ABI1_RAT
ID ABI1_RAT Reviewed; 476 AA.
AC Q9QZM5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Abl interactor 1;
DE AltName: Full=Abelson interactor 1;
DE Short=Abi-1;
DE AltName: Full=Eps8 SH3 domain-binding protein;
DE Short=Eps8-binding protein;
DE AltName: Full=e3B1;
GN Name=Abi1 {ECO:0000312|RGD:621008};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Nicolas G., Galand C., Lecomte M.C.;
RT "cDNA sequence of the rat eps8 binding protein (e3B1).";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10995551; DOI=10.1006/mcne.2000.0865;
RA Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
RA Pendergast A.M.;
RT "Localization and phosphorylation of Abl-interactor proteins, Abi-1 and
RT Abi-2, in the developing nervous system.";
RL Mol. Cell. Neurosci. 16:244-257(2000).
RN [3]
RP FUNCTION IN NEUROGENESIS, INTERACTION WITH EPS8; MYC; MAX; SHANK2; SHANK3
RP AND WASF1, PHOSPHORYLATION AT TYR-53, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-53.
RX PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
RA Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
RA Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
RT "Abelson interacting protein 1 (Abi-1) is essential for dendrite
RT morphogenesis and synapse formation.";
RL EMBO J. 26:1397-1409(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May act in negative regulation of cell growth and
CC transformation by interacting with nonreceptor tyrosine kinases ABL1
CC and/or ABL2. May play a role in regulation of EGF-induced Erk pathway
CC activation. Involved in cytoskeletal reorganization and EGFR signaling.
CC Together with EPS8 participates in transduction of signals from Ras to
CC Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac
CC specific guanine nucleotide exchange factor (GEF) activity and ABI1
CC seems to act as an adapter in the complex. Regulates ABL1/c-Abl-
CC mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and
CC there seems to regulate WASF1 protein level. In brain, seems to
CC regulate the dendritic outgrowth and branching as well as to determine
CC the shape and number of synaptic contacts of developing neurons.
CC {ECO:0000269|PubMed:17304222}.
CC -!- SUBUNIT: Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, SOS1,
CC SOS2, GRB2, SPTA1, NCKAP1/NAP1, the first SH3 domain of NCK1 and
CC through its N-terminus with WASF1. Part of a complex consisting of
CC ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and
CC SOS1. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2.
CC Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the
CC interaction is direct. Interacts with the heterodimer MYC:MAX; the
CC interaction may enhance MYC:MAX transcriptional activity. Interacts
CC with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the
CC presence of FNBP1L (By similarity). {ECO:0000250|UniProtKB:Q8IZP0,
CC ECO:0000269|PubMed:17304222}.
CC -!- INTERACTION:
CC Q9QZM5; P52164: Max; NbExp=2; IntAct=EBI-920097, EBI-1184963;
CC Q9QZM5; Q9JLU4: Shank3; NbExp=7; IntAct=EBI-920097, EBI-6271152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:17304222}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:17304222}. Cell projection, filopodium
CC {ECO:0000269|PubMed:17304222}. Cell projection, growth cone
CC {ECO:0000269|PubMed:10995551}. Postsynaptic density
CC {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:17304222}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:17304222}. Note=Localized to
CC protruding lamellipodia and filopodia tips. May shuttle from the
CC postsynaptic densities to the nucleus. {ECO:0000269|PubMed:10995551,
CC ECO:0000269|PubMed:17304222}.
CC -!- TISSUE SPECIFICITY: Widely expressed in brain, high levels detected in
CC cortex, hippocampus and cerebellum (at protein level).
CC {ECO:0000269|PubMed:17304222}.
CC -!- DEVELOPMENTAL STAGE: Low protein levels at birth that increase
CC progressively at least until 14 days after birth.
CC {ECO:0000269|PubMed:17304222}.
CC -!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
CC sufficient for interaction with STX1A. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues after serum stimulation or
CC induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1,
CC required for nuclear but not for synaptic localization.
CC {ECO:0000269|PubMed:17304222}.
CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR EMBL; AF176784; AAD55263.1; -; mRNA.
DR RefSeq; XP_006254416.1; XM_006254354.3.
DR AlphaFoldDB; Q9QZM5; -.
DR SMR; Q9QZM5; -.
DR BioGRID; 249447; 1.
DR DIP; DIP-36968N; -.
DR IntAct; Q9QZM5; 8.
DR MINT; Q9QZM5; -.
DR STRING; 10116.ENSRNOP00000054381; -.
DR iPTMnet; Q9QZM5; -.
DR PhosphoSitePlus; Q9QZM5; -.
DR jPOST; Q9QZM5; -.
DR PaxDb; Q9QZM5; -.
DR PRIDE; Q9QZM5; -.
DR GeneID; 79249; -.
DR UCSC; RGD:621008; rat.
DR CTD; 10006; -.
DR RGD; 621008; Abi1.
DR VEuPathDB; HostDB:ENSRNOG00000031325; -.
DR eggNOG; KOG2546; Eukaryota.
DR InParanoid; Q9QZM5; -.
DR PhylomeDB; Q9QZM5; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q9QZM5; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000031325; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; Q9QZM5; baseline and differential.
DR Genevisible; Q9QZM5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0031209; C:SCAR complex; ISO:RGD.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:RGD.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISO:RGD.
DR GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR CDD; cd11971; SH3_Abi1; 1.
DR InterPro; IPR028457; ABI.
DR InterPro; IPR028456; ABI1.
DR InterPro; IPR035725; Abi1_SH3.
DR InterPro; IPR012849; Abl-interactor_HHR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR10460; PTHR10460; 1.
DR PANTHER; PTHR10460:SF2; PTHR10460:SF2; 1.
DR Pfam; PF07815; Abi_HHR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT CHAIN 2..476
FT /note="Abl interactor 1"
FT /id="PRO_0000191789"
FT DOMAIN 45..107
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 414..473
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 150..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17304222"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 208
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 423
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MUTAGEN 53
FT /note="Y->A: Not phosphorylated and perinuclear upon NMDA
FT treatment."
FT /evidence="ECO:0000269|PubMed:17304222"
SQ SEQUENCE 476 AA; 51705 MW; A2B8CC377090BEA6 CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP
VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG
SGSRENSGSS SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG
YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV ARVQENIADS
PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS DPYADGDPAW APKNYIEKVV
AIYDYTKDKD DELSFKEGAI IYVIKKNDDG WFEGVCNRVT GLFPGNYVES IMHYTD
