Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division control protein 4

Gene

CDC4

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

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.9 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • phosphoserine binding Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: SGD
  • G2/M transition of mitotic cell cycle Source: SGD
  • meiotic nuclear division Source: SGD
  • mitotic nuclear division Source: UniProtKB-KW
  • protein ubiquitination Source: SGD
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Sporulation, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-30447-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 4
Alternative name(s):
E3 ubiquitin ligase complex SCF subunit CDC4
F-box protein CDC4
Gene namesi
Name:CDC4
Ordered Locus Names:YFL009W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL009W.
SGDiS000001885. CDC4.

Subcellular locationi

GO - Cellular componenti

  • nuclear matrix Source: SGD
  • nuclear SCF ubiquitin ligase complex Source: SGD
  • nucleus Source: SGD
  • SCF ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821K → A: Prevents nuclear localization; when associated with A-83 and A-85.
Mutagenesisi83 – 831R → A: Prevents nuclear localization; when associated with A-82 and A-85.
Mutagenesisi83 – 831R → G: Prevents nuclear localization.
Mutagenesisi85 – 851K → A: Prevents nuclear localization; when associated with A-82 and A-83. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 779779Cell division control protein 4PRO_0000050899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07834.
PRIDEiP07834.

PTM databases

iPTMnetiP07834.

Interactioni

Subunit structurei

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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC53Q120188EBI-4434,EBI-4321
CIC1P387792EBI-4434,EBI-24538
HRT1Q082733EBI-4434,EBI-31686
SKP1P5228610EBI-4434,EBI-4090

GO - Molecular functioni

  • phosphoserine binding Source: SGD
  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi31138. 131 interactions.
DIPiDIP-1625N.
IntActiP07834. 10 interactions.
MINTiMINT-389524.

Structurei

Secondary structure

1
779
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi228 – 2347Combined sources
Helixi235 – 2373Combined sources
Helixi242 – 25312Combined sources
Helixi256 – 27116Combined sources
Helixi274 – 2774Combined sources
Helixi280 – 2878Combined sources
Helixi292 – 2998Combined sources
Helixi303 – 3097Combined sources
Helixi313 – 32210Combined sources
Turni328 – 3303Combined sources
Helixi331 – 34111Combined sources
Helixi347 – 36620Combined sources
Beta strandi373 – 3786Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi385 – 3917Combined sources
Beta strandi394 – 3996Combined sources
Beta strandi404 – 4085Combined sources
Turni409 – 4124Combined sources
Beta strandi413 – 4186Combined sources
Beta strandi425 – 4306Combined sources
Turni432 – 4343Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi445 – 4495Combined sources
Turni450 – 4534Combined sources
Beta strandi454 – 4596Combined sources
Beta strandi466 – 47611Combined sources
Beta strandi478 – 4847Combined sources
Beta strandi489 – 4935Combined sources
Beta strandi509 – 5146Combined sources
Helixi516 – 5183Combined sources
Beta strandi522 – 5265Combined sources
Beta strandi533 – 5397Combined sources
Beta strandi542 – 5476Combined sources
Beta strandi552 – 5565Combined sources
Turni557 – 5604Combined sources
Beta strandi561 – 5666Combined sources
Beta strandi573 – 5797Combined sources
Turni580 – 5834Combined sources
Beta strandi584 – 5896Combined sources
Beta strandi594 – 5985Combined sources
Beta strandi624 – 6285Combined sources
Beta strandi635 – 6406Combined sources
Beta strandi642 – 6498Combined sources
Beta strandi652 – 6587Combined sources
Turni659 – 6613Combined sources
Beta strandi664 – 6696Combined sources
Beta strandi676 – 6816Combined sources
Beta strandi683 – 6908Combined sources
Beta strandi693 – 6986Combined sources
Turni699 – 7013Combined sources
Beta strandi704 – 7074Combined sources
Turni709 – 7124Combined sources
Beta strandi714 – 7229Combined sources
Beta strandi725 – 7328Combined sources
Beta strandi735 – 7428Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEXX-ray2.70B/D263-744[»]
2P63X-ray2.67A/B/C/D222-273[»]
3MKSX-ray2.60B/D263-744[»]
3V7DX-ray2.31B/D263-744[»]
ProteinModelPortaliP07834.
SMRiP07834. Positions 222-744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07834.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 31948F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati380 – 40829WD 1Add
BLAST
Repeati420 – 44930WD 2Add
BLAST
Repeati461 – 49333WD 3Add
BLAST
Repeati528 – 55629WD 4Add
BLAST
Repeati568 – 59831WD 5Add
BLAST
Repeati630 – 65829WD 6Add
BLAST
Repeati669 – 69830WD 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi82 – 854Nuclear localization signal

