Q07912 (ACK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Activated CDC42 kinase 1
Short name=ACK-1
EC=2.7.10.2
EC=2.7.11.1

Alternative name(s):
Tyrosine kinase non-receptor protein 2

Gene names

Name:	TNK2
Synonyms:	ACK1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1038 AA.
Sequence status	Complete.
Protein existence	Evidence 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.6 Ref.7 Ref.12 Ref.15 Ref.17 Ref.18 Ref.23 Ref.24 Ref.27 Ref.31 Ref.32
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.39 ATP + a protein = ADP + a phosphoprotein. Ref.39
Cofactor	Magnesium.
Enzyme regulation	Inhibited by AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine), which suppresses activating phosphorylation at Tyr-284. Repressed by dasatinib. Ref.31 Ref.33
Subunit structure	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. Ref.1 Ref.5 Ref.10 Ref.11 Ref.12 Ref.17 Ref.21 Ref.22 Ref.26 Ref.27 Ref.30 Ref.32 Ref.34
Subcellular location	Cell membrane. Nucleus. Endosome. Cell junction › adherens junction By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle › clathrin-coated vesicle. Membrane › clathrin-coated pit. 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.9 Ref.11 Ref.24 Ref.30 Ref.32 Ref.35
Tissue specificity	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. Ref.15 Ref.32 Ref.33
Domain	The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR By similarity. Ref.30 The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation. Ref.30 The UBA domain binds both poly- and mono-ubiquitin. Ref.30
Post-translational modification	Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-518 is required for interaction with SRC and is observed during association with clathrin-coated pits. Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent By similarity.
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 AAH08884.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell junction Cell membrane Coated pit Cytoplasmic vesicle Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell surface receptor linked signaling pathway Traceable author statement Ref.36. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.5. Source: UniProtKB protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of clathrin-mediated endocytosis Inferred from direct assay Ref.24. Source: UniProtKB small GTPase mediated signal transduction Traceable author statement. Source: ProtInc
Cellular component	adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell clathrin-coated vesicle Inferred from direct assay Ref.24. Source: UniProtKB coated pit Inferred from direct assay Ref.35. Source: UniProtKB cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay Ref.32. Source: UniProtKB plasma membrane Inferred from direct assay Ref.32Ref.30. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase inhibitor activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.32. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q07912-1)

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: Q07912-2)

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.

Isoform 3 (identifier: Q07912-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1038

1038

Activated CDC42 kinase 1

PRO_0000088058

Regions

Domain

126 – 385

260

Protein kinase

Domain

386 – 448

63

SH3

Domain

454 – 466

13

CRIB

Domain

958 – 996

39

UBA

Nucleotide binding

132 – 140

9

ATP

Region

1 – 110

110

SAM-like domain

Region

623 – 652

30

Required for interaction with SRC

Region

632 – 635

4

Required for interaction with NEDD4 By similarity

Region

733 – 876

144

EBD domain By similarity

Compositional bias

577 – 958

382

Pro-rich

Sites

Active site

252

1

Proton acceptor

Binding site

158

1

ATP

Amino acid modifications

Modified residue

101

1

Phosphothreonine Ref.25 Ref.29

Modified residue

149

1

Phosphoserine Ref.16

Modified residue

284

1

Phosphotyrosine; by SRC and autocatalysis Ref.18 Ref.20 Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.35 Ref.38

Modified residue

517

1

Phosphothreonine Ref.29

Modified residue

518

1

Phosphotyrosine Ref.14 Ref.19 Ref.20 Ref.29 Ref.35

Modified residue

724

1

Phosphoserine Ref.29

Modified residue

728

1

Phosphoserine Ref.29

Modified residue

785

1

Phosphoserine Ref.25 Ref.29

Modified residue

827

1

Phosphotyrosine Ref.8 Ref.16 Ref.29 Ref.35

Modified residue

859

1

Phosphotyrosine Ref.8 Ref.13 Ref.19 Ref.20 Ref.35

Modified residue

860

1

Phosphotyrosine Ref.8 Ref.13 Ref.20 Ref.28

Modified residue

872

1

Phosphotyrosine Ref.35

Modified residue

881

1

Phosphoserine Ref.25

Modified residue

925

1

Phosphothreonine Ref.29

Natural variations

Alternative sequence

1

1

M → MLEARPPRTQGSDAAGAAAG RGLRALLLSLTAAAGIWGSM GERSAYQRLAGGEEGPQRLG GGRM in isoform 3.

