Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O54967 (ACK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activated CDC42 kinase 1

Short name=ACK-1
EC=2.7.10.2
EC=2.7.11.1
Alternative name(s):
Non-receptor protein tyrosine kinase Ack
Tyrosine kinase non-receptor protein 2
Gene names
Name:Tnk2
Synonyms:Ack1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1055 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.11

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Subunit structure

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. Ref.5 Ref.7 Ref.10 Ref.11

Subcellular location

Cell membrane. Nucleus. Endosome. Cell junctionadherens junction. Cytoplasmic vesicle membrane; Peripheral membrane protein; 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. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12

Tissue specificity

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. Ref.1 Ref.5 Ref.6

Developmental stage

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. Ref.5 Ref.6

Induction

Down-regulated by EGF. Ref.10

Domain

The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR. Ref.7 Ref.10

The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation. Ref.7 Ref.10

The UBA domain binds both poly- and mono-ubiquitin. Ref.7 Ref.10

Post-translational modification

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.

Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Contains 1 SH3 domain.

Contains 1 UBA domain.

Sequence caution

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

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell junction
Cell membrane
Coated pit
Cytoplasmic vesicle
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentadherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from direct assay Ref.5. Source: MGI

clathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay Ref.5. Source: MGI

endosome

Inferred from direct assay Ref.7. Source: UniProtKB

growth cone

Inferred from direct assay Ref.5. Source: MGI

neuronal cell body

Inferred from direct assay Ref.5. Source: MGI

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

WW domain binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.7Ref.10Ref.11. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O54967-1)

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.
Isoform 2 (identifier: O54967-2)

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.
Isoform 3 (identifier: O54967-3)

The sequence of this isoform differs from the canonical sequence as follows:
     515-531: REPPPRPPQPAIFTQKT → KP
Note: Contains a phosphotyrosine at position 518.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10551055Activated CDC42 kinase 1
PRO_0000088059

Regions

Domain126 – 385260Protein kinase
Domain386 – 44863SH3
Domain454 – 46613CRIB
Domain973 – 101341UBA
Nucleotide binding132 – 1409ATP By similarity
Region1 – 110110SAM-like domain
Region638 – 66730Required for interaction with SRC
Region647 – 6504Required for interaction with NEDD4
Region748 – 891144EBD domain
Compositional bias517 – 950434Pro-rich

Sites

Active site2521Proton acceptor By similarity
Binding site1581ATP

Amino acid modifications

Modified residue2841Phosphotyrosine; by SRC and autocatalysis By similarity
Modified residue5331Phosphotyrosine Ref.12
Modified residue8421Phosphotyrosine By similarity
Modified residue8741Phosphotyrosine By similarity
Modified residue8871Phosphotyrosine By similarity
Modified residue8961Phosphoserine By similarity

Natural variations

Alternative sequence515 – 53117REPPP…FTQKT → KP in isoform 2 and isoform 3.
VSP_008657
Alternative sequence980 – 101132Missing in isoform 2.
VSP_008658

Experimental info

Mutagenesis1581K → A: Loss of kinase activity. Ref.1
Mutagenesis4241W → K: Increase in autophosphorylation activity. Ref.1
Mutagenesis4641H → D: Loss of CDC42-binding and impairment of autophosphorylation. Ref.1
Mutagenesis6501Y → A: Loss of interaction with NEDD4 and drastic reduction in its ubiquitination. Ref.7
Sequence conflict57 – 582RR → SG in AAC04786. Ref.2
Sequence conflict5311T → P in ABG46266. Ref.1
Sequence conflict5741K → E in ABG46266. Ref.1
Sequence conflict6491A → V in AAC04786. Ref.2
Sequence conflict8181L → V in BAC40063. Ref.3
Sequence conflict9551A → T in AAH52421. Ref.2
Sequence conflict9551A → T in BAC40063. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 4A029C67C350B89A

FASTA1,055116,975
        10         20         30         40         50         60 
MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NITRLSHFEY VKNEDLEKIG MGRPGQRRLW 

        70         80         90        100        110        120 
EAVKRRKAMC KRKSWMSKVF SGKRLEAEFP SQHSQSTFRK PSPTPGSLPG EGTLQSLTCL 

       130        140        150        160        170        180 
IGEKDLRLLE KLGDGSFGVV RRGEWDAPAG KTVSVAVKCL KPDVLSQPEA MDDFIREVNA 

       190        200        210        220        230        240 
MHSLDHRNLI RLYGVVLTLP MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM 

       250        260        270        280        290        300 
AYLESKRFIH RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE 

       310        320        330        340        350        360 
SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL PRPEDCPQDI 

       370        380        390        400        410        420 
YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE EPDKLHIQMN DVITVIEGRA 

       430        440        450        460        470        480 
ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS AQDISQPLQN SFIHTGHGDS DPRHCWGFPD 

       490        500        510        520        530        540 
RIDELYLGNP MDPPDLLSVE LSTSRPTQHL GRVKREPPPR PPQPAIFTQK TTYDPVSEDP 

       550        560        570        580        590        600 
DPLSSDFKRL GLRKPALPRG LWLAKPSARV PGTKADRSSG GEVTLIDFGE EPVVPTPRPC 

       610        620        630        640        650        660 
APSLAQLAMD ACSLLDKTPP QSPTRALPRP LHPTPVVDWD ARPLPPPPAY DDVAQDEDDF 

       670        680        690        700        710        720 
EVCSINSTLV GAGLPAGPSQ GETNYAFVPE QAQMPPALED NLFLPPQGGG KPPSSVQTAE 

       730        740        750        760        770        780 
IFQALQQECM RQLQVPTGQL TPSPTPGGDD KPQVPPRVPI PPRPTRPRVE LSPAPSGEEE 

       790        800        810        820        830        840 
TSRWPGPASP PRVPPREPLS PQGSRTPSPL VPPGSSPLPH RLSSSPGKTM PTTQSFASDP 

       850        860        870        880        890        900 
KYATPQVIQA PGPRAGPCIL PIVRDGRKVS STHYYLLPER PPYLERYQRF LREAQSPEEP 

       910        920        930        940        950        960 
AALPVPPLLP PPSTPAPAAP TATVRPMPQA APDPKANFST NNSNPGARPP SLRAAARLPQ 

       970        980        990       1000       1010       1020 
RGCPGDGQEA ARPADKVQML QAMVHGVTTE ECQAALQSHS WSVQRAAQYL KVEQLFGLGL 

      1030       1040       1050 
RPRVECHKVL EMFDWNLEQA GCHLLGSCGP AHHKR 

« Hide

Isoform 2 [UniParc].

Checksum: 09718C0B88D4F2D1
Show »

FASTA1,008111,704
Isoform 3 [UniParc].

Checksum: A2401DAFB05715E0
Show »

FASTA1,040115,258

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation."
Mahajan K., Coppola D., Challa S., Fang B., Chen Y.A., Zhu W., Lopez A.S., Koomen J., Engelman R.W., Rivera C., Muraoka-Cook R.S., Cheng J.Q., Schoenbrunn E., Sebti S.M., Earp H.S., Mahajan N.P.
PLoS ONE 5:E9646-E9646(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37313.1. [O54967-1]
CCDS49828.1. [O54967-2]
RefSeqNP_001103617.1. NM_001110147.1.
NP_001276372.1. NM_001289443.1.
NP_058068.2. NM_016788.3.
UniGeneMm.251115.

3D structure databases

ProteinModelPortalO54967.
SMRO54967. Positions 80-489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206174. 7 interactions.
IntActO54967. 1 interaction.

Chemistry

ChEMBLCHEMBL2079848.

PTM databases

PhosphoSiteO54967.

Proteomic databases

PaxDbO54967.
PRIDEO54967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115125; ENSMUSP00000110778; ENSMUSG00000022791.
GeneID51789.
KEGGmmu:51789.
UCSCuc007yzc.2. mouse. [O54967-2]

Organism-specific databases

CTD10188.
MGIMGI:1858308. Tnk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115195.
HOGENOMHOG000168225.
HOVERGENHBG100429.
InParanoidO54967.
KOK08886.
PhylomeDBO54967.

Gene expression databases

ArrayExpressO54967.
BgeeO54967.
CleanExMM_TNK2.
GenevestigatorO54967.

Family and domain databases

Gene3D4.10.680.10. 1 hit.
InterProIPR015116. 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]
PfamPF09027. 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]
PRINTSPR00109. TYRKINASE.
SMARTSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNK2. mouse.
NextBio308016.
PROO54967.
SOURCESearch...

Entry information

Entry nameACK1_MOUSE
AccessionPrimary (citable) accession number: O54967
Secondary accession number(s): Q0Z844, Q8C2U0, Q8K0K4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot