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Q8CBW3

- ABI1_MOUSE

UniProt

Q8CBW3 - ABI1_MOUSE

Protein

Abl interactor 1

Gene

Abi1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the transforming activity of Abelson murine leukemia virus (v-Abl) after overexpression in fibroblasts. May play a role in regulation EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.6 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein tyrosine kinase activator activity Source: MGI

    GO - Biological processi

    1. cellular component movement Source: Ensembl
    2. cellular process Source: MGI
    3. lamellipodium morphogenesis Source: MGI
    4. megakaryocyte development Source: MGI
    5. peptidyl-tyrosine phosphorylation Source: MGI
    6. positive regulation of protein tyrosine kinase activity Source: GOC
    7. somitogenesis Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abl interactor 1
    Alternative name(s):
    Abelson interactor 1
    Short name:
    Abi-1
    Ablphilin-1
    Eps8 SH3 domain-binding protein
    Short name:
    Eps8-binding protein
    Spectrin SH3 domain-binding protein 1
    e3B1
    Gene namesi
    Name:Abi1
    Synonyms:Ssh3bp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:104913. Abi1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell projectiongrowth cone By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cytoplasmcytoskeleton By similarity
    Note: Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell leading edge Source: MGI
    3. cytoplasm Source: UniProtKB-SubCell
    4. filopodium Source: UniProtKB-SubCell
    5. growth cone Source: UniProtKB-SubCell
    6. intracellular Source: MGI
    7. lamellipodium Source: MGI
    8. neuron projection Source: BHF-UCL
    9. nucleus Source: UniProtKB-SubCell
    10. postsynaptic density Source: UniProtKB-SubCell
    11. postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 481480Abl interactor 1PRO_0000191788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei53 – 531PhosphotyrosineBy similarity
    Modified residuei183 – 1831Phosphoserine3 Publications
    Modified residuei213 – 2131Phosphotyrosine; alternate2 Publications
    Modified residuei213 – 2131Phosphotyrosine; by ABL1; alternateBy similarity
    Modified residuei216 – 2161PhosphoserineBy similarity
    Modified residuei222 – 2221PhosphoserineBy similarity
    Modified residuei225 – 2251PhosphoserineBy similarity
    Modified residuei296 – 2961PhosphoserineBy similarity
    Modified residuei428 – 4281Phosphotyrosine2 Publications
    Modified residuei480 – 4801PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1, required for nuclear but not for synaptic localization By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8CBW3.
    PaxDbiQ8CBW3.
    PRIDEiQ8CBW3.

    PTM databases

    PhosphoSiteiQ8CBW3.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in bone marrow, spleen, brain, testes, and embryonic brain. In adult brain prominently expressed in the neocortex, hippocampus and dentate gyrus.2 Publications

    Developmental stagei

    Detected at E10 and E12 in developing brain, but does not appear more prominent in the neuroepithelium compared to the surrounding tissue.1 Publication

    Gene expression databases

    ArrayExpressiQ8CBW3.
    BgeeiQ8CBW3.
    CleanExiMM_ABI1.
    GenevestigatoriQ8CBW3.

    Interactioni

    Subunit structurei

    Interacts with ENAH, Abelson murine leukemia virus V-ABL, ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1. Part of a complex consisting of ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with EPS8, SOS1, SOS2, GRB2, SPTA1, and the first SH3 domain of NCK1 By similarity. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is direct. Interacts with the heterodimer MYC:MAX; the interaction may enhance MYC:MAX transcriptional activity.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eps8Q085092EBI-375511,EBI-375596
    Sos2Q023842EBI-375511,EBI-395573

    Protein-protein interaction databases

    BioGridi197905. 7 interactions.
    DIPiDIP-29534N.
    IntActiQ8CBW3. 30 interactions.
    MINTiMINT-128698.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CBW3.
    SMRiQ8CBW3. Positions 1-154, 409-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 10763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini419 – 47860SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 7962Required for binding to WASF1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi337 – 39155Pro-richAdd
    BLAST

    Domaini

    The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.

    Sequence similaritiesi

    Belongs to the ABI family.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG262939.
    GeneTreeiENSGT00390000003756.
    HOGENOMiHOG000293213.
    HOVERGENiHBG050446.
    InParanoidiQ8CBW3.
    OMAiMPMFDDS.
    OrthoDBiEOG7J17ZT.
    PhylomeDBiQ8CBW3.
    TreeFamiTF314303.