VSP_037284

Alternative sequence

485 – 528

44

LYLGN…DQDPL → CPFSAFSPGHPPAETCGQVL WTGRREACASDPRLHPVSSR TKGL in isoform 2.

VSP_008655

Alternative sequence

514

1

K → KREPPPRPPQPAFFTQ in isoform 3.

VSP_037285

Alternative sequence

529 – 1038

510

Missing in isoform 2.

VSP_008656

Alternative sequence

965 – 994

30

Missing in isoform 3.

VSP_037286

Natural variant

34

1

R → L in a lung adenocarcinoma sample; somatic mutation. Ref.40

VAR_032792

Natural variant

71

1

K → R. Ref.40
Corresponds to variant rs56036945 [ dbSNP | Ensembl ].

VAR_032793

Natural variant

99

1

R → Q in an ovarian mucinous carcinoma sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Tyr-284 leading to activation of AKT1. Ref.40

VAR_032794

Natural variant

99

1

R → W. Ref.40
Corresponds to variant rs3747673 [ dbSNP | Ensembl ].

VAR_032795

Natural variant

152

1

T → M. Ref.40
Corresponds to variant rs56161912 [ dbSNP | Ensembl ].

VAR_032796

Natural variant

346

1

E → K in an ovarian endometrioid cancer sample; somatic mutation. Ref.32 Ref.40

VAR_032797

Natural variant

409

1

M → I in a gastric adenocarcinoma sample; somatic mutation. Ref.40

VAR_032798

Natural variant

507

1

P → S. Ref.40
Corresponds to variant rs35759128 [ dbSNP | Ensembl ].

VAR_032799

Natural variant

725

1

P → L. Ref.2 Ref.40
Corresponds to variant rs56260729 [ dbSNP | Ensembl ].

VAR_032800

Natural variant

748

1

R → Q. Ref.40
Corresponds to variant rs57872314 [ dbSNP | Ensembl ].

VAR_032801

Natural variant

802

1

P → L.
Corresponds to variant rs3749333 [ dbSNP | Ensembl ].

VAR_057115

Natural variant

1038

1

R → H. Ref.40
Corresponds to variant rs13433937 [ dbSNP | Ensembl ].

VAR_032802

Experimental info

Mutagenesis

158

1

K → R: Loss of autophosphorylation. Ref.10

Mutagenesis

487

1

L → F: Constantly active kinase. Ref.10

Sequence conflict

138

1

G → V in AAH08884. Ref.4

Sequence conflict

304 – 352

49

TRTFS…ERLPR → PPWRDISASSSTQFPHAVPC FPTSLLAKLLLRHSVPASSR EIKLVSILC in AAH08884. Ref.4

Sequence conflict

353 – 1038

686

Missing in AAH08884. Ref.4

Sequence conflict

586

1

A → P in AAA53570. Ref.1

Sequence conflict

722

1

Missing in AAA53570. Ref.1

Sequence conflict

838 – 840

3

PRA → AG in AAA53570. Ref.1

Secondary structure

1

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1038

Helix Strand Turn

Details...

