ABI3_HUMAN
ID ABI3_HUMAN Reviewed; 366 AA.
AC Q9P2A4; C9IZN8; Q9H0P6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ABI gene family member 3;
DE AltName: Full=New molecule including SH3;
DE Short=Nesh;
GN Name=ABI3; Synonyms=NESH;
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), TISSUE SPECIFICITY, AND VARIANT
RP SER-209.
RC TISSUE=Placenta;
RX PubMed=10978530; DOI=10.1016/s0167-4781(00)00158-5;
RA Miyazaki K., Matsuda S., Ichigotani Y., Takenouchi Y., Hayashi K.,
RA Fukuda Y., Nimura Y., Hamaguchi M.;
RT "Isolation and characterization of a novel human gene (NESH) which encodes
RT a putative signaling molecule similar to e3B1 protein.";
RL Biochim. Biophys. Acta 1493:237-241(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-44 AND
RP SER-209.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-209.
RC TISSUE=B-cell;
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 [5]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11956071;
RA Ichigotani Y., Yokozaki S., Fukuda Y., Hamaguchi M., Matsuda S.;
RT "Forced expression of NESH suppresses motility and metastatic dissemination
RT of malignant cells.";
RL Cancer Res. 62:2215-2219(2002).
RN [6]
RP INTERACTION WITH TARSH.
RX PubMed=11501947; DOI=10.1007/s100380170049;
RA Matsuda S., Iriyama C., Yokozaki S., Ichigotani Y., Shirafuji N.,
RA Yamaki K., Hayakawa T., Hamaguchi M.;
RT "Cloning and sequencing of a novel human gene that encodes a putative
RT target protein of Nesh-SH3.";
RL J. Hum. Genet. 46:483-486(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-216 AND SER-342,
RP VARIANT [LARGE SCALE ANALYSIS] SER-209, AND IDENTIFICATION BY MASS
RP 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: May inhibit tumor metastasis (By similarity). In vitro,
CC reduces cell motility. {ECO:0000250, ECO:0000269|PubMed:11956071}.
CC -!- SUBUNIT: May interact with PAK1 and PAK2. Probably interacts with
CC TARSH. {ECO:0000269|PubMed:11501947}.
CC -!- INTERACTION:
CC Q9P2A4; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-742038, EBI-11096309;
CC Q9P2A4; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-742038, EBI-742038;
CC Q9P2A4; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-742038, EBI-750254;
CC Q9P2A4; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-742038, EBI-742909;
CC Q9P2A4; Q13515: BFSP2; NbExp=5; IntAct=EBI-742038, EBI-10229433;
CC Q9P2A4; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-742038, EBI-465861;
CC Q9P2A4; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-742038, EBI-2350265;
CC Q9P2A4; Q9C0F1: CEP44; NbExp=9; IntAct=EBI-742038, EBI-744115;
CC Q9P2A4; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-742038, EBI-2806959;
CC Q9P2A4; O60941: DTNB; NbExp=3; IntAct=EBI-742038, EBI-740402;
CC Q9P2A4; O15372: EIF3H; NbExp=6; IntAct=EBI-742038, EBI-709735;
CC Q9P2A4; Q7L2H7: EIF3M; NbExp=3; IntAct=EBI-742038, EBI-353901;
CC Q9P2A4; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-742038, EBI-10184995;
CC Q9P2A4; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-742038, EBI-11748557;
CC Q9P2A4; Q9UI08: EVL; NbExp=4; IntAct=EBI-742038, EBI-346653;
CC Q9P2A4; Q9UI08-2: EVL; NbExp=3; IntAct=EBI-742038, EBI-6448852;
CC Q9P2A4; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-742038, EBI-11986315;
CC Q9P2A4; Q9Y285: FARSA; NbExp=3; IntAct=EBI-742038, EBI-725361;
CC Q9P2A4; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-742038, EBI-10244131;
CC Q9P2A4; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-742038, EBI-11427343;
CC Q9P2A4; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-742038, EBI-712073;
CC Q9P2A4; P62993: GRB2; NbExp=3; IntAct=EBI-742038, EBI-401755;
CC Q9P2A4; Q86YM7: HOMER1; NbExp=4; IntAct=EBI-742038, EBI-746815;
CC Q9P2A4; Q9NSB8-2: HOMER2; NbExp=3; IntAct=EBI-742038, EBI-12017090;
CC Q9P2A4; Q9NSC5: HOMER3; NbExp=8; IntAct=EBI-742038, EBI-748420;
CC Q9P2A4; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-742038, EBI-9091197;
CC Q9P2A4; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-742038, EBI-8638439;
