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P36037

- DOA1_YEAST

UniProt

P36037 - DOA1_YEAST

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Protein

Protein DOA1

Gene

DOA1

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

Functioni

Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.2 Publications

GO - Molecular functioni

  1. ubiquitin binding Source: SGD

GO - Biological processi

  1. double-strand break repair via nonhomologous end joining Source: SGD
  2. ubiquitin-dependent protein catabolic process Source: SGD
  3. ubiquitin homeostasis Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31971-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DOA1
Gene namesi
Name:DOA1
Synonyms:UFD3, ZZZ4
Ordered Locus Names:YKL213C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL213c.
SGDiS000001696. DOA1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi541 – 5411R → A: Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. 1 Publication
Mutagenesisi669 – 6691R → A: Depletion of cellular ubiquitin pools and reduced activity of the ubiquitin fusion degradation pathway. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Protein DOA1PRO_0000050958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei332 – 3321Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36037.
PaxDbiP36037.
PeptideAtlasiP36037.

Expressioni

Gene expression databases

GenevestigatoriP36037.

Interactioni

Subunit structurei

Interacts with CDC48, OTU1 and ubiquitin.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC48P256945EBI-6017,EBI-4308
HSE1P387533EBI-6017,EBI-1382
UBP3Q014774EBI-6017,EBI-19834

Protein-protein interaction databases

BioGridi33952. 441 interactions.
DIPiDIP-6274N.
IntActiP36037. 9 interactions.
MINTiMINT-606421.
STRINGi4932.YKL213C.

Structurei

Secondary structure

1
715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi16 – 238Combined sources
Beta strandi26 – 316Combined sources
Beta strandi34 – 5219Combined sources
Beta strandi57 – 637Combined sources
Turni64 – 674Combined sources
Beta strandi68 – 736Combined sources
Beta strandi78 – 825Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi140 – 1478Combined sources
Turni148 – 1514Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi169 – 1746Combined sources
Beta strandi182 – 1898Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi200 – 2067Combined sources
Turni207 – 2093Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi241 – 2466Combined sources
Turni248 – 2503Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi284 – 2896Combined sources
Helixi291 – 2933Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi383 – 3919Combined sources
Beta strandi400 – 4045Combined sources
Helixi410 – 42011Combined sources
Helixi425 – 4273Combined sources
Helixi428 – 43811Combined sources
Helixi480 – 49415Combined sources
Helixi499 – 50911Combined sources
Helixi512 – 52918Combined sources
Helixi534 – 54310Combined sources
Helixi544 – 5463Combined sources
Helixi550 – 5534Combined sources
Helixi554 – 5607Combined sources
Helixi566 – 57914Combined sources
Turni583 – 5853Combined sources
Helixi586 – 5905Combined sources
Helixi593 – 5964Combined sources
Helixi599 – 6024Combined sources
Beta strandi608 – 6103Combined sources
Helixi612 – 63423Combined sources
Helixi642 – 65110Combined sources
Turni652 – 6565Combined sources
Helixi658 – 6625Combined sources
Helixi664 – 68017Combined sources
Helixi682 – 6854Combined sources
Turni688 – 6903Combined sources
Helixi692 – 70110Combined sources
Helixi705 – 71410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GAEX-ray1.60A/B464-715[»]
3L3FX-ray1.90X354-715[»]
3ODTX-ray1.35A/B2-300[»]
3PSPX-ray2.42A325-715[»]
3PSTX-ray2.00A325-715[»]
ProteinModelPortaliP36037.
SMRiP36037. Positions 2-295, 334-362, 376-715.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36037.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 4030WD 1Add
BLAST
Repeati53 – 8230WD 2Add
BLAST
Repeati97 – 12529WD 3Add
BLAST
Repeati135 – 16632WD 4Add
BLAST
Repeati177 – 20630WD 5Add
BLAST
Repeati218 – 24730WD 6Add
BLAST
Repeati259 – 28830WD 7Add
BLAST
Domaini352 – 44998PFUPROSITE-ProRule annotationAdd
BLAST
Domaini465 – 715251PULPROSITE-ProRule annotationAdd
BLAST
Repeati478 – 51235ARM 1Add
BLAST
Repeati513 – 54331ARM 2Add
BLAST
Repeati544 – 58239ARM 3Add
BLAST
Repeati583 – 63553ARM 4Add
BLAST
Repeati636 – 68045ARM 5Add
BLAST
Repeati681 – 71535ARM 6Add
BLAST

Domaini

The PUL domain is composed of 6 armadillo-like repeats and mediates the interaction with CDC48 C-terminus.
The PFU domain mediates interaction with ubiquitin.

