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O54967

- ACK1_MOUSE

UniProt

O54967 - ACK1_MOUSE

Protein

Activated CDC42 kinase 1

Gene

Tnk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR.2 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation
    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei158 – 1581ATP
    Active sitei252 – 2521Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi132 – 1409ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB-KW
    6. WW domain binding Source: BHF-UCL

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activated CDC42 kinase 1 (EC:2.7.10.2, EC:2.7.11.1)
    Short name:
    ACK-1
    Alternative name(s):
    Non-receptor protein tyrosine kinase Ack
    Tyrosine kinase non-receptor protein 2
    Gene namesi
    Name:Tnk2
    Synonyms:Ack1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1858308. Tnk2.

    Subcellular locationi

    Cell membrane. Nucleus. Endosome. Cell junctionadherens junction. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleclathrin-coated vesicle By similarity. Membraneclathrin-coated pit By similarity
    Note: The Tyr-284 phosphorylated form is found both in the membrane and nucleus. Co-localizes with EGFR on endosomes. Nuclear translocation is CDC42-dependent.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. axon Source: MGI
    3. clathrin-coated vesicle Source: UniProtKB-SubCell
    4. coated pit Source: UniProtKB-SubCell
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    7. dendrite Source: MGI
    8. endosome Source: UniProtKB
    9. growth cone Source: MGI
    10. neuronal cell body Source: MGI
    11. nucleus Source: UniProtKB
    12. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Coated pit, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi158 – 1581K → A: Loss of kinase activity. 1 Publication
    Mutagenesisi424 – 4241W → K: Increase in autophosphorylation activity. 1 Publication
    Mutagenesisi464 – 4641H → D: Loss of CDC42-binding and impairment of autophosphorylation. 1 Publication
    Mutagenesisi650 – 6501Y → A: Loss of interaction with NEDD4 and drastic reduction in its ubiquitination. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10551055Activated CDC42 kinase 1PRO_0000088059Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei284 – 2841Phosphotyrosine; by SRC and autocatalysisBy similarity
    Modified residuei533 – 5331Phosphotyrosine1 Publication
    Modified residuei842 – 8421PhosphotyrosineBy similarity
    Modified residuei874 – 8741PhosphotyrosineBy similarity
    Modified residuei887 – 8871PhosphotyrosineBy similarity
    Modified residuei896 – 8961PhosphoserineBy similarity

    Post-translational modificationi

    Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-533 is required for interaction with SRC and is observed during association with clathrin-coated pits By similarity.By similarity
    Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO54967.
    PRIDEiO54967.

    PTM databases

    PhosphoSiteiO54967.

    Expressioni

    Tissue specificityi

    Ubiquitously present in all tissues tested. Highly expressed in the adult central nervous system (CNS); hippocampus, neocortex, and cerebellum, both at dendritic spines and presynaptic axon terminals. Levels are strongly increased during enhanced neural activity.3 Publications

    Developmental stagei

    Highly expressed at E14-E16 in the forebrain, in the proliferative ventricular zone of the neocortex and hippocampus, and in the cortical and hippocampal plates. Also observed in the septal area, the ganglionic eminence, and in the dorsal thalamus and hypothalamus. In the hindbrain, expressed in many nuclei in the brain stem and in the cerebellar anlage, external granule cell layer, in Purkinje cells and the deep cerebellar nuclei.2 Publications

    Inductioni

    Down-regulated by EGF.1 Publication

    Gene expression databases

    ArrayExpressiO54967.
    BgeeiO54967.
    CleanExiMM_TNK2.
    GenevestigatoriO54967.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CSPG4 (activated). Interacts with MERTK (activated); stimulates autophosphorylation. May interact (phosphorylated) with HSP90AB1; maintains kinase activity. Interacts with NPHP1. Interacts with SNX9 (via SH3 domain). Interacts with SRC (via SH2 and SH3 domain). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with BCAR1/p130cas via SH3 domains. Forms complexes with GRB2 and numerous receptor tyrosine kinases (RTK) including LTK, AXL or PDGFRL, in which GRB2 promotes RTK recruitment by TNK2 By similarity. Interacts with CDC42. Interacts with EGFR, and this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts (via kinase domain) with AKT1. Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi206174. 7 interactions.
    IntActiO54967. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO54967.
    SMRiO54967. Positions 80-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini126 – 385260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 44863SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 46613CRIBAdd
    BLAST
    Domaini973 – 101341UBAAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 110110SAM-like domainAdd
    BLAST
    Regioni638 – 66730Required for interaction with SRCAdd
    BLAST
    Regioni647 – 6504Required for interaction with NEDD4
    Regioni748 – 891144EBD domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi517 – 950434Pro-richAdd
    BLAST

    Domaini

    The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR.
    The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation.
    The UBA domain binds both poly- and mono-ubiquitin.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 1 CRIB domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.Curated

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115195.
    HOGENOMiHOG000168225.
    HOVERGENiHBG100429.
    InParanoidiO54967.
    KOiK08886.
    PhylomeDBiO54967.

    Family and domain databases

    Gene3Di4.10.680.10. 1 hit.
    InterProiIPR015116. Cdc42_binding_dom_like.
    IPR021619. Inhibitor_Mig-6.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR009060. UBA-like.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PfamiPF09027. GTPase_binding. 1 hit.
    PF11555. Inhibitor_Mig-6. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O54967-1) [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

    MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NITRLSHFEY VKNEDLEKIG     50
    MGRPGQRRLW EAVKRRKAMC KRKSWMSKVF SGKRLEAEFP SQHSQSTFRK 100
    PSPTPGSLPG EGTLQSLTCL IGEKDLRLLE KLGDGSFGVV RRGEWDAPAG 150
    KTVSVAVKCL KPDVLSQPEA MDDFIREVNA MHSLDHRNLI RLYGVVLTLP 200
    MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM AYLESKRFIH 250
    RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE 300
    SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL 350
    PRPEDCPQDI YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE 400
    EPDKLHIQMN DVITVIEGRA ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS 450
    AQDISQPLQN SFIHTGHGDS DPRHCWGFPD RIDELYLGNP MDPPDLLSVE 500
    LSTSRPTQHL GRVKREPPPR PPQPAIFTQK TTYDPVSEDP DPLSSDFKRL 550
    GLRKPALPRG LWLAKPSARV PGTKADRSSG GEVTLIDFGE EPVVPTPRPC 600
    APSLAQLAMD ACSLLDKTPP QSPTRALPRP LHPTPVVDWD ARPLPPPPAY 650
    DDVAQDEDDF EVCSINSTLV GAGLPAGPSQ GETNYAFVPE QAQMPPALED 700
    NLFLPPQGGG KPPSSVQTAE IFQALQQECM RQLQVPTGQL TPSPTPGGDD 750
    KPQVPPRVPI PPRPTRPRVE LSPAPSGEEE TSRWPGPASP PRVPPREPLS 800
    PQGSRTPSPL VPPGSSPLPH RLSSSPGKTM PTTQSFASDP KYATPQVIQA 850
    PGPRAGPCIL PIVRDGRKVS STHYYLLPER PPYLERYQRF LREAQSPEEP 900
    AALPVPPLLP PPSTPAPAAP TATVRPMPQA APDPKANFST NNSNPGARPP 950
    SLRAAARLPQ RGCPGDGQEA ARPADKVQML QAMVHGVTTE ECQAALQSHS 1000
    WSVQRAAQYL KVEQLFGLGL RPRVECHKVL EMFDWNLEQA GCHLLGSCGP 1050
    AHHKR 1055
    Length:1,055
    Mass (Da):116,975
    Last modified:December 4, 2007 - v2
    Checksum:i4A029C67C350B89A
    GO
    Isoform 2 (identifier: O54967-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         515-531: REPPPRPPQPAIFTQKT → KP
         980-1011: Missing.

    Note: No experimental confirmation available. Contains a phosphotyrosine at position 518.

    Show »
    Length:1,008
    Mass (Da):111,704
    Checksum:i09718C0B88D4F2D1
    GO
    Isoform 3 (identifier: O54967-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         515-531: REPPPRPPQPAIFTQKT → KP

    Note: Contains a phosphotyrosine at position 518.

    Show »
    Length:1,040
    Mass (Da):115,258
    Checksum:iA2401DAFB05715E0
    GO

    Sequence cautioni

    The sequence AAH31168.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 582RR → SG in AAC04786. 1 PublicationCurated
    Sequence conflicti531 – 5311T → P in ABG46266. (PubMed:16777958)Curated
    Sequence conflicti574 – 5741K → E in ABG46266. (PubMed:16777958)Curated
    Sequence conflicti649 – 6491A → V in AAC04786. 1 PublicationCurated
    Sequence conflicti818 – 8181L → V in BAC40063. (PubMed:15489334)Curated
    Sequence conflicti955 – 9551A → T in AAH52421. 1 PublicationCurated
    Sequence conflicti955 – 9551A → T in BAC40063. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei515 – 53117REPPP…FTQKT → KP in isoform 2 and isoform 3. 2 PublicationsVSP_008657Add
    BLAST
    Alternative sequencei980 – 101132Missing in isoform 2. 1 PublicationVSP_008658Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ666696 mRNA. Translation: ABG46266.1.
    AF037260 mRNA. Translation: AAC04786.1.
    BC031168 mRNA. Translation: AAH31168.1. Sequence problems.
    BC052421 mRNA. Translation: AAH52421.1.
    AK087965 mRNA. Translation: BAC40063.1.
    CCDSiCCDS37313.1. [O54967-1]
    CCDS49828.1. [O54967-2]
    RefSeqiNP_001103617.1. NM_001110147.1.
    NP_001276372.1. NM_001289443.1.
    NP_058068.2. NM_016788.3.
    UniGeneiMm.251115.

    Genome annotation databases

    EnsembliENSMUST00000115125; ENSMUSP00000110778; ENSMUSG00000022791.
    GeneIDi51789.
    KEGGimmu:51789.
    UCSCiuc007yzc.2. mouse. [O54967-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ666696 mRNA. Translation: ABG46266.1 .
    AF037260 mRNA. Translation: AAC04786.1 .
    BC031168 mRNA. Translation: AAH31168.1 . Sequence problems.
    BC052421 mRNA. Translation: AAH52421.1 .
    AK087965 mRNA. Translation: BAC40063.1 .
    CCDSi CCDS37313.1. [O54967-1 ]
    CCDS49828.1. [O54967-2 ]
    RefSeqi NP_001103617.1. NM_001110147.1.
    NP_001276372.1. NM_001289443.1.
    NP_058068.2. NM_016788.3.
    UniGenei Mm.251115.

    3D structure databases

    ProteinModelPortali O54967.
    SMRi O54967. Positions 80-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206174. 7 interactions.
    IntActi O54967. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL2079848.

    PTM databases

    PhosphoSitei O54967.

    Proteomic databases

    PaxDbi O54967.
    PRIDEi O54967.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000115125 ; ENSMUSP00000110778 ; ENSMUSG00000022791 .
    GeneIDi 51789.
    KEGGi mmu:51789.
    UCSCi uc007yzc.2. mouse. [O54967-2 ]

    Organism-specific databases

    CTDi 10188.
    MGIi MGI:1858308. Tnk2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115195.
    HOGENOMi HOG000168225.
    HOVERGENi HBG100429.
    InParanoidi O54967.
    KOi K08886.
    PhylomeDBi O54967.

    Miscellaneous databases

    ChiTaRSi TNK2. mouse.
    NextBioi 308016.
    PROi O54967.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54967.
    Bgeei O54967.
    CleanExi MM_TNK2.
    Genevestigatori O54967.

    Family and domain databases

    Gene3Di 4.10.680.10. 1 hit.
    InterProi IPR015116. Cdc42_binding_dom_like.
    IPR021619. Inhibitor_Mig-6.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR009060. UBA-like.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    Pfami PF09027. GTPase_binding. 1 hit.
    PF11555. Inhibitor_Mig-6. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Activation of the nonreceptor protein tyrosine kinase Ack by multiple extracellular stimuli."
      Galisteo M.L., Yang Y., Urena J., Schlessinger J.
      Proc. Natl. Acad. Sci. U.S.A. 103:9796-9801(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-158; TRP-424 AND HIS-464.
    2. "The protein tyrosine kinase Ack is associated with and activated in vivo by CDC42Hs."
      Her J.-H., Bolen J.B.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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] (ISOFORMS 2 AND 3).
      Strain: C57BL/6.
      Tissue: Brain and Colon.
    4. "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] OF 121-1055 (ISOFORM 3).
      Strain: NOD.
      Tissue: Thymus.
    5. "Expression, synaptic localization, and developmental regulation of Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the developing and adult brain."
      Urena J.M., La Torre A., Martinez A., Lowenstein E., Franco N., Winsky-Sommerer R., Fontana X., Casaroli-Marano R., Ibanez-Sabio M.A., Pascual M., Del Rio J.A., de Lecea L., Soriano E.
      J. Comp. Neurol. 490:119-132(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC42, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    6. "Expression pattern of ACK1 tyrosine kinase during brain development in the mouse."
      La Torre A., del Rio J.A., Soriano E., Urena J.M.
      Gene Expr. Patterns 6:886-892(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation."
      Shen F., Lin Q., Gu Y., Childress C., Yang W.
      Mol. Biol. Cell 18:732-742(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGFR, SUBCELLULAR LOCATION, DOMAIN EBD AND UBA, MUTAGENESIS OF TYR-650.
    8. "Nephrocystin-1 interacts directly with Ack1 and is expressed in human collecting duct."
      Eley L., Moochhala S.H., Simms R., Hildebrandt F., Sayer J.A.
      Biochem. Biophys. Res. Commun. 371:877-882(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "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-518 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "HECT E3 ubiquitin ligase Nedd4-1 ubiquitinates ACK and regulates epidermal growth factor (EGF)-induced degradation of EGF receptor and ACK."
      Lin Q., Wang J., Childress C., Sudol M., Carey D.J., Yang W.
      Mol. Cell. Biol. 30:1541-1554(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4 AND NEDD4L, UBIQUITINATION, INDUCTION, DOMAIN SAM-LIKE AND UBA.
    11. Cited for: FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION.
    12. "Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin."
      Shen H., Ferguson S.M., Dephoure N., Park R., Yang Y., Volpicelli-Daley L., Gygi S., Schlessinger J., De Camilli P.
      Mol. Biol. Cell 22:493-502(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284 AND TYR-533.

    Entry informationi

    Entry nameiACK1_MOUSE
    AccessioniPrimary (citable) accession number: O54967
    Secondary accession number(s): Q0Z844, Q8C2U0, Q8K0K4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3