Protein detail

ACK1

Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Tyrosine kinase non-receptor protein 2)

Entry name ACK1	UniProt ID Q07912	EVMP confidence score 0.50
Supporting publications (n) 2	Transmembrane count	Protein classification Cancer-related genesEnzymesPlasma proteinsPredicted intracellular proteins

EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information11

Protein Names

Activated CDC42 kinase 1 (ACK-1) (EC 2.7.10.2) (EC 2.7.11.1) (Tyrosine kinase non-receptor protein 2)

Protein Class (4)

Cancer-related genesEnzymesPlasma proteinsPredicted intracellular proteins

Protein Function (5)

Predicted intracellular proteins
ENZYME proteins:Transferases
Enzymes
Cancer-related genes:Candidate cancer biomarkers
Kinases:Tyr protein kinases

Ensembl

ENSG00000061938

Entrez Gene Symbol

TNK2

Gene Synonym (3)

ACKACK1p21cdc42Hs

Gene Description

Tyrosine kinase non receptor 2

Chromosome

Position

195863364-195911945

Supporting publications (n)

EVMP confidence score

0.50

Fluorescence & Localization1

Cell SpecificAdipocytes

Function & Pathway6

Protein Function (5)

Predicted intracellular proteins
ENZYME proteins:Transferases
Enzymes
Cancer-related genes:Candidate cancer biomarkers
Kinases:Tyr protein kinases

Cellular Component (14)

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Molecular Function (13)

Page 1 of 2

Biological Process (3)

Reactome (2)

Mediation Categories (4)

Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationReceptor-signaling mediation

Relations & Evidence37

Enzyme-Mediated Modification (12)

12 records.

Substrate Gene Symbol	Enzyme Gene Symbol	Enzyme UniProt ID	Residue Type	Residue Offset	Modification	Database	References
TNK2	CDC42	P60953	Y	284	phosphorylation	REACH_ProtMapperProtMapper	ProtMapper:21637378
TNK2	CSNK1A1	P48729	Y	284	phosphorylation	KEA	KEA:14506255

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Ligand-Receptor Signaling (9)

9 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
receptor	receptor	OmniPath	No	Yes	No	No	No
intracellular	intracellular	LOCATE	No	No	No	No	No
intracellular	intracellular	ComPPI	No	No	No	No	No
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	UniProt_location	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No
plasma_membrane	plasma_membrane	UniProt_location	No	No	No	No	No
plasma_membrane	plasma_membrane	OmniPath	No	No	No	No	No
receptor	receptor	scConnect	No	Yes	No	No	No

Regulatory Interaction Network (10)

10 records.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
PGFRB	P09619	ACK1	Q07912	Yes	Yes	No	PhosphoSite_norefSIGNORiPTMnetProtMapperInnateDBPhosphoSite_ProtMapper	SIGNOR:25257795 InnateDB:19815557
SRC	P12931	ACK1	Q07912	Yes	Yes	No	iPTMnetSIGNORdbPTMCui2007HINTWang	dbPTM:17389395 SIGNOR:26677978 HINT:21309750 HINT:19144635 HINT:36178070 dbPTM:21309750 dbPTM:19369195 dbPTM:21169560 HINT:14506255 dbPTM:20623637 SIGNOR:36178070 dbPTM:20979614 dbPTM:15308621 dbPTM:20333297 dbPTM:16472662
ACK1	Q07912	WWP2	O00308	Yes	Yes	No	SIGNOR	SIGNOR:36773333
ACK1	Q07912	STAT3	P40763	Yes	Yes	No	Sparser_ProtMapperSIGNORProtMapperCui2007WangREACH_ProtMapper	SIGNOR:28739485 ProtMapper:28739485
ACK1	Q07912	STAT1	P42224	Yes	Yes	No	REACH_ProtMapperSIGNORSparser_ProtMapperProtMapper	SIGNOR:28739485 ProtMapper:28739485
ACK1	Q07912	AKT1	P31749	Yes	Yes	No	iPTMnetSIGNORProtMapperdbPTMACSNSIGNOR_ProtMapper	ProtMapper:20333297 SIGNOR:20333297 ACSN:10652228 dbPTM:20333297 ACSN:11394904
ACK1	Q07912	ANDR	P10275	Yes	Yes	No	Sparser_ProtMapperPhosphoSite_MIMPMIMPPhosphoSite_norefSIGNORiPTMnetProtMapperRLIMS-P_ProtMapperdbPTMBioGRIDWangREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper	ProtMapper:22566699 PhosphoSite:31819114 dbPTM:17494760 SIGNOR:20383201 PhosphoSite:17045208 PhosphoSite:25950519 ProtMapper:25950519 PhosphoSite:20383201 ProtMapper:21318111 PhosphoSite:20623637 ProtMapper:25699576 PhosphoSite:17494760 ProtMapper:22168167 ProtMapper:26546517 ProtMapper:23424109 ProtMapper:25347744 PhosphoSite:28055971 ProtMapper:28055971 SIGNOR:25950519 ProtMapper:30228349 ProtMapper:23597703 ProtMapper:33495411 dbPTM:20623637 BioGRID:31819114 ProtMapper:31819114 ProtMapper:20383201 ProtMapper:17494760 ProtMapper:26814148 ProtMapper:20623637 dbPTM:17045208
ACK1	Q07912	KDM3A	Q9Y4C1	Yes	No	Yes	Sparser_ProtMapperiPTMnetSIGNORProtMapperPhosphoSitePhosphoSite_ProtMapper	SIGNOR:25148682 ProtMapper:32354028 PhosphoSite:25148682
ACK1	Q07912	SNX9	Q9Y5X1	Yes	Yes	No	DOMINOiPTMnetPhosphoPointSIGNORHPRDBioGRIDSPIKE_LCLit-BM-17	SPIKE_LC:11799118 BioGRID:16316319 HPRD:11799118 DOMINO:16137687 Lit-BM-17:16137687 SIGNOR:16316319 HPRD:16137687 Lit-BM-17:16316319
ACK1	Q07912	H4	P62805	Yes	No	No	PhosphoSitePhosphoSite_ProtMapperProtMapper	PhosphoSite:28609657

