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Protein

Protein SRN2

Gene

SRN2

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

Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for normal endocytic and biosynthetic traffic to the yeast vacuole.

GO - Biological processi

  • protein targeting to membrane Source: SGD
  • protein targeting to vacuole Source: SGD
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32264-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SRN2
Alternative name(s):
ESCRT-I complex subunit VPS37
Vacuolar protein sorting-associated protein 37
Gene namesi
Name:SRN2
Synonyms:SRN10, VPS37
Ordered Locus Names:YLR119W
ORF Names:L2958, L9233.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR119W.
SGDiS000004109. SRN2.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: SGD
  • ESCRT I complex Source: SGD
  • late endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671L → D: Defective in ESCRT-I cargo sorting. 1 Publication
Mutagenesisi75 – 751L → D: Defective in ESCRT-I cargo sorting. 1 Publication
Mutagenesisi79 – 791V → D: Defective in ESCRT-I cargo sorting. 1 Publication
Mutagenesisi88 – 881F → D: Defective in ESCRT-I cargo sorting; when associated with D-99. 1 Publication
Mutagenesisi92 – 921I → D: Defective in ESCRT-I cargo sorting; when associated with D-102. 1 Publication
Mutagenesisi95 – 951F → D: Defective in ESCRT-I cargo sorting; when associated with D-99. 1 Publication
Mutagenesisi99 – 991F → D: Defective in ESCRT-I cargo sorting; when associated with D-88. 1 Publication
Mutagenesisi99 – 991F → D: Defective in ESCRT-I cargo sorting; when associated with D-95. 1 Publication
Mutagenesisi102 – 1021L → D: Defective in ESCRT-I cargo sorting; when associated with D-92. 1 Publication
Mutagenesisi181 – 1811L → R: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVB); when associated with R-185. 1 Publication
Mutagenesisi185 – 1851I → R: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVB); when associated with R-181. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Protein SRN2PRO_0000072191Add
BLAST

Proteomic databases

MaxQBiQ99176.

Interactioni

Subunit structurei

Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoechiometry. Interacts with STP22 and MVB12.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MVB12P429396EBI-18076,EBI-23478
STP22P256045EBI-18076,EBI-411625

Protein-protein interaction databases

BioGridi31391. 177 interactions.
DIPiDIP-2130N.
IntActiQ99176. 4 interactions.
MINTiMINT-505977.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3311Combined sources
Helixi55 – 573Combined sources
Helixi62 – 709Combined sources
Helixi72 – 787Combined sources
Helixi79 – 824Combined sources
Helixi86 – 14358Combined sources
Beta strandi144 – 1463Combined sources
Helixi147 – 17024Combined sources
Helixi178 – 20528Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CAZX-ray3.60C/F130-213[»]
2F66X-ray2.80C/F132-213[»]
2P22X-ray2.70C22-213[»]
ProteinModelPortaliQ99176.
SMRiQ99176. Positions 22-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 21386VPS37 C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the VPS37 family.Curated
Contains 1 VPS37 C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000154416.
InParanoidiQ99176.
OMAiNERTEYH.
OrthoDBiEOG728938.

Family and domain databases

InterProiIPR017435. ESCRT-1_cplx_Vps37_fungi.
IPR009851. Mod_r.
[Graphical view]
PfamiPF07200. Mod_r. 1 hit.
[Graphical view]
PIRSFiPIRSF038214. ESCRT1_Vps37_fungi. 1 hit.
PROSITEiPS51314. VPS37_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVKATKLRI KQRRKNKGLN ISRLDIIRAE MDVVPSPGLP EKVNEKSKNI
60 70 80 90 100
PLPEGINLLS SKEIIDLIQT HRHQLELYVT KFNPLTDFAG KIHAFRDQFK
110 120 130 140 150
QLEENFEDLH EQKDKVQALL ENCRILESKY VASWQDYHSE FSKKYGDIAL
160 170 180 190 200
KKKLEQNTKK LDEESSQLET TTRSIDSADD LDQFIKNYLD IRTQYHLRRE
210
KLATWDKQGN LKY
Length:213
Mass (Da):25,101
Last modified:November 1, 1997 - v1
Checksum:i4E99806CED03E345
GO

