SH3G1_HUMAN
ID SH3G1_HUMAN Reviewed; 368 AA.
AC Q99961; B4DRA1; E7EVZ4; M0QZV5; Q99668;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=EEN fusion partner of MLL;
DE AltName: Full=Endophilin-2;
DE AltName: Full=Extra eleven-nineteen leukemia fusion gene protein;
DE Short=EEN;
DE AltName: Full=SH3 domain protein 2B;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
GN Name=SH3GL1; Synonyms=CNSA1, SH3D2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9169142; DOI=10.1006/geno.1997.4645;
RA Giachino C., Lantelme E., Lanzetti L., Saccone S., Della Valle G.,
RA Migone N.;
RT "A novel SH3-containing human gene family preferentially expressed in the
RT central nervous system.";
RL Genomics 41:427-434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9122235; DOI=10.1073/pnas.94.6.2563;
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RT "EEN encodes for a member of a new family of proteins containing an Src
RT homology 3 domain and is the third gene located on chromosome 19p13 that
RT fuses to MLL in human leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2563-2568(1997).
RN [3]
RP SEQUENCE REVISION.
RA So C.W., Caldas C., Liu M.-M., Chen S.-J., Huang Q.-H., Gu L.-J.,
RA Sham M.H., Wiedemann L.M., Chan L.C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen S., Xiong H., Dong H., Lin W., Zhang C., Fu G., Qi Z., Huang G.M.;
RT "Homo sapiens SH3-containing protein EEN gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH SYNJ1.
RX PubMed=10542231; DOI=10.1074/jbc.274.45.32001;
RA Cestra G., Castagnoli L., Dente L., Minenkova O., Petrelli A., Migone N.,
RA Hoffmueller U., Schneider-Mergener J., Cesareni G.;
RT "The SH3 domains of endophilin and amphiphysin bind to the proline-rich
RT region of synaptojanin 1 at distinct sites that display an unconventional
RT binding specificity.";
RL J. Biol. Chem. 274:32001-32007(1999).
RN [9]
RP INTERACTION WITH PDCD6IP.
RX PubMed=17350572; DOI=10.1016/j.cell.2007.01.035;
RA Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P.;
RT "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus
RT budding.";
RL Cell 128:841-852(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP INTERACTION WITH BIN2, AND SUBCELLULAR LOCATION.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-292 AND THR-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with SYNJ1 and
CC DNM1. Interacts with PDCD6IP. Interacts with BIN2. {ECO:0000250,
CC ECO:0000269|PubMed:10542231, ECO:0000269|PubMed:17350572,
CC ECO:0000269|PubMed:23285027}.
CC -!- INTERACTION:
CC Q99961; O14672: ADAM10; NbExp=2; IntAct=EBI-697911, EBI-1536151;
CC Q99961; Q07960: ARHGAP1; NbExp=3; IntAct=EBI-697911, EBI-602762;
CC Q99961; P85298-4: ARHGAP8; NbExp=3; IntAct=EBI-697911, EBI-9523517;
CC Q99961; Q8IVM0: CCDC50; NbExp=3; IntAct=EBI-697911, EBI-723996;
CC Q99961; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-697911, EBI-11522780;
CC Q99961; Q7L190: DPPA4; NbExp=9; IntAct=EBI-697911, EBI-710457;
CC Q99961; Q5T9C2-3: FAM102A; NbExp=3; IntAct=EBI-697911, EBI-11980989;
CC Q99961; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-697911, EBI-10220102;
CC Q99961; Q92917: GPKOW; NbExp=8; IntAct=EBI-697911, EBI-746309;
CC Q99961; P42858: HTT; NbExp=3; IntAct=EBI-697911, EBI-466029;
CC Q99961; Q5S007: LRRK2; NbExp=3; IntAct=EBI-697911, EBI-5323863;
CC Q99961; Q969L2: MAL2; NbExp=5; IntAct=EBI-697911, EBI-944295;
CC Q99961; Q13330: MTA1; NbExp=3; IntAct=EBI-697911, EBI-714236;
CC Q99961; Q04118: PRB3; NbExp=3; IntAct=EBI-697911, EBI-13360404;
CC Q99961; B1AHC3: PRR5-ARHGAP8; NbExp=3; IntAct=EBI-697911, EBI-17437404;
CC Q99961; P20618: PSMB1; NbExp=3; IntAct=EBI-697911, EBI-372273;
CC Q99961; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-697911, EBI-18304046;
CC Q99961; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-697911, EBI-2695784;
CC Q99961; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-697911, EBI-747035;
CC Q99961; Q99961: SH3GL1; NbExp=6; IntAct=EBI-697911, EBI-697911;
CC Q99961; Q99962: SH3GL2; NbExp=4; IntAct=EBI-697911, EBI-77938;
CC Q99961; Q99963: SH3GL3; NbExp=4; IntAct=EBI-697911, EBI-473910;
CC Q99961; O15524: SOCS1; NbExp=3; IntAct=EBI-697911, EBI-968198;
CC Q99961; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-697911, EBI-742688;
CC Q99961; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-697911, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
CC projection, podosome {ECO:0000269|PubMed:23285027}. Note=Associated
CC with postsynaptic endosomes in hippocampal neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99961-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99961-2; Sequence=VSP_045837;
CC Name=3;
CC IsoId=Q99961-3; Sequence=VSP_047037;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression in pancreas,
CC placenta, prostate, testis and uterus.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second
CC amphipathic helix inserted into helix 1 of the BAR domain (N-BAR
CC domain) induce membrane curvature and bind curved membranes.
