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Protein

Activated CDC42 kinase 1

Gene

TNK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.11 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation5 Publications
ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+3 Publications

Enzyme regulationi

Inhibited by AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine), which suppresses activating phosphorylation at Tyr-284. Repressed by dasatinib.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei158ATP1
Active sitei252Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi132 – 140ATP9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • epidermal growth factor receptor binding Source: BHF-UCL
  • GTPase inhibitor activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: ProtInc
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW
  • protein tyrosine kinase activity Source: UniProtKB
  • WW domain binding Source: BHF-UCL

GO - Biological processi

  • cell differentiation Source: GO_Central
  • cell migration Source: GO_Central
  • cell surface receptor signaling pathway Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • innate immune response Source: GO_Central
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • phosphorylation Source: UniProtKB
  • positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • regulation of cell proliferation Source: GO_Central
  • regulation of clathrin-dependent endocytosis Source: UniProtKB
  • small GTPase mediated signal transduction Source: ProtInc
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
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

Enzyme and pathway databases

BioCyciZFISH:HS00763-MONOMER.
BRENDAi2.7.10.2. 2681.
SignaLinkiQ07912.
SIGNORiQ07912.

Names & Taxonomyi

Protein namesi
Recommended name:
Activated CDC42 kinase 1 (EC:2.7.10.25 Publications, EC:2.7.11.12 Publications)
Short name:
ACK-1
Alternative name(s):
Tyrosine kinase non-receptor protein 2
Gene namesi
Name:TNK2
Synonyms:ACK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:19297. TNK2.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • clathrin-coated pit Source: UniProtKB
  • clathrin-coated vesicle Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • Grb2-EGFR complex Source: BHF-UCL
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi158K → R: Loss of autophosphorylation. 1 Publication1
Mutagenesisi487L → F: Constantly active kinase. 1 Publication1

Organism-specific databases

DisGeNETi10188.
MalaCardsiTNK2.
OpenTargetsiENSG00000061938.
Orphaneti391316. Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression.
PharmGKBiPA134909759.

Chemistry databases

ChEMBLiCHEMBL4599.
DrugBankiDB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi2246.

Polymorphism and mutation databases

BioMutaiTNK2.
DMDMi229462980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880581 – 1038Activated CDC42 kinase 1Add BLAST1038

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei284Phosphotyrosine; by SRC and autocatalysisCombined sources7 Publications1
Modified residuei518Phosphotyrosine1 Publication1
Modified residuei724PhosphoserineCombined sources1
Modified residuei827Phosphotyrosine1 Publication1
Modified residuei839Omega-N-methylarginineBy similarity1
Modified residuei859Phosphotyrosine1 Publication1
Modified residuei872Phosphotyrosine1 Publication1
Modified residuei881PhosphoserineCombined sources1

Post-translational modificationi

Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-518 is required for interaction with SRC and is observed during association with clathrin-coated pits.7 Publications
Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ07912.
MaxQBiQ07912.
PaxDbiQ07912.
PeptideAtlasiQ07912.
PRIDEiQ07912.

PTM databases

iPTMnetiQ07912.
PhosphoSitePlusiQ07912.

Expressioni

Tissue specificityi

The Tyr-284 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages. It also shows a significant increase in expression in prostate cancers during the progressive stages.3 Publications

Gene expression databases

BgeeiENSG00000061938.
CleanExiHS_TNK2.
ExpressionAtlasiQ07912. baseline and differential.
GenevisibleiQ07912. HS.

Organism-specific databases

HPAiCAB009948.
HPA041954.

Interactioni

Subunit structurei

Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4 (By similarity). Homodimer. Interacts with AR, CDC42, WWASL and WWOX. 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). Interacts with EGFR, and this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts (via kinase domain) with AKT1. 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 similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-603457,EBI-603457
AQP1P299723EBI-603457,EBI-745213
BCAR1P569455EBI-603457,EBI-702093
CDC42P60953-22EBI-603457,EBI-287394
CLTCQ006102EBI-603457,EBI-354967
GALTP079023EBI-603457,EBI-750827
NEK6Q9HC983EBI-603457,EBI-740364
NOTCH2NLQ7Z3S93EBI-603457,EBI-945833
SH2D1AO608803EBI-603457,EBI-6983382

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: BHF-UCL
  • WW domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi115485. 77 interactors.
DIPiDIP-33858N.
IntActiQ07912. 33 interactors.
MINTiMINT-1382124.
STRINGi9606.ENSP00000371341.

Chemistry databases

BindingDBiQ07912.

