ACK1_MOUSE - dbPTM
ACK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACK1_MOUSE
UniProt AC O54967
Protein Name Activated CDC42 kinase 1
Gene Name Tnk2
Organism Mus musculus (Mouse).
Sequence Length 1055
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. The Tyr-284 phosphorylated f
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..
Protein Sequence MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNITRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKAMCKRKSWMSKVFSGKRLEAEFPSQHSQSTFRKPSPTPGSLPGEGTLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPAGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTLPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMAYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPTQHLGRVKREPPPRPPQPAIFTQKTTYDPVSEDPDPLSSDFKRLGLRKPALPRGLWLAKPSARVPGTKADRSSGGEVTLIDFGEEPVVPTPRPCAPSLAQLAMDACSLLDKTPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEVCSINSTLVGAGLPAGPSQGETNYAFVPEQAQMPPALEDNLFLPPQGGGKPPSSVQTAEIFQALQQECMRQLQVPTGQLTPSPTPGGDDKPQVPPRVPIPPRPTRPRVELSPAPSGEEETSRWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPHRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGRKVSSTHYYLLPERPPYLERYQRFLREAQSPEEPAALPVPPLLPPPSTPAPAAPTATVRPMPQAAPDPKANFSTNNSNPGARPPSLRAAARLPQRGCPGDGQEAARPADKVQMLQAMVHGVTTEECQAALQSHSWSVQRAAQYLKVEQLFGLGLRPRVECHKVLEMFDWNLEQAGCHLLGSCGPAHHKR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
33PhosphorylationLRDDLNITRLSHFEY
HHCCCCCCCCCCEEE		25.2022817900
40PhosphorylationTRLSHFEYVKNEDLE
CCCCCEEEECCHHHH		18.7715582259
94PhosphorylationAEFPSQHSQSTFRKP
EECCCCCCCCCCCCC		20.4226060331
96PhosphorylationFPSQHSQSTFRKPSP
CCCCCCCCCCCCCCC		32.3126060331
97PhosphorylationPSQHSQSTFRKPSPT
CCCCCCCCCCCCCCC		21.5926060331
102PhosphorylationQSTFRKPSPTPGSLP
CCCCCCCCCCCCCCC		44.4326824392
104PhosphorylationTFRKPSPTPGSLPGE
CCCCCCCCCCCCCCC		44.6225619855
107PhosphorylationKPSPTPGSLPGEGTL
CCCCCCCCCCCCCCH		32.3725619855
113PhosphorylationGSLPGEGTLQSLTCL
CCCCCCCCHHHHHEE		19.8121082442
116PhosphorylationPGEGTLQSLTCLIGE
CCCCCHHHHHEEECH		28.8525619855
118PhosphorylationEGTLQSLTCLIGEKD
CCCHHHHHEEECHHH		15.5425619855
131UbiquitinationKDLRLLEKLGDGSFG
HHHHHHHHHCCCCCE		58.71-
284PhosphorylationLPQNDDHYVMQEHRK
CCCCCCCCCCCCCCC		12.4720623637
430PhosphorylationYWWRGQNTRTLCVGP
CEECCCCCCEEEECC		19.6922871156
517 (in isoform 2)Phosphorylation-48.5022499769
517 (in isoform 3)Phosphorylation-48.5022499769
518 (in isoform 2)Phosphorylation-32.5522499769
518 (in isoform 3)Phosphorylation-32.5522499769
522 (in isoform 2)Phosphorylation-54.8122499769
522 (in isoform 3)Phosphorylation-54.8122499769
528PhosphorylationPPQPAIFTQKTTYDP
CCCCCCEECCCCCCC		24.0452677249
529 (in isoform 2)Phosphorylation-30.2822499769
529 (in isoform 3)Phosphorylation-30.2822499769
530 (in isoform 2)Phosphorylation-39.5122499769
530 (in isoform 3)Phosphorylation-39.5122499769
532PhosphorylationAIFTQKTTYDPVSED
CCEECCCCCCCCCCC		32.728572385
533PhosphorylationIFTQKTTYDPVSEDP
CEECCCCCCCCCCCC		24.3921169560
565UbiquitinationPRGLWLAKPSARVPG
CCCCEECCCCCCCCC		37.02-
