LOCUS       NP_003016                368 aa            linear   PRI 27-APR-2025
DEFINITION  endophilin-A2 isoform 1 [Homo sapiens].
ACCESSION   NP_003016
VERSION     NP_003016.1
DBSOURCE    REFSEQ: accession NM_003025.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Sim,P.F., Chek,M.F., Nguyen,N.T.H., Nishimura,T., Inaba,T.,
            Hakoshima,T. and Suetsugu,S.
  TITLE     The SH3 binding site in front of the WH1 domain contributes to the
            membrane binding of the BAR domain protein endophilin A2
  JOURNAL   J Biochem 175 (1), 57-67 (2023)
   PUBMED   37812440
  REMARK    GeneRIF: The SH3 binding site in front of the WH1 domain
            contributes to the membrane binding of the BAR domain protein
            endophilin A2.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Malinova,D., Wasim,L., Newman,R., Martinez-Riano,A., Engels,N. and
            Tolar,P.
  TITLE     Endophilin A2 regulates B-cell endocytosis and is required for
            germinal center and humoral responses
  JOURNAL   EMBO Rep 22 (9), e51328 (2021)
   PUBMED   34323351
  REMARK    GeneRIF: Endophilin A2 regulates B-cell endocytosis and is required
            for germinal center and humoral responses.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 368)
  AUTHORS   So,C.W., Sham,M.H., Chew,S.L., Cheung,N., So,C.K., Chung,S.K.,
            Caldas,C., Wiedemann,L.M. and Chan,L.C.
  TITLE     Expression and protein-binding studies of the EEN gene family, new
            interacting partners for dynamin, synaptojanin and huntingtin
            proteins
  JOURNAL   Biochem J 348 Pt 2 (Pt 2), 447-458 (2000)
   PUBMED   10816441
REFERENCE   7  (residues 1 to 368)
  AUTHORS   So,C.W., So,C.K., Cheung,N., Chew,S.L., Sham,M.H. and Chan,L.C.
  TITLE     The interaction between EEN and Abi-1, two MLL fusion partners, and
            synaptojanin and dynamin: implications for leukaemogenesis
  JOURNAL   Leukemia 14 (4), 594-601 (2000)
   PUBMED   10764144
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Cestra,G., Castagnoli,L., Dente,L., Minenkova,O., Petrelli,A.,
            Migone,N., Hoffmuller,U., Schneider-Mergener,J. and Cesareni,G.
  TITLE     The SH3 domains of endophilin and amphiphysin bind to the
            proline-rich region of synaptojanin 1 at distinct sites that
            display an unconventional binding specificity
  JOURNAL   J Biol Chem 274 (45), 32001-32007 (1999)
   PUBMED   10542231
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Giachino,C., Lantelme,E., Lanzetti,L., Saccone,S., Bella Valle,G.
            and Migone,N.
  TITLE     A novel SH3-containing human gene family preferentially expressed
            in the central nervous system
  JOURNAL   Genomics 41 (3), 427-434 (1997)
   PUBMED   9169142
REFERENCE   10 (residues 1 to 368)
  AUTHORS   So,C.W., Caldas,C., Liu,M.M., Chen,S.J., Huang,Q.H., Gu,L.J.,
            Sham,M.H., Wiedemann,L.M. and Chan,L.C.
  TITLE     EEN encodes for a member of a new family of proteins containing an
            Src homology 3 domain and is the third gene located on chromosome
            19p13 that fuses to MLL in human leukemia
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2563-2568 (1997)
   PUBMED   9122235
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU838380.1, BC001270.1 and
            AC007292.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the endophilin family of Src
            homology 3 domain-containing proteins. The encoded protein is
            involved in endocytosis and may also play a role in the cell cycle.
            Overexpression of this gene may play a role in leukemogenesis, and
            the encoded protein has been implicated in acute myeloid leukemia
            as a fusion partner of the myeloid-lymphoid leukemia protein.
            Pseudogenes of this gene are located on the long arm of chromosomes
            11 and 17. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098565.1, SRR1163657.444973.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269886.7/ ENSP00000269886.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..368
                     /product="endophilin-A2 isoform 1"
                     /note="SH3-domain GRB2-like 1; endophilin-A2; extra 11-19
                     leukemia fusion; SH3-containing Grb-2-like 1 protein;
                     endophilin-2; SH3 domain protein 2B; EEN fusion partner of
                     MLL; SH3 domain-containing GRB2-like protein 1; extra
                     eleven-nineteen leukemia fusion gene protein"
                     /calculated_mol_wt=41359
     Region          1..21
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Site            15..16
                     /site_type="other"
                     /note="Breakpoint for translocation to form KMT2A/MLL1-EEN
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Region          25..247
                     /region_name="BAR_Endophilin_A"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of
                     Endophilin-A; cd07592"
                     /db_xref="CDD:153276"
     Site            order(38..39,42..43,45..46,49..50,53,57,60..61,89..90,
                     92..93,96..97,100,103..104,108..110,113..114,208..209,
                     211..213,215..216,219,222..223,225..227,229..230,233..234,
                     236..237,240,244)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153276"
     Site            order(45,53,65,152,156,159,164..165,173..174,177,184)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153276"
     Region          60..87
                     /region_name="Required for dimerization upon membrane
                     association. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Region          218..254
                     /region_name="Interaction with ARC. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Region          244..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99961.1)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99961.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99961.1)"
     Region          309..363
                     /region_name="SH3_Endophilin_A"
                     /note="Src homology 3 domain of Endophilin-A; cd11803"
                     /db_xref="CDD:212737"
     Site            order(315,317,320,324,342..343,356,358..359)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212737"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62419; propagated from
                     UniProtKB/Swiss-Prot (Q99961.1)"
     CDS             1..368
                     /gene="SH3GL1"
                     /gene_synonym="CNSA1; EEN; SH3D2B; SH3P8"
                     /coded_by="NM_003025.4:180..1286"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32874.1"
                     /db_xref="GeneID:6455"
                     /db_xref="HGNC:HGNC:10830"
                     /db_xref="MIM:601768"
ORIGIN      
        1 msvaglkkqf ykasqlvsek vggaegtkld ddfkemekkv dvtskavtev lartieylqp
       61 npasrakltm lntvskirgq vknpgypqse gllgecmirh gkelggesnf gdalldages
      121 mkrlaevkds ldievkqnfi dplqnlcekd lkeiqhhlkk legrrldfdy kkkrqgkipd
      181 eelrqalekf eeskevaets mhnlletdie qvsqlsalvd aqldyhrqav qildelaekl
      241 krrmreassr pkreykpkpr epfdlgepeq snggfpctta pkiaasssfr ssdkpirtps
      301 rsmppldqps ckalydfepe ndgelgfheg dvitltnqid enwyegmldg qsgffplsyv
      361 evlvplpq
//