Structurei

Secondary structure

11038
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi118 – 120Combined sources3
Helixi123 – 125Combined sources3
Beta strandi126 – 133Combined sources8
Beta strandi140 – 146Combined sources7
Beta strandi148 – 150Combined sources3
Beta strandi152 – 159Combined sources8
Turni164 – 166Combined sources3
Helixi171 – 181Combined sources11
Beta strandi192 – 196Combined sources5
Beta strandi198 – 200Combined sources3
Beta strandi202 – 206Combined sources5
Helixi213 – 219Combined sources7
Helixi221 – 223Combined sources3
Helixi226 – 245Combined sources20
Helixi255 – 257Combined sources3
Beta strandi258 – 262Combined sources5
Beta strandi265 – 268Combined sources4
Helixi273 – 276Combined sources4
Beta strandi283 – 285Combined sources3
Helixi288 – 290Combined sources3
Helixi294 – 296Combined sources3
Helixi299 – 304Combined sources6
Beta strandi306 – 308Combined sources3
Helixi309 – 324Combined sources16
Turni325 – 327Combined sources3
Turni330 – 333Combined sources4
Helixi336 – 344Combined sources9
Helixi358 – 367Combined sources10
Helixi372 – 374Combined sources3
Helixi378 – 387Combined sources10
Beta strandi392 – 394Combined sources3
Beta strandi402 – 404Combined sources3
Beta strandi412 – 417Combined sources6
Beta strandi419 – 421Combined sources3
Beta strandi423 – 432Combined sources10
Beta strandi435 – 439Combined sources5
Helixi440 – 443Combined sources4
Beta strandi449 – 451Combined sources3
Turni484 – 486Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF4NMR-B448-489[»]
1U46X-ray2.00A/B109-395[»]
1U4DX-ray2.10A/B109-395[»]
1U54X-ray2.80A/B109-395[»]
3EQPX-ray2.30A/B117-392[»]
3EQRX-ray2.00A/B117-392[»]
4EWHX-ray2.50A/B117-391[»]
4HZRX-ray1.31A/B115-389[»]
4HZSX-ray3.23A/B/C/D115-453[»]
4ID7X-ray3.00A117-389[»]
ProteinModelPortaliQ07912.
SMRiQ07912.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini126 – 385Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini386 – 448SH3PROSITE-ProRule annotationAdd BLAST63
Domaini454 – 466CRIBAdd BLAST13
Domaini958 – 996UBAAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 110SAM-like domainAdd BLAST110
Regioni623 – 652Required for interaction with SRC1 PublicationAdd BLAST30
Regioni632 – 635Required for interaction with NEDD4By similarity4
Regioni733 – 876EBD domainBy similarityAdd BLAST144

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi577 – 958Pro-richAdd BLAST382

Domaini

The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR.By similarity
The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation.1 Publication
The UBA domain binds both poly- and mono-ubiquitin.1 Publication

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

eggNOGiKOG0199. Eukaryota.
ENOG410XPRC. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000168225.
HOVERGENiHBG100429.
InParanoidiQ07912.
KOiK08886.
OMAiKTMPTTQ.
OrthoDBiEOG091G03HT.
PhylomeDBiQ07912.
TreeFamiTF316643.

Family and domain databases

Gene3Di4.10.680.10. 1 hit.
InterProiIPR015116. Cdc42_binding_dom-like.
IPR011009. Kinase-like_dom.
IPR021619. Mig-6.
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.
[Graphical view]
PfamiPF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. 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. AlignAdd to basket

Isoform 1 (identifier: Q07912-1) [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 NVTRLSHFEY VKNEDLEKIG
60 70 80 90 100
MGRPGQRRLW EAVKRRKALC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK
110 120 130 140 150
TSPAPGGPAG EGPLQSLTCL IGEKDLRLLE KLGDGSFGVV RRGEWDAPSG
160 170 180 190 200
KTVSVAVKCL KPDVLSQPEA MDDFIREVNA MHSLDHRNLI RLYGVVLTPP
210 220 230 240 250
MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM GYLESKRFIH
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
LSTSRPPQHL GGVKKPTYDP VSEDQDPLSS DFKRLGLRKP GLPRGLWLAK
560 570 580 590 600
PSARVPGTKA SRGSGAEVTL IDFGEEPVVP ALRPCAPSLA QLAMDACSLL
610 620 630 640 650
DETPPQSPTR ALPRPLHPTP VVDWDARPLP PPPAYDDVAQ DEDDFEICSI
660 670 680 690 700
NSTLVGAGVP AGPSQGQTNY AFVPEQARPP PPLEDNLFLP PQGGGKPPSS
710 720 730 740 750
AQTAEIFQAL QQECMRQLQA PAGSPAPSPS PGGDDKPQVP PRVPIPPRPT
760 770 780 790 800
RPHVQLSPAP PGEEETSQWP GPASPPRVPP REPLSPQGSR TPSPLVPPGS
810 820 830 840 850
SPLPPRLSSS PGKTMPTTQS FASDPKYATP QVIQAPGPRA GPCILPIVRD
860 870 880 890 900
GKKVSSTHYY LLPERPSYLE RYQRFLREAQ SPEEPTPLPV PLLLPPPSTP
910 920 930 940 950
APAAPTATVR PMPQAALDPK ANFSTNNSNP GARPPPPRAT ARLPQRGCPG
960 970 980 990 1000
DGPEAGRPAD KIQMAMVHGV TTEECQAALQ CHGWSVQRAA QYLKVEQLFG
1010 1020 1030
LGLRPRGECH KVLEMFDWNL EQAGCHLLGS WGPAHHKR
Length:1,038
Mass (Da):114,569
Last modified:May 5, 2009 - v3
Checksum:i74A1980665BC3E6B
GO
Isoform 2 (identifier: Q07912-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     485-528: LYLGNPMDPP...DPVSEDQDPL → CPFSAFSPGH...HPVSSRTKGL
     529-1038: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:528
Mass (Da):60,062
Checksum:i6CE378AE9D186C20
GO
Isoform 3 (identifier: Q07912-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLEARPPRTQGSDAAGAAAGRGLRALLLSLTAAAGIWGSMGERSAYQRLAGGEEGPQRLGGGRM
     514-514: K → KREPPPRPPQPAFFTQ
     965-994: Missing.