    Family and domain databases

    InterProiIPR028457. ABI.
    IPR028456. ABI1.
    IPR012849. Abl-interactor_HHR_dom.
    IPR001452. SH3_domain.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PANTHERiPTHR10460. PTHR10460. 1 hit.
    PTHR10460:SF2. PTHR10460:SF2. 1 hit.
    PfamiPF07815. Abi_HHR. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    PS50192. T_SNARE. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CBW3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET    50
    KAYTTQSLAS VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH 100
    KEKVARREIG ILTTNKNTSR THKIIAPANM ERPVRYIRKP IDYTVLDDVG 150
    HGVKWLKAKH GNNQPARTGT LSRTNPPTQK PPSPPVSGRG TLGRNTPYKT 200
    LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS GSSGGSGSRE 250
    NSGSSSIGIP IAVPTPSPPT AGPAAPGAAP GSQYGTMTRQ ISRHNSTTSS 300
    TSSGGYRRTP SVAAQFSAQP HVNGGPLYSQ NSISVAPPPP PMPQLTPQIP 350
    LTGFVARVQE NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA 400
    VVQYSDPYAD GDPAWAPKNY IEKVVAIYDY TKDKDDELSF KEGAIIYVIK 450
    KNDDGWFEGV CNRVTGLFPG NYVESIMHYT D 481
    Length:481
    Mass (Da):52,288
    Last modified:January 23, 2007 - v3
    Checksum:i1654A1E89438BC1D
    GO
    Isoform 2 (identifier: Q8CBW3-2) [UniParc]FASTAAdd to Basket

    Also known as: short

    The sequence of this isoform differs from the canonical sequence as follows:
         154-158: Missing.
         274-274: Missing.
         333-361: Missing.

    Show »
    Length:446
    Mass (Da):48,512
    Checksum:i805A2F6072F1D24B
    GO
    Isoform 3 (identifier: Q8CBW3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-158: Missing.

    Show »
    Length:476
    Mass (Da):51,661
    Checksum:iB7E38AA1E9ED7FA6
    GO
    Isoform 4 (identifier: Q8CBW3-4) [UniParc]FASTAAdd to Basket

    Also known as: long

    The sequence of this isoform differs from the canonical sequence as follows:
         154-158: Missing.
         274-274: Missing.

    Show »
    Length:475
    Mass (Da):51,590
    Checksum:iA0A613AAD091B0F0
    GO
    Isoform 5 (identifier: Q8CBW3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-158: Missing.
         274-362: AAPGAAPGSQ...GFVARVQENI → V

    Show »
    Length:388
    Mass (Da):42,548
    Checksum:i27FAB95E05BCA655
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti313 – 3131A → T in AAH04657. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei154 – 1585Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 5 PublicationsVSP_010756
    Alternative sequencei274 – 36289AAPGA…VQENI → V in isoform 5. 1 PublicationVSP_022636Add
    BLAST
    Alternative sequencei274 – 2741Missing in isoform 2 and isoform 4. 3 PublicationsVSP_010757
    Alternative sequencei333 – 36129Missing in isoform 2. 1 PublicationVSP_010758Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420251 mRNA. Translation: AAL16036.1.
    AY033645 mRNA. Translation: AAK59381.1.
    AK034476 mRNA. Translation: BAC28722.1.
    AK152061 mRNA. Translation: BAE30917.1.
    AK152184 mRNA. Translation: BAE31015.1.
    AK151026 mRNA. Translation: BAE30044.1.
    BC004657 mRNA. Translation: AAH04657.1.
    U17698 mRNA. Translation: AAB00373.1. Sequence problems.
    CCDSiCCDS38058.1. [Q8CBW3-5]
    CCDS38059.1. [Q8CBW3-3]
    CCDS38060.1. [Q8CBW3-2]
    CCDS38061.1. [Q8CBW3-1]
    CCDS50513.1. [Q8CBW3-4]
    RefSeqiNP_001070658.1. NM_001077190.2. [Q8CBW3-1]
    NP_001070660.1. NM_001077192.2. [Q8CBW3-2]
    NP_001070661.1. NM_001077193.2. [Q8CBW3-5]
    NP_031406.2. NM_007380.3. [Q8CBW3-4]
    UniGeneiMm.205647.
    Mm.249752.

    Genome annotation databases

    EnsembliENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835. [Q8CBW3-5]
    ENSMUST00000123948; ENSMUSP00000118491; ENSMUSG00000058835. [Q8CBW3-1]
    ENSMUST00000126112; ENSMUSP00000117335; ENSMUSG00000058835. [Q8CBW3-3]
    ENSMUST00000140164; ENSMUSP00000120462; ENSMUSG00000058835. [Q8CBW3-4]
    ENSMUST00000149719; ENSMUSP00000120621; ENSMUSG00000058835. [Q8CBW3-2]
    GeneIDi11308.
    KEGGimmu:11308.
    UCSCiuc008ins.1. mouse. [Q8CBW3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420251 mRNA. Translation: AAL16036.1 .
    AY033645 mRNA. Translation: AAK59381.1 .
    AK034476 mRNA. Translation: BAC28722.1 .
    AK152061 mRNA. Translation: BAE30917.1 .
    AK152184 mRNA. Translation: BAE31015.1 .
    AK151026 mRNA. Translation: BAE30044.1 .
    BC004657 mRNA. Translation: AAH04657.1 .
    U17698 mRNA. Translation: AAB00373.1 . Sequence problems.
    CCDSi CCDS38058.1. [Q8CBW3-5 ]
    CCDS38059.1. [Q8CBW3-3 ]
    CCDS38060.1. [Q8CBW3-2 ]
    CCDS38061.1. [Q8CBW3-1 ]
    CCDS50513.1. [Q8CBW3-4 ]
    RefSeqi NP_001070658.1. NM_001077190.2. [Q8CBW3-1 ]
    NP_001070660.1. NM_001077192.2. [Q8CBW3-2 ]
    NP_001070661.1. NM_001077193.2. [Q8CBW3-5 ]
    NP_031406.2. NM_007380.3. [Q8CBW3-4 ]
    UniGenei Mm.205647.
    Mm.249752.