Sequence cautioni

The sequence AAB88577.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901G → E in AAB88577 (PubMed:9790597).Curated
Sequence conflicti140 – 1401E → D in AAB88577 (PubMed:9790597).Curated
Sequence conflicti143 – 1431K → E in AAB88577 (PubMed:9790597).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40562 Genomic DNA. Translation: AAB88577.1. Different initiation.
X89514 Genomic DNA. Translation: CAA61698.1.
U53877 Genomic DNA. Translation: AAB82366.1.
Z73291 Genomic DNA. Translation: CAA97687.1.
BK006945 Genomic DNA. Translation: DAA09433.1.
PIRiS64956.
RefSeqiNP_013220.1. NM_001182006.1.

Genome annotation databases

EnsemblFungiiYLR119W; YLR119W; YLR119W.
GeneIDi850810.
KEGGisce:YLR119W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40562 Genomic DNA. Translation: AAB88577.1. Different initiation.
X89514 Genomic DNA. Translation: CAA61698.1.
U53877 Genomic DNA. Translation: AAB82366.1.
Z73291 Genomic DNA. Translation: CAA97687.1.
BK006945 Genomic DNA. Translation: DAA09433.1.
PIRiS64956.
RefSeqiNP_013220.1. NM_001182006.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CAZX-ray3.60C/F130-213[»]
2F66X-ray2.80C/F132-213[»]
2P22X-ray2.70C22-213[»]
ProteinModelPortaliQ99176.
SMRiQ99176. Positions 22-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31391. 177 interactions.
DIPiDIP-2130N.
IntActiQ99176. 4 interactions.
MINTiMINT-505977.

Proteomic databases

MaxQBiQ99176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR119W; YLR119W; YLR119W.
GeneIDi850810.
KEGGisce:YLR119W.

Organism-specific databases

EuPathDBiFungiDB:YLR119W.
SGDiS000004109. SRN2.

Phylogenomic databases

HOGENOMiHOG000154416.
InParanoidiQ99176.
OMAiNERTEYH.
OrthoDBiEOG728938.

Enzyme and pathway databases

BioCyciYEAST:G3O-32264-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ99176.
NextBioi967046.
PROiQ99176.

Family and domain databases

InterProiIPR017435. ESCRT-1_cplx_Vps37_fungi.
IPR009851. Mod_r.
[Graphical view]
PfamiPF07200. Mod_r. 1 hit.
[Graphical view]
PIRSFiPIRSF038214. ESCRT1_Vps37_fungi. 1 hit.
PROSITEiPS51314. VPS37_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of an extragenic suppressor of the rna1-1 mutation in Saccharomyces cerevisiae."
    Hong S.J., Yi Y.S., Koh S.S., Park O.K., Kang H.S.
    Mol. Gen. Genet. 259:404-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH RNA1, SUBCELLULAR LOCATION.
  2. "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
    Verhasselt P., Volckaert G.
    Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90840 / EAY235 / FY23.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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. "ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes."
    Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y., Emr S.D., Williams R.L.
    Cell 125:99-111(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 130-213 IN COMPLEX WITH STP22 AND VPS28.
  6. "Structural and functional organization of the ESCRT-I trafficking complex."
    Kostelansky M.S., Sun J., Lee S., Kim J., Ghirlando R., Hierro A., Emr S.D., Hurley J.H.
    Cell 125:113-126(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 132-213 IN COMPLEX WITH STP22 AND VPS28, MUTAGENESIS OF LEU-181 AND ILE-185.
  7. "Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer."
    Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B., Conibear E., Hurley J.H.
    Cell 129:485-498(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-213, COMPOSITION OF THE ESCRT-I COMPLEX, INTERACTION WITH STP22 AND MVB12, MUTAGENESIS OF LEU-67; LEU-75; VAL-79; PHE-88; ILE-92; PHE-95; PHE-99 AND LEU-102.

Entry informationi

Entry nameiSRN2_YEAST
AccessioniPrimary (citable) accession number: Q99176
Secondary accession number(s): D6VYB7, Q02806
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.