dbPTM

PAK2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAK2_RAT
UniProt AC	Q64303
Protein Name	Serine/threonine-protein kinase PAK 2
Gene Name	Pak2
Organism	Rattus norvegicus (Rat).
Sequence Length	524
Subcellular Localization	Serine/threonine-protein kinase PAK 2: Cytoplasm. MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane.. PAK-2p34: Nucleus. Cytoplasm, perinuclear region. Membrane Lipid-anchor. I
Protein Description	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. 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. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (By similarity)..
Protein Sequence	MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSSTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNTKGSETSAVVTEEDDDDEDAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSNVDSGAKSSDKQKKKAKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDNGELED ------CCCCCCCCC	39.52	-
2	Phosphorylation	------MSDNGELED ------CCCCCCCCC	39.52	27097102
19	Phosphorylation	PAPPVRMSSTIFSTG CCCCCEEECEEEECC	17.48	28432305
20	Phosphorylation	APPVRMSSTIFSTGG CCCCEEECEEEECCC	19.04	27097102
21	Phosphorylation	PPVRMSSTIFSTGGK CCCEEECEEEECCCC	20.80	28432305
24	Phosphorylation	RMSSTIFSTGGKDPL EEECEEEECCCCCCC	23.45	30181290
25	Phosphorylation	MSSTIFSTGGKDPLS EECEEEECCCCCCCC	38.92	30181290
38	Acetylation	LSANHSLKPLPSVPE CCCCCCCCCCCCCCC	47.74	22902405
55	Phosphorylation	KPRNKIISIFSSTEK CCCCCEEECCCCCCC	22.51	22108457
58	Phosphorylation	NKIISIFSSTEKGSK CCEEECCCCCCCCCC	34.38	27097102
59	Phosphorylation	KIISIFSSTEKGSKK CEEECCCCCCCