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Protein

Autophagy-related protein 19

Gene

ATG19

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

Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth.16 Publications

GO - Molecular functioni

  • protein binding, bridging Source: SGD

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • CVT pathway Source: SGD
  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • protein complex localization Source: SGD
  • protein processing Source: SGD
  • vesicle organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33485-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Autophagy-related protein 19
Alternative name(s):
Cytoplasm-to-vacuole targeting protein 19
Gene namesi
Name:ATG19
Synonyms:CVT19
Ordered Locus Names:YOL082W
ORF Names:O0980, YOL01
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL082W.
SGDiS000005442. ATG19.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extrinsic component of membrane Source: SGD
  • pre-autophagosomal structure Source: SGD
  • pre-autophagosomal structure membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Biotechnological usei

ATG19 is important for yeast autolysis which is the source of several molecules responsible for the quality of wines aged in contact with yeast cells.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi412 – 4121W → A: Impairs vacuolar transport of LAP4. 1 Publication
Mutagenesisi415 – 4151L → A: Impairs vacuolar transport of LAP4. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Autophagy-related protein 19PRO_0000064722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei141 – 1411PhosphoserineCombined sources
Cross-linki213 – 213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki216 – 216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei243 – 2431PhosphoserineCombined sources

Post-translational modificationi

Polyubiquitinated at Lys-213 and Lys-216. Deubiquitination by UBP3 is required for full activity of ATG19.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35193.

PTM databases

iPTMnetiP35193.

Interactioni

Subunit structurei

Interacts with the vacuolar aminopeptidase 1 (LAP4) precursor and mature forms. Also interacts with AMS1, APE4, ATG8 ATG11, and UBP3.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG1P531042EBI-29291,EBI-2657
ATG11Q125274EBI-29291,EBI-31977
HRR25P292952EBI-29291,EBI-8536

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi34320. 56 interactions.
DIPiDIP-1407N.
IntActiP35193. 22 interactions.
MINTiMINT-387666.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi262 – 2698Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi295 – 2995Combined sources
Beta strandi318 – 3225Combined sources
Beta strandi335 – 3384Combined sources
Beta strandi342 – 3487Combined sources
Beta strandi352 – 3543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZBNMR-A254-367[»]
2ZPNX-ray2.70E/F/G/H412-415[»]
ProteinModelPortaliP35193.
SMRiP35193. Positions 254-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35193.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 288ATG11-binding
Regioni254 – 367114AMS1-bindingAdd
BLAST
Regioni406 – 41510ATG8-binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili157 – 18731Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi412 – 4154WXXL

Domaini

The coiled coil domain is required for the interaction with LAP4.
The C-terminal WXXL motif is crucial for ATG8-binding and Cvt pathway.

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00530000068761.
InParanoidiP35193.
OrthoDBiEOG7WX0JR.

Family and domain databases

InterProiIPR024543. Atg19/Atg34_C.
[Graphical view]
PfamiPF12744. ATG19_autophagy. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNSKTNQQM NTSMGYPLTV YDECNKFQLI VPTLDANIML WCIGQLSLLN
60 70 80 90 100
DSNGCKHLFW QPNDKSNVRI LLNNYDYGHL FKYLQCQRKC SVYIGEGTLK
110 120 130 140 150
KYNLTISTSF DNFLDLTPSE EKESLCREDA HEDPVSPKAG SEEEISPNST
160 170 180 190 200
SNVVVSRECL DNFMKQLLKL EESLNKLELE QKVTNKEPNH RISGTIDIPE
210 220 230 240 250
DRSELVNFFT ELKTVKQLED VFQRYHDYER LSQECDSKTE IASDHSKKET
260 270 280 290 300
KIEVEPPNER SLQITMNQRD NSLYFQLFNN TNSVLAGNCK LKFTDAGDKP
310 320 330 340 350
TTQIIDMGPH EIGIKEYKEY RYFPYALDLE AGSTIEIENQ YGEVIFLGKY
360 370 380 390 400
GSSPMINLRP PSRLSAESLQ ASQEPFYSFQ IDTLPELDDS SIISTSISLS
410
YDGDDNEKAL TWEEL
Length:415
Mass (Da):47,599
Last modified:February 1, 1994 - v1
Checksum:iB49DA1DF83A04070
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti412 – 4121W → R in AAT93193 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75449 Genomic DNA. Translation: CAA53201.1.
X83121 Genomic DNA. Translation: CAA58199.1.
Z74824 Genomic DNA. Translation: CAA99094.1.
AY693174 Genomic DNA. Translation: AAT93193.1.
BK006948 Genomic DNA. Translation: DAA10702.1.
PIRiS48253.
RefSeqiNP_014559.1. NM_001183336.1.

Genome annotation databases

EnsemblFungiiYOL082W; YOL082W; YOL082W.
GeneIDi854072.
KEGGisce:YOL082W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75449 Genomic DNA. Translation: CAA53201.1.
X83121 Genomic DNA. Translation: CAA58199.1.
Z74824 Genomic DNA. Translation: CAA99094.1.
AY693174 Genomic DNA. Translation: AAT93193.1.
BK006948 Genomic DNA. Translation: DAA10702.1.
PIRiS48253.
RefSeqiNP_014559.1. NM_001183336.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZBNMR-A254-367[»]
2ZPNX-ray2.70E/F/G/H412-415[»]
ProteinModelPortaliP35193.
SMRiP35193. Positions 254-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34320. 56 interactions.
DIPiDIP-1407N.
IntActiP35193. 22 interactions.
MINTiMINT-387666.

PTM databases

iPTMnetiP35193.

Proteomic databases

MaxQBiP35193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL082W; YOL082W; YOL082W.
GeneIDi854072.
KEGGisce:YOL082W.

Organism-specific databases

EuPathDBiFungiDB:YOL082W.
SGDiS000005442. ATG19.

Phylogenomic databases

GeneTreeiENSGT00530000068761.
InParanoidiP35193.
OrthoDBiEOG7WX0JR.

Enzyme and pathway databases

BioCyciYEAST:G3O-33485-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35193.
NextBioi975692.
PROiP35193.

Family and domain databases

InterProiIPR024543. Atg19/Atg34_C.
[Graphical view]
PfamiPF12744. ATG19_autophagy. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 10.27 kb segment on the left arm of chromosome XV from Saccharomyces cerevisiae includes part of the IRA2 gene and a putative new gene."
    Zumstein E., Griffin H., Schweizer M.
    Yeast 10:1383-1387(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames."
    Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.
    Yeast 11:975-986(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Yol082p, a novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole."
    Leber R., Silles E., Sandoval I.V., Mazon M.J.
    J. Biol. Chem. 276:29210-29217(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LAP4.
  7. "Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway."
    Scott S.V., Guan J., Hutchins M.U., Kim J., Klionsky D.J.
    Mol. Cell 7:1131-1141(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LAP4.
  8. "Studies of cargo delivery to the vacuole mediated by autophagosomes in Saccharomyces cerevisiae."
    Suzuki K., Kamada Y., Ohsumi Y.
    Dev. Cell 3:815-824(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway."
    Shintani T., Huang W.-P., Stromhaug P.E., Klionsky D.J.
    Dev. Cell 3:825-837(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LAP4; AMS1; ATG8 AND ATG11.
  10. "Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation."
    Kim J., Huang W.-P., Stromhaug P.E., Klionsky D.J.
    J. Biol. Chem. 277:763-773(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ATG8.
  11. Cited for: NOMENCLATURE.
  12. "Vps51 is part of the yeast Vps fifty-three tethering complex essential for retrograde traffic from the early endosome and Cvt vesicle completion."
    Reggiori F., Wang C.-W., Stromhaug P.E., Shintani T., Klionsky D.J.
    J. Biol. Chem. 278:5009-5020(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  15. "Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway."
    Shintani T., Klionsky D.J.
    J. Biol. Chem. 279:29889-29894(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Atg21 is required for effective recruitment of Atg8 to the preautophagosomal structure during the Cvt pathway."
    Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D., Thumm M.
    J. Biol. Chem. 279:37741-37750(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Evidence for yeast autophagy during simulation of sparkling wine aging: a reappraisal of the mechanism of yeast autolysis in wine."
    Cebollero E., Carrascosa A.V., Gonzalez R.
    Biotechnol. Prog. 21:614-616(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOTECHNOLOGY.
  18. "Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in yeast."
    Baxter B.K., Abeliovich H., Zhang X., Stirling A.G., Burlingame A.L., Goldfarb D.S.
    J. Biol. Chem. 280:39067-39076(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-213 AND LYS-216, INTERACTION WITH UBP3, FUNCTION.
  19. "Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway."
    Yorimitsu T., Klionsky D.J.
    Mol. Biol. Cell 16:1593-1605(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG11.
  20. "Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response."
    Bernales S., McDonald K.L., Walter P.
    PLoS Biol. 4:E423-E423(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Overexpression of autophagy-related genes inhibits yeast filamentous growth."
    Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.
    Autophagy 3:604-609(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy."
    Chang C.Y., Huang W.P.
    Mol. Biol. Cell 18:919-929(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG8 AND ATG11, SUBCELLULAR LOCATION.
  23. "Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway."
    Mazon M.J., Eraso P., Portillo F.
    Mol. Microbiol. 63:1069-1077(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Localization of autophagy-related proteins in yeast using a versatile plasmid-based resource of fluorescent protein fusions."
    Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.
    Autophagy 4:792-800(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  26. "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-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Mutation at the cargo-receptor binding site of Atg8 also affects its general autophagy regulation function."
    Ho K.H., Chang H.E., Huang W.P.
    Autophagy 5:461-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG8.
  28. "Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae."
    Kageyama T., Suzuki K., Ohsumi Y.
    Biochem. Biophys. Res. Commun. 378:551-557(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "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-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "A new autophagy-related checkpoint in the degradation of an ERAD-M target."
    Kario E., Amar N., Elazar Z., Navon A.
    J. Biol. Chem. 286:11479-11491(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae."
    Yuga M., Gomi K., Klionsky D.J., Shintani T.
    J. Biol. Chem. 286:13704-13713(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APE4.
  32. "Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle formation in cytoplasm-to-vacuole targeting pathway."
    Morales Quinones M., Winston J.T., Stromhaug P.E.
    J. Biol. Chem. 287:10121-10133(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAP4.
  33. "Structural basis of target recognition by Atg8/LC3 during selective autophagy."
    Noda N.N., Kumeta H., Nakatogawa H., Satoo K., Adachi W., Ishii J., Fujioka Y., Ohsumi Y., Inagaki F.
    Genes Cells 13:1211-1218(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 412-415 IN COMPLEX WITH ATG8, DOMAIN, MUTAGENESIS OF TRP-412 AND LEU-415, FUNCTION.
  34. "Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34."
    Watanabe Y., Noda N.N., Kumeta H., Suzuki K., Ohsumi Y., Inagaki F.
    J. Biol. Chem. 285:30026-30033(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 254-367, FUNCTION, DOMAIN, INTERACTION WITH AMS1.

Entry informationi

Entry nameiATG19_YEAST
AccessioniPrimary (citable) accession number: P35193
Secondary accession number(s): D6W1Y6, Q6B1A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 131 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 1250 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.