Protein Complex Composition (5)

5 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs
BTBD3 CRTC2 FAM83A FAM83H OCRL PKP2 PKP3 SEC24B SEC24C TNK2 USO1	O60763 O95487 P53992 Q01968 Q07912 Q53ET0 Q6ZRV2 Q86UY5 Q99959 Q9Y2F9 Q9Y446	0:0:0:0:0:0:0:0:0:0:0	hu.MAP
BTBD3 CRTC2 FAM83A GLDC PKP2 SEC23B SEC24C SEC24D TNK2	O94855 P23378 P53992 Q07912 Q15437 Q53ET0 Q86UY5 Q99959 Q9Y2F9	0:0:0:0:0:0:0:0:0	hu.MAP
CDC42 TNK2	P60953 Q07912	1:1	PDB	PDB:1cf4
TNK2	Q07912	2	PDB	PDB:3eqpPDB:4hzsPDB:7kp6PDB:1u46PDB:3eqrPDB:5zxbPDB:1u4dPDB:6vqmPDB:4ewhPDB:8hmtPDB:1u54PDB:8fz3PDB:4hzr
SETD2 TNK2	Q07912 Q9BYW2	1:1	PDB	PDB:8q5p

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
		1	32384937

Sequence, Structure & Domains15

Sequences

Length

1,038

Mass

114,569

Sequence

MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR

Alternative Products

Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q07912-1; Sequence=Displayed; Name=2; IsoId=Q07912-2; Sequence=VSP_008655, VSP_008656; Name=3; IsoId=Q07912-3; Sequence=VSP_037284, VSP_037285, VSP_037286

Alternative Sequence

1; M -> MGERSAYQRLAGGEEGPQRLGGGRM (in isoform 3); 485..528; LYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPL -> CPFSAFSPGHPPAETCGQVLWTGRREACASDPRLHPVSSRTKGL (in isoform 2); 514; K -> KREPPPRPPQPAFFTQ (in isoform 3); 529..1038; Missing (in isoform 2); 965..994; Missing (in isoform 3)

3D Structural Models

Turn

164..166; 325..327; 330..333; 484..486

Helix

123..125; 171..181; 213..219; 221..223; 226..245; 255..257; 273..276; 288..290; 294..296; 299..304; 309..324; 336..344; 358..367; 372..374; 378..387; 440..443

Beta Strand

118..120; 126..133; 140..146; 148..150; 152..159; 192..196; 198..200; 202..206; 209..212; 258..262; 265..268; 283..285; 306..308; 392..394; 402..404; 412..417; 419..421; 423..432; 435..439; 449..451

3D Structure

NMR spectroscopy (1); X-ray crystallography (17)

Domain & Motif Annotations

Compositional Bias

738..749; Pro residues; 772..783; Pro residues; 794..805; Pro residues

Domain (CC)

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

Domain (FT)

126..385; Protein kinase; 388..448; SH3; 454..466; CRIB; 958..996; UBA

Region

1..110; SAM-like domain; 90..114; Disordered; 497..535; Disordered; 623..652; Required for interaction with SRC; 632..635; Required for interaction with NEDD4; 659..702; Disordered; 718..840; Disordered; 733..876; EBD domain; 917..957; Disordered

Protein Families (2)

Protein kinase superfamily
Tyr protein kinase family

Sequence Similarities

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

Clinical Relevance7

Disease Involvement

Cancer-related genes

Drug Targets

Patented-recorded target

Drugs (19)

ALISERTIB CHEMBL:CHEMBL379975 ZM447439 NULL NVP-TAE684 GEFITINIB PP2 PAZOPANIB CHEMBL:CHEMBL1997335 PD-0166285 ILORASERTIB ADAVOSERTIB DASATINIB ANHYDROUS ENTRECTINIB RG-1530 TAMATINIB PF-562271 CENISERTIB CYC-116

Antibody (2)

HPA041954 HPA069561

Interaction Protein (7)

ENSG00000050820ENSG00000071051ENSG00000096384ENSG00000130340ENSG00000141367ENSG00000158092ENSG00000177885

Interaction Count

Interaction Dataset (2)

intact_biogridbiogrid_bioplex

Supporting Publications2

PMID	Title	Abstract
34265469	Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.	Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.
40689422	Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.	No abstract available