567PhosphorylationGLWLAKPSARVPGTK
CCEECCCCCCCCCCC		28.1828066266
578PhosphorylationPGTKADRSSGGEVTL
CCCCCCCCCCCCEEE		33.6025338131
579PhosphorylationGTKADRSSGGEVTLI
CCCCCCCCCCCEEEE		52.2725338131
613PhosphorylationQLAMDACSLLDKTPP
HHHHHHHHHHCCCCC		33.4226643407
618PhosphorylationACSLLDKTPPQSPTR
HHHHHCCCCCCCCCC		39.6126643407
622PhosphorylationLDKTPPQSPTRALPR
HCCCCCCCCCCCCCC		33.7331437595
624PhosphorylationKTPPQSPTRALPRPL
CCCCCCCCCCCCCCC		33.5521743459
650PhosphorylationPLPPPPAYDDVAQDE
CCCCCCCCCCCCCCC		20.608502309
737PhosphorylationMRQLQVPTGQLTPSP
HHHCCCCCCCCCCCC		38.4121183079
741PhosphorylationQVPTGQLTPSPTPGG
CCCCCCCCCCCCCCC		17.529396461
743PhosphorylationPTGQLTPSPTPGGDD
CCCCCCCCCCCCCCC		35.855640681
772PhosphorylationTRPRVELSPAPSGEE
CCCCEEEECCCCCCC		12.9025521595
776PhosphorylationVELSPAPSGEEETSR
EEEECCCCCCCCCCC		62.0325619855
789PhosphorylationSRWPGPASPPRVPPR
CCCCCCCCCCCCCCC		38.2721082442
800PhosphorylationVPPREPLSPQGSRTP
CCCCCCCCCCCCCCC		26.3726824392
804PhosphorylationEPLSPQGSRTPSPLV
CCCCCCCCCCCCCCC		27.9428066266
806PhosphorylationLSPQGSRTPSPLVPP
CCCCCCCCCCCCCCC		29.8026643407
808PhosphorylationPQGSRTPSPLVPPGS
CCCCCCCCCCCCCCC		30.1926824392
815PhosphorylationSPLVPPGSSPLPHRL
CCCCCCCCCCCCCCC		34.2625338131
816PhosphorylationPLVPPGSSPLPHRLS
CCCCCCCCCCCCCCC		36.0526370283
823PhosphorylationSPLPHRLSSSPGKTM
CCCCCCCCCCCCCCC		28.8228285833
824PhosphorylationPLPHRLSSSPGKTMP
CCCCCCCCCCCCCCC		45.1828066266
825PhosphorylationLPHRLSSSPGKTMPT
CCCCCCCCCCCCCCC		34.0045560515
832O-linked_GlycosylationSPGKTMPTTQSFASD
CCCCCCCCCCHHCCC		27.0130059200
833O-linked_GlycosylationPGKTMPTTQSFASDP
CCCCCCCCCHHCCCC		19.1530059200
842PhosphorylationSFASDPKYATPQVIQ
HHCCCCCCCCCCEEE		22.5425521595
844PhosphorylationASDPKYATPQVIQAP
CCCCCCCCCCEEECC		15.9125619855
854MethylationVIQAPGPRAGPCILP
EEECCCCCCCCEEEE		59.0824129315
870PhosphorylationVRDGRKVSSTHYYLL
EECCEEEECCEEECC		32.3322499769
871PhosphorylationRDGRKVSSTHYYLLP
ECCEEEECCEEECCC		23.3822499769
872PhosphorylationDGRKVSSTHYYLLPE
CCEEEECCEEECCCC		13.3422499769
874PhosphorylationRKVSSTHYYLLPERP
EEEECCEEECCCCCC		8.9018515860
875PhosphorylationKVSSTHYYLLPERPP
EEECCEEECCCCCCH		8.3122499769
883PhosphorylationLLPERPPYLERYQRF
CCCCCCHHHHHHHHH		24.7122499769
887PhosphorylationRPPYLERYQRFLREA
CCHHHHHHHHHHHHC		8.48-
896PhosphorylationRFLREAQSPEEPAAL
HHHHHCCCCCCCCCC		41.138570647
943PhosphorylationANFSTNNSNPGARPP
CCCCCCCCCCCCCCH		46.6129472430
951PhosphorylationNPGARPPSLRAAARL
CCCCCCHHHHHHHCC		32.9226824392
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
284YPhosphorylationKinaseSRCP05480
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACK1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH1_MOUSECltcphysical
21169560
PSMD1_MOUSEPsmd1physical
17182860
PSMD6_MOUSEPsmd6physical
17182860
NCK1_MOUSENck1physical
16777958
UBC_MOUSEUbcphysical
17182860
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 AND TYR-533.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533 AND TYR-874, ANDMASS SPECTROMETRY.

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