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Protein

Proteasome assembly chaperone 2

Gene

ADD66

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in 20S proteasome assembly. Required for maximal proteasome activity. Affects the chymotrypsin-like activity of the proteasome. Can be degraded by the proteasome. Involved in the endoplasmic reticulum-associated degradation (ERAD).3 Publications

GO - Biological processi

  • proteasome assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-31965-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome assembly chaperone 2
Alternative name(s):
Alpha-1-proteinase inhibitor-degradation deficient protein 66
Proteasome biogenesis-associated protein 2
Gene namesi
Name:ADD66
Synonyms:PBA2, POC2
Ordered Locus Names:YKL206C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL206C.
SGDiS000001689. ADD66.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Proteasome assembly chaperone 2PRO_0000203132Add
BLAST

Proteomic databases

MaxQBiP36040.
PeptideAtlasiP36040.

Interactioni

Subunit structurei

Component of the 20S proteasome chaperone. Forms a heterodimer with PBA1 that binds to proteasome precursors.2 Publications

Protein-protein interaction databases

BioGridi33917. 35 interactions.
DIPiDIP-6515N.
MINTiMINT-700530.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi11 – 133Combined sources
Helixi14 – 2512Combined sources
Beta strandi28 – 358Combined sources
Beta strandi51 – 544Combined sources
Beta strandi67 – 759Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 856Combined sources
Helixi92 – 943Combined sources
Helixi95 – 10814Combined sources
Helixi109 – 1113Combined sources
Beta strandi113 – 1186Combined sources
Helixi183 – 1886Combined sources
Helixi220 – 2289Combined sources
Helixi247 – 2515Combined sources
Helixi258 – 2669Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G4SX-ray2.49P1-267[»]
ProteinModelPortaliP36040.
SMRiP36040. Positions 1-127, 181-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PSMG2 family.Curated

Phylogenomic databases

HOGENOMiHOG000066091.
InParanoidiP36040.
KOiK11880.
OrthoDBiEOG7T4MWK.

Family and domain databases

InterProiIPR019151. Proteasome_assmbl_chaperone_2.
IPR016562. Proteasome_assmbl_chp_2_euk.
[Graphical view]
PfamiPF09754. PAC2. 1 hit.
[Graphical view]
PIRSFiPIRSF010044. UCP010044. 1 hit.

Sequencei

Sequence statusi: Complete.

P36040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCLVLPLVS VGNIPQLSID WLLNSQANEW EYLEALDSKY LVEFVGPLDR
60 70 80 90 100
PEDGSDSLYK DADMKYSSAL EVFYNKKRGL FAIQQRTPLV SVNYLNNFIV
110 120 130 140 150
EIILPFLSKY NISEICIWDS LYAMEDENGV IVRPQEVYSL GEFYFDDEAE
160 170 180 190 200
LLSNLHLNDQ ESMVNNWLHF TPTSFQDKIS VDQPIFKILF QILNASQRPK
210 220 230 240 250
ALRSIKYCSC LANEGDNSLD SQQFLQWIIS QKVIKNAPPI VKFVRPISWQ
260
GAYGMADARD KFVDLYN
Length:267
Mass (Da):30,739
Last modified:June 1, 1994 - v1
Checksum:iD635C3EBC2E37C11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28206 Genomic DNA. Translation: CAA82051.1.
AY558394 Genomic DNA. Translation: AAS56720.1.
BK006944 Genomic DNA. Translation: DAA08963.1.
PIRiS38044.
RefSeqiNP_012716.1. NM_001179771.1.

Genome annotation databases

EnsemblFungiiYKL206C; YKL206C; YKL206C.
GeneIDi853629.
KEGGisce:YKL206C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28206 Genomic DNA. Translation: CAA82051.1.
AY558394 Genomic DNA. Translation: AAS56720.1.
BK006944 Genomic DNA. Translation: DAA08963.1.
PIRiS38044.
RefSeqiNP_012716.1. NM_001179771.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G4SX-ray2.49P1-267[»]
ProteinModelPortaliP36040.
SMRiP36040. Positions 1-127, 181-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33917. 35 interactions.
DIPiDIP-6515N.
MINTiMINT-700530.

Proteomic databases

MaxQBiP36040.
PeptideAtlasiP36040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL206C; YKL206C; YKL206C.
GeneIDi853629.
KEGGisce:YKL206C.

Organism-specific databases

EuPathDBiFungiDB:YKL206C.
SGDiS000001689. ADD66.

Phylogenomic databases

HOGENOMiHOG000066091.
InParanoidiP36040.
KOiK11880.
OrthoDBiEOG7T4MWK.

Enzyme and pathway databases

BioCyciYEAST:G3O-31965-MONOMER.

Miscellaneous databases

PROiP36040.

Family and domain databases

InterProiIPR019151. Proteasome_assmbl_chaperone_2.
IPR016562. Proteasome_assmbl_chp_2_euk.
[Graphical view]
PfamiPF09754. PAC2. 1 hit.
[Graphical view]
PIRSFiPIRSF010044. UCP010044. 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(1994) [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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Beta-subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint."
    Li X., Kusmierczyk A.R., Wong P., Emili A., Hochstrasser M.
    EMBO J. 26:2339-2349(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-76; 79-86; 179-187 AND 243-259, GENE NAME, INTERACTION WITH PBA1, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation."
    Palmer E.A., Kruse K.B., Fewell S.W., Buchanan S.M., Brodsky J.L., McCracken A.A.
    J. Cell Sci. 116:2361-2373(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME, FUNCTION, DELETION MUTANT.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly."
    Scott C.M., Kruse K.B., Schmidt B.Z., Perlmutter D.H., McCracken A.A., Brodsky J.L.
    Mol. Biol. Cell 18:3776-3787(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals."
    Le Tallec B., Barrault M.-B., Courbeyrette R., Guerois R., Marsolier-Kergoat M.-C., Peyroche A.
    Mol. Cell 27:660-674(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME, FUNCTION, INTERACTION WITH PBA1, SUBUNIT.

Entry informationi

Entry nameiPOC2_YEAST
AccessioniPrimary (citable) accession number: P36040
Secondary accession number(s): D6VWZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 112 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
Deletion induces the unfolded protein response (UPR).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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