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Protein

Endophilin-A2

Gene

Sh3gl1

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

Functioni

Implicated in endocytosis. May recruit other proteins to membranes with high curvature (By similarity).By similarity

GO - Molecular functioni

  • GTPase binding Source: RGD
  • lipid binding Source: UniProtKB-KW
  • phosphatase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-A2
Alternative name(s):
Endophilin-2
SH3 domain protein 2B
SH3 domain-containing GRB2-like protein 1
SH3p8
Gene namesi
Name:Sh3gl1
Synonyms:Sh3p8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi708456. Sh3gl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Endophilin-A2PRO_0000146746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei315 – 3151PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35964.
PRIDEiO35964.

PTM databases

iPTMnetiO35964.

Expressioni

Tissue specificityi

Detected in brain and testis (at protein level). Ubiquitous.2 Publications

Gene expression databases

GenevisibleiO35964. RN.

Interactioni

Subunit structurei

Interacts with ARC, SYNJ1 and DNM1. Interacts with PDCD6IP (By similarity). Interacts with BIN2.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAPH1Q70E7313EBI-1149235,EBI-3940924From a different organism.
SRGAP3O432953EBI-1149235,EBI-368166From a different organism.

GO - Molecular functioni

  • GTPase binding Source: RGD
  • phosphatase binding Source: RGD

Protein-protein interaction databases

BioGridi249697. 2 interactions.
IntActiO35964. 9 interactions.
MINTiMINT-1526331.
STRINGi10116.ENSRNOP00000066789.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi310 – 3156Combined sources
Beta strandi332 – 3387Combined sources
Beta strandi340 – 3489Combined sources
Beta strandi351 – 3566Combined sources
Helixi357 – 3593Combined sources
Beta strandi360 – 3645Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C0CX-ray1.70A303-368[»]
ProteinModelPortaliO35964.
SMRiO35964. Positions 9-247, 305-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35964.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 249232BARPROSITE-ProRule annotationAdd
BLAST
Domaini306 – 36560SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2121Membrane-binding amphipathic helixBy similarityAdd
BLAST
Regioni60 – 8728Required for dimerization upon membrane associationBy similarityAdd
BLAST
Regioni218 – 25437Interaction with ARCAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili180 – 25071Sequence 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.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOVERGENiHBG052866.
InParanoidiO35964.
KOiK11247.
OMAiKPRETYD.
OrthoDBiEOG7G1V6H.
PhylomeDBiO35964.

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.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFREMEKKV DITSKAVAEV
60 70 80 90 100
LVRTIEYLQP NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMVRH
110 120 130 140 150
GKELGGESNF GDALLDAGES MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD
160 170 180 190 200
LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD EELRQALEKF EESKEVAETS
210 220 230 240 250
MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILEELADKL KRRVREASSR
260 270 280 290 300
PRREFKPRPQ EPFELGELEQ PNGGFPCASA PKITASSSFR SGDKPTRTPS
310 320 330 340 350
KSMPPLDQPS CKALYDFEPE NDGELGFREG DLITLTNQID ENWYEGMLHG
360
QSGFFPLSYV QVLVPLPQ
Length:368
Mass (Da):41,492
Last modified:January 1, 1998 - v1
Checksum:iC14F4357386F35FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009602 mRNA. Translation: AAC14882.1.
AB008161 mRNA. Translation: BAA22921.1.
BC070893 mRNA. Translation: AAH70893.1.
RefSeqiNP_112518.1. NM_031239.2.
UniGeneiRn.8762.

Genome annotation databases

EnsembliENSRNOT00000074695; ENSRNOP00000066789; ENSRNOG00000049683.
GeneIDi81922.
KEGGirno:81922.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009602 mRNA. Translation: AAC14882.1.
AB008161 mRNA. Translation: BAA22921.1.
BC070893 mRNA. Translation: AAH70893.1.
RefSeqiNP_112518.1. NM_031239.2.
UniGeneiRn.8762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C0CX-ray1.70A303-368[»]
ProteinModelPortaliO35964.
SMRiO35964. Positions 9-247, 305-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249697. 2 interactions.
IntActiO35964. 9 interactions.
MINTiMINT-1526331.
STRINGi10116.ENSRNOP00000066789.

PTM databases

iPTMnetiO35964.

Proteomic databases

PaxDbiO35964.
PRIDEiO35964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074695; ENSRNOP00000066789; ENSRNOG00000049683.
GeneIDi81922.
KEGGirno:81922.

Organism-specific databases

CTDi6455.
RGDi708456. Sh3gl1.

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOVERGENiHBG052866.
InParanoidiO35964.
KOiK11247.
OMAiKPRETYD.
OrthoDBiEOG7G1V6H.
PhylomeDBiO35964.

Miscellaneous databases

EvolutionaryTraceiO35964.
PROiO35964.

Gene expression databases

GenevisibleiO35964. 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.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain."
    Ringstad N., Nemoto Y., De Camilli P.
    Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH DNM1 AND SYNJ1.
    Tissue: Brain.
  2. "Rattus norvegicus SH3P8 mRNA, complete cds."
    Yamagata K.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "Arc/Arg3.1 interacts with the endocytic machinery to regulate AMPA receptor trafficking."
    Chowdhury S., Shepherd J.D., Okuno H., Lyford G., Petralia R.S., Plath N., Kuhl D., Huganir R.L., Worley P.F.
    Neuron 52:445-459(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ARC.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis."
    Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J., Veprintsev D.B., Evans P.R., McMahon H.T.
    PLoS ONE 7:E52401-E52401(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIN2, TISSUE SPECIFICITY.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 303-368.

Entry informationi

Entry nameiSH3G1_RAT
AccessioniPrimary (citable) accession number: O35964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 112 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.