Sequence similaritiesi

Belongs to the WD repeat PLAP family.Curated
Contains 6 ARM repeats.Curated
Contains 1 PFU domain.PROSITE-ProRule annotation
Contains 1 PUL domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000074944.
HOGENOMiHOG000174247.
InParanoidiP36037.
KOiK14018.
OMAiPAYDIVR.
OrthoDBiEOG7FR7QW.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR020472. G-protein_beta_WD-40_rep.
IPR015155. PLAA_fam_Ub-bd_PFU.
IPR013535. PUL.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF09070. PFU. 1 hit.
PF08324. PUL. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEiPS51394. PFU. 1 hit.
PS51396. PUL. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36037-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGYQLSATLK GHDQDVRDVV AVDDSKVASV SRDGTVRLWS KDDQWLGTVV
60 70 80 90 100
YTGQGFLNSV CYDSEKELLL FGGKDTMING VPLFATSGED PLYTLIGHQG
110 120 130 140 150
NVCSLSFQDG VVISGSWDKT AKVWKEGSLV YNLQAHNASV WDAKVVSFSE
160 170 180 190 200
NKFLTASADK TIKLWQNDKV IKTFSGIHND VVRHLAVVDD GHFISCSNDG
210 220 230 240 250
LIKLVDMHTG DVLRTYEGHE SFVYCIKLLP NGDIVSCGED RTVRIWSKEN
260 270 280 290 300
GSLKQVITLP AISIWSVDCM SNGDIIVGSS DNLVRIFSQE KSRWASEDEI
310 320 330 340 350
NELSTQVEKS TISSKTIEFD ESKLSPYEIL QSPGRKEGQI VVVKSPQGTI
360 370 380 390 400
EAHQFSNSSW KKVGDVVGAG ATGNDKKIEF EGKTYDYVFD VDIEDGKPPL
410 420 430 440 450
KLPINVSDNP YTAADNFLAR YELPMSYRDQ VVQFILKNTN GISLDQPNDN
460 470 480 490 500
ASSSAVSPSK TSVMKVLPVK QYLIMENYNP DTIFNGIVKI NSNEKTFDDE
510 520 530 540 550
ILAQIGGALH DIDESWELLL SFANTIRSNW EIKTPAYDIV RLIVKKLPYS
560 570 580 590 600
SDIKDYIEEG LGNKNITLTM LTVRILVNCF NNENWGVKLL ESNQVYKSIF
610 620 630 640 650
ETIDTEFSQA SAKQSQNLAI AVSTLIFNYS ALVTKGNSDL ELLPIVADAI
660 670 680 690 700
NTKYGPLEEY QECEEAAYRL TVAYGNLATV EPTLRQFANS VTWLANIKRS
710
YGNVPRFKDI FDDLS
Length:715
Mass (Da):79,506
Last modified:June 1, 1994 - v1
Checksum:i593B808169283B5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801D → DI AA sequence (PubMed:15096053)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39947 Genomic DNA. Translation: AAA82258.1.
X75951 Genomic DNA. Translation: CAA53560.1.
Z28213 Genomic DNA. Translation: CAA82058.1.
BK006944 Genomic DNA. Translation: DAA08956.1.
PIRiS38051.
RefSeqiNP_012709.1. NM_001179778.1.

Genome annotation databases

EnsemblFungiiYKL213C; YKL213C; YKL213C.
GeneIDi853667.
KEGGisce:YKL213C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39947 Genomic DNA. Translation: AAA82258.1 .
X75951 Genomic DNA. Translation: CAA53560.1 .
Z28213 Genomic DNA. Translation: CAA82058.1 .
BK006944 Genomic DNA. Translation: DAA08956.1 .
PIRi S38051.
RefSeqi NP_012709.1. NM_001179778.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GAE X-ray 1.60 A/B 464-715 [» ]
3L3F X-ray 1.90 X 354-715 [» ]
3ODT X-ray 1.35 A/B 2-300 [» ]
3PSP X-ray 2.42 A 325-715 [» ]
3PST X-ray 2.00 A 325-715 [» ]
ProteinModelPortali P36037.
SMRi P36037. Positions 2-295, 334-362, 376-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33952. 441 interactions.
DIPi DIP-6274N.
IntActi P36037. 9 interactions.
MINTi MINT-606421.
STRINGi 4932.YKL213C.

Proteomic databases

MaxQBi P36037.
PaxDbi P36037.
PeptideAtlasi P36037.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL213C ; YKL213C ; YKL213C .
GeneIDi 853667.
KEGGi sce:YKL213C.

Organism-specific databases

CYGDi YKL213c.
SGDi S000001696. DOA1.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00550000074944.
HOGENOMi HOG000174247.
InParanoidi P36037.
KOi K14018.
OMAi PAYDIVR.
OrthoDBi EOG7FR7QW.

Enzyme and pathway databases

BioCyci YEAST:G3O-31971-MONOMER.

Miscellaneous databases

EvolutionaryTracei P36037.
NextBioi 974605.
PROi P36037.

Gene expression databases

Genevestigatori P36037.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR016024. ARM-type_fold.
IPR020472. G-protein_beta_WD-40_rep.
IPR015155. PLAA_fam_Ub-bd_PFU.
IPR013535. PUL.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF09070. PFU. 1 hit.
PF08324. PUL. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEi PS51394. PFU. 1 hit.
PS51396. PUL. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Hochstrasser M., Gang G.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein."
    Tzermia M., Horaitis O., Alexandraki D.
    Yeast 10:663-679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues."
    Russell N.S., Wilkinson K.D.
    Biochemistry 43:4844-4854(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 126-144; 173-183; 215-227; 316-335; 345-361; 384-420; 534-541; 598-613; 654-685 AND 700-706, FUNCTION.
  6. "Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae."
    Ghislain M., Dohmen R.J., Levy F., Varshavsky A.
    EMBO J. 15:4884-4899(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone."
    Rumpf S., Jentsch S.
    Mol. Cell 21:261-269(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OTU1 AND CDC48.
  10. "Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain."
    Mullally J.E., Chernova T., Wilkinson K.D.
    Mol. Cell. Biol. 26:822-830(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBIQUITIN AND CDC48.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation."
    Zhao G., Li G., Schindelin H., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 106:16197-16202(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 464-715, INTERACTION WITH CDC48, ARM REPEATS, MUTAGENESIS OF ARG-541 AND ARG-669.
  15. "Crystal structure of a PFU-PUL domain pair of Saccharomyces cerevisiae Doa1/Ufd3."
    Nishimasu R., Komori H., Higuchi Y., Nishimasu H., Hiroaki H.
    Kobe J. Med. Sci. 56:E125-E139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 354-715, ARM REPEATS.

Entry informationi

Entry nameiDOA1_YEAST
AccessioniPrimary (citable) accession number: P36037
Secondary accession number(s): D6VWZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 136 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 6800 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3