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Q9NYB9

- ABI2_HUMAN

UniProt

Q9NYB9 - ABI2_HUMAN

Protein

Abl interactor 2

Gene

ABI2

Organism
Homo sapiens (Human)
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 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May act in regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA.3 Publications

    GO - Molecular functioni

    1. cytoskeletal adaptor activity Source: UniProtKB
    2. DNA binding Source: ProtInc
    3. kinase binding Source: UniProtKB
    4. proline-rich region binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein complex binding Source: UniProt
    7. SH3 domain binding Source: UniProtKB
    8. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. actin polymerization or depolymerization Source: UniProtKB
    2. camera-type eye development Source: Ensembl
    3. cell migration Source: UniProtKB
    4. cellular component movement Source: UniProtKB
    5. cytoskeleton organization Source: UniProtKB
    6. dendrite development Source: Ensembl
    7. learning or memory Source: Ensembl
    8. peptidyl-tyrosine phosphorylation Source: MGI
    9. positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
    10. Rac protein signal transduction Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abl interactor 2
    Alternative name(s):
    Abelson interactor 2
    Short name:
    Abi-2
    Abl-binding protein 3
    Short name:
    AblBP3
    Arg-binding protein 1
    Short name:
    ArgBP1
    Gene namesi
    Name:ABI2
    Synonyms:ARGBPIA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:24011. ABI2.

    Subcellular locationi

    Cytoplasm By similarity
    Isoform 1 : Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cytoplasmcytoskeleton By similarity
    Note: Isoform 1 but not isoform 3 is localized to protruding lamellipodia and filopodia tips.By similarity

    GO - Cellular componenti

    1. cell-cell adherens junction Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: BHF-UCL
    5. dendrite Source: Ensembl
    6. filopodium Source: UniProtKB
    7. lamellipodium Source: UniProtKB
    8. SCAR complex Source: UniProt

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134977642.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513Abl interactor 2PRO_0000191790Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei227 – 2271Phosphoserine4 Publications
    Modified residuei368 – 3681Phosphoserine2 Publications

    Post-translational modificationi

    Is a substrate for ABL1.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYB9.
    PaxDbiQ9NYB9.
    PRIDEiQ9NYB9.

    PTM databases

    PhosphoSiteiQ9NYB9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NYB9.
    BgeeiQ9NYB9.
    CleanExiHS_ABI2.
    GenevestigatoriQ9NYB9.

    Interactioni

    Subunit structurei

    Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the complex to dissociate, releasing activated WASF1. The complex can also be activated by NCK1 By similarity. Interacts with ABL1 and ABL2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005192EBI-743598,EBI-375543
    Caskin1Q8VHK23EBI-743598,EBI-7049475From a different organism.

    Protein-protein interaction databases

    BioGridi115454. 21 interactions.
    DIPiDIP-37566N.
    IntActiQ9NYB9. 23 interactions.
    MINTiMINT-252647.
    STRINGi9606.ENSP00000261017.

    Structurei

    Secondary structure

    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 99
    Helixi11 – 3929
    Helixi43 – 11068
    Beta strandi123 – 1253
    Turni143 – 1519
    Beta strandi453 – 4586
    Beta strandi477 – 4837
    Beta strandi485 – 4939
    Beta strandi496 – 5016
    Beta strandi504 – 5074

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ED0NMR-A444-508[»]
    3P8CX-ray2.29F1-164[»]
    4N78X-ray2.43F1-513[»]
    ProteinModelPortaliQ9NYB9.
    SMRiQ9NYB9. Positions 1-154, 444-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NYB9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 10763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini451 – 51060SH3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi172 – 423252Pro-richAdd
    BLAST

    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.
    HOGENOMiHOG000293213.
    HOVERGENiHBG050446.
    InParanoidiQ9NYB9.
    KOiK05751.
    PhylomeDBiQ9NYB9.
    TreeFamiTF314303.

    Family and domain databases

    InterProiIPR028457. ABI.
    IPR028454. Abi2.
    IPR012849. Abl-interactor_HHR_dom.
    IPR001452. SH3_domain.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PANTHERiPTHR10460. PTHR10460. 1 hit.
    PTHR10460:SF3. PTHR10460:SF3. 1 hit.
    PfamiPF07815. Abi_HHR. 1 hit.
    PF14604. SH3_9. 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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NYB9-1) [UniParc]FASTAAdd to Basket

