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Protein

Multivesicular body sorting factor 12

Gene

MVB12

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. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Appears to be involved in cargo sorting and release of the ESCRT-I complex from the MVBs.1 Publication

GO - Molecular functioni

  1. ubiquitin binding Source: SGD

GO - Biological processi

  1. endosome transport via multivesicular body sorting pathway Source: SGD
  2. negative regulation of protein complex assembly Source: SGD
  3. protein targeting to vacuole Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30889-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Multivesicular body sorting factor 12
Alternative name(s):
12 kDa multivesicular body sorting factor
ESCRT-I complex subunit MVB12
Gene namesi
Name:MVB12
Ordered Locus Names:YGR206W
ORF Names:G7740
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR206w.
SGDiS000003438. MVB12.

Subcellular locationi

Cytoplasm 1 Publication. Endosome 1 Publication. Late endosome membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. endosome Source: SGD
  3. ESCRT I complex Source: SGD
  4. late endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471L → D: Defective in MVB12 incorporation in ESCRT-I complex; reduces localization to MVBs; abolishes interaction with STP22 and SRN2; when associated with D-57.
Mutagenesisi54 – 541C → D: Defective in MVB12 incorporation in ESCRT-I complex; when associated with D-57. 1 Publication
Mutagenesisi57 – 571I → D: Defective in MVB12 incorporation in ESCRT-I complex; reduces localization to MVBs; abolishes interaction with STP22 and SRN2; when associated with D-47. 1 Publication
Mutagenesisi64 – 641H → D: Defective in MVB12 incorporation in ESCRT-I complex; when associated with D-47. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Multivesicular body sorting factor 12PRO_0000202845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei94 – 941Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42939.
PaxDbiP42939.

Expressioni

Gene expression databases

GenevestigatoriP42939.

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 SRN2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SRN2Q991766EBI-23478,EBI-18076
STP22P256046EBI-23478,EBI-411625

Protein-protein interaction databases

BioGridi33459. 29 interactions.
DIPiDIP-5332N.
IntActiP42939. 3 interactions.
MINTiMINT-508989.
STRINGi4932.YGR206W.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Beta strandi15 – 195Combined sources
Helixi41 – 6525Combined sources
Helixi67 – 7812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P22X-ray2.70D4-81[»]
ProteinModelPortaliP42939.
SMRiP42939. Positions 4-81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42939.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG71344.
HOGENOMiHOG000000939.
InParanoidiP42939.
KOiK12187.
OMAiEECDNIT.
OrthoDBiEOG72C5D4.

Family and domain databases

InterProiIPR019014. ESCRT-I_cplx_su_Mvb12.
[Graphical view]
PfamiPF09452. Mvb12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42939-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNNVEELLR RIPLYNKYGK DFPQETVTRF QMPEFKLPAL QPTRDLLCPW
60 70 80 90 100
YEECDNITKV CQLHDSSNKK FDQWYKEQYL SKKPPGIVGN TLLSPSRKDN

S
Length:101
Mass (Da):11,968
Last modified:November 1, 1995 - v1
Checksum:iE48B085E0FACBAC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49133 Genomic DNA. Translation: CAA88999.1.
Z72991 Genomic DNA. Translation: CAA97233.1.
AY692570 Genomic DNA. Translation: AAT92589.1.
BK006941 Genomic DNA. Translation: DAA08300.1.
PIRiS53929.
RefSeqiNP_011722.3. NM_001181335.3.

Genome annotation databases

EnsemblFungiiYGR206W; YGR206W; YGR206W.
GeneIDi853120.
KEGGisce:YGR206W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49133 Genomic DNA. Translation: CAA88999.1.
Z72991 Genomic DNA. Translation: CAA97233.1.
AY692570 Genomic DNA. Translation: AAT92589.1.
BK006941 Genomic DNA. Translation: DAA08300.1.
PIRiS53929.
RefSeqiNP_011722.3. NM_001181335.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P22X-ray2.70D4-81[»]
ProteinModelPortaliP42939.
SMRiP42939. Positions 4-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33459. 29 interactions.
DIPiDIP-5332N.
IntActiP42939. 3 interactions.
MINTiMINT-508989.
STRINGi4932.YGR206W.

Proteomic databases

MaxQBiP42939.
PaxDbiP42939.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR206W; YGR206W; YGR206W.
GeneIDi853120.
KEGGisce:YGR206W.

Organism-specific databases

CYGDiYGR206w.
SGDiS000003438. MVB12.

Phylogenomic databases

eggNOGiNOG71344.
HOGENOMiHOG000000939.
InParanoidiP42939.
KOiK12187.
OMAiEECDNIT.
OrthoDBiEOG72C5D4.

Enzyme and pathway databases

BioCyciYEAST:G3O-30889-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP42939.
NextBioi973154.

Gene expression databases

GenevestigatoriP42939.

Family and domain databases

InterProiIPR019014. ESCRT-I_cplx_su_Mvb12.
[Graphical view]
PfamiPF09452. Mvb12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
    Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
    Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking."
    Gill D.J., Teo H., Sun J., Perisic O., Veprintsev D.B., Emr S.D., Williams R.L.
    EMBO J. 26:600-612(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ESCRT-I COMPLEX, COMPOSITION OF THE ESCRT-I COMPLEX.
  7. "Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I from multivesicular bodies requires the subunit Mvb12."
    Curtiss M., Jones C., Babst M.
    Mol. Biol. Cell 18:636-645(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE ESCRT-I COMPLEX.
  8. "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-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 4-81, COMPOSITION OF THE ESCRT-I COMPLEX, INTERACTION WITH STP22 AND SRN2, MUTAGENESIS OF CYS-54; ILE-57 AND HIS-64.

Entry informationi

Entry nameiMVB12_YEAST
AccessioniPrimary (citable) accession number: P42939
Secondary accession number(s): D6VUY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 114 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 752 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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 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.