    3D structure databases

    ProteinModelPortali Q8CBW3.
    SMRi Q8CBW3. Positions 1-154, 409-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197905. 7 interactions.
    DIPi DIP-29534N.
    IntActi Q8CBW3. 30 interactions.
    MINTi MINT-128698.

    PTM databases

    PhosphoSitei Q8CBW3.

    Proteomic databases

    MaxQBi Q8CBW3.
    PaxDbi Q8CBW3.
    PRIDEi Q8CBW3.

    Protocols and materials databases

    DNASUi 11308.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000114544 ; ENSMUSP00000110191 ; ENSMUSG00000058835 . [Q8CBW3-5 ]
    ENSMUST00000123948 ; ENSMUSP00000118491 ; ENSMUSG00000058835 . [Q8CBW3-1 ]
    ENSMUST00000126112 ; ENSMUSP00000117335 ; ENSMUSG00000058835 . [Q8CBW3-3 ]
    ENSMUST00000140164 ; ENSMUSP00000120462 ; ENSMUSG00000058835 . [Q8CBW3-4 ]
    ENSMUST00000149719 ; ENSMUSP00000120621 ; ENSMUSG00000058835 . [Q8CBW3-2 ]
    GeneIDi 11308.
    KEGGi mmu:11308.
    UCSCi uc008ins.1. mouse. [Q8CBW3-1 ]

    Organism-specific databases

    CTDi 10006.
    MGIi MGI:104913. Abi1.

    Phylogenomic databases

    eggNOGi NOG262939.
    GeneTreei ENSGT00390000003756.
    HOGENOMi HOG000293213.
    HOVERGENi HBG050446.
    InParanoidi Q8CBW3.
    OMAi MPMFDDS.
    OrthoDBi EOG7J17ZT.
    PhylomeDBi Q8CBW3.
    TreeFami TF314303.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi ABI1. mouse.
    NextBioi 278608.
    PROi Q8CBW3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CBW3.
    Bgeei Q8CBW3.
    CleanExi MM_ABI1.
    Genevestigatori Q8CBW3.

    Family and domain databases

    InterProi IPR028457. ABI.
    IPR028456. ABI1.
    IPR012849. Abl-interactor_HHR_dom.
    IPR001452. SH3_domain.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    PANTHERi PTHR10460. PTHR10460. 1 hit.
    PTHR10460:SF2. PTHR10460:SF2. 1 hit.
    Pfami PF07815. Abi_HHR. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    PS50192. T_SNARE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of v-Abl transformation in 3T3 cells overexpressing different forms of the Abelson interactor protein Abi-1."
      Ikeguchi A., Yang H.-Y., Gao G., Goff S.P.
      Oncogene 20:4926-4934(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION.
      Strain: BALB/c.
    2. "t(10;11)-acute leukemias with MLL-AF10 and MLL-ABI1 chimeric transcripts: specific expression patterns of ABI1 gene in leukemia and solid tumor cell lines."
      Shibuya N., Taki T., Mugishima H., Chin M., Tsuchida M., Sako M., Kawa K., Ishii E., Miura I., Yanagisawa M., Hayashi Y.
      Genes Chromosomes Cancer 32:1-10(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
      Strain: C57BL/6J.
      Tissue: Bone marrow and Diencephalon.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. "Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity."
      Shi Y., Alin K., Goff S.P.
      Genes Dev. 9:2583-2597(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-360 (ISOFORM 4), FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH ABL1 AND V-ABL.
    6. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH EPS8 AND SOS1.
    7. "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase."
      Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., Shishido T.
      J. Biol. Chem. 278:21685-21692(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ENAH.
    8. "Abl interactor 1 (Abi-1) wave-binding and SNARE domains regulate its nucleocytoplasmic shuttling, lamellipodium localization, and wave-1 levels."
      Echarri A., Lai M.J., Robinson M.R., Pendergast A.M.
      Mol. Cell. Biol. 24:4979-4993(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX1A; SNAP25; VAMP2 AND WASF1.
    9. "Localization and phosphorylation of Abl-interactor proteins, Abi-1 and Abi-2, in the developing nervous system."
      Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S., Pendergast A.M.
      Mol. Cell. Neurosci. 16:244-257(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. "The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia."
      Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V., Pendergast A.M.
      Curr. Biol. 11:891-895(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation."
      Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J., Stradal T.E.B.
      EMBO J. 23:749-759(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF WAVE2 COMPLEX.
      Strain: C57BL/6.
      Tissue: Brain.
    12. "Eps8 controls actin-based motility by capping the barbed ends of actin filaments."
      Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E., Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.
      Nat. Cell Biol. 6:1180-1188(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPS8.
    13. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    14. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiABI1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CBW3
    Secondary accession number(s): Q3U8V0
    , Q60747, Q91ZM5, Q923I9, Q99KH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3