Note: No experimental confirmation available.
Show »
Length:1,086
Mass (Da):119,349
Checksum:i6FC37F9EFDF69D5E
GO

Sequence cautioni

The sequence AAH08884 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti138G → V in AAH08884 (PubMed:15489334).Curated1
Sequence conflicti304 – 352TRTFS…ERLPR → PPWRDISASSSTQFPHAVPC FPTSLLAKLLLRHSVPASSR EIKLVSILC in AAH08884 (PubMed:15489334).CuratedAdd BLAST49
Sequence conflicti353 – 1038Missing in AAH08884 (PubMed:15489334).CuratedAdd BLAST686
Sequence conflicti586A → P in AAA53570 (PubMed:8497321).Curated1
Sequence conflicti722Missing in AAA53570 (PubMed:8497321).Curated1
Sequence conflicti838 – 840PRA → AG in AAA53570 (PubMed:8497321).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03279234R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_03279371K → R.1 PublicationCorresponds to variant rs56036945dbSNPEnsembl.1
Natural variantiVAR_03279499R → Q in an ovarian mucinous carcinoma sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Tyr-284 leading to activation of AKT1. 1 PublicationCorresponds to variant rs113498671dbSNPEnsembl.1
Natural variantiVAR_03279599R → W.1 PublicationCorresponds to variant rs3747673dbSNPEnsembl.1
Natural variantiVAR_032796152T → M.1 PublicationCorresponds to variant rs56161912dbSNPEnsembl.1
Natural variantiVAR_032797346E → K in an ovarian endometrioid cancer sample; somatic mutation. 2 Publications1
Natural variantiVAR_032798409M → I in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_032799507P → S.1 PublicationCorresponds to variant rs35759128dbSNPEnsembl.1
Natural variantiVAR_076966638V → M Found in patients with childhood-onset epilepsy; unknown pathological significance; loss of interaction with NEDD4 and NEDD4L; increased protein abundance. 1 Publication1
Natural variantiVAR_032800725P → L.2 PublicationsCorresponds to variant rs56260729dbSNPEnsembl.1
Natural variantiVAR_032801748R → Q.1 PublicationCorresponds to variant rs57872314dbSNPEnsembl.1
Natural variantiVAR_057115802P → L.Corresponds to variant rs3749333dbSNPEnsembl.1
Natural variantiVAR_0328021038R → H.1 PublicationCorresponds to variant rs13433937dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0372841M → MLEARPPRTQGSDAAGAAAG RGLRALLLSLTAAAGIWGSM GERSAYQRLAGGEEGPQRLG GGRM in isoform 3. 1 Publication1
Alternative sequenceiVSP_008655485 – 528LYLGN…DQDPL → CPFSAFSPGHPPAETCGQVL WTGRREACASDPRLHPVSSR TKGL in isoform 2. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_037285514K → KREPPPRPPQPAFFTQ in isoform 3. 1 Publication1
Alternative sequenceiVSP_008656529 – 1038Missing in isoform 2. 1 PublicationAdd BLAST510
Alternative sequenceiVSP_037286965 – 994Missing in isoform 3. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13738 mRNA. Translation: AAA53570.2.
AK131539 mRNA. Translation: BAD18675.1.
AC124944 Genomic DNA. No translation available.
BC008884 mRNA. Translation: AAH08884.1. Sequence problems.
BC028164 mRNA. Translation: AAH28164.1.
CCDSiCCDS33927.1. [Q07912-3]
CCDS33928.1. [Q07912-1]
PIRiS33596.
RefSeqiNP_001010938.1. NM_001010938.1. [Q07912-3]
NP_001294975.1. NM_001308046.1.
NP_005772.3. NM_005781.4. [Q07912-1]
UniGeneiHs.518513.

