dbPTM

ACK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACK1_HUMAN
UniProt AC	Q07912
Protein Name	Activated CDC42 kinase 1
Gene Name	TNK2
Organism	Homo sapiens (Human).
Sequence Length	1038
Subcellular Localization	Cell membrane. Nucleus. Endosome. Cell junction, adherens junction. Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Membrane, clathrin-coated pit. Cytoplasm, perinuclear region . N
Protein Description	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. Phosphorylates WASP. [PubMed: 20110370]
Protein Sequence	MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29 (in isoform 3)	Phosphorylation	-	33.44	-
33	Phosphorylation	LRDDLNVTRLSHFEY HHCCCCCCCCCCEEE	25.48	4113757
36	Phosphorylation	DLNVTRLSHFEYVKN CCCCCCCCCEEEECC	23.88	50563191
39 (in isoform 3)	Phosphorylation	-	43.95	-
40	Phosphorylation	TRLSHFEYVKNEDLE CCCCCEEEECCHHHH	18.77	24719451
48	Ubiquitination	VKNEDLEKIGMGRPG ECCHHHHHCCCCCCH	52.43	-
74	Phosphorylation	KALCKRKSWMSKVFS HHHHHCCHHHHHHHC	31.85	20809857
77	Phosphorylation	CKRKSWMSKVFSGKR HHCCHHHHHHHCCCC	21.29	113314191
81	Phosphorylation	SWMSKVFSGKRLEAE HHHHHHHCCCCEEEE	46.52	27251275
100	Ubiquitination	HSQSTFRKTSPAPGG CCCCCCCCCCCCCCC	49.52	-
101	Phosphorylation	SQSTFRKTSPAPGGP CCCCCCCCCCCCCCC	35.37	30278072
102	Phosphorylation	QSTFRKTSPAPGGPA CCCCCCCCCCCCCCC	23.31	30278072
116	Phosphorylation	AGEGPLQSLTCLIGE CCCCCCCEEEHEEEH	33.07	22210691
118	Phosphorylation	EGPLQSLTCLIGEKD CCCCCEEEHEEEHHH	15.54	22210691
124	Ubiquitination	LTCLIGEKDLRLLEK EEHEEEHHHHHHHHH	57.77	-
131	Ubiquitination	KDLRLLEKLGDGSFG HHHHHHHHHCCCCCE	58.71	-
136	Phosphorylation	LEKLGDGSFGVVRRG HHHHCCCCCEEEECC	24.46	21722762
149	Phosphorylation	RGEWDAPSGKTVSVA CCCCCCCCCCEEEEE	55.43	109877
193	Phosphorylation	HRNLIRLYGVVLTPP CCHHHHHHCEEECCC	9.68	21722762
194 (in isoform 3)	Ubiquitination	-	13.98	-
205	Phosphorylation	TPPMKMVTELAPLGS CCCCHHHHHHHCHHH	23.06	55818025
212	Phosphorylation	TELAPLGSLLDRLRK HHHHCHHHHHHHHHH	33.18	55818027
283	Phosphorylation	ALPQNDDHYVMQEHR HCCCCCCCCCCCCCC	21.68	17016520
284	Phosphorylation	LPQNDDHYVMQEHRK CCCCCCCCCCCCCCC	12.47	16472662
445	Phosphorylation	FPRNVVTSVAGLSAQ CCHHHHHHHHCCCHH	9.81	-
455	Phosphorylation	GLSAQDISQPLQNSF CCCHHHCCHHHHHCC	33.75	27251275
461	Phosphorylation	ISQPLQNSFIHTGHG CCHHHHHCCCCCCCC	16.77	27251275
465	Phosphorylation	LQNSFIHTGHGDSDP HHHCCCCCCCCCCCC	26.51	46157771
514 (in isoform 2)	Phosphorylation	-	57.20	25690035
515	Ubiquitination	QHLGGVKKPTYDPVS CCCCCCCCCCCCCCC	39.94	-
517	Phosphorylation	LGGVKKPTYDPVSED CCCCCCCCCCCCCCC	49.81	21945579
518	Phosphorylation	GGVKKPTYDPVSEDQ CCCCCCCCCCCCCCC	27.12	25159151
522	Phosphorylation	KPTYDPVSEDQDPLS CCCCCCCCCCCCCCC	40.62	21945579
529	Phosphorylation	SEDQDPLSSDFKRLG CCCCCCCCHHHHHHC	33.00	26356563
530	Phosphorylation	EDQDPLSSDFKRLGL CCCCCCCHHHHHHCC	55.54	23186163
533	Ubiquitination	DPLSSDFKRLGLRKP CCCCHHHHHHCCCCC	52.26	-
552	Phosphorylation	GLWLAKPSARVPGTK CCEECCCCCCCCCCC	28.18	28348404
595 (in isoform 3)	Phosphorylation	-	38.52	17016520
596 (in isoform 3)	Phosphorylation	-	3.32	19901323
603	Phosphorylation	ACSLLDETPPQSPTR HHHHHCCCCCCCCCC	39.68	26074081
607	Phosphorylation	LDETPPQSPTRALPR HCCCCCCCCCCCCCC	33.73	31437597