CC Q9P2A4; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-742038, EBI-2556193;
CC Q9P2A4; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-742038, EBI-739493;
CC Q9P2A4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-742038, EBI-14069005;
CC Q9P2A4; Q6P597: KLC3; NbExp=3; IntAct=EBI-742038, EBI-1643885;
CC Q9P2A4; Q9NSK0: KLC4; NbExp=3; IntAct=EBI-742038, EBI-949319;
CC Q9P2A4; A1A4E9: KRT13; NbExp=3; IntAct=EBI-742038, EBI-10171552;
CC Q9P2A4; P02533: KRT14; NbExp=3; IntAct=EBI-742038, EBI-702178;
CC Q9P2A4; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-742038, EBI-2952736;
CC Q9P2A4; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-742038, EBI-11980489;
CC Q9P2A4; Q15323: KRT31; NbExp=3; IntAct=EBI-742038, EBI-948001;
CC Q9P2A4; Q92764: KRT35; NbExp=3; IntAct=EBI-742038, EBI-1058674;
CC Q9P2A4; O76013-2: KRT36; NbExp=3; IntAct=EBI-742038, EBI-11958506;
CC Q9P2A4; O76015: KRT38; NbExp=3; IntAct=EBI-742038, EBI-1047263;
CC Q9P2A4; P43365: MAGEA12; NbExp=3; IntAct=EBI-742038, EBI-749530;
CC Q9P2A4; Q9NX70: MED29; NbExp=3; IntAct=EBI-742038, EBI-394656;
CC Q9P2A4; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-742038, EBI-1104552;
CC Q9P2A4; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-742038, EBI-995714;
CC Q9P2A4; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-742038, EBI-748896;
CC Q9P2A4; O43639: NCK2; NbExp=6; IntAct=EBI-742038, EBI-713635;
CC Q9P2A4; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-742038, EBI-928842;
CC Q9P2A4; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-742038, EBI-2859639;
CC Q9P2A4; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-742038, EBI-2811583;
CC Q9P2A4; O43482: OIP5; NbExp=3; IntAct=EBI-742038, EBI-536879;
CC Q9P2A4; P25786: PSMA1; NbExp=3; IntAct=EBI-742038, EBI-359352;
CC Q9P2A4; Q7L099: RUFY3; NbExp=3; IntAct=EBI-742038, EBI-722392;
CC Q9P2A4; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-742038, EBI-11984663;
CC Q9P2A4; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-742038, EBI-10224192;
CC Q9P2A4; Q9Y3L3: SH3BP1; NbExp=3; IntAct=EBI-742038, EBI-346869;
CC Q9P2A4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-742038, EBI-358489;
CC Q9P2A4; Q16623: STX1A; NbExp=3; IntAct=EBI-742038, EBI-712466;
CC Q9P2A4; P32856-2: STX2; NbExp=3; IntAct=EBI-742038, EBI-11956649;
CC Q9P2A4; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-742038, EBI-740595;
CC Q9P2A4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-742038, EBI-3650647;
CC Q9P2A4; Q99757: TXN2; NbExp=3; IntAct=EBI-742038, EBI-2932492;
CC Q9P2A4; Q5ST30: VARS2; NbExp=3; IntAct=EBI-742038, EBI-2116622;
CC Q9P2A4; P50552: VASP; NbExp=9; IntAct=EBI-742038, EBI-748201;
CC Q9P2A4; P42768: WAS; NbExp=4; IntAct=EBI-742038, EBI-346375;
CC Q9P2A4; Q92558: WASF1; NbExp=3; IntAct=EBI-742038, EBI-1548747;
CC Q9P2A4; B2R8Y4; NbExp=3; IntAct=EBI-742038, EBI-10175581;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11956071}.
CC Note=Colocalizes with PAK2 at leading edge of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2A4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2A4-2; Sequence=VSP_041467;
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, liver, pancreas, kidney,
CC placenta and at low levels in brain and skeletal muscle.
CC {ECO:0000269|PubMed:10978530}.
CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR EMBL; AB037886; BAA90667.1; -; mRNA.
DR EMBL; AL136709; CAB66644.1; -; mRNA.
DR EMBL; AC004797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007780; AAH07780.1; -; mRNA.
DR CCDS; CCDS11546.1; -. [Q9P2A4-1]
DR CCDS; CCDS45725.1; -. [Q9P2A4-2]
DR RefSeq; NP_001128658.1; NM_001135186.1. [Q9P2A4-2]
DR RefSeq; NP_057512.1; NM_016428.2. [Q9P2A4-1]
DR AlphaFoldDB; Q9P2A4; -.
DR SMR; Q9P2A4; -.
DR BioGRID; 119389; 91.
DR CORUM; Q9P2A4; -.
DR IntAct; Q9P2A4; 75.
DR MINT; Q9P2A4; -.
DR STRING; 9606.ENSP00000225941; -.
DR iPTMnet; Q9P2A4; -.
DR PhosphoSitePlus; Q9P2A4; -.
DR BioMuta; ABI3; -.
DR DMDM; 296434384; -.
DR EPD; Q9P2A4; -.
DR jPOST; Q9P2A4; -.
DR MassIVE; Q9P2A4; -.
DR MaxQB; Q9P2A4; -.
DR PaxDb; Q9P2A4; -.
DR PeptideAtlas; Q9P2A4; -.
