 Inferred from direct assay. Source: SGD meiosis Inferred from mutant phenotype. Source: SGD protein ubiquitination during ubiquitin-dependent protein catabolic process Ref.6 Ref.7 Inferred from direct assay. Source: SGD
Cellular component	nuclear SCF ubiquitin ligase complex Ref.15 Inferred from direct assay. Source: SGD nuclear matrix Inferred from direct assay. Source: SGD
Molecular function	protein binding Ref.11 Ref.16 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC53	Q12018	2	EBI-4434,EBI-4321
CIC1	P38779	1	EBI-4434,EBI-24538
SKP1	P52286	3	EBI-4434,EBI-4090

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 779

779

Cell division control protein 4

Regions

Domain

272 – 319

48

F-box

Repeat

380 – 408

29

WD 1

Repeat

420 – 449

30

WD 2

Repeat

461 – 493

33

WD 3

Repeat

528 – 556

29

WD 4

Repeat

568 – 598

31

WD 5

Repeat

630 – 658

29

WD 6

Repeat

669 – 698

30

WD 7

Motif

82 – 85

4

Nuclear localization signal

Amino acid modifications

Modified residue

3

1

Phosphoserine

Modified residue

31

1

Phosphoserine

Experimental info

Mutagenesis

82

1

K → A: Prevents nuclear localization; when associated with A-83 and A-85

Mutagenesis

83

1

R → A: Prevents nuclear localization; when associated with A-82 and A-85

Mutagenesis

83

1

R → G: Prevents nuclear localization

Mutagenesis

85

1

K → A: Prevents nuclear localization; when associated with A-82 and A-83

Sequence conflict

460

1

K → E in CAA29113. Ref.1

Secondary structure

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779

Helix Strand Turn

Details...

Helix

228 – 234

7

Helix

235 – 237

3

Helix

242 – 253

12

Helix

274 – 277

4

Helix

280 – 287

8

Helix

292 – 298

7

Turn

299 – 301

3

Helix

303 – 310

8

Helix

314 – 322

9

Turn

328 – 330

3

Helix

331 – 341

11

Helix

347 – 366

20

Beta strand

373 – 378

6

Beta strand

381 – 383

3

Beta strand

385 – 391

7

Beta strand

394 – 399

6

Beta strand

402 – 408

7

Turn

409 – 412

4

Beta strand

413 – 419

7

Beta strand

425 – 431

7

Turn

432 – 434

3

Beta strand

435 – 440

6

Beta strand

445 – 449

5

Turn

450 – 453

4

Beta strand

454 – 459

6

Beta strand

466 – 474

9

Beta strand

477 – 484

8

Beta strand

487 – 493

7

Beta strand

511 – 514

4

Turn

516 – 518

3

Beta strand

522 – 527

6

Beta strand

533 – 539

7

Beta strand

542 – 547

6

Beta strand

552 – 556

5

Turn

557 – 560

4

Beta strand

561 – 566

6

Beta strand

573 – 579

7

Turn

580 – 583

4

Beta strand

584 – 589

6

Beta strand

594 – 598

5

Turn

599 – 601

3

Beta strand

624 – 628

5

Beta strand

637 – 640

4

Beta strand

642 – 648

7

Beta strand

652 – 658

7

Turn

659 – 661

3

Beta strand

664 – 669

6

Beta strand

678 – 681

4

Beta strand

683 – 690

8

Beta strand

693 – 698

6

Turn

699 – 701

3

Turn

709 – 712

4

Beta strand

714 – 722

9

Beta strand

725 – 734

10

Beta strand

736 – 742

7

Sequences

	Sequence		Length	Mass (Da)
	P07834-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 0348F2F8FA78F3BC	FASTA	779	86,090
	10 20 30 40 50 60 MGSFPLAEFP LRDIPVPYSY RVSGGIASSG SVTALVTAAG THRNSSTAKT VETEDGEEDI 70 80 90 100 110 120 DEYQRKRAAG SGESTPERSD FKRVKHDNHK TLHPVNLQNT GAASVDNDGL HNLTDISNDA 130 140 150 160 170 180 EKLLMSVDDG SAAPSTLSVN MGVASHNVAA PTTVNAATIT GSDVSNNVNS ATINNPMEEG 190 200 210 220 230 240 ALPLSPTASS PGTTTPLAKT TKTINNNNNI ADLIESKDSI ISPEYLSDEI FSAINNNLPH 250 260 270 280 290 300 AYFKNLLFRL VANMDRSELS DLGTLIKDNL KRDLITSLPF EISLKIFNYL QFEDIINSLG 310 320 330 340 350 360 VSQNWNKIIR KSTSLWKKLL ISENFVSPKG FNSLNLKLSQ KYPKLSQQDR LRLSFLENIF 370 380 390 400 410 420 ILKNWYNPKF VPQRTTLRGH MTSVITCLQF EDNYVITGAD DKMIRVYDSI NKKFLLQLSG 430 440 450 460 470 480 HDGGVWALKY AHGGILVSGS TDRTVRVWDI KKGCCTHVFK GHNSTVRCLD IVEYKNIKYI 490 500 510 520 530 540 VTGSRDNTLH VWKLPKESSV PDHGEEHDYP LVFHTPEENP YFVGVLRGHM ASVRTVSGHG 550 560 570 580 590 600 NIVVSGSYDN TLIVWDVAQM KCLYILSGHT DRIYSTIYDH ERKRCISASM DTTIRIWDLE 610 620 630 640 650 660 NIWNNGECSY ATNSASPCAK ILGAMYTLQG HTALVGLLRL SDKFLVSAAA DGSIRGWDAN 670 680 690 700 710 720 DYSRKFSYHH TNLSAITTFY VSDNILVSGS ENQFNIYNLR SGKLVHANIL KDADQIWSVN 730 740 750 760 770 FKGKTLVAAV EKDGQSFLEI LDFSKASKIN YVSNPVNSSS SSLESISTSL GLTRTTIIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural comparison of the yeast cell division cycle gene CDC4 and a related pseudogene." Yochem J., Byers B. J. Mol. Biol. 195:233-245(1987) [PubMed: 3309335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed: 7670463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Barrell B.G., Churcher C., Rajandream M.A. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-579. Strain: ATCC 204511 / S288c / AB972.
[4]	"Regulated degradation of the transcription factor Gcn4." Kornitzer D., Raboy B., Kulka R.G., Fink G.R. EMBO J. 13:6021-6030(1994) [PubMed: 7813440] [Abstract] Cited for: FUNCTION.
[5]	"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box." Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J. Cell 86:263-274(1996) [PubMed: 8706131] [Abstract] Cited for: INTERACTION WITH SKP1/CBF3D. Strain: ATCC 204508 / S288c.
[6]	"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex." Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W. Cell 91:209-219(1997) [PubMed: 9346238] [Abstract] Cited for: FUNCTION, SUBUNIT.
[7]	"A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the