Helix

123 – 125

3

Beta strand

126 – 133

8

Beta strand

140 – 146

7

Beta strand

152 – 158

7

Helix

169 – 183

15

Beta strand

192 – 196

5

Beta strand

198 – 200

3

Beta strand

202 – 206

5

Helix

213 – 220

8

Helix

221 – 223

3

Helix

226 – 245

20

Helix

255 – 257

3

Beta strand

258 – 262

5

Beta strand

265 – 268

4

Beta strand

283 – 285

3

Helix

294 – 296

3

Helix

299 – 304

6

Beta strand

306 – 308

3

Helix

309 – 324

16

Turn

330 – 333

4

Helix

336 – 344

9

Helix

358 – 367

10

Helix

372 – 374

3

Helix

378 – 388

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 74A1980665BC3E6B	FASTA	1,038	114,569
	10 20 30 40 50 60 MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NVTRLSHFEY VKNEDLEKIG MGRPGQRRLW 70 80 90 100 110 120 EAVKRRKALC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK TSPAPGGPAG EGPLQSLTCL 130 140 150 160 170 180 IGEKDLRLLE KLGDGSFGVV RRGEWDAPSG KTVSVAVKCL KPDVLSQPEA MDDFIREVNA 190 200 210 220 230 240 MHSLDHRNLI RLYGVVLTPP MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM 250 260 270 280 290 300 GYLESKRFIH 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 LSTSRPPQHL GGVKKPTYDP VSEDQDPLSS DFKRLGLRKP 550 560 570 580 590 600 GLPRGLWLAK PSARVPGTKA SRGSGAEVTL IDFGEEPVVP ALRPCAPSLA QLAMDACSLL 610 620 630 640 650 660 DETPPQSPTR ALPRPLHPTP VVDWDARPLP PPPAYDDVAQ DEDDFEICSI NSTLVGAGVP 670 680 690 700 710 720 AGPSQGQTNY AFVPEQARPP PPLEDNLFLP PQGGGKPPSS AQTAEIFQAL QQECMRQLQA 730 740 750 760 770 780 PAGSPAPSPS PGGDDKPQVP PRVPIPPRPT RPHVQLSPAP PGEEETSQWP GPASPPRVPP 790 800 810 820 830 840 REPLSPQGSR TPSPLVPPGS SPLPPRLSSS PGKTMPTTQS FASDPKYATP QVIQAPGPRA 850 860 870 880 890 900 GPCILPIVRD GKKVSSTHYY LLPERPSYLE RYQRFLREAQ SPEEPTPLPV PLLLPPPSTP 910 920 930 940 950 960 APAAPTATVR PMPQAALDPK ANFSTNNSNP GARPPPPRAT ARLPQRGCPG DGPEAGRPAD 970 980 990 1000 1010 1020 KIQMAMVHGV TTEECQAALQ CHGWSVQRAA QYLKVEQLFG LGLRPRGECH KVLEMFDWNL 1030 EQAGCHLLGS WGPAHHKR
	Isoform 2 [UniParc]. Checksum: 6CE378AE9D186C20	FASTA	528	60,062
	10 20 30 40 50 60 MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NVTRLSHFEY VKNEDLEKIG MGRPGQRRLW 70 80 90 100 110 120 EAVKRRKALC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK TSPAPGGPAG EGPLQSLTCL 130 140 150 160 170 180 IGEKDLRLLE KLGDGSFGVV RRGEWDAPSG KTVSVAVKCL KPDVLSQPEA MDDFIREVNA 190 200 210 220 230 240 MHSLDHRNLI RLYGVVLTPP MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM 250 260 270 280 290 300 GYLESKRFIH 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 RIDECPFSAF SPGHPPAETC GQVLWTGRRE ACASDPRLHP VSSRTKGL
	Isoform 3 [UniParc]. Checksum: 6FC37F9EFDF69D5E	FASTA	1,086	119,349
	10 20 30 40 50 60 MLEARPPRTQ GSDAAGAAAG RGLRALLLSL TAAAGIWGSM GERSAYQRLA GGEEGPQRLG 70 80 90 100 110 120 GGRMQPEEGT GWLLELLSEV QLQQYFLRLR DDLNVTRLSH FEYVKNEDLE KIGMGRPGQR 130 140 150 160 170 180 RLWEAVKRRK ALCKRKSWMS KVFSGKRLEA EFPPHHSQST FRKTSPAPGG PAGEGPLQSL 190 200 210 220 230 240 TCLIGEKDLR LLEKLGDGSF GVVRRGEWDA PSGKTVSVAV KCLKPDVLSQ PEAMDDFIRE 250 260 270 280 290 300 VNAMHSLDHR NLIRLYGVVL TPPMKMVTEL APLGSLLDRL RKHQGHFLLG TLSRYAVQVA 310 320 330 340 350 360 EGMGYLESKR FIHRDLAARN LLLATRDLVK IGDFGLMRAL PQNDDHYVMQ EHRKVPFAWC 370 380 390 400 410 420 APESLKTRTF SHASDTWMFG VTLWEMFTYG QEPWIGLNGS QILHKIDKEG ERLPRPEDCP 430 440 450 460 470 480 QDIYNVMVQC WAHKPEDRPT FVALRDFLLE AQPTDMRALQ DFEEPDKLHI QMNDVITVIE 490 500 510 520 530 540 GRAENYWWRG QNTRTLCVGP FPRNVVTSVA GLSAQDISQP LQNSFIHTGH GDSDPRHCWG 550 560 570 580 590 600 FPDRIDELYL GNPMDPPDLL SVELSTSRPP QHLGGVKREP PPRPPQPAFF TQKPTYDPVS 610 620 630 640 650 660 EDQDPLSSDF KRLGLRKPGL PRGLWLAKPS ARVPGTKASR GSGAEVTLID FGEEPVVPAL 670 680 690 700 710 720 RPCAPSLAQL AMDACSLLDE TPPQSPTRAL PRPLHPTPVV DWDARPLPPP PAYDDVAQDE 730 740 750 760 770 780 DDFEICSINS TLVGAGVPAG PSQGQTNYAF VPEQARPPPP LEDNLFLPPQ GGGKPPSSAQ 790 800 810 820 830 840 TAEIFQALQQ ECMRQLQAPA GSPAPSPSPG GDDKPQVPPR VPIPPRPTRP HVQLSPAPPG 850 860 870 880 890 900 EEETSQWPGP ASPPRVPPRE PLSPQGSRTP SPLVPPGSSP LPPRLSSSPG KTMPTTQSFA 910 920 930 940 950 960 SDPKYATPQV IQAPGPRAGP CILPIVRDGK KVSSTHYYLL PERPSYLERY QRFLREAQSP 970 980 990 1000 1010 1020 EEPTPLPVPL LLPPPSTPAP AAPTATVRPM PQAALDPKAN FSTNNSNPGA RPPPPRATAR 1030 1040 1050 1060 1070 1080 LPQRGCPGDG PEAGRPADKI QMVEQLFGLG LRPRGECHKV LEMFDWNLEQ AGCHLLGSWG PAHHKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42." Manser E., Leung T., Salihuddin H., Tan L., Lim L. Nature 363:364-367(1993) [PubMed: 8497321] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC42. Tissue: Hippocampus.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-725. Tissue: Brain.
