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Protein

Endophilin-A1

Gene

Sh3gl2

Organism
Mus musculus (Mouse)
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.1 Publication

GO - Molecular functioni

GO - Biological processi

  • regulation of receptor internalization Source: MGI
  • synaptic vesicle endocytosis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-177504. Retrograde neurotrophin signalling.
R-MMU-182971. EGFR downregulation.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-437239. Recycling pathway of L1.

Protein family/group databases

TCDBi8.A.34.1.1. the endophilin (endophilin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Endophilin-A1
Alternative name(s):
Endophilin-1
SH3 domain protein 2A
SH3 domain-containing GRB2-like protein 2
SH3p4
Gene namesi
Name:Sh3gl2
Synonyms:Sh3d2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:700009. Sh3gl2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Endophilin-A1PRO_0000146748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ62420.
MaxQBiQ62420.
PaxDbiQ62420.
PRIDEiQ62420.

PTM databases

iPTMnetiQ62420.
PhosphoSiteiQ62420.
SwissPalmiQ62420.

Expressioni

Gene expression databases

BgeeiQ62420.
CleanExiMM_SH3GL2.
ExpressionAtlasiQ62420. baseline and differential.
GenevisibleiQ62420. MM.

Interactioni

Subunit structurei

Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with OPHN1 (By similarity). Interacts with PDCD6IP. Interacts with BIN2 (By similarity). Interacts with ATX2. Interacts with ADAM9 and ADAM15 cytoplasmic tails.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dennd1aQ8K3822EBI-77971,EBI-7186684

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203206. 12 interactions.
DIPiDIP-30992N.
IntActiQ62420. 14 interactions.
MINTiMINT-238723.
STRINGi10090.ENSMUSP00000030212.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 5828Combined sources
Turni62 – 643Combined sources
Helixi89 – 10416Combined sources
Beta strandi106 – 1094Combined sources
Helixi110 – 13829Combined sources
Helixi140 – 1489Combined sources
Helixi150 – 17324Combined sources
Turni174 – 1774Combined sources
Helixi180 – 20627Combined sources
Helixi209 – 24537Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZWWX-ray2.30A/B1-256[»]
ProteinModelPortaliQ62420.
SMRiQ62420. Positions 26-247, 291-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62420.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 249232BARPROSITE-ProRule annotationAdd
BLAST
Domaini290 – 34960SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 125125Binds and tubulates liposomesBy similarityAdd
BLAST
Regioni1 – 2121Membrane-binding amphipathic helixBy similarityAdd
BLAST
Regioni60 – 8728Required for dimerization upon membrane associationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili181 – 24868Sequence 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). 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.By similarity1 Publication

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.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiQ62420.
KOiK11247.
TreeFamiTF313281.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
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.

Q62420-1 [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 LDMEVKQNFI 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 MSLEFATGDS TQPNGGLSHT GTPKPPGVQM DQPCCRALYD
310 320 330 340 350
FEPENEGELG FKEGDIITLT NQIDENWYEG MLHGQSGFFP INYVEILVAL

PH
Length:352
Mass (Da):39,955
Last modified:October 23, 2007 - v2
Checksum:i8C2B6F0FB245DCD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281K → N in BAC31888 (PubMed:16141072).Curated
Sequence conflicti54 – 541T → K in BAE23963 (PubMed:16141072).Curated
Sequence conflicti69 – 691S → G in BAE23963 (PubMed:16141072).Curated
Sequence conflicti169 – 1691D → G in AAC71774 (PubMed:9630982).Curated
Sequence conflicti301 – 3011F → L in AAC71774 (PubMed:9630982).Curated
Sequence conflicti310 – 3101G → A in AAC71774 (PubMed:9630982).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58886 mRNA. Translation: AAC71774.1.
AF326561 mRNA. Translation: AAL37407.1.
AF326562 mRNA. Translation: AAL37408.1.
AK044370 mRNA. Translation: BAC31888.1.
AK134970 mRNA. Translation: BAE22364.1.
AK139337 mRNA. Translation: BAE23963.1.
AL805970, AL806524 Genomic DNA. Translation: CAM24397.1.
AL806524, AL805970 Genomic DNA. Translation: CAM15712.1.
BC018385 mRNA. Translation: AAH18385.1.
CCDSiCCDS18303.1.
RefSeqiNP_062408.2. NM_019535.2.
UniGeneiMm.143603.