    Also known as: Abi-2b

    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 EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET    50
    KAYTTQSLAS VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH 100
    KEKVARREIG ILTTNKNTSR THKIIAPANL ERPVRYIRKP IDYTILDDIG 150
    HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK PPSPPMSGKG TLGRHSPYRT 200
    LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT YSSSGSSGGS 250
    HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS 300
    APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF 350
    YSMNRPASRH TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD 400
    TPPPPPPVEE PVFDESPPPP PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR 450
    SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV IKKNDDGWYE GVMNGVTGLF 500
    PGNYVESIMH YSE 513
    Length:513
    Mass (Da):55,663
    Last modified:October 1, 2000 - v1
    Checksum:i822983A69E5EA512
    GO
    Isoform 2 (identifier: Q9NYB9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-159: Missing.
         284-344: Missing.
         399-399: S → SLAPPPPSILQVTPQLPLMGFVARVQENIS

    Show »
    Length:475
    Mass (Da):52,446
    Checksum:i3AF8B713FD40FA90
    GO
    Isoform 3 (identifier: Q9NYB9-3) [UniParc]FASTAAdd to Basket

    Also known as: Abi-2a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: Missing.
         46-95: ALEETKAYTT...MESSINHISQ → MSCRCWISRH...GNNCSLRLNE
         154-159: Missing.
         284-344: Missing.

    Show »
    Length:401
    Mass (Da):44,409
    Checksum:i5D009A269B2B2FFF
    GO
    Isoform 4 (identifier: Q9NYB9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-159: Missing.

    Show »
    Length:507
    Mass (Da):54,819
    Checksum:iC0CE1E991D695FC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221S → R in CAA64885. (PubMed:8649853)Curated
    Sequence conflicti69 – 691A → D in CAA64885. (PubMed:8649853)Curated
    Sequence conflicti243 – 2431S → T in AAA75446. 1 PublicationCurated
    Sequence conflicti249 – 2491G → P in AAA92289. (PubMed:7590236)Curated
    Sequence conflicti317 – 3171N → D in BAG61693. (PubMed:14702039)Curated
    Sequence conflicti324 – 3252PN → QT in BAG61693. (PubMed:14702039)Curated
    Sequence conflicti432 – 4321A → V in AAA75446. 1 PublicationCurated
    Sequence conflicti500 – 5001F → S in AAA75446. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4545Missing in isoform 3. 1 PublicationVSP_010759Add
    BLAST
    Alternative sequencei46 – 9550ALEET…NHISQ → MSCRCWISRHPSYEGWNLQS IIFHKQIRGVDLESTFVTKF GNNCSLRLNE in isoform 3. 1 PublicationVSP_010760Add
    BLAST
    Alternative sequencei154 – 1596Missing in isoform 2, isoform 3 and isoform 4. 6 PublicationsVSP_010761
    Alternative sequencei284 – 34461Missing in isoform 2 and isoform 3. 5 PublicationsVSP_010762Add
    BLAST
    Alternative sequencei399 – 3991S → SLAPPPPSILQVTPQLPLMG FVARVQENIS in isoform 2. 4 PublicationsVSP_010763

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23435 mRNA. Translation: AAA92289.1.
    U31089 mRNA. Translation: AAA75446.1.
    AF260261 mRNA. Translation: AAF70308.1.
    X95632 mRNA. Translation: CAA64885.1.
    BT009920 mRNA. Translation: AAP88922.1.
    AK299824 mRNA. Translation: BAG61693.1.
    BC001439 mRNA. Translation: AAH01439.1.
    CCDSiCCDS2358.1. [Q9NYB9-2]
    CCDS63093.1. [Q9NYB9-1]
    CCDS63094.1. [Q9NYB9-4]
    CCDS63096.1. [Q9NYB9-3]
    PIRiG01936.
    RefSeqiNP_001269854.1. NM_001282925.1.
    NP_001269855.1. NM_001282926.1.
    NP_001269856.1. NM_001282927.1. [Q9NYB9-3]
    NP_005750.4. NM_005759.5. [Q9NYB9-2]
    XP_006712248.1. XM_006712185.1. [Q9NYB9-3]
    UniGeneiHs.471156.