DR PRIDE; Q9P2A4; -.
DR ProteomicsDB; 83763; -. [Q9P2A4-1]
DR ProteomicsDB; 83764; -. [Q9P2A4-2]
DR Antibodypedia; 53503; 100 antibodies from 23 providers.
DR DNASU; 51225; -.
DR Ensembl; ENST00000225941.6; ENSP00000225941.1; ENSG00000108798.9. [Q9P2A4-1]
DR Ensembl; ENST00000419580.6; ENSP00000406651.2; ENSG00000108798.9. [Q9P2A4-2]
DR GeneID; 51225; -.
DR KEGG; hsa:51225; -.
DR MANE-Select; ENST00000225941.6; ENSP00000225941.1; NM_016428.3; NP_057512.2.
DR UCSC; uc002iop.1; human. [Q9P2A4-1]
DR CTD; 51225; -.
DR DisGeNET; 51225; -.
DR GeneCards; ABI3; -.
DR HGNC; HGNC:29859; ABI3.
DR HPA; ENSG00000108798; Tissue enhanced (lymphoid).
DR MIM; 606363; gene.
DR neXtProt; NX_Q9P2A4; -.
DR OpenTargets; ENSG00000108798; -.
DR PharmGKB; PA134951642; -.
DR VEuPathDB; HostDB:ENSG00000108798; -.
DR eggNOG; KOG2546; Eukaryota.
DR GeneTree; ENSGT00940000161380; -.
DR HOGENOM; CLU_035421_0_0_1; -.
DR InParanoid; Q9P2A4; -.
DR OMA; DQMVNMH; -.
DR OrthoDB; 1478981at2759; -.
DR PhylomeDB; Q9P2A4; -.
DR TreeFam; TF314303; -.
DR PathwayCommons; Q9P2A4; -.
DR SignaLink; Q9P2A4; -.
DR BioGRID-ORCS; 51225; 6 hits in 1058 CRISPR screens.
DR ChiTaRS; ABI3; human.
DR GeneWiki; ABI3; -.
DR GenomeRNAi; 51225; -.
DR Pharos; Q9P2A4; Tbio.
DR PRO; PR:Q9P2A4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P2A4; protein.
DR Bgee; ENSG00000108798; Expressed in granulocyte and 136 other tissues.
DR ExpressionAtlas; Q9P2A4; baseline and differential.
DR Genevisible; Q9P2A4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0043198; C:dendritic shaft; ISS:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:ARUK-UCL.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:ARUK-UCL.
DR GO; GO:0031209; C:SCAR complex; IDA:ARUK-UCL.
DR GO; GO:0051015; F:actin filament binding; ISS:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0002357; P:defense response to tumor cell; IMP:ARUK-UCL.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISS:ARUK-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISS:ARUK-UCL.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; NAS:ARUK-UCL.
DR GO; GO:2000774; P:positive regulation of cellular senescence; IMP:ARUK-UCL.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:ARUK-UCL.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:ARUK-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISS:ARUK-UCL.
DR InterPro; IPR028457; ABI.
DR InterPro; IPR028455; ABI3.
DR InterPro; IPR012849; Abl-interactor_HHR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10460; PTHR10460; 1.
DR PANTHER; PTHR10460:SF7; PTHR10460:SF7; 1.
DR Pfam; PF07815; Abi_HHR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..366
FT /note="ABI gene family member 3"
FT /id="PRO_0000191792"
FT DOMAIN 308..366
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 161..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..61
FT /evidence="ECO:0000255"
FT COMPBIAS 228..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 90..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041467"
FT VARIANT 44
FT /note="R -> Q (in dbSNP:rs2233369)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_022030"
FT VARIANT 203
FT /note="S -> F (in dbSNP:rs616338)"
FT /id="VAR_060243"
FT VARIANT 209
FT /note="F -> S (in dbSNP:rs616338)"
FT /evidence="ECO:0000269|PubMed:10978530,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:15489334,
FT ECO:0007744|PubMed:24275569"
FT /id="VAR_060993"
SQ SEQUENCE 366 AA; 39035 MW; 23EC3838E41D8ECD CRC64;
MAELQQLQEF EIPTGREALR GNHSALLRVA DYCEDNYVQA TDKRKALEET MAFTTQALAS
VAYQVGNLAG HTLRMLDLQG AALRQVEARV STLGQMVNMH MEKVARREIG TLATVQRLPP
GQKVIAPENL PPLTPYCRRP LNFGCLDDIG HGIKDLSTQL SRTGTLSRKS IKAPATPASA
TLGRPPRIPE PVHLPVVPDG RLSAASSAFS LASAGSAEGV GGAPTPKGQA APPAPPLPSS
LDPPPPPAAV EVFQRPPTLE ELSPPPPDEE LPLPLDLPPP PPLDGDELGL PPPPPGFGPD
EPSWVPASYL EKVVTLYPYT SQKDNELSFS EGTVICVTRR YSDGWCEGVS SEGTGFFPGN
YVEPSC
