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Q05785 (ENT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Epsin-2
Gene names
Name:ENT2
Ordered Locus Names:YLR206W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Ref.3

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Localizes in a punctate pattern. Found in the actin cortical patches, although the majority is located at the cell periphery. Ref.3 Ref.4

Post-translational modification

Phosphorylated by PRK1. Ref.4

Miscellaneous

Present with 1970 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the epsin family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Epsin-2
PRO_0000074525

Regions

Domain11 – 143133ENTH
Repeat175 – 19420UIM 1
Repeat206 – 22520UIM 2
Compositional bias138 – 16629Arg-rich
Compositional bias192 – 606415Gln-rich

Amino acid modifications

Modified residue1651Phosphothreonine Ref.6 Ref.9
Modified residue1671Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue4301Phosphothreonine Ref.7
Modified residue4341Phosphoserine Ref.7
Modified residue4501Phosphothreonine Ref.8
Modified residue4681Phosphothreonine Ref.6 Ref.9
Modified residue4701Phosphothreonine Ref.9

Secondary structure

..................... 613
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05785 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CEC1B2D04C0F7D86

FASTA61371,807
        10         20         30         40         50         60 
MSKQFVRSAK NMMKGYSSTQ VLVRDATAND SRTPSIDTLD DLAQRSYDSV DFFEIMDMLD 

        70         80         90        100        110        120 
KRLNDKGKYW RHVAKSLTVL DYLVRFGSEN CVLWCRENFY VIKTLREFRH ENESGFDEGQ 

       130        140        150        160        170        180 
IIRVKAKELV SLLNDEERLR EERSMNTRNR RANRAARPRP RRQRTRSNPH DSSPSYQDDL 

       190        200        210        220        230        240 
EKALEESRIT AQEDEQRRRE LAQYDDEDPD FQAALQLSKE EEELKQLQEL QRLQKQQQSL 

       250        260        270        280        290        300 
SQFQAPLQQQ QPQQQPAYYD IFGNPISQDE YLQYQYQQDQ EQAMAQQRWL DQQQEQQQLA 

       310        320        330        340        350        360 
EQQYFQQQQQ AAAAASALQQ QQTAANMQQQ QQQPADFQQP LPTGSNNPFS MDNLERQKQE 

       370        380        390        400        410        420 
QQHAQLQRQQ EEARQQQEQL KLQQLQRQQQ EEAQLHQKRQ EEAQLQQQQA QLLQQQAQFQ 

       430        440        450        460        470        480 
QQQPLKQTRT GNQSISDKYS DLNTLLATGT GIDTFGNTGE ARIPAQHTKT GTFINSQGTG 

       490        500        510        520        530        540 
YKQVTNEPKN NPFLSNQYTG LPSTNIVPTQ TGYGFGNQPQ SPPTNSPQQN PTGISYSQPQ 

       550        560        570        580        590        600 
QQQQPQQQPQ YMQNFQQQQP QYAQNFQQQP QYTQNYQQQP QYIQPHQQQQ QQQQQQQQQQ 

       610 
GYTPDQGVSL IDL 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis."
Wendland B., Steece K.E., Emr S.D.
EMBO J. 18:4383-4393(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation."
Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.
Mol. Biol. Cell 12:3668-3679(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[5]"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].
[6]"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 THR-165; SER-167 AND THR-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"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 THR-430 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-167 AND THR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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 THR-165; SER-167; THR-468 AND THR-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14913 Genomic DNA. Translation: AAB67428.1.
BK006945 Genomic DNA. Translation: DAA09523.1.
PIRS48557.
RefSeqNP_013307.1. NM_001182093.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GZCX-ray1.30A1-149[»]
4GZDX-ray1.75A1-149[»]
ProteinModelPortalQ05785.
SMRQ05785. Positions 15-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31474. 56 interactions.
DIPDIP-2698N.
IntActQ05785. 16 interactions.
MINTMINT-687167.
STRING4932.YLR206W.

Proteomic databases

MaxQBQ05785.
PaxDbQ05785.
PeptideAtlasQ05785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR206W; YLR206W; YLR206W.
GeneID850903.
KEGGsce:YLR206W.

Organism-specific databases

CYGDYLR206w.
SGDS000004196. ENT2.

Phylogenomic databases

eggNOGNOG263730.
GeneTreeENSGT00720000109538.
HOGENOMHOG000216614.
KOK12471.
OMAFRHENES.
OrthoDBEOG7KM63T.

Enzyme and pathway databases

BioCycYEAST:G3O-32324-MONOMER.

Gene expression databases

GenevestigatorQ05785.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamPF01417. ENTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio967293.

Entry information

Entry nameENT2_YEAST
AccessionPrimary (citable) accession number: Q05785
Secondary accession number(s): D6VYK7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references