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Uterus.
[5]	"Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas." Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J. Nat. Cell Biol. 1:507-513(1999) [PubMed: 10587647] [Abstract] Cited for: INTERACTION WITH CSPG4.
[6]	"Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation." Kato J., Kaziro Y., Satoh T. Biochem. Biophys. Res. Commun. 268:141-147(2000) [PubMed: 10652228] [Abstract] Cited for: FUNCTION AS MCF2 KINASE.
[7]	"The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors." Teo M., Tan L., Lim L., Manser E. J. Biol. Chem. 276:18392-18398(2001) [PubMed: 11278436] [Abstract] Cited for: FUNCTION.
[8]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-827; TYR-859 AND TYR-860, MASS SPECTROMETRY.
[9]	"Cdc42-dependent nuclear translocation of non-receptor tyrosine kinase, ACK." Ahmed I., Calle Y., Sayed M.A., Kamal J.M., Rengaswamy P., Manser E., Meiners S., Nur-E-Kamal A. Biochem. Biophys. Res. Commun. 314:571-579(2004) [PubMed: 14733946] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role of Ack1 in polyubiquitination of tumor suppressor Wwox." Mahajan N.P., Whang Y.E., Mohler J.L., Earp H.S. Cancer Res. 65:10514-10523(2005) [PubMed: 16288044] [Abstract] Cited for: AUTOPHOSPHORYLATION, INTERACTION WITH HSP90AB1; MTERK AND WWOX, MUTAGENESIS OF LYS-158 AND LEU-487.
[11]	"SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1." Yeow-Fong L., Lim L., Manser E. FEBS Lett. 579:5040-5048(2005) [PubMed: 16137687] [Abstract] Cited for: INTERACTION WITH SNX9, SUBCELLULAR LOCATION.
[12]	"Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual hydroxyamino acid specificity in a tyrosine kinase." Yokoyama N., Lougheed J., Miller W.T. J. Biol. Chem. 280:42219-42226(2005) [PubMed: 16257963] [Abstract] Cited for: FUNCTION AS WAS KINASE, INTERACTION WITH WASL.
[13]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-859 AND TYR-860, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, MASS SPECTROMETRY.
[15]	"Metastatic properties and genomic amplification of the tyrosine kinase gene ACK1." van der Horst E.H., Degenhardt Y.Y., Strelow A., Slavin A., Chinn L., Orf J., Rong M., Li S., See L.-H., Nguyen K.Q.C., Hoey T., Wesche H., Powers S. Proc. Natl. Acad. Sci. U.S.A. 102:15901-15906(2005) [PubMed: 16247015] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND TYR-827, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas." Modzelewska K., Newman L.P., Desai R., Keely P.J. J. Biol. Chem. 281:37527-37535(2006) [PubMed: 17038317] [Abstract] Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
[18]	"Purification and enzyme activity of ACK1." Yokoyama N., Miller W.T. Methods Enzymol. 406:250-260(2006) [PubMed: 16472662] [Abstract] Cited for: FUNCTION, AUTOPHOSPHORYLATION AT TYR-284.
[19]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518 AND TYR-859, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[20]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-284; TYR-518; TYR-859 AND TYR-860, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[21]	"Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation." Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E., Mohler J.L., Earp H.S., Whang Y.E. Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007) [PubMed: 17494760] [Abstract] Cited for: INTERACTION WITH AR.
[22]	"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: 18477472] [Abstract] Cited for: INTERACTION WITH NPHP1.
[23]	"TNK2 preserves epidermal growth factor receptor expression on the cell surface and enhances migration and invasion of human breast cancer cells." Howlin J., Rosenkvist J., Andersson T. Breast Cancer Res. 10:R36-R36(2008) [PubMed: 18435854] [Abstract] Cited for: FUNCTION.
