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O54967

- ACK1_MOUSE

UniProt

O54967 - ACK1_MOUSE

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Protein

Activated CDC42 kinase 1

Gene

Tnk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 serine/threonine kinase activity Source: UniProtKB-KW
  5. WW domain binding Source: BHF-UCL

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. phosphorylation Source: UniProtKB
Complete GO annotation...

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. axon Source: MGI
  2. cell junction Source: UniProtKB-KW
  3. coated pit Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB
  5. cytoplasmic vesicle Source: UniProtKB-KW
  6. dendrite Source: MGI
  7. endosome Source: UniProtKB
  8. growth cone Source: MGI
  9. neuronal cell body Source: MGI
  10. nucleus Source: UniProtKB
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

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

MaxQBiO54967.
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

BgeeiO54967.
CleanExiMM_TNK2.
ExpressionAtlasiO54967. baseline and differential.
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 81-489.
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.
GeneTreeiENSGT00760000118799.
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

        10         20         30         40         50
MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NITRLSHFEY VKNEDLEKIG
60 70 80 90 100
MGRPGQRRLW EAVKRRKAMC KRKSWMSKVF SGKRLEAEFP SQHSQSTFRK
110 120 130 140 150
PSPTPGSLPG EGTLQSLTCL IGEKDLRLLE KLGDGSFGVV RRGEWDAPAG
160 170 180 190 200
KTVSVAVKCL KPDVLSQPEA MDDFIREVNA MHSLDHRNLI RLYGVVLTLP
210 220 230 240 250
MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM AYLESKRFIH
260 270 280 290 300
RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE
310 320 330 340 350
SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL
360 370 380 390 400
PRPEDCPQDI YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE
410 420 430 440 450
EPDKLHIQMN DVITVIEGRA ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS
460 470 480 490 500
AQDISQPLQN SFIHTGHGDS DPRHCWGFPD RIDELYLGNP MDPPDLLSVE
510 520 530 540 550
LSTSRPTQHL GRVKREPPPR PPQPAIFTQK TTYDPVSEDP DPLSSDFKRL
560 570 580 590 600
GLRKPALPRG LWLAKPSARV PGTKADRSSG GEVTLIDFGE EPVVPTPRPC
610 620 630 640 650
APSLAQLAMD ACSLLDKTPP QSPTRALPRP LHPTPVVDWD ARPLPPPPAY
660 670 680 690 700
DDVAQDEDDF EVCSINSTLV GAGLPAGPSQ GETNYAFVPE QAQMPPALED
710 720 730 740 750
NLFLPPQGGG KPPSSVQTAE IFQALQQECM RQLQVPTGQL TPSPTPGGDD
760 770 780 790 800
KPQVPPRVPI PPRPTRPRVE LSPAPSGEEE TSRWPGPASP PRVPPREPLS
810 820 830 840 850
PQGSRTPSPL VPPGSSPLPH RLSSSPGKTM PTTQSFASDP KYATPQVIQA
860 870 880 890 900
PGPRAGPCIL PIVRDGRKVS STHYYLLPER PPYLERYQRF LREAQSPEEP
910 920 930 940 950
AALPVPPLLP PPSTPAPAAP TATVRPMPQA APDPKANFST NNSNPGARPP
960 970 980 990 1000
SLRAAARLPQ RGCPGDGQEA ARPADKVQML QAMVHGVTTE ECQAALQSHS
1010 1020 1030 1040 1050
WSVQRAAQYL KVEQLFGLGL RPRVECHKVL EMFDWNLEQA GCHLLGSCGP

AHHKR
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 81-489.
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

MaxQBi O54967.
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 ENSGT00760000118799.
HOGENOMi HOG000168225.
HOVERGENi HBG100429.
InParanoidi O54967.
KOi K08886.
PhylomeDBi O54967.

Miscellaneous databases

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

Gene expression databases

Bgeei O54967.
CleanExi MM_TNK2.
ExpressionAtlasi O54967. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 135 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