PAK3_MOUSE - dbPTM
PAK3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAK3_MOUSE
UniProt AC Q61036
Protein Name Serine/threonine-protein kinase PAK 3
Gene Name Pak3
Organism Mus musculus (Mouse).
Sequence Length 559
Subcellular Localization Cytoplasm.
Protein Description Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. [PubMed: 25851601 Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. May also be involved in early neuronal development.]
Protein Sequence MSDSLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHQSNTKTASEPPLAPPVSEEEDEEEEEEEDDNEPPPVIAPRPEHTKSIYTRSVVESIASPAAPNKEDIPPSAENANSTTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR
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
2Phosphorylation------MSDSLDNEE
------CCCCCCCCC
35.5926824392
4Phosphorylation----MSDSLDNEEKP
----CCCCCCCCCCC
30.2526643407
20PhosphorylationAPPLRMNSNNRDSSA
CCCCCCCCCCCCCCC
26.5829514104
25PhosphorylationMNSNNRDSSALNHSS
CCCCCCCCCCCCCCC
17.8029550500
26PhosphorylationNSNNRDSSALNHSSK
CCCCCCCCCCCCCCC
40.8529550500
45AcetylationAPEEKNKKARLRSIF
CCHHHCHHHHHHHHC
48.407619027
50PhosphorylationNKKARLRSIFPGGGD
CHHHHHHHHCCCCCC
32.9229899451
120PhosphorylationWARLLQTSNITKLEQ
HHHHHHHCCCHHHHH
17.1829514104
124AcetylationLQTSNITKLEQKKNP
HHHCCCHHHHHCCCH
46.3522826441
139UbiquitinationQAVLDVLKFYDSKET
HHHHHHHHHHCCCCC
41.55-
143PhosphorylationDVLKFYDSKETVNNQ
HHHHHHCCCCCCCCE
22.4725338131
146PhosphorylationKFYDSKETVNNQKYM
HHHCCCCCCCCEEEE
32.0729899451
154PhosphorylationVNNQKYMSFTSGDKS
CCCEEEEEEECCCCC
23.4526824392
156PhosphorylationNQKYMSFTSGDKSAH
CEEEEEEECCCCCCC
25.2129550500
157PhosphorylationQKYMSFTSGDKSAHG
EEEEEEECCCCCCCE
42.8829899451
161PhosphorylationSFTSGDKSAHGYIAA
EEECCCCCCCEEEEE
30.1823684622
165PhosphorylationGDKSAHGYIAAHQSN
CCCCCCEEEEEECCC
4.2229514104
171PhosphorylationGYIAAHQSNTKTASE
EEEEEECCCCCCCCC
36.2823684622
175PhosphorylationAHQSNTKTASEPPLA
EECCCCCCCCCCCCC
33.1225619855
177PhosphorylationQSNTKTASEPPLAPP
CCCCCCCCCCCCCCC
56.7325619855
186PhosphorylationPPLAPPVSEEEDEEE
CCCCCCCCHHHCHHH
45.0925521595
213PhosphorylationIAPRPEHTKSIYTRS
CCCCHHCCCCCHHHH
25.4825619855
215PhosphorylationPRPEHTKSIYTRSVV
CCHHCCCCCHHHHHH
23.2229550500
217PhosphorylationPEHTKSIYTRSVVES
HHCCCCCHHHHHHHH
11.8229550500
218PhosphorylationEHTKSIYTRSVVESI
HCCCCCHHHHHHHHH
18.1329550500
220PhosphorylationTKSIYTRSVVESIAS
CCCCHHHHHHHHHCC
23.7927180971
224PhosphorylationYTRSVVESIASPAAP
HHHHHHHHHCCCCCC
16.3126643407
227PhosphorylationSVVESIASPAAPNKE
HHHHHHCCCCCCCCC
17.2526643407
239PhosphorylationNKEDIPPSAENANST
CCCCCCCCCCCCCCC
42.7525777480
245PhosphorylationPSAENANSTTLYRNT
CCCCCCCCCCEECCC
21.9925777480
246PhosphorylationSAENANSTTLYRNTD
CCCCCCCCCEECCCH
22.1925777480
247PhosphorylationAENANSTTLYRNTDR
CCCCCCCCEECCCHH
22.9325777480
249PhosphorylationNANSTTLYRNTDRQR
CCCCCCEECCCHHHH
10.3425777480
259PhosphorylationTDRQRKKSKMTDEEI
CHHHHHHHCCCHHHH
30.6029899451
272PhosphorylationEILEKLRSIVSVGDP
HHHHHHHHHHCCCCC
37.4725521595
275PhosphorylationEKLRSIVSVGDPKKK
HHHHHHHCCCCCCCC
20.79-
404UbiquitinationQVIHRDIKSDNILLG
CCEECCCCCCCEEEC
56.92-
435PhosphorylationTPEQSKRSTMVGTPY
CHHHHCCCCCCCCCC
25.2925266776
436PhosphorylationPEQSKRSTMVGTPYW
HHHHCCCCCCCCCCC
21.6525521595
440PhosphorylationKRSTMVGTPYWMAPE
CCCCCCCCCCCCCCH
11.2022322096
442PhosphorylationSTMVGTPYWMAPEVV
CCCCCCCCCCCCHHH
13.9829550500
538SuccinylationHPFLKLAKPLSSLTP
CHHHHHHCCHHHCHH
57.8523806337
538AcetylationHPFLKLAKPLSSLTP
CHHHHHHCCHHHCHH
57.8523806337

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

Oops, there are no upstream regulatory protein records of PAK3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAK3_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 PAK3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOQ_HUMANRHOQphysical
10445846
ARHG7_MOUSEArhgef7physical
9726964

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAK3_MOUSE

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Related Literatures of Post-Translational Modification

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