[24]	"Dysregulation of Ack1 inhibits down-regulation of the EGF receptor." Groevdal L.M., Johannessen L.E., Roedland M.S., Madshus I.H., Stang E. Exp. Cell Res. 314:1292-1300(2008) [PubMed: 18262180] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[25]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-785 AND SER-881, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Down-regulation of active ACK1 is mediated by association with the E3 ubiquitin ligase Nedd4-2." Chan W., Tian R., Lee Y.-F., Sit S.T., Lim L., Manser E. J. Biol. Chem. 284:8185-8194(2009) [PubMed: 19144635] [Abstract] Cited for: INTERACTION WITH NEDD4, UBIQUITINATION.
[27]	"Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is mediated by Grb2: an analysis of ACK1 effects on Axl signaling." Pao-Chun L., Chan P.M., Chan W., Manser E. J. Biol. Chem. 284:34954-34963(2009) [PubMed: 19815557] [Abstract] Cited for: FUNCTION, INTERACTION WITH AXL; LTK; PDGFRL AND GRB2.
[28]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-860, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[29]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; TYR-284; THR-517; TYR-518; SER-724; SER-728; SER-785; TYR-827 AND THR-925, MASS SPECTROMETRY.
[30]	"Regulation of Ack1 localization and activity by the amino-terminal SAM domain." Prieto-Echaguee V., Gucwa A., Brown D.A., Miller W.T. BMC Biochem. 11:42-42(2010) [PubMed: 20979614] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284, DOMAIN SAM-LIKE.
[31]	"Dasatinib inhibits site-specific tyrosine phosphorylation of androgen receptor by Ack1 and Src kinases." Liu Y., Karaca M., Zhang Z., Gioeli D., Earp H.S., Whang Y.E. Oncogene 29:3208-3216(2010) [PubMed: 20383201] [Abstract] Cited for: FUNCTION AS AR KINASE, ENZYME REGULATION.
[32]	"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: 20333297] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LYS-346, PHOSPHORYLATION AT TYR-284, TISSUE SPECIFICITY.
[33]	"Effect of Ack1 tyrosine kinase inhibitor on ligand-independent androgen receptor activity." Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H., Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P. Prostate 70:1274-1285(2010) [PubMed: 20623637] [Abstract] Cited for: PHOSPHORYLATION AT TYR-284, TISSUE SPECIFICITY, ENZYME REGULATION.
[34]	"The Cdc42-associated kinase ACK1 is not auto-inhibited but requires Src for activation." Chan W., Sit S.T., Manser E. Biochem. J. 435:355-364(2011) [PubMed: 21309750] [Abstract] Cited for: PHOSPHORYLATION AT TYR-284, INTERACTION WITH SRC.
[35]	"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: 21169560] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284; TYR-518; TYR-827; TYR-859 AND TYR-872.
[36]	"Shepherding AKT and androgen receptor by Ack1 tyrosine kinase." Mahajan K., Mahajan N.P. J. Cell. Physiol. 224:327-333(2010) [PubMed: 20432460] [Abstract] Cited for: REVIEW ON TUMOR GROWTH.
[37]	"Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK." Mott H.R., Owen D., Nietlispach D., Lowe P.N., Manser E., Lim L., Laue E.D. Nature 399:384-388(1999) [PubMed: 10360579] [Abstract] Cited for: STRUCTURE BY NMR OF 448-489.
[38]	"Crystal structures of the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1." Lougheed J.C., Chen R.-H., Mak P., Stout T.J. J. Biol. Chem. 279:44039-44045(2004) [PubMed: 15308621] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-395, PHOSPHORYLATION AT TYR-284.
[39]	"Identification and optimization of N3,N6-diaryl-1H-pyrazolo[3,4-d]pyrimidine-3,6-diamines as a novel class of ACK1 inhibitors." Kopecky D.J., Hao X., Chen Y., Fu J., Jiao X., Jaen J.C., Cardozo M.G., Liu J., Wang Z., Walker N.P., Wesche H., Li S., Farrelly E., Xiao S.H., Kayser F. Bioorg. Med. Chem. Lett. 18:6352-6356(2008) [PubMed: 18993068] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-392 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY.
[40]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS LEU-34; ARG-71; GLN-99; TRP-99; MET-152; LYS-346; ILE-409; SER-507; LEU-725; GLN-748 AND HIS-1038.
+	Additional computationally mapped references.