609	Phosphorylation	ETPPQSPTRALPRPL CCCCCCCCCCCCCCC	33.55	26074081
635	Phosphorylation	PLPPPPAYDDVAQDE CCCCCCCCCCCCCCC	20.60	8502311
724	Phosphorylation	QLQAPAGSPAPSPSP HCCCCCCCCCCCCCC	21.72	29255136
728	Phosphorylation	PAGSPAPSPSPGGDD CCCCCCCCCCCCCCC	39.87	29255136
730	Phosphorylation	GSPAPSPSPGGDDKP CCCCCCCCCCCCCCC	40.28	17192257
750	Phosphorylation	VPIPPRPTRPHVQLS CCCCCCCCCCCCCCC	59.10	28270605
757	Phosphorylation	TRPHVQLSPAPPGEE CCCCCCCCCCCCCCC	11.26	28270605
766	Phosphorylation	APPGEEETSQWPGPA CCCCCCCCCCCCCCC	29.51	28270605
767	Phosphorylation	PPGEEETSQWPGPAS CCCCCCCCCCCCCCC	33.26	28270605
774	Phosphorylation	SQWPGPASPPRVPPR CCCCCCCCCCCCCCC	38.27	25850435
785	Phosphorylation	VPPREPLSPQGSRTP CCCCCCCCCCCCCCC	26.37	27794612
789	Phosphorylation	EPLSPQGSRTPSPLV CCCCCCCCCCCCCCC	27.94	82313409
791	Phosphorylation	LSPQGSRTPSPLVPP CCCCCCCCCCCCCCC	29.80	23312004
793	Phosphorylation	PQGSRTPSPLVPPGS CCCCCCCCCCCCCCC	30.19	28985074
800	Phosphorylation	SPLVPPGSSPLPPRL CCCCCCCCCCCCCCC	34.26	22210691
801	Phosphorylation	PLVPPGSSPLPPRLS CCCCCCCCCCCCCCC	36.05	27794612
808	Phosphorylation	SPLPPRLSSSPGKTM CCCCCCCCCCCCCCC	30.01	21722762
809	Phosphorylation	PLPPRLSSSPGKTMP CCCCCCCCCCCCCCC	45.18	21722762
810	Phosphorylation	LPPRLSSSPGKTMPT CCCCCCCCCCCCCCC	34.00	30576142
814	Phosphorylation	LSSSPGKTMPTTQSF CCCCCCCCCCCCCHH	34.01	23312004
814	O-linked_Glycosylation	LSSSPGKTMPTTQSF CCCCCCCCCCCCCHH	34.01	30059200
817	Phosphorylation	SPGKTMPTTQSFASD CCCCCCCCCCHHCCC	27.01	23312004
817	O-linked_Glycosylation	SPGKTMPTTQSFASD CCCCCCCCCCHHCCC	27.01	30059200
818	Phosphorylation	PGKTMPTTQSFASDP CCCCCCCCCHHCCCC	19.15	46157777
818	O-linked_Glycosylation	PGKTMPTTQSFASDP CCCCCCCCCHHCCCC	19.15	30059200
820	Phosphorylation	KTMPTTQSFASDPKY CCCCCCCHHCCCCCC	22.23	23312004
823	Phosphorylation	PTTQSFASDPKYATP CCCCHHCCCCCCCCC	53.05	26330541
826	Phosphorylation	QSFASDPKYATPQVI CHHCCCCCCCCCCEE	53.13	17081983
826	Acetylation	QSFASDPKYATPQVI CHHCCCCCCCCCCEE	53.13	19823597
827	Phosphorylation	SFASDPKYATPQVIQ HHCCCCCCCCCCEEE	22.54	29255136
829	Phosphorylation	ASDPKYATPQVIQAP CCCCCCCCCCEEECC	15.91	30266825
839	Methylation	VIQAPGPRAGPCILP EEECCCCCCCCEEEE	59.08	-
855	Phosphorylation	VRDGKKVSSTHYYLL EECCEEECCCEEEEC	38.10	28796482
856	Phosphorylation	RDGKKVSSTHYYLLP ECCEEECCCEEEECC	23.38	22322096
857	Phosphorylation	DGKKVSSTHYYLLPE CCEEECCCEEEECCC	13.34	22322096
858	Phosphorylation	GKKVSSTHYYLLPER CEEECCCEEEECCCC	15.93	12522270
859	Phosphorylation	KKVSSTHYYLLPERP EEECCCEEEECCCCH	8.90	27273156
860	Phosphorylation	KVSSTHYYLLPERPS EECCCEEEECCCCHH	8.31	27273156
867	Phosphorylation	YLLPERPSYLERYQR EECCCCHHHHHHHHH	48.88	22322096
868	Phosphorylation	LLPERPSYLERYQRF ECCCCHHHHHHHHHH	18.44	22322096
872	Phosphorylation	RPSYLERYQRFLREA CHHHHHHHHHHHHHC	8.48	19060867
881	Phosphorylation	RFLREAQSPEEPTPL HHHHHCCCCCCCCCC	41.13	23686771
886	Phosphorylation	AQSPEEPTPLPVPLL CCCCCCCCCCCCCCC	40.51	25850435
898	Phosphorylation	PLLLPPPSTPAPAAP CCCCCCCCCCCCCCC	53.44	25850435
899	Phosphorylation	LLLPPPSTPAPAAPT CCCCCCCCCCCCCCC	29.28	25850435
925	Phosphorylation	DPKANFSTNNSNPGA CCCCCCCCCCCCCCC	33.99	19060867
