LOCUS       NP_001138360             534 aa            linear   PRI 29-APR-2025
DEFINITION  BAR/IMD domain-containing adapter protein 2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001138360
VERSION     NP_001138360.1
DBSOURCE    REFSEQ: accession NM_001144888.2
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 534)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Mukherjee,A., Ron,J.E., Hu,H.T., Nishimura,T., Hanawa-Suetsugu,K.,
            Behkam,B., Mimori-Kiyosue,Y., Gov,N.S., Suetsugu,S. and Nain,A.S.
  TITLE     Actin Filaments Couple the Protrusive Tips to the Nucleus through
            the I-BAR Domain Protein IRSp53 during the Migration of Cells on 1D
            Fibers
  JOURNAL   Adv Sci (Weinh) 10 (7), e2207368 (2023)
   PUBMED   36698307
  REMARK    GeneRIF: Actin Filaments Couple the Protrusive Tips to the Nucleus
            through the I-BAR Domain Protein IRSp53 during the Migration of
            Cells on 1D Fibers.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 534)
  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   6  (residues 1 to 534)
  AUTHORS   Miyahara,A., Okamura-Oho,Y., Miyashita,T., Hoshika,A. and Yamada,M.
  TITLE     Genomic structure and alternative splicing of the insulin receptor
            tyrosine kinase substrate of 53-kDa protein
  JOURNAL   J Hum Genet 48 (8), 410-414 (2003)
   PUBMED   12884081
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Fujiwara,T., Mammoto,A., Kim,Y. and Takai,Y.
  TITLE     Rho small G-protein-dependent binding of mDia to an Src homology 3
            domain-containing IRSp53/BAIAP2
  JOURNAL   Biochem Biophys Res Commun 271 (3), 626-629 (2000)
   PUBMED   10814512
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Abbott,M.A., Wells,D.G. and Fallon,J.R.
  TITLE     The insulin receptor tyrosine kinase substrate p58/53 and the
            insulin receptor are components of CNS synapses
  JOURNAL   J Neurosci 19 (17), 7300-7308 (1999)
   PUBMED   10460236
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Okamura-Oho,Y., Miyashita,T., Ohmi,K. and Yamada,M.
  TITLE     Dentatorubral-pallidoluysian atrophy protein interacts through a
            proline-rich region near polyglutamine with the SH3 domain of an
            insulin receptor tyrosine kinase substrate
  JOURNAL   Hum Mol Genet 8 (6), 947-957 (1999)
   PUBMED   10332026
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Oda,K., Shiratsuchi,T., Nishimori,H., Inazawa,J., Yoshikawa,H.,
            Taketani,Y., Nakamura,Y. and Tokino,T.
  TITLE     Identification of BAIAP2 (BAI-associated protein 2), a novel human
            homologue of hamster IRSp53, whose SH3 domain interacts with the
            cytoplasmic domain of BAI1
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 75-82 (1999)
   PUBMED   10343108
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB153324.1, BC002495.2 and
            AC115099.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene has been identified as a
            brain-specific angiogenesis inhibitor (BAI1)-binding protein. This
            adaptor protein links membrane bound G-proteins to cytoplasmic
            effector proteins. This protein functions as an insulin receptor
            tyrosine kinase substrate and suggests a role for insulin in the
            central nervous system. It also associates with a downstream
            effector of Rho small G proteins, which is associated with the
            formation of stress fibers and cytokinesis. This protein is
            involved in lamellipodia and filopodia formation in motile cells
            and may affect neuronal growth-cone guidance. This protein has also
            been identified as interacting with the
            dentatorubral-pallidoluysian atrophy gene, which is associated with
            an autosomal dominant neurodegenerative disease. Alternative
            splicing results in multiple transcript variants encoding distinct
            isoforms.[provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (4) shares identical sequence with
            variants 1, 2 and 3, but diverges after amino acid 511 resulting in
            a distinct 23 amino acid sequence at the C-terminus. This
            transcript variant encodes isoform 4 and is alternatively referred
            to as variant M.
            
            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 :: AK225612.1, SRR7410570.636458.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428708.7/ ENSP00000401022.2
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..534
                     /product="BAR/IMD domain-containing adapter protein 2
                     isoform 4"
                     /note="brain-specific angiogenesis inhibitor 1-associated
                     protein 2; insulin receptor substrate p53/p58; fas
                     ligand-associated factor 3; WASP and MIM like; IRS-58;
                     IRSp53/58; BAR/IMD domain-containing adapter protein 2;
                     insulin receptor substrate protein of 53 kDa; insulin
                     receptor substrate of 53 kDa; BAI1 associated protein 2"
                     /calculated_mol_wt=58883
     Region          5..236
                     /region_name="I-BAR_IMD_IRSp53"
                     /note="Inverse (I)-BAR, also known as the IRSp53/MIM
                     homology Domain (IMD), of Insulin Receptor tyrosine kinase
                     Substrate p53; cd07646"
                     /db_xref="CDD:153330"
     Site            order(5,9,12,15..16,23..24,27..28,31,34..35,37..38,41..42,
                     44..45,48..49,51..52,55..56,58..59,62..63,66..69,71..72,
                     75..76,79,86,97,101,176,180,183..184,187..188,190..192,
                     194..195,197..199,201..202,205..206,208..209,211..213,216,
                     219,223,226..227,229..230,232..233,235..236)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153330"
     Site            order(11,23,143)
                     /site_type="other"
                     /note="putative Rac binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:153330"
     Site            order(108,130,147,171)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153330"
     Site            order(142,145,147)
                     /site_type="other"
                     /note="putative actin binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:153330"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Region          295..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Region          377..435
                     /region_name="SH3_Irsp53"
                     /note="Src Homology 3 domain of Insulin Receptor tyrosine
                     kinase Substrate p53; cd11915"
                     /db_xref="CDD:212848"
     Site            order(382..383,385,392..393,405..406,411..413,415,
                     425..426,428..431)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212848"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKX1; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Region          447..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB8.1)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB8.1)"
     CDS             1..534
                     /gene="BAIAP2"
                     /gene_synonym="BAP2; FLAF3; IRSP53; WAML"
                     /coded_by="NM_001144888.2:105..1709"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45806.1"
                     /db_xref="GeneID:10458"
                     /db_xref="HGNC:HGNC:947"
                     /db_xref="MIM:605475"
ORIGIN      
        1 mslsrseemh rltenvykti meqfnpslrn fiamgknyek alagvtyaak gyfdalvkmg
       61 elasesqgsk elgdvlfqma evhrqiqnql eemlksfhne lltqleqkve ldsrylsaal
      121 kkyqteqrsk gdaldkcqae lkklrkksqg sknpqkysdk elqyidaisn kqgelenyvs
      181 dgyktaltee rrrfcflvek qcavaknsaa yhskgkella qklplwqqac adpskipera
      241 vqlmqqvasn gatlpsalsa sksnlvisdp ipgakplpvp pelapfvgrm saqestpimn
      301 gvtgpdgedy spwadrkaaq pkslsppqsq sklsdsysnt lpvrksvtpk nsyattenkt
      361 lprsssmaag lerngrmrvk aifshaagdn stllsfkegd litllvpear dgwhygesek
      421 tkmrgwfpfs ytrvldsdgs drlhmslqqg kssstgnlld kddlaipppd ygaasrafpa
      481 qtasgfkqrp ysvavpafsq glddygarsm srnpfahvql kptvtndrsa plls
//
