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Protein

E3 ubiquitin-protein ligase PIB1

Gene

PIB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as an E3 ubiquitin-protein ligase. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 8872FYVE-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri225 – 28359RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate binding Source: SGD
  • ubiquitin-protein transferase activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein ubiquitination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29872-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase PIB1 (EC:6.3.2.-)
Alternative name(s):
Phosphatidylinositol 3-phosphate-binding protein 1
Gene namesi
Name:PIB1
Ordered Locus Names:YDR313C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR313C.
SGDiS000002721. PIB1.

Subcellular locationi

GO - Cellular componenti

  • endosome membrane Source: UniProtKB-SubCell
  • fungal-type vacuole membrane Source: SGD
  • late endosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231C → S: Abolishes endosomal targeting. 1 Publication
Mutagenesisi225 – 2251C → S: Abolishes E3 activity, strongly reduces zinc binding and destabilizes the protein, but no effect on subcellular location. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286E3 ubiquitin-protein ligase PIB1PRO_0000245839Add
BLAST

Proteomic databases

MaxQBiQ06651.

Interactioni

Protein-protein interaction databases

BioGridi32366. 22 interactions.
DIPiDIP-1514N.
IntActiQ06651. 1 interaction.
MINTiMINT-400272.

Structurei

3D structure databases

ProteinModelPortaliQ06651.
SMRiQ06651. Positions 13-87.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The FYVE domain mediates phosphatidylinositol 3-phosphate binding and is necessary and sufficient for targeting to endosome and vacuole membranes.

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 8872FYVE-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri225 – 28359RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000065938.
InParanoidiQ06651.
OMAiRLECLCV.
OrthoDBiEOG7SN8QC.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIKEDCINN LARWQADEEA HSCFQCKTNF SFLVRRHHCR CCGRIFCSSC
60 70 80 90 100
TENFVNYNKK RVHALQKKNS DVESPPYRTC NECYDNLLHL NLLVSSTNRD
110 120 130 140 150
VRLSQTSVPP NALALSAPDS NTDEDAEILE DSVDQSGTAC RSEESSQNEE
160 170 180 190 200
DHFCPICNSD LTQFPDEEET RKHVEDCIQR AENAQQHTNT SDAADDSVKE
210 220 230 240 250
SPAFQNRMLV YKISPNTTDN AIKECPICFE NMEPGEKVGR LECLCVFHYK
260 270 280
CIKNWFHKRA QMTAAQKGNG HAFVKRNFCP FHDAVF
Length:286
Mass (Da):32,675
Last modified:November 1, 1996 - v1
Checksum:iE7E9DCDEC9BAA183
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661D → G in AAS56068 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64749.1.
AY557742 Genomic DNA. Translation: AAS56068.1.
BK006938 Genomic DNA. Translation: DAA12152.1.
PIRiS61199.
RefSeqiNP_010599.1. NM_001180621.1.

Genome annotation databases

EnsemblFungiiYDR313C; YDR313C; YDR313C.
GeneIDi851908.
KEGGisce:YDR313C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64749.1.
AY557742 Genomic DNA. Translation: AAS56068.1.
BK006938 Genomic DNA. Translation: DAA12152.1.
PIRiS61199.
RefSeqiNP_010599.1. NM_001180621.1.

3D structure databases

ProteinModelPortaliQ06651.
SMRiQ06651. Positions 13-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32366. 22 interactions.
DIPiDIP-1514N.
IntActiQ06651. 1 interaction.
MINTiMINT-400272.

Proteomic databases

MaxQBiQ06651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR313C; YDR313C; YDR313C.
GeneIDi851908.
KEGGisce:YDR313C.

Organism-specific databases

EuPathDBiFungiDB:YDR313C.
SGDiS000002721. PIB1.

Phylogenomic databases

HOGENOMiHOG000065938.
InParanoidiQ06651.
OMAiRLECLCV.
OrthoDBiEOG7SN8QC.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-29872-MONOMER.

Miscellaneous databases

PROiQ06651.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains."
    Burd C.G., Emr S.D.
    Mol. Cell 2:157-162(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "FYVE domain targets Pib1p ubiquitin ligase to endosome and vacuolar membranes."
    Shin M.E., Ogburn K.D., Varban O.A., Gilbert P.M., Burd C.G.
    J. Biol. Chem. 276:41388-41393(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-23 AND CYS-225.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPIB1_YEAST
AccessioniPrimary (citable) accession number: Q06651
Secondary accession number(s): D6VSU2, Q6Q5S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 123 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 195 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.