CC {ECO:0000250}.
CC -!- DISEASE: Note=In some cases of acute leukemia, a translocation results
CC in the formation of a KMT2A/MLL1-EEN fusion gene.
CC {ECO:0000269|PubMed:9122235}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EENID8.html";
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DR EMBL; X99656; CAA67970.1; -; mRNA.
DR EMBL; U65999; AAB86800.1; -; mRNA.
DR EMBL; AF190465; AAF04290.1; -; Genomic_DNA.
DR EMBL; AK299166; BAG61213.1; -; mRNA.
DR EMBL; AK097616; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001270; AAH01270.1; -; mRNA.
DR CCDS; CCDS32874.1; -. [Q99961-1]
DR CCDS; CCDS56076.1; -. [Q99961-2]
DR CCDS; CCDS59335.1; -. [Q99961-3]
DR RefSeq; NP_001186872.1; NM_001199943.1. [Q99961-2]
DR RefSeq; NP_001186873.1; NM_001199944.1. [Q99961-3]
DR RefSeq; NP_003016.1; NM_003025.3. [Q99961-1]
DR AlphaFoldDB; Q99961; -.
DR SMR; Q99961; -.
DR BioGRID; 112352; 146.
DR DIP; DIP-29452N; -.
DR IntAct; Q99961; 67.
DR MINT; Q99961; -.
DR STRING; 9606.ENSP00000269886; -.
DR GlyGen; Q99961; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99961; -.
DR MetOSite; Q99961; -.
DR PhosphoSitePlus; Q99961; -.
DR BioMuta; SH3GL1; -.
DR DMDM; 12643797; -.
DR OGP; Q99961; -.
DR EPD; Q99961; -.
DR jPOST; Q99961; -.
DR MassIVE; Q99961; -.
DR MaxQB; Q99961; -.
DR PaxDb; Q99961; -.
DR PeptideAtlas; Q99961; -.
DR PRIDE; Q99961; -.
DR ProteomicsDB; 18733; -.
DR ProteomicsDB; 78545; -. [Q99961-1]
DR Antibodypedia; 11454; 389 antibodies from 35 providers.
DR DNASU; 6455; -.
DR Ensembl; ENST00000269886.7; ENSP00000269886.2; ENSG00000141985.9. [Q99961-1]
DR Ensembl; ENST00000417295.6; ENSP00000404568.2; ENSG00000141985.9. [Q99961-2]
DR Ensembl; ENST00000598564.5; ENSP00000470792.1; ENSG00000141985.9. [Q99961-3]
DR GeneID; 6455; -.
DR KEGG; hsa:6455; -.
DR MANE-Select; ENST00000269886.7; ENSP00000269886.2; NM_003025.4; NP_003016.1.
DR UCSC; uc002maj.4; human. [Q99961-1]
DR CTD; 6455; -.
DR DisGeNET; 6455; -.
DR GeneCards; SH3GL1; -.
DR HGNC; HGNC:10830; SH3GL1.
DR HPA; ENSG00000141985; Low tissue specificity.
DR MalaCards; SH3GL1; -.
DR MIM; 601768; gene.
DR neXtProt; NX_Q99961; -.
DR OpenTargets; ENSG00000141985; -.
DR PharmGKB; PA35736; -.
DR VEuPathDB; HostDB:ENSG00000141985; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000154737; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q99961; -.
DR OMA; QYLSETM; -.
DR PhylomeDB; Q99961; -.
DR TreeFam; TF313281; -.
DR PathwayCommons; Q99961; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR SignaLink; Q99961; -.
DR SIGNOR; Q99961; -.
DR BioGRID-ORCS; 6455; 40 hits in 1084 CRISPR screens.
DR ChiTaRS; SH3GL1; human.
DR GeneWiki; SH3GL1; -.
DR GenomeRNAi; 6455; -.
DR Pharos; Q99961; Tbio.
DR PRO; PR:Q99961; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q99961; protein.
DR Bgee; ENSG00000141985; Expressed in lower esophagus mucosa and 195 other tissues.
DR ExpressionAtlas; Q99961; baseline and differential.
DR Genevisible; Q99961; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR CDD; cd11803; SH3_Endophilin_A; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028501; Endophilin-A.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF63; PTHR14167:SF63; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Endocytosis; Endosome;
KW Lipid-binding; Membrane; Phosphoprotein; Proto-oncogene;
KW Reference proteome; SH3 domain.
FT CHAIN 1..368
FT /note="Endophilin-A2"
FT /id="PRO_0000146744"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 306..365
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..21
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT REGION 60..87
FT /note="Required for dimerization upon membrane association"
FT /evidence="ECO:0000250"
FT REGION 218..254
FT /note="Interaction with ARC"
FT /evidence="ECO:0000250"
FT REGION 244..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..250
FT /evidence="ECO:0000255"
FT COMPBIAS 244..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 15..16
FT /note="Breakpoint for translocation to form KMT2A/MLL1-EEN
FT oncogene"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62419"
FT VAR_SEQ 63..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045837"
FT VAR_SEQ 80..143
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047037"
FT CONFLICT 316
FT /note="D -> G (in Ref. 5; BAG61213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41490 MW; 6E5BE978BC955077 CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DVTSKAVTEV LARTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMIRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCEKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILDELAEKL
KRRMREASSR PKREYKPKPR EPFDLGEPEQ SNGGFPCTTA PKIAASSSFR SSDKPIRTPS
RSMPPLDQPS CKALYDFEPE NDGELGFHEG DVITLTNQID ENWYEGMLDG QSGFFPLSYV
EVLVPLPQ
