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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: -Experimental evidence at protein leveli

Functioni

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

Miscellaneous

Present with 195 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

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)DescriptionActionsGraphical viewLength
Zinc fingeri17 – 88FYVE-typePROSITE-ProRule annotationAdd BLAST72
Zinc fingeri225 – 283RING-type; atypicalPROSITE-ProRule annotationAdd BLAST59

GO - Molecular functioni

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

GO - Biological processi

  • protein ubiquitination Source: SGD

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29872-MONOMER
UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase PIB1 (EC:2.3.2.27)
Alternative name(s):
Phosphatidylinositol 3-phosphate-binding protein 1
RING-type E3 ubiquitin transferase PIB1Curated
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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endosome, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23C → S: Abolishes endosomal targeting. 1 Publication1
Mutagenesisi225C → S: Abolishes E3 activity, strongly reduces zinc binding and destabilizes the protein, but no effect on subcellular location. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002458391 – 286E3 ubiquitin-protein ligase PIB1Add BLAST286

Proteomic databases

MaxQBiQ06651
PaxDbiQ06651
PRIDEiQ06651

Interactioni

Protein-protein interaction databases

BioGridi32366, 87 interactors
DIPiDIP-1514N
IntActiQ06651, 5 interactors
MINTiQ06651
STRINGi4932.YDR313C

Structurei

3D structure databases

ProteinModelPortaliQ06651
SMRiQ06651
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.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri17 – 88FYVE-typePROSITE-ProRule annotationAdd BLAST72
Zinc fingeri225 – 283RING-type; atypicalPROSITE-ProRule annotationAdd BLAST59

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000065938
InParanoidiQ06651
OMAiCIKDWFN
OrthoDBiEOG092C15HX

Family and domain databases

Gene3Di3.30.40.10, 2 hits
InterProiView protein in InterPro
IPR000306 Znf_FYVE
IPR017455 Znf_FYVE-rel
IPR011011 Znf_FYVE_PHD
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF01363 FYVE, 1 hit
PF13639 zf-RING_2, 1 hit
SMARTiView protein in SMART
SM00064 FYVE, 1 hit
SM00184 RING, 2 hits
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50178 ZF_FYVE, 1 hit
PS50089 ZF_RING_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti166D → G in AAS56068 (PubMed:17322287).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPIB1_YEAST
AccessioniPrimary (citable) accession number: Q06651
Secondary accession number(s): D6VSU2, Q6Q5S5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health