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ABI3_MOUSE
ID   ABI3_MOUSE              Reviewed;         367 AA.
AC   Q8BYZ1; Q3TA46; Q6PE63; Q9D7S4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=ABI gene family member 3;
DE   AltName: Full=New molecule including SH3;
DE            Short=Nesh;
GN   Name=Abi3; Synonyms=Nesh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, Spleen, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
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.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-219, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Inhibits ectopic tumor cell metastasis of SRD cells. In
CC       vitro, reduces cell motility. {ECO:0000269|PubMed:11956071}.
CC   -!- SUBUNIT: May interact with PAK1 and PAK2. Probably interacts with TARSH
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYZ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYZ1-2; Sequence=VSP_010773;
CC   -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR   EMBL; AK008928; BAB25972.1; -; mRNA.
DR   EMBL; AK037144; BAC29720.1; -; mRNA.
DR   EMBL; AK172098; BAE42824.1; -; mRNA.
DR   EMBL; AL593858; CAM15513.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL15995.1; -; Genomic_DNA.
DR   EMBL; BC058260; AAH58260.1; -; mRNA.
DR   CCDS; CCDS25283.1; -. [Q8BYZ1-1]
DR   RefSeq; NP_001156936.1; NM_001163464.1. [Q8BYZ1-2]
DR   RefSeq; NP_079935.1; NM_025659.4. [Q8BYZ1-1]
DR   RefSeq; XP_017170199.1; XM_017314710.1. [Q8BYZ1-2]
DR   AlphaFoldDB; Q8BYZ1; -.
DR   SMR; Q8BYZ1; -.
DR   BioGRID; 211593; 4.
DR   IntAct; Q8BYZ1; 1.
DR   MINT; Q8BYZ1; -.
DR   STRING; 10090.ENSMUSP00000061893; -.
DR   iPTMnet; Q8BYZ1; -.
DR   PhosphoSitePlus; Q8BYZ1; -.
DR   EPD; Q8BYZ1; -.
DR   jPOST; Q8BYZ1; -.
DR   MaxQB; Q8BYZ1; -.
DR   PaxDb; Q8BYZ1; -.
DR   PRIDE; Q8BYZ1; -.
DR   ProteomicsDB; 285629; -. [Q8BYZ1-1]
DR   ProteomicsDB; 285630; -. [Q8BYZ1-2]
DR   Antibodypedia; 53503; 100 antibodies from 23 providers.
DR   DNASU; 66610; -.
DR   Ensembl; ENSMUST00000059026; ENSMUSP00000061893; ENSMUSG00000018381. [Q8BYZ1-1]
DR   GeneID; 66610; -.
DR   KEGG; mmu:66610; -.
DR   UCSC; uc007lat.2; mouse. [Q8BYZ1-1]
DR   CTD; 51225; -.
DR   MGI; MGI:1913860; Abi3.
DR   VEuPathDB; HostDB:ENSMUSG00000018381; -.
DR   eggNOG; KOG2546; Eukaryota.
DR   GeneTree; ENSGT00940000161380; -.
DR   HOGENOM; CLU_035421_0_0_1; -.
DR   InParanoid; Q8BYZ1; -.
DR   OMA; DQMVNMH; -.
DR   OrthoDB; 1478981at2759; -.
DR   PhylomeDB; Q8BYZ1; -.
DR   TreeFam; TF314303; -.
DR   BioGRID-ORCS; 66610; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Abi3; mouse.
DR   PRO; PR:Q8BYZ1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8BYZ1; protein.
DR   Bgee; ENSMUSG00000018381; Expressed in thymus and 114 other tissues.
DR   ExpressionAtlas; Q8BYZ1; baseline and differential.
DR   Genevisible; Q8BYZ1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:ARUK-UCL.
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; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR   GO; GO:0002357; P:defense response to tumor cell; IDA:ARUK-UCL.
DR   GO; GO:0010593; P:negative regulation of lamellipodium assembly; IMP:ARUK-UCL.
DR   GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; ISS:ARUK-UCL.
DR   GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:ARUK-UCL.
DR   GO; GO:0030334; P:regulation of cell migration; ISO: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..367
FT                   /note="ABI gene family member 3"
FT                   /id="PRO_0000191793"
FT   DOMAIN          309..367
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          163..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..64
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2A4"
FT   VAR_SEQ         1..53
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010773"
FT   CONFLICT        339
FT                   /note="T -> I (in Ref. 4; AAH58260)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  39107 MW;  0CEC0279F45A62F7 CRC64;
     MAELQQLQQL QEFDIPTGRE ALRGNHSALL RVANYCEDNY LQATDKRKAL EETMAFTTQA
     LASVAYQVGN LAGHTLRMLD LQGAALRQVE AKMSTLGQMV NMHMEKVARR EIGTLATVVR
     LPSNQKVIPP ESLPSLTPYH RKPLNFACLD DIGHGVKDLS TQLSRTGTLS RKSIKAPATP
     VSATLGRPPR IPEPVQLPAV PDGKLSAASS ASSLASAGSA EGASGIPQSK GQVAPATPPP
     PPVAPVTPPP PPLSAEVFLP PPPLEVSQPP LEAELPLPPP PALEGDELGL LPPPPPGFGP
     DEPSWVPASY LEKVVTLYPY TRQKDNELSF SEGTVICVTR RYSDGWCEGV SSEGTGFFPG
     NYVEPSC
 
 
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