    Genome annotation databases

    EnsembliENST00000261016; ENSP00000261016; ENSG00000138443. [Q9NYB9-3]
    ENST00000261017; ENSP00000261017; ENSG00000138443. [Q9NYB9-2]
    ENST00000424558; ENSP00000391433; ENSG00000138443.
    GeneIDi10152.
    KEGGihsa:10152.
    UCSCiuc002uzz.3. human. [Q9NYB9-2]
    uc002vab.3. human. [Q9NYB9-3]

    Polymorphism databases

    DMDMi50400673.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23435 mRNA. Translation: AAA92289.1 .
    U31089 mRNA. Translation: AAA75446.1 .
    AF260261 mRNA. Translation: AAF70308.1 .
    X95632 mRNA. Translation: CAA64885.1 .
    BT009920 mRNA. Translation: AAP88922.1 .
    AK299824 mRNA. Translation: BAG61693.1 .
    BC001439 mRNA. Translation: AAH01439.1 .
    CCDSi CCDS2358.1. [Q9NYB9-2 ]
    CCDS63093.1. [Q9NYB9-1 ]
    CCDS63094.1. [Q9NYB9-4 ]
    CCDS63096.1. [Q9NYB9-3 ]
    PIRi G01936.
    RefSeqi NP_001269854.1. NM_001282925.1.
    NP_001269855.1. NM_001282926.1.
    NP_001269856.1. NM_001282927.1. [Q9NYB9-3 ]
    NP_005750.4. NM_005759.5. [Q9NYB9-2 ]
    XP_006712248.1. XM_006712185.1. [Q9NYB9-3 ]
    UniGenei Hs.471156.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ED0 NMR - A 444-508 [» ]
    3P8C X-ray 2.29 F 1-164 [» ]
    4N78 X-ray 2.43 F 1-513 [» ]
    ProteinModelPortali Q9NYB9.
    SMRi Q9NYB9. Positions 1-154, 444-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115454. 21 interactions.
    DIPi DIP-37566N.
    IntActi Q9NYB9. 23 interactions.
    MINTi MINT-252647.
    STRINGi 9606.ENSP00000261017.

    PTM databases

    PhosphoSitei Q9NYB9.

    Polymorphism databases

    DMDMi 50400673.

    Proteomic databases

    MaxQBi Q9NYB9.
    PaxDbi Q9NYB9.
    PRIDEi Q9NYB9.

    Protocols and materials databases

    DNASUi 10152.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261016 ; ENSP00000261016 ; ENSG00000138443 . [Q9NYB9-3 ]
    ENST00000261017 ; ENSP00000261017 ; ENSG00000138443 . [Q9NYB9-2 ]
    ENST00000424558 ; ENSP00000391433 ; ENSG00000138443 .
    GeneIDi 10152.
    KEGGi hsa:10152.
    UCSCi uc002uzz.3. human. [Q9NYB9-2 ]
    uc002vab.3. human. [Q9NYB9-3 ]

    Organism-specific databases

    CTDi 10152.
    GeneCardsi GC02P204192.
    H-InvDB HIX0002759.
    HGNCi HGNC:24011. ABI2.
    MIMi 606442. gene.
    neXtProti NX_Q9NYB9.
    PharmGKBi PA134977642.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262939.
    HOGENOMi HOG000293213.
    HOVERGENi HBG050446.
    InParanoidi Q9NYB9.
    KOi K05751.
    PhylomeDBi Q9NYB9.
    TreeFami TF314303.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi ABI2. human.
    EvolutionaryTracei Q9NYB9.
    GeneWikii ABI2.
    GenomeRNAii 10152.
    NextBioi 38426.
    PROi Q9NYB9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYB9.
    Bgeei Q9NYB9.
    CleanExi HS_ABI2.
    Genevestigatori Q9NYB9.

    Family and domain databases

    InterProi IPR028457. ABI.
    IPR028454. Abi2.
    IPR012849. Abl-interactor_HHR_dom.
    IPR001452. SH3_domain.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    PANTHERi PTHR10460. PTHR10460. 1 hit.
    PTHR10460:SF3. PTHR10460:SF3. 1 hit.
    Pfami PF07815. Abi_HHR. 1 hit.
    PF14604. SH3_9. 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. "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity."
      Dai Z., Pendergast A.M.
      Genes Dev. 9:2569-2582(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH ABL1.
    2. "Cloning of a binding substrate of the Abl protein tyrosine kinase."
      Ren R.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Identification of ArgBP1, an Arg protein tyrosine kinase binding protein that is the human homologue of a CNS-specific Xenopus gene."
      Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R., Golemis E.A., Kruh G.D.
      Oncogene 12:1921-1929(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ABL2.
      Tissue: Brain.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    6. "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 2).
      Tissue: Placenta.
    7. "Drosophila abelson interacting protein (dAbi) is a positive regulator of abelson tyrosine kinase activity."
      Juang J.L., Hoffmann F.M.
      Oncogene 18:5138-5147(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "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.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of the SH3 domain of Abl interactor 2 (Abelson interactor 2)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 444-508.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, SUBUNIT.

    Entry informationi

    Entry nameiABI2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYB9
    Secondary accession number(s): B4DSN1
    , Q13147, Q13249, Q13801, Q9BV70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3