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Protein

Endophilin-B1

Gene

Sh3glb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion. Involved in activation of caspase-dependent apoptosis by promoting BAX/BAK1 activation. Involved in caspase-independent apoptosis during nutrition starvation and involved in the regulation of autophagy. Activates lipid kinase activity of PIK3C3 during autophagy probably by associating with the PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate the trafficking of ATG9A from the Golgi complex to the peripheral cytoplasm for the formation of autophagosomes by inducing Golgi membrane tubulation and fragmentation. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-B1
Alternative name(s):
SH3 domain-containing GRB2-like protein B1
Gene namesi
Name:Sh3glb1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1304859. Sh3glb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Endophilin-B1PRO_0000307711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei145 – 1451Phosphothreonine; by CDK5By similarity

Post-translational modificationi

Phosphorylated at Thr-145 by CDK5; this phosphorylation is required for autophagy induction in starved neurons and facilitates homodimerization.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6AYE2.
PRIDEiQ6AYE2.

PTM databases

iPTMnetiQ6AYE2.
PhosphoSiteiQ6AYE2.

Expressioni

Tissue specificityi

Expressed in brain, heart, lung and spleen. Low level in liver and testis.1 Publication

Gene expression databases

BgeeiENSRNOG00000012957.
ExpressionAtlasiQ6AYE2. baseline and differential.
GenevisibleiQ6AYE2. RN.

Interactioni

Subunit structurei

Homodimer, and heterodimer with SH3GLB2. Binds BAX; induction of apoptosis augments BAX binding. Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1. Interacts with UVRAG; UVRAG bridges the interaction to BECN1 indicative for an association with the PI3K complex II (PI3KC3-C2) (By similarity).By similarity

Protein-protein interaction databases

BioGridi253783. 1 interaction.
STRINGi10116.ENSRNOP00000017771.

Structurei

3D structure databases

ProteinModelPortaliQ6AYE2.
SMRiQ6AYE2. Positions 298-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 261235BARPROSITE-ProRule annotationAdd
BLAST
Domaini305 – 36561SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3737Required for membrane bindingBy similarityAdd
BLAST
Regioni1 – 3030Membrane-binding amphipathic helixBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili156 – 18530Sequence analysisAdd
BLAST

Domaini

An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes.1 Publication

Sequence similaritiesi

Belongs to the endophilin family.Sequence analysis
Contains 1 BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG3725. Eukaryota.
ENOG410XPA6. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000232056.
HOVERGENiHBG054448.
InParanoidiQ6AYE2.
KOiK11248.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AYE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE
60 70 80 90 100
CTKVWTEKIM KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY
110 120 130 140 150
MIDAGTEFGP GTAYGNALIK CGETQKRIGT ADRELIQTSA LNFLTPLRNF
160 170 180 190 200
IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK KAKAAETKSS SEQELRITQS
210 220 230 240 250
EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ CYQYMLDLQK
260 270 280 290 300
QLGSFPSNYV SNNNQTSGTP VPYTLSNTIG PSAVASTGSL VITCPPNLSD
310 320 330 340 350
LKDSSSTRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG
360
NQKGKVPITY LELLN
Length:365
Mass (Da):40,787
Last modified:September 13, 2004 - v1
Checksum:iAF6950A4820FB470
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079085 mRNA. Translation: AAH79085.1.
RefSeqiNP_001011929.1. NM_001011929.1.
UniGeneiRn.203013.

Genome annotation databases

EnsembliENSRNOT00000017770; ENSRNOP00000017771; ENSRNOG00000012957.
GeneIDi292156.
KEGGirno:292156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079085 mRNA. Translation: AAH79085.1.
RefSeqiNP_001011929.1. NM_001011929.1.
UniGeneiRn.203013.

3D structure databases

ProteinModelPortaliQ6AYE2.
SMRiQ6AYE2. Positions 298-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253783. 1 interaction.
STRINGi10116.ENSRNOP00000017771.

PTM databases

iPTMnetiQ6AYE2.
PhosphoSiteiQ6AYE2.

Proteomic databases

PaxDbiQ6AYE2.
PRIDEiQ6AYE2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017770; ENSRNOP00000017771; ENSRNOG00000012957.
GeneIDi292156.
KEGGirno:292156.

Organism-specific databases

CTDi51100.
RGDi1304859. Sh3glb1.

Phylogenomic databases

eggNOGiKOG3725. Eukaryota.
ENOG410XPA6. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000232056.
HOVERGENiHBG054448.
InParanoidiQ6AYE2.
KOiK11248.

Miscellaneous databases

PROiQ6AYE2.

Gene expression databases

BgeeiENSRNOG00000012957.
ExpressionAtlasiQ6AYE2. baseline and differential.
GenevisibleiQ6AYE2. RN.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSHLB1_RAT
AccessioniPrimary (citable) accession number: Q6AYE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: September 13, 2004
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.