Genome annotation databases

EnsembliENST00000333602; ENSP00000329425; ENSG00000061938. [Q07912-1]
ENST00000381916; ENSP00000371341; ENSG00000061938. [Q07912-3]
ENST00000439230; ENSP00000395588; ENSG00000061938. [Q07912-2]
GeneIDi10188.
KEGGihsa:10188.
UCSCiuc003fvt.2. human. [Q07912-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13738 mRNA. Translation: AAA53570.2.
AK131539 mRNA. Translation: BAD18675.1.
AC124944 Genomic DNA. No translation available.
BC008884 mRNA. Translation: AAH08884.1. Sequence problems.
BC028164 mRNA. Translation: AAH28164.1.
CCDSiCCDS33927.1. [Q07912-3]
CCDS33928.1. [Q07912-1]
PIRiS33596.
RefSeqiNP_001010938.1. NM_001010938.1. [Q07912-3]
NP_001294975.1. NM_001308046.1.
NP_005772.3. NM_005781.4. [Q07912-1]
UniGeneiHs.518513.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF4NMR-B448-489[»]
1U46X-ray2.00A/B109-395[»]
1U4DX-ray2.10A/B109-395[»]
1U54X-ray2.80A/B109-395[»]
3EQPX-ray2.30A/B117-392[»]
3EQRX-ray2.00A/B117-392[»]
4EWHX-ray2.50A/B117-391[»]
4HZRX-ray1.31A/B115-389[»]
4HZSX-ray3.23A/B/C/D115-453[»]
4ID7X-ray3.00A117-389[»]
ProteinModelPortaliQ07912.
SMRiQ07912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115485. 77 interactors.
DIPiDIP-33858N.
IntActiQ07912. 33 interactors.
MINTiMINT-1382124.
STRINGi9606.ENSP00000371341.

Chemistry databases

BindingDBiQ07912.
ChEMBLiCHEMBL4599.
DrugBankiDB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi2246.

PTM databases

iPTMnetiQ07912.
PhosphoSitePlusiQ07912.

Polymorphism and mutation databases

BioMutaiTNK2.
DMDMi229462980.

Proteomic databases

EPDiQ07912.
MaxQBiQ07912.
PaxDbiQ07912.
PeptideAtlasiQ07912.
PRIDEiQ07912.

Protocols and materials databases

DNASUi10188.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333602; ENSP00000329425; ENSG00000061938. [Q07912-1]
ENST00000381916; ENSP00000371341; ENSG00000061938. [Q07912-3]
ENST00000439230; ENSP00000395588; ENSG00000061938. [Q07912-2]
GeneIDi10188.
KEGGihsa:10188.
UCSCiuc003fvt.2. human. [Q07912-1]

Organism-specific databases

CTDi10188.
DisGeNETi10188.
GeneCardsiTNK2.
H-InvDBHIX0003961.
HGNCiHGNC:19297. TNK2.
HPAiCAB009948.
HPA041954.
MalaCardsiTNK2.
MIMi606994. gene.
neXtProtiNX_Q07912.
OpenTargetsiENSG00000061938.
Orphaneti391316. Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression.
PharmGKBiPA134909759.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0199. Eukaryota.
ENOG410XPRC. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000168225.
HOVERGENiHBG100429.
InParanoidiQ07912.
KOiK08886.
OMAiKTMPTTQ.
OrthoDBiEOG091G03HT.
PhylomeDBiQ07912.
TreeFamiTF316643.

Enzyme and pathway databases

BioCyciZFISH:HS00763-MONOMER.
BRENDAi2.7.10.2. 2681.
SignaLinkiQ07912.
SIGNORiQ07912.

Miscellaneous databases

ChiTaRSiTNK2. human.
EvolutionaryTraceiQ07912.
GeneWikiiTNK2.
GenomeRNAii10188.
PROiQ07912.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000061938.
CleanExiHS_TNK2.
ExpressionAtlasiQ07912. baseline and differential.
GenevisibleiQ07912. HS.

Family and domain databases

Gene3Di4.10.680.10. 1 hit.
InterProiIPR015116. Cdc42_binding_dom-like.
IPR011009. Kinase-like_dom.
IPR021619. Mig-6.
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.
[Graphical view]
PfamiPF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiACK1_HUMAN
AccessioniPrimary (citable) accession number: Q07912
Secondary accession number(s): Q6ZMQ0, Q8N6U7, Q96H59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: May 5, 2009
Last modified: November 30, 2016
This is version 178 of the entry and version 3 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.