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P01123

- YPT1_YEAST

UniProt

P01123 - YPT1_YEAST

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Protein

GTP-binding protein YPT1

Gene
YPT1, YP2, YFL038C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Regulates correct targeting and tethering of vesicles to target membranes by catalyzing the selective recruitment of proteins required for tethering and fusion onto membranes. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Required for sorting and transport of proteins from the ER through the Golgi compartment. Also involved in the recycling of membrane proteins.6 Publications

Enzyme regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factors (GEFs) DSS4 and TRAPP complex, and inactivated by GTPase-activating proteins (GAPs) GYP1, GYP5 and GYP8.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 228GTP By similarity
Nucleotide bindingi63 – 675GTP By similarity
Nucleotide bindingi121 – 1244GTP By similarity

GO - Molecular functioni

  1. GTPase activity Source: SGD
  2. GTP binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. SNARE binding Source: SGD

GO - Biological processi

  1. COPII-coated vesicle budding Source: SGD
  2. CVT pathway Source: SGD
  3. early endosome to Golgi transport Source: SGD
  4. endocytic recycling Source: SGD
  5. ER to Golgi vesicle-mediated transport Source: SGD
  6. Golgi vesicle budding Source: SGD
  7. Golgi vesicle docking Source: SGD
  8. GTP catabolic process Source: GOC
  9. macroautophagy Source: SGD
  10. pre-mRNA catabolic process Source: SGD
  11. protein complex assembly Source: SGD
  12. regulation of endoplasmic reticulum unfolded protein response Source: SGD
  13. retrograde vesicle-mediated transport, Golgi to ER Source: SGD
  14. small GTPase mediated signal transduction Source: InterPro
  15. SNARE complex disassembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30424-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein YPT1
Alternative name(s):
Protein YP2
Rab GTPase YPT1
Transport GTPase YPT1
Gene namesi
Name:YPT1
Synonyms:YP2
Ordered Locus Names:YFL038C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFL038c.
SGDiS000001856. YPT1.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cytoplasm
Note: ER and Golgi when GTP-bound. Cytoplasmic when bound to GDI1.1 Publication

GO - Cellular componenti

  1. cytoplasmic vesicle Source: SGD
  2. endoplasmic reticulum membrane Source: SGD
  3. Golgi membrane Source: SGD
  4. Golgi stack Source: SGD
  5. pre-autophagosomal structure Source: SGD
  6. trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171S → G: Decreases GTP binding and increases GTP hydrolysis. 1 Publication
Mutagenesisi21 – 211K → M: Abolishes GTP binding. 1 Publication
Mutagenesisi37 – 371Y → F: No change. 1 Publication
Mutagenesisi39 – 391S → A: No change. 1 Publication
Mutagenesisi40 – 401T → S: No change. 1 Publication
Mutagenesisi41 – 411I → M: Lethal. 1 Publication
Mutagenesisi43 – 431V → E: No change. 1 Publication
Mutagenesisi44 – 441D → N: Temperature-sensitive phenotype. 1 Publication
Mutagenesisi65 – 651A → T: Decreases GTP binding and GTP hydrolysis. 1 Publication
Mutagenesisi67 – 671Q → L: Locks YPT1 in the GTP-bound form by reducing GTP hydrolysis rate 40-fold. 2 Publications
Mutagenesisi121 – 1211N → I: Abolishes GTP binding. 1 Publication
Mutagenesisi136 – 1361A → D: Loss of function at 37 degrees Celsius. 2 Publications
Mutagenesisi205 – 2051C → S: Abolishes membrane association. Lethal; when associated with S-206. 2 Publications
Mutagenesisi206 – 2061C → S: Abolishes membrane association. Lethal; when associated with S-205. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206GTP-binding protein YPT1PRO_0000121318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei172 – 1721Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
Lipidationi205 – 2051N-palmitoyl cysteine; alternate1 Publication
Lipidationi205 – 2051S-geranylgeranyl cysteine; alternate1 Publication
Lipidationi206 – 2061N-palmitoyl cysteine; alternate1 Publication
Lipidationi206 – 2061S-geranylgeranyl cysteine; alternate1 Publication

Post-translational modificationi

Prenylation is required for interaction with GDI1 and YIP1.

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP01123.
PaxDbiP01123.
PeptideAtlasiP01123.
PRIDEiP01123.

Expressioni

Gene expression databases

GenevestigatoriP01123.

Interactioni

Subunit structurei

Forms a complex with the Rab escort protein (REP) MRS6, which is recognized by Rab geranylgeranyltransferase BET2-BET4. Interacts with the Rab GDP dissociation inhibitor GDI1, which can retrieve from and deliver to membranes the GDP-bound and prenylated form of YPT1. Interacts with YIP1, which is required for proper membrane targeting of prenylated YPT1. Interacts with YIF1, YIP3, YIP4 and YIP5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GDI1P399585EBI-29496,EBI-7517
YIF1P538453EBI-29496,EBI-28230
YIP3P536332EBI-29496,EBI-25301
YIP4P530932EBI-29496,EBI-24124

Protein-protein interaction databases

BioGridi31108. 132 interactions.
DIPiDIP-2019N.
IntActiP01123. 23 interactions.
MINTiMINT-389361.
STRINGi4932.YFL038C.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1611
Helixi21 – 3010
Beta strandi45 – 528
Beta strandi55 – 628
Turni65 – 717
Helixi75 – 784
Beta strandi82 – 898
Helixi93 – 10917
Beta strandi115 – 1217
Turni126 – 1283
Helixi133 – 14210
Beta strandi147 – 1493
Turni152 – 1543
Helixi158 – 17215
Helixi175 – 1795
Helixi183 – 1853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKVX-ray1.50Y1-206[»]
1YZNX-ray2.06A3-172[»]
2BCGX-ray1.48Y1-206[»]
3CUEX-ray3.70F/L/R/X1-206[»]
ProteinModelPortaliP01123.
SMRiP01123. Positions 3-196.

Miscellaneous databases

EvolutionaryTraceiP01123.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 8018Interaction with GDI1Add
BLAST
Regioni189 – 1957Interaction with GDI1

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 459Effector region Inferred

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00720000108592.
HOGENOMiHOG000233968.
KOiK07874.
OMAiTMHASEY.
OrthoDBiEOG7BGHXR.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01123-1 [UniParc]FASTAAdd to Basket

« Hide

MNSEYDYLFK LLLIGNSGVG KSCLLLRFSD DTYTNDYIST IGVDFKIKTV    50
ELDGKTVKLQ IWDTAGQERF RTITSSYYRG SHGIIIVYDV TDQESFNGVK 100
MWLQEIDRYA TSTVLKLLVG NKCDLKDKRV VEYDVAKEFA DANKMPFLET 150
SALDSTNVED AFLTMARQIK ESMSQQNLNE TTQKKEDKGN VNLKGQSLTN 200
TGGGCC 206
Length:206
Mass (Da):23,214
Last modified:November 1, 1995 - v2
Checksum:iF8C704F6BF2D227B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711E → Q in CAA25036. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00209 Genomic DNA. Translation: CAA25036.1.
D50617 Genomic DNA. Translation: BAA09201.1.
AY558467 Genomic DNA. Translation: AAS56793.1.
BK006940 Genomic DNA. Translation: DAA12402.1.
PIRiS56216. TVBYQ2.
RefSeqiNP_116615.1. NM_001179928.1.

Genome annotation databases

EnsemblFungiiYFL038C; YFL038C; YFL038C.
GeneIDi850505.
KEGGisce:YFL038C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00209 Genomic DNA. Translation: CAA25036.1 .
D50617 Genomic DNA. Translation: BAA09201.1 .
AY558467 Genomic DNA. Translation: AAS56793.1 .
BK006940 Genomic DNA. Translation: DAA12402.1 .
PIRi S56216. TVBYQ2.
RefSeqi NP_116615.1. NM_001179928.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UKV X-ray 1.50 Y 1-206 [» ]
1YZN X-ray 2.06 A 3-172 [» ]
2BCG X-ray 1.48 Y 1-206 [» ]
3CUE X-ray 3.70 F/L/R/X 1-206 [» ]
ProteinModelPortali P01123.
SMRi P01123. Positions 3-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31108. 132 interactions.
DIPi DIP-2019N.
IntActi P01123. 23 interactions.
MINTi MINT-389361.
STRINGi 4932.YFL038C.

Proteomic databases

MaxQBi P01123.
PaxDbi P01123.
PeptideAtlasi P01123.
PRIDEi P01123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFL038C ; YFL038C ; YFL038C .
GeneIDi 850505.
KEGGi sce:YFL038C.

Organism-specific databases

CYGDi YFL038c.
SGDi S000001856. YPT1.

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00720000108592.
HOGENOMi HOG000233968.
KOi K07874.
OMAi TMHASEY.
OrthoDBi EOG7BGHXR.

Enzyme and pathway databases

BioCyci YEAST:G3O-30424-MONOMER.

Miscellaneous databases

EvolutionaryTracei P01123.
NextBioi 966209.
PROi P01123.