Web resources

CGP resequencing studies

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00167089.
IPI00442025.
IPI00552750.

PIR

S33596.

RefSeq

NP_001010938.1. NM_001010938.1.
NP_005772.3. NM_005781.4.

UniGene

Hs.518513.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CF4	NMR	-	B	448-489	[»]
1U46	X-ray	2.00	A/B	109-395	[»]
1U4D	X-ray	2.10	A/B	109-395	[»]
1U54	X-ray	2.80	A/B	109-395	[»]
3EQP	X-ray	2.30	A/B	117-392	[»]
3EQR	X-ray	2.00	A/B	117-392	[»]

ProteinModelPortal

Q07912.

SMR

Q07912. Positions 117-390, 447-489, 995-1032.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q07912. 15 interactions.

MINT

MINT-1382124.

STRING

Q07912.

PTM databases

PhosphoSite

Q07912.

Polymorphism databases

DMDM

229462980.

Proteomic databases

PRIDE

Q07912.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000333602; ENSP00000329425; ENSG00000061938.
ENST00000392400; ENSP00000376201; ENSG00000061938.
ENST00000414741; ENSP00000413373; ENSG00000061938.

GeneID

10188.

KEGG

hsa:10188.

UCSC

uc003fvs.1. human.
uc003fvu.1. human.

Organism-specific databases

CTD

10188.

GeneCards

GC03M195590.

H-InvDB

HIX0003961.

HGNC

HGNC:19297. TNK2.

HPA

CAB009948.
HPA041954.

MIM

606994. gene.

neXtProt

NX_Q07912.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06071.

GeneTree

ENSGT00600000084141.

HOVERGEN

HBG100429.

OMA

PRVPPRE.

OrthoDB

EOG4Q58NQ.

PhylomeDB

Q07912.

Gene expression databases

ArrayExpress

Q07912.

Bgee

Q07912.

CleanEx

HS_TNK2.

Genevestigator

Q07912.

GermOnline

ENSG00000061938. Homo sapiens.

Family and domain databases

InterPro

IPR015116. GTPase_binding.
IPR021619. Inhibitor_Mig-6.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

KO

K08886.

Pfam

PF09027. GTPase_binding. 1 hit.
PF11555. Inhibitor_Mig-6. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

SMART

SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50108. CRIB. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50002. SH3. 1 hit.
PS50030. UBA. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q07912.

DrugBank

DB00171. Adenosine triphosphate.

NextBio

38556.

SOURCE

Search...

Entry information

Entry name

ACK1_HUMAN

Accession

Primary (citable) accession number: Q07912
Secondary accession number(s): Q6ZMQ0, Q8N6U7, Q96H59

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.