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00820000127926.
HOGENOMiHOG000111495.
InParanoidiP07834.
KOiK03361.
OMAiCLQHDDE.
OrthoDBiEOG7X0VRS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR031740. Cdc4_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16856. CDC4_D. 1 hit.
PF12937. F-box-like. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSFPLAEFP LRDIPVPYSY RVSGGIASSG SVTALVTAAG THRNSSTAKT
60 70 80 90 100
VETEDGEEDI DEYQRKRAAG SGESTPERSD FKRVKHDNHK TLHPVNLQNT
110 120 130 140 150
GAASVDNDGL HNLTDISNDA EKLLMSVDDG SAAPSTLSVN MGVASHNVAA
160 170 180 190 200
PTTVNAATIT GSDVSNNVNS ATINNPMEEG ALPLSPTASS PGTTTPLAKT
210 220 230 240 250
TKTINNNNNI ADLIESKDSI ISPEYLSDEI FSAINNNLPH AYFKNLLFRL
260 270 280 290 300
VANMDRSELS DLGTLIKDNL KRDLITSLPF EISLKIFNYL QFEDIINSLG
310 320 330 340 350
VSQNWNKIIR KSTSLWKKLL ISENFVSPKG FNSLNLKLSQ KYPKLSQQDR
360 370 380 390 400
LRLSFLENIF ILKNWYNPKF VPQRTTLRGH MTSVITCLQF EDNYVITGAD
410 420 430 440 450
DKMIRVYDSI NKKFLLQLSG HDGGVWALKY AHGGILVSGS TDRTVRVWDI
460 470 480 490 500
KKGCCTHVFK GHNSTVRCLD IVEYKNIKYI VTGSRDNTLH VWKLPKESSV
510 520 530 540 550
PDHGEEHDYP LVFHTPEENP YFVGVLRGHM ASVRTVSGHG NIVVSGSYDN
560 570 580 590 600
TLIVWDVAQM KCLYILSGHT DRIYSTIYDH ERKRCISASM DTTIRIWDLE
610 620 630 640 650
NIWNNGECSY ATNSASPCAK ILGAMYTLQG HTALVGLLRL SDKFLVSAAA
660 670 680 690 700
DGSIRGWDAN DYSRKFSYHH TNLSAITTFY VSDNILVSGS ENQFNIYNLR
710 720 730 740 750
SGKLVHANIL KDADQIWSVN FKGKTLVAAV EKDGQSFLEI LDFSKASKIN
760 770
YVSNPVNSSS SSLESISTSL GLTRTTIIP
Length:779
Mass (Da):86,090
Last modified:November 1, 1995 - v2
Checksum:i0348F2F8FA78F3BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti460 – 4601K → E in CAA29113 (PubMed:3309335).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05625 Genomic DNA. Translation: CAA29113.1.
D50617 Genomic DNA. Translation: BAA09229.1.
Z46255 Genomic DNA. Translation: CAA86341.1.
BK006940 Genomic DNA. Translation: DAA12431.1.
PIRiS56245.
RefSeqiNP_116585.1. NM_001179957.1.

Genome annotation databases

EnsemblFungiiBAA09229; BAA09229; BAA09229.
YFL009W; YFL009W; YFL009W.
GeneIDi850539.
KEGGisce:YFL009W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05625 Genomic DNA. Translation: CAA29113.1.
D50617 Genomic DNA. Translation: BAA09229.1.
Z46255 Genomic DNA. Translation: CAA86341.1.
BK006940 Genomic DNA. Translation: DAA12431.1.
PIRiS56245.
RefSeqiNP_116585.1. NM_001179957.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEXX-ray2.70B/D263-744[»]
2P63X-ray2.67A/B/C/D222-273[»]
3MKSX-ray2.60B/D263-744[»]
3V7DX-ray2.31B/D263-744[»]
ProteinModelPortaliP07834.
SMRiP07834. Positions 222-744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31138. 131 interactions.
DIPiDIP-1625N.
IntActiP07834. 10 interactions.
MINTiMINT-389524.

PTM databases

iPTMnetiP07834.

Proteomic databases

MaxQBiP07834.
PRIDEiP07834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09229; BAA09229; BAA09229.
YFL009W; YFL009W; YFL009W.
GeneIDi850539.
KEGGisce:YFL009W.

Organism-specific databases

EuPathDBiFungiDB:YFL009W.
SGDiS000001885. CDC4.

Phylogenomic databases

GeneTreeiENSGT00820000127926.
HOGENOMiHOG000111495.
InParanoidiP07834.
KOiK03361.
OMAiCLQHDDE.
OrthoDBiEOG7X0VRS.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-30447-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07834.
PROiP07834.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR031740. Cdc4_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF16856. CDC4_D. 1 hit.
PF12937. F-box-like. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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.
  5. "Regulated degradation of the transcription factor Gcn4."
    Kornitzer D., Raboy B., Kulka R.G., Fink G.R.
    EMBO J. 13:6021-6030(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1/CBF3D.
    Strain: ATCC 204508 / S288c.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p."
    Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.
    Cell 91:221-230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle."
    Li F.N., Johnston M.
    EMBO J. 16:5629-5638(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SKP1.
  10. "The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast."
    Drury L.S., Perkins G., Diffley J.F.
    EMBO J. 16:5966-5976(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC6.
  11. "The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex."
    Jaquenoud M., Gulli M.P., Peter K., Peter M.
    EMBO J. 17:5360-5373(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  12. "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast."
    Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M.
    Genes Dev. 12:692-705(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC53.
  13. "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34."
    Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C., Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K., Shevchenko A., Deshaies R.J.
    Genes Dev. 13:1614-1626(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRT1.
  14. "Cdc4, a protein required for the onset of S phase, serves an essential function during G(2)/M transition in Saccharomyces cerevisiae."
    Goh P.Y., Surana U.
    Mol. Cell. Biol. 19:5512-5522(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1."
    Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W., Elledge S.J., Harper J.W.
    Science 284:662-665(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RECONSTITUTION OF THE SKF(GRR1)COMPLEX.
  16. "Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4."
    Blondel M., Galan J.M., Chi Y., Lafourcade C., Longaretti C., Deshaies R.J., Peter M.
    EMBO J. 19:6085-6097(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 82-LYS-ARG-83 AND LYS-85.
  17. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
    Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
    EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIC1.
  18. "Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro."
    Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.
    Proteins 54:455-467(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1, RECONSTITUTION OF THE SCF(CDC4) COMPLEX.
  19. "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases."
    Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.
    Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH SIC1.
  20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC4_YEAST
AccessioniPrimary (citable) accession number: P07834
Secondary accession number(s): D6VTM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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