Gene expression databases

Genevestigatori P01123.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product."
    Gallwitz D., Donath C., Sander C.
    Nature 306:704-707(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-46; 49-55; 59-69; 72-79; 101-116 AND 130-167, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Biochemical properties of the ras-related YPT protein in yeast: a mutational analysis."
    Wagner P., Molenaar C.M.T., Rauh A.J.G., Broekel R., Schmitt H.D., Gallwitz D.
    EMBO J. 6:2373-2379(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-17; LYS-21; ALA-65 AND ASN-121.
  7. "A carboxyl-terminal cysteine residue is required for palmitic acid binding and biological activity of the ras-related yeast YPT1 protein."
    Molenaar C.M.T., Prange R., Gallwitz D.
    EMBO J. 7:971-976(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF CYS-205 AND CYS-206.
  8. "Study of a temperature-sensitive mutant of the ras-related YPT1 gene product in yeast suggests a role in the regulation of intracellular calcium."
    Schmitt H.D., Puzicha M., Gallwitz D.
    Cell 53:635-647(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, POSSIBLE FUNCTION.
  9. "Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity."
    Becker J., Tan T.J., Trepte H.-H., Gallwitz D.
    EMBO J. 10:785-792(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-37; SER-39; THR-40; ILE-41; VAL-43 AND ASP-44.
  10. "The Ypt1 GTPase is essential for the first two steps of the yeast secretory pathway."
    Jedd G., Richardson C.J., Litt R.J., Segev N.
    J. Cell Biol. 131:583-590(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-136.
  11. "Amino- and carboxy-terminal domains of the yeast Rab escort protein are both required for binding of Ypt small G proteins."
    Bauer B.E., Lorenzetti S., Miaczynska M., Bui D.M., Schweyen R.J., Ragnini A.
    Mol. Biol. Cell 7:1521-1533(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MRS6.
  12. "GTP hydrolysis is not important for Ypt1 GTPase function in vesicular transport."
    Richardson C.J., Jones S., Litt R.J., Segev N.
    Mol. Cell. Biol. 18:827-838(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLN-67.
  13. "Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner."
    Day G.-J., Mosteller R.D., Broek D.
    Mol. Cell. Biol. 18:7444-7454(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  14. "Functional implications of genetic interactions between genes encoding small GTPases involved in vesicular transport in yeast."
    Yoo J.S., Grabowski R., Xing L., Trepte H.H., Schmitt H.D., Gallwitz D.
    Mol. Gen. Genet. 261:80-91(1999)
    Cited for: ISOPRENYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF CYS-205 AND CYS-206, FUNCTION.
  15. "The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32."
    Jones S., Newman C., Liu F., Segev N.
    Mol. Biol. Cell 11:4403-4411(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  16. "Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p."
    Du L.-L., Novick P.
    Mol. Biol. Cell 12:1215-1226(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  17. "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins."
    Calero M., Collins R.N.
    Biochem. Biophys. Res. Commun. 290:676-681(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YIP3.
  18. "The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus."
    Morsomme P., Riezman H.
    Dev. Cell 2:307-317(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors."
    Calero M., Winand N.J., Collins R.N.
    FEBS Lett. 515:89-98(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YIF1; YIP4 AND YIP5.
  20. "Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs."
    De Antoni A., Schmitzova J., Trepte H.-H., Gallwitz D., Albert S.
    J. Biol. Chem. 277:41023-41031(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  21. "Dual prenylation is required for Rab protein localization and function."
    Calero M., Chen C.Z., Zhu W., Winand N.J., Havas K.A., Gilbert P.M., Burd C.G., Collins R.N.
    Mol. Biol. Cell 14:1852-1867(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YIP1, SUBCELLULAR LOCATION.
  22. "The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p."
    Lafourcade C., Galan J.-M., Gloor Y., Haguenauer-Tsapis R., Peter M.
    Mol. Cell. Biol. 24:3815-3826(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-67.
  23. "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-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase."
    Rak A., Pylypenko O., Durek T., Watzke A., Kushnir S., Brunsveld L., Waldmann H., Goody R.S., Alexandrov K.
    Science 302:646-650(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH GDI1.

Entry informationi

Entry nameiYPT1_YEAST
AccessioniPrimary (citable) accession number: P01123
Secondary accession number(s): D6VTJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

In 1 Publication the location of any palmitoylation was not determined. Mutagenesis of either Cys-205 or Cys-206 would disrupt normal geranylgeranylation, and there would be no primary membrane association for secondary S-palmitoylation to occur at some other position, for example Cys-23. Mutagenesis of both Cys-205 and Cys-206 is lethal, so protein production could not have been observed.

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

External Data

Dasty 3

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