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Protein

Endophilin-A1

Gene

SH3GL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Biological processEndocytosis
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-182971. EGFR downregulation.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-432720. Lysosome Vesicle Biogenesis.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-437239. Recycling pathway of L1.
R-HSA-6807004. Negative regulation of MET activity.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8875360. InlB-mediated entry of Listeria monocytogenes into host cell.
SignaLinkiQ99962.
SIGNORiQ99962.

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-A1
Alternative name(s):
EEN-B1
Endophilin-1
SH3 domain protein 2A
SH3 domain-containing GRB2-like protein 2
Gene namesi
Name:SH3GL2
Synonyms:CNSA2, SH3D2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10831. SH3GL2.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63A → S: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-66 or with S-66 and Q-70. 1 Publication1
Mutagenesisi66A → D: Loss of tubulation of liposomes, no effect on liposome binding. 1 Publication1
Mutagenesisi66A → S: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 or with S-63 and Q-70. 1 Publication1
Mutagenesisi66A → W: Vesiculation of liposomes, no effect on liposome binding, indol ring located in hydrophobic core of the membrane. 1 Publication1
Mutagenesisi70M → Q: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 and S-66. 1 Publication1
Mutagenesisi202F → W: No effect. Indol ring not associated with the membrane. 1 Publication1

Organism-specific databases

DisGeNETi6456.
OpenTargetsiENSG00000107295.
PharmGKBiPA35737.

Polymorphism and mutation databases

BioMutaiSH3GL2.
DMDMi10720276.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467471 – 352Endophilin-A1Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei262PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99962.
MaxQBiQ99962.
PaxDbiQ99962.
PeptideAtlasiQ99962.
PRIDEiQ99962.

PTM databases

iPTMnetiQ99962.
PhosphoSitePlusiQ99962.

Expressioni

Tissue specificityi

Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.

Gene expression databases

BgeeiENSG00000107295.
CleanExiHS_SH3GL2.
GenevisibleiQ99962. HS.

Organism-specific databases

HPAiCAB010056.
HPA026685.
HPA063573.

Interactioni

Subunit structurei

Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with PDCD6IP. Interacts with ATX2. Interacts with ADAM9 and ADAM15 cytoplasmic tails. Interacts with BIN2.By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112353. 59 interactors.
DIPiDIP-30996N.
IntActiQ99962. 47 interactors.
MINTiMINT-108776.
STRINGi9606.ENSP00000369981.

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 21Combined sources10
Helixi24 – 58Combined sources35
Helixi62 – 64Combined sources3
Helixi65 – 68Combined sources4
Helixi89 – 104Combined sources16
Beta strandi106 – 109Combined sources4
Helixi110 – 138Combined sources29
Helixi140 – 148Combined sources9
Helixi150 – 175Combined sources26
Helixi180 – 246Combined sources67
Beta strandi294 – 299Combined sources6
Beta strandi316 – 318Combined sources3
Beta strandi323 – 332Combined sources10
Beta strandi335 – 348Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X03X-ray3.10A1-247[»]
1X04X-ray2.90A1-58[»]
A89-247[»]
2D4CX-ray2.40A/B/C/D1-247[»]
2DBMNMR-A293-352[»]
ProteinModelPortaliQ99962.
SMRiQ99962.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99962.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 249BARPROSITE-ProRule annotationAdd BLAST232
Domaini290 – 349SH3PROSITE-ProRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 125Binds and tubulates liposomesBy similarityAdd BLAST125
Regioni1 – 21Membrane-binding amphipathic helix1 PublicationAdd BLAST21
Regioni60 – 87Required for dimerization upon membrane associationBy similarityAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili181 – 248Sequence analysisAdd BLAST68

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. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface.1 Publication

Sequence similaritiesi

Belongs to the endophilin family.Curated

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiQ99962.
KOiK11247.
OMAiGGLSHTS.
OrthoDBiEOG091G16FW.
PhylomeDBiQ99962.
TreeFamiTF313281.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiView protein in InterPro
IPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
PfamiView protein in Pfam
PF03114. BAR. 1 hit.
PF07653. SH3_2. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiView protein in SMART
SM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiView protein in PROSITE
PS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99962-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI
60 70 80 90 100
MTKTIEYLQP NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF
110 120 130 140 150
GRELGDDCNF GPALGEVGEA MRELSEVKDS LDIEVKQNFI DPLQNLHDKD
160 170 180 190 200
LREIQHHLKK LEGRRLDFDY KKKRQGKIPD EELRQALEKF DESKEIAESS
210 220 230 240 250
MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL EERIRQASSQ
260 270 280 290 300
PRREYQPKPR MSLEFPTGDS TQPNGGLSHT GTPKPSGVQM DQPCCRALYD
310 320 330 340 350
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGHSGFFP INYVEILVAL

PH
Length:352
Mass (Da):39,962
Last modified:May 1, 1997 - v1
Checksum:iF3AE2353E1EB7CF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99657 mRNA. Translation: CAA67971.1.
AF036268 mRNA. Translation: AAC04764.1.
CR542086 mRNA. Translation: CAG46883.1.
CR542102 mRNA. Translation: CAG46899.1.
BT019682 mRNA. Translation: AAV38488.1.
AK312400 mRNA. Translation: BAG35315.1.
AL139115, AL133214 Genomic DNA. Translation: CAB92765.2.
AL133214, AL139115 Genomic DNA. Translation: CAH70742.1.
CH471071 Genomic DNA. Translation: EAW58661.1.
CCDSiCCDS6483.1.
RefSeqiNP_003017.1. NM_003026.3.
UniGeneiHs.743740.
Hs.75149.

Genome annotation databases

EnsembliENST00000380607; ENSP00000369981; ENSG00000107295.
GeneIDi6456.
KEGGihsa:6456.
UCSCiuc003zna.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99657 mRNA. Translation: CAA67971.1.
AF036268 mRNA. Translation: AAC04764.1.
CR542086 mRNA. Translation: CAG46883.1.
CR542102 mRNA. Translation: CAG46899.1.
BT019682 mRNA. Translation: AAV38488.1.
AK312400 mRNA. Translation: BAG35315.1.
AL139115, AL133214 Genomic DNA. Translation: CAB92765.2.
AL133214, AL139115 Genomic DNA. Translation: CAH70742.1.
CH471071 Genomic DNA. Translation: EAW58661.1.
CCDSiCCDS6483.1.
RefSeqiNP_003017.1. NM_003026.3.
UniGeneiHs.743740.
Hs.75149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X03X-ray3.10A1-247[»]
1X04X-ray2.90A1-58[»]
A89-247[»]
2D4CX-ray2.40A/B/C/D1-247[»]
2DBMNMR-A293-352[»]
ProteinModelPortaliQ99962.
SMRiQ99962.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112353. 59 interactors.
DIPiDIP-30996N.
IntActiQ99962. 47 interactors.
MINTiMINT-108776.
STRINGi9606.ENSP00000369981.

PTM databases

iPTMnetiQ99962.
PhosphoSitePlusiQ99962.

Polymorphism and mutation databases

BioMutaiSH3GL2.
DMDMi10720276.

Proteomic databases

EPDiQ99962.
MaxQBiQ99962.
PaxDbiQ99962.
PeptideAtlasiQ99962.
PRIDEiQ99962.

Protocols and materials databases

DNASUi6456.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380607; ENSP00000369981; ENSG00000107295.
GeneIDi6456.
KEGGihsa:6456.
UCSCiuc003zna.4. human.

Organism-specific databases

CTDi6456.
DisGeNETi6456.
GeneCardsiSH3GL2.
HGNCiHGNC:10831. SH3GL2.
HPAiCAB010056.
HPA026685.
HPA063573.
MIMi604465. gene.
neXtProtiNX_Q99962.
OpenTargetsiENSG00000107295.
PharmGKBiPA35737.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiQ99962.
KOiK11247.
OMAiGGLSHTS.
OrthoDBiEOG091G16FW.
PhylomeDBiQ99962.
TreeFamiTF313281.

Enzyme and pathway databases

ReactomeiR-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-182971. EGFR downregulation.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-432720. Lysosome Vesicle Biogenesis.
R-HSA-432722. Golgi Associated Vesicle Biogenesis.
R-HSA-437239. Recycling pathway of L1.
R-HSA-6807004. Negative regulation of MET activity.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8875360. InlB-mediated entry of Listeria monocytogenes into host cell.
SignaLinkiQ99962.
SIGNORiQ99962.

Miscellaneous databases

ChiTaRSiSH3GL2. human.
EvolutionaryTraceiQ99962.
GeneWikiiSH3GL2.
GenomeRNAii6456.
PROiQ99962.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107295.
CleanExiHS_SH3GL2.
GenevisibleiQ99962. HS.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiView protein in InterPro
IPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
PfamiView protein in Pfam
PF03114. BAR. 1 hit.
PF07653. SH3_2. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiView protein in SMART
SM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiView protein in PROSITE
PS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSH3G2_HUMAN
AccessioniPrimary (citable) accession number: Q99962
Secondary accession number(s): B2R618, Q9NQK5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: March 15, 2017
This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.