Reviewed, UniProtKB/Swiss-Prot Q07912 (ACK1_HUMAN)

Names and origin

Protein names

Recommended name:
    Activated CDC42 kinase 1
      Short name=ACK-1
    EC=2.7.10.2
Alternative name(s):
    Tyrosine kinase non-receptor protein 2

Gene names

Name:	TNK2
Synonyms:	ACK1

Organism

Homo sapiens (Human) [Complete proteome]

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR. Participates in clathrin-mediated endocytosis. May be involved both in adult synaptic function and plasticity and in brain development. Ref.6 Ref.11
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Magnesium.
Enzyme regulation	The SH3 domain appears to play an autoinhibitory role By similarity.
Subunit structure	Interacts with CDC42. Interacts with activated CSPG4. Ref.1 Ref.5 Ref.13
Subcellular location	Cell membrane 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.
Sequence caution	The sequence AAH08884.1 differs from that shown. Reason: Miscellaneous discrepancy. Unlikely isoform. Aberrant splice sites.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	positive regulation of peptidyl-tyrosine phosphorylation Ref.5 Inferred from direct assay. Source: UniProtKB protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase inhibitor activity Ref.1 Traceable author statement. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.15 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953-2	1	EBI-603457,EBI-287394
PTPN12	Q05209	1	EBI-603457,EBI-2266035
PTPRC	P08575	1	EBI-603457,EBI-1341
PTPRJ	Q12913	1	EBI-603457,EBI-2264500

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. Probable target of 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

Nucleotide binding

132 – 140

9

ATP

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.14

Modified residue

149

1

Phosphoserine Ref.10

Modified residue

284

1

Phosphotyrosine; by autocatalysis Ref.11 Ref.16

Modified residue

518

1

Phosphotyrosine Ref.9 Ref.12

Modified residue

785

1

Phosphoserine

Modified residue

827

1

Phosphotyrosine

Modified residue

859

1

Phosphotyrosine

Modified residue

860

1

Phosphotyrosine

Modified residue

881

1

Phosphoserine

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.17

VAR_032792

Natural variant

71

1

K → R Ref.17

VAR_032793

Natural variant

99

1

R → Q in an ovarian mucinous carcinoma sample; somatic mutation. Ref.17

VAR_032794

Natural variant

99

1

R → W Ref.17

VAR_032795

Natural variant

152

1

T → M Ref.17

VAR_032796

Natural variant

346

1

E → K in an ovarian endometrioid cancer sample; somatic mutation. Ref.17

VAR_032797

Natural variant

409

1

M → I in a gastric adenocarcinoma sample; somatic mutation. Ref.17

VAR_032798

Natural variant

507

1

P → S Ref.17

VAR_032799

Natural variant

725

1

P → L

VAR_032800

Natural variant

748

1

R → Q

VAR_032801

Natural variant

802

1

P → L: dbSNP rs3749333.

VAR_057115

Natural variant

1038

1

R → H

VAR_032802

Experimental info

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. 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. 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]	"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.
[7]	"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.
[8]	"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: Epithelium.
[9]	"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.
[10]	"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: Epithelium.
[11]	"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.
[12]	"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.
[13]	"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: 17182860] [Abstract] Cited for: INTERACTION WITH UBA.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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

EMBLGenBankDDBJ

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.
NP_005772.3.

UniGene

Hs.518513

3D structure databases

PDBPDBe

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	109-395	[»]
			B	109-395	[»]
3EQP	X-ray	2.30	A/B	117-392	[»]
3EQR	X-ray	2.00	A/B	117-392	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q07912. 15 interactions.

PTM databases

PhosphoSite

Q07912.

Proteomic databases

PRIDE

Q07912.

Genome annotation databases

Ensembl

ENSG00000061938. Homo sapiens. [Contig view]

GeneID

10188.

KEGG

hsa:10188.

UCSC

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

Organism-specific databases

GeneCards

GC03M197080.

H-InvDB

HIX0003961.

HGNC

HGNC:19297. TNK2.

HPA

CAB009948.

MIM

606994. gene.

PharmGKB

PA134888760.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q07912.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Gene expression databases

ArrayExpress

Q07912.

Bgee

Q07912.

CleanEx

HS_TNK2.

GermOnline

ENSG00000061938. Homo sapiens.

Family and domain databases

InterPro

IPR015779. ACK_tyr_kin_N.
IPR015116. GTPase_binding.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR000449. UBA/transl_elong_EF1B_N.
[Graphical view]

PANTHER

PTHR23256:SF265. ACK_tyr_kin_N. 1 hit.

Pfam

PF09027. GTPase_binding. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00018. SH3_1. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

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.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	July 7, 2009
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)