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Protein

Coenzyme A biosynthesis protein 3

Gene

CAB3

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

Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis.2 Publications

GO - Molecular functioni

  1. phosphopantothenoylcysteine decarboxylase activity Source: SGD
  2. purine nucleotide binding Source: SGD

GO - Biological processi

  1. coenzyme A biosynthetic process Source: SGD
  2. response to salt stress Source: SGD
Complete GO annotation...

Keywords - Biological processi

Coenzyme A biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-299.
YEAST:MONOMER3O-299.
ReactomeiREACT_290756. Coenzyme A biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Coenzyme A biosynthesis protein 3
Gene namesi
Name:CAB3
Ordered Locus Names:YKL088W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

CYGDiYKL088w.
SGDiS000001571. CAB3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. CoA-synthesizing protein complex Source: SGD
  2. phosphopantothenoylcysteine decarboxylase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi478 – 4781C → S: Abolishes PPCDC activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571Coenzyme A biosynthesis protein 3PRO_0000182039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine3 Publications
Modified residuei116 – 1161Phosphoserine2 Publications
Modified residuei121 – 1211Phosphoserine2 Publications
Modified residuei124 – 1241Phosphoserine1 Publication
Modified residuei264 – 2641Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36076.
PaxDbiP36076.

Expressioni

Gene expression databases

GenevestigatoriP36076.

Interactioni

Subunit structurei

Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) complex, a heterotrimer composed of CAB3, HAL3 and VHS3.

Binary interactionsi

WithEntry#Exp.IntActNotes
PPZ1P265706EBI-26778,EBI-13807
PPZ2P333294EBI-26778,EBI-13815
SIS2P360243EBI-26778,EBI-17250
VHS3Q084384EBI-26778,EBI-30482

Protein-protein interaction databases

BioGridi34045. 28 interactions.
DIPiDIP-4475N.
IntActiP36076. 67 interactions.
MINTiMINT-541287.
STRINGi4932.YKL088W.

Structurei

3D structure databases

ProteinModelPortaliP36076.
SMRiP36076. Positions 307-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi508 – 57063Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0452.
GeneTreeiENSGT00440000038107.
InParanoidiP36076.
KOiK01598.
OMAiISIQLIV.
OrthoDBiEOG7N906N.

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.

Sequencei

Sequence statusi: Complete.

P36076-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDEKVNSDQ NMNGKQGVNL ISSLPTTQVP VSILTNKERR KSIHDESNFE
60 70 80 90 100
RSDSHEDQSK SNSNRRNIYK NDYSTNLRDF SFANLKQNSE RNKDGHEIQI
110 120 130 140 150
NTSMPANTNG QQKRFSPSLP SAVSFTVPEV ERLPYHRYSI SNKPGKQQQQ
160 170 180 190 200
QEQLQQNQQQ EEQQKAQLQE QNQRAKQQEE VKQIQEQVQK KQTERQQLID
210 220 230 240 250
EKERIANAIF KENTTNDGTD IRKHSVSSGT SNSEDEVDSP SMEKNSIVHM
260 270 280 290 300
PGDFIYFNPK SNASKPITAK AAPLSANNST HKNKEVITAP TGPRVPFTEF
310 320 330 340 350
FQKEDDKKFH ILIGATGSVA TIKVPLIIDK LFKIYGPEKI SIQLIVTKPA
360 370 380 390 400
EHFLKGLKMS THVKIWREED AWVFDAVNKN DTSLSLNLIL HHELRKWADI
410 420 430 440 450
FLIAPLSANT LAKLANGICN NLLTSVMRDW SPLTPVLIAP AMNTFMYINP
460 470 480 490 500
MTKKHLTSLV QDYPFIQVLK PVEKVLICGD IGMGGMREWT DIVEIVRRRI
510 520 530 540 550
NEIRKARDEE TGDKEQEQEE QEGADNEDDD DEDDEEDEED EEEEEALNET
560 570
ASDESNDEED EEDEEDVKTE V
Length:571
Mass (Da):65,238
Last modified:May 31, 1994 - v1
Checksum:i9C674C2394EFCEAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28088 Genomic DNA. Translation: CAA81926.1.
BK006944 Genomic DNA. Translation: DAA09070.1.
PIRiS37913.
RefSeqiNP_012835.1. NM_001179654.1.

Genome annotation databases

EnsemblFungiiYKL088W; YKL088W; YKL088W.
GeneIDi853774.
KEGGisce:YKL088W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28088 Genomic DNA. Translation: CAA81926.1.
BK006944 Genomic DNA. Translation: DAA09070.1.
PIRiS37913.
RefSeqiNP_012835.1. NM_001179654.1.

3D structure databases

ProteinModelPortaliP36076.
SMRiP36076. Positions 307-497.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34045. 28 interactions.
DIPiDIP-4475N.
IntActiP36076. 67 interactions.
MINTiMINT-541287.
STRINGi4932.YKL088W.

Proteomic databases

MaxQBiP36076.
PaxDbiP36076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL088W; YKL088W; YKL088W.
GeneIDi853774.
KEGGisce:YKL088W.

Organism-specific databases

CYGDiYKL088w.
SGDiS000001571. CAB3.

Phylogenomic databases

eggNOGiCOG0452.
GeneTreeiENSGT00440000038107.
InParanoidiP36076.
KOiK01598.
OMAiISIQLIV.
OrthoDBiEOG7N906N.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-299.
YEAST:MONOMER3O-299.
ReactomeiREACT_290756. Coenzyme A biosynthesis.

Miscellaneous databases

NextBioi974879.

Gene expression databases

GenevestigatoriP36076.

Family and domain databases

Gene3Di3.40.50.1950. 1 hit.
InterProiIPR003382. Flavoprotein.
[Graphical view]
PfamiPF02441. Flavoprotein. 1 hit.
[Graphical view]
SUPFAMiSSF52507. SSF52507. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-121 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1."
    Olzhausen J., Schuebbe S., Schueller H.-J.
    Curr. Genet. 55:163-173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis."
    Ruiz A., Gonzalez A., Munoz I., Serrano R., Abrie J.A., Strauss E., Arino J.
    Nat. Chem. Biol. 5:920-928(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-478, INTERACTION WITH HAL3 AND VHS3.
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAB3_YEAST
AccessioniPrimary (citable) accession number: P36076
Secondary accession number(s): D6VXK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: May 31, 1994
Last modified: March 31, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

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 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.