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Q03233 (ADD37_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha1-proteinase inhibitor-degradation deficient protein 37
Gene names
Name:ADD37
Ordered Locus Names:YMR184W
ORF Names:YM8010.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in ER-associated protein degradation (ERAD). Ref.4

Subcellular location

Cytoplasm Ref.5.

Induction

In response to the DNA-damaging agent MMS. Ref.9

Miscellaneous

Present with 1270 molecules/cell in log phase SD medium.

Ontologies

Keywords
   Cellular componentCytoplasm
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated protein catabolic process

Inferred from mutant phenotype Ref.4. Source: SGD

   Cellular_componentcytoplasm

Inferred from direct assay Ref.5. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Alpha1-proteinase inhibitor-degradation deficient protein 37
PRO_0000203321

Amino acid modifications

Modified residue701Phosphothreonine Ref.10
Modified residue791Phosphoserine Ref.7 Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q03233 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2716B90391A82092

FASTA19822,110
        10         20         30         40         50         60 
MAIKPTKSFQ NCLEAEVPGY NDCPTVLFSI DPNSGPRSKS KQRTKSKRCV SGRLATEVLD 

        70         80         90        100        110        120 
LYGNTKTATT PPPVLRRPSV TAAQQESACE GVLVKDQGDR QLQPILCSKE ELVAKINDLC 

       130        140        150        160        170        180 
VCGSKLSSKE LEFYKKKLDS NITKILQNEH TKTVLSQIFN EKDKNMAVKT IKHWMVTDTT 

       190 
ISNWCPAFLK IFENAMPN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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: FUNCTION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY.
Strain: ADR376.
[8]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY.
[9]"Global protein expression profiling of budding yeast in response to DNA damage."
Lee M.-W., Kim B.-J., Choi H.-K., Ryu M.-J., Kim S.-B., Kang K.-M., Cho E.-J., Youn H.-D., Huh W.-K., Kim S.-T.
Yeast 24:145-154(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"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 THR-70, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49808 Genomic DNA. Translation: CAA89917.1.
AY557970 Genomic DNA. Translation: AAS56296.1.
BK006946 Genomic DNA. Translation: DAA10082.1.
PIRS55131.
RefSeqNP_013909.1. NM_001182690.1.

3D structure databases

ProteinModelPortalQ03233.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3848N.
IntActQ03233. 1 interaction.
MINTMINT-536444.
STRING4932.YMR184W.

Proteomic databases

PaxDbQ03233.
PeptideAtlasQ03233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR184W; YMR184W; YMR184W.
GeneID855222.
KEGGsce:YMR184W.

Organism-specific databases

CYGDYMR184w.
SGDS000004796. ADD37.

Phylogenomic databases

eggNOGNOG69217.
HOGENOMHOG000033805.
OMAPGYNDCP.
OrthoDBEOG4MKRS5.

Gene expression databases

GenevestigatorQ03233.
GermOnlineYMR184W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other

NextBio978744.

Entry information

Entry nameADD37_YEAST
AccessionPrimary (citable) accession number: Q03233
Secondary accession number(s): D6W008
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names