928	Phosphorylation	ANFSTNNSNPGARPP CCCCCCCCCCCCCCC	46.61	23898821
933	Methylation	NNSNPGARPPPPRAT CCCCCCCCCCCCCCC	50.61	-
1011	Ubiquitination	RPRGECHKVLEMFDW CCCCHHHHHHHHHCC	61.24	-
1037	Ubiquitination	SWGPAHHKR------ CCCCCCCCC------	50.35	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
284	Y	Phosphorylation	Kinase	TNK2	Q07912	GPS
284	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
635	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
859	Y	Phosphorylation	Kinase	BMX	P51813	GPS
860	Y	Phosphorylation	Kinase	BMX	P51813	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:19144635
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:19144635
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:23208506

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACK1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ACK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRB2_HUMAN	GRB2	physical	8647288
CDC42_HUMAN	CDC42	physical	11394904
CLH1_HUMAN	CLTC	physical	11278436
HSH2D_HUMAN	HSH2D	physical	11700021
MCF2_HUMAN	MCF2	physical	10652228
NEDD4_HUMAN	NEDD4	physical	20086093
GRB2_HUMAN	GRB2	physical	20086093
CDC42_HUMAN	CDC42	physical	20086093
CLCA_HUMAN	CLTA	physical	19144635
AMPH_HUMAN	AMPH	physical	19144635
BIN1_HUMAN	BIN1	physical	19144635
FABP4_HUMAN	FABP4	physical	19144635
NED4L_HUMAN	NEDD4L	physical	19144635
UFO_HUMAN	AXL	physical	19815557
PGFRB_HUMAN	PDGFRB	physical	19815557
LTK_HUMAN	LTK	physical	19815557
EGFR_HUMAN	EGFR	physical	19815557
ALK_HUMAN	ALK	physical	19815557
BCAR1_HUMAN	BCAR1	physical	17038317
HS90A_HUMAN	HSP90AA1	physical	16288044
WWOX_HUMAN	WWOX	physical	16288044
GRB2_HUMAN	GRB2	physical	22553920
ANDR_HUMAN	AR	physical	17494760
NPHP1_HUMAN	NPHP1	physical	18477472
WASP_HUMAN	WAS	physical	16257963
EGFR_HUMAN	EGFR	physical	18435854
CDC42_HUMAN	CDC42	physical	15123659
YES_HUMAN	YES1	physical	21309750
HCK_HUMAN	HCK	physical	21309750
SRC_HUMAN	SRC	physical	21309750
LYN_HUMAN	LYN	physical	21309750
NCK1_HUMAN	NCK1	physical	21309750
GRB2_HUMAN	GRB2	physical	21309750
NPHP1_HUMAN	NPHP1	physical	21309750
SRC8_HUMAN	CTTN	physical	22952966
ACK1_HUMAN	TNK2	physical	14506255
KCNA5_HUMAN	KCNA5	physical	14506255
CLH1_HUMAN	CLTC	physical	19798056
SIAH1_HUMAN	SIAH1	physical	23208506
ACK1_HUMAN	TNK2	physical	16472662
CDC42_HUMAN	CDC42	physical	24413169
EGFR_HUMAN	EGFR	physical	24413169
SQSTM_HUMAN	SQSTM1	physical	24413169
NBR1_HUMAN	NBR1	physical	24413169
NTRK1_HUMAN	NTRK1	physical	23598414
NTRK2_HUMAN	NTRK2	physical	23598414
NTRK3_HUMAN	NTRK3	physical	23598414
NED4L_HUMAN	NEDD4L	physical	23686771
NEDD4_HUMAN	NEDD4	physical	23686771
TRI50_HUMAN	TRIM50	physical	24308962
ACK1_HUMAN	TNK2	physical	25416956
NEK6_HUMAN	NEK6	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
ACK1_HUMAN	TNK2	physical	20979614
AMPH_RAT	Amph	physical	19144635
CLCA_RAT	Clta	physical	19144635
BIN2_RAT	Bin2	physical	19144635
CDC42_HUMAN	CDC42	physical	16052498
KDM3A_HUMAN	KDM3A	physical	25148682
AKT1_HUMAN	AKT1	physical	25257795
PGFRB_HUMAN	PDGFRB	physical	25257795
PDK1_HUMAN	PDK1	physical	25257795
FGFR1_HUMAN	FGFR1	physical	25945695
ISG15_HUMAN	ISG15	physical	28514442
CDC37_HUMAN	CDC37	physical	28514442
LCP2_HUMAN	LCP2	physical	28188290
HS90A_HUMAN	HSP90AA1	physical	28739485
HS90B_HUMAN	HSP90AB1	physical	28739485
GRP75_HUMAN	HSPA9	physical	28739485
CLH1_HUMAN	CLTC	physical	28739485
ADT2_HUMAN	SLC25A5	physical	28739485
CDC37_HUMAN	CDC37	physical	28739485
GRB2_HUMAN	GRB2	physical	28739485
CSK_HUMAN	CSK	physical	28739485
HAX1_HUMAN	HAX1	physical	28739485
CRKL_HUMAN	CRKL	physical	28739485
CDC42_HUMAN	CDC42	physical	28539360

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171	Adenosine triphosphate

Regulatory Network of ACK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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). 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, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-785 ANDSER-881, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND TYR-827, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Crystal structures of the phosphorylated and unphosphorylated kinasedomains 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). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-395, AND PHOSPHORYLATIONAT TYR-284.	15308621 [Abstract]
"Constitutive activated Cdc42-associated kinase (Ack) phosphorylationat arrested endocytic clathrin-coated pits of cells that lackdynamin."; 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). Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-284; TYR-518;TYR-827; TYR-859 AND TYR-872.	21169560 [Abstract]
"The Cdc42-associated kinase ACK1 is not auto-inhibited but requiresSrc for activation."; Chan W., Sit S.T., Manser E.; Biochem. J. 435:355-364(2011). Cited for: PHOSPHORYLATION AT TYR-284, AND INTERACTION WITH SRC.	21309750 [Abstract]
"Effect of Ack1 tyrosine kinase inhibitor on ligand-independentandrogen 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). Cited for: PHOSPHORYLATION AT TYR-284, TISSUE SPECIFICITY, AND ENZYME REGULATION.	20623637 [Abstract]
"Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates itsactivation."; 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). Cited for: FUNCTION, INTERACTION WITH AKT1, SUBCELLULAR LOCATION,CHARACTERIZATION OF VARIANT LYS-346, PHOSPHORYLATION AT TYR-284, ANDTISSUE SPECIFICITY.	20333297 [Abstract]
"Regulation of Ack1 localization and activity by the amino-terminalSAM domain."; Prieto-Echaguee V., Gucwa A., Brown D.A., Miller W.T.; BMC Biochem. 11:42-42(2010). Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-284, AND DOMAINSAM-LIKE.	20979614 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-860, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-284; TYR-518; TYR-859AND TYR-860, AND MASS SPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518 AND TYR-859, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Purification and enzyme activity of ACK1."; Yokoyama N., Miller W.T.; Methods Enzymol. 406:250-260(2006). Cited for: FUNCTION, AND AUTOPHOSPHORYLATION AT TYR-284.	16472662 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-859 AND TYR-860, ANDMASS SPECTROMETRY.	15951569 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-827; TYR-859 ANDTYR-860, AND MASS SPECTROMETRY.	12522270 [Abstract]