Genome annotation databases

EnsembliENSMUST00000030212; ENSMUSP00000030212; ENSMUSG00000028488.
GeneIDi20404.
KEGGimmu:20404.
UCSCiuc008tlo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58886 mRNA. Translation: AAC71774.1.
AF326561 mRNA. Translation: AAL37407.1.
AF326562 mRNA. Translation: AAL37408.1.
AK044370 mRNA. Translation: BAC31888.1.
AK134970 mRNA. Translation: BAE22364.1.
AK139337 mRNA. Translation: BAE23963.1.
AL805970, AL806524 Genomic DNA. Translation: CAM24397.1.
AL806524, AL805970 Genomic DNA. Translation: CAM15712.1.
BC018385 mRNA. Translation: AAH18385.1.
CCDSiCCDS18303.1.
RefSeqiNP_062408.2. NM_019535.2.
UniGeneiMm.143603.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZWWX-ray2.30A/B1-256[»]
ProteinModelPortaliQ62420.
SMRiQ62420. Positions 26-247, 291-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203206. 12 interactions.
DIPiDIP-30992N.
IntActiQ62420. 14 interactions.
MINTiMINT-238723.
STRINGi10090.ENSMUSP00000030212.

Protein family/group databases

TCDBi8.A.34.1.1. the endophilin (endophilin) family.

PTM databases

iPTMnetiQ62420.
PhosphoSiteiQ62420.
SwissPalmiQ62420.

Proteomic databases

EPDiQ62420.
MaxQBiQ62420.
PaxDbiQ62420.
PRIDEiQ62420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030212; ENSMUSP00000030212; ENSMUSG00000028488.
GeneIDi20404.
KEGGimmu:20404.
UCSCiuc008tlo.1. mouse.

Organism-specific databases

CTDi6456.
MGIiMGI:700009. Sh3gl2.

Phylogenomic databases

eggNOGiKOG1118. Eukaryota.
ENOG410XNYB. LUCA.
GeneTreeiENSGT00550000074464.
HOGENOMiHOG000231641.
HOVERGENiHBG052866.
InParanoidiQ62420.
KOiK11247.
TreeFamiTF313281.

Enzyme and pathway databases

ReactomeiR-MMU-177504. Retrograde neurotrophin signalling.
R-MMU-182971. EGFR downregulation.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-432722. Golgi Associated Vesicle Biogenesis.
R-MMU-437239. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiSh3gl2. mouse.
EvolutionaryTraceiQ62420.
PROiQ62420.
SOURCEiSearch...

Gene expression databases

BgeeiQ62420.
CleanExiMM_SH3GL2.
ExpressionAtlasiQ62420. baseline and differential.
GenevisibleiQ62420. MM.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
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. "Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
    Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
    Nat. Biotechnol. 14:741-744(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as a candidate gene."
    Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.
    J. Neurosci. 22:3730-3738(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J and DBA/2J.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain cortex, Olfactory bulb and Retina.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: C57BL/6J.
    Tissue: Retina.
  6. Lubec G., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 54-65; 228-239 AND 297-312, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
    Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
    J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM9 AND ADAM15.
  8. "Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid."
    Schmidt A., Wolde M., Thiele C., Fest W., Kratzin H., Podtelejnikov A.V., Witke W., Huttner W.B., Soeling H.-D.
    Nature 401:133-141(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1.
  9. "Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
    Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
    Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATX2.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  11. "Crystal structure of the endophilin-A1 BAR domain."
    Weissenhorn W.
    J. Mol. Biol. 351:653-661(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-256, DOMAIN.

Entry informationi

Entry nameiSH3G2_MOUSE
AccessioniPrimary (citable) accession number: Q62420
Secondary accession number(s): Q3UTL7
, Q3UY49, Q8BXS6, Q8VBV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 23, 2007
Last modified: July 6, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to have lysophosphatidic acid acyltransferase activity, but has since been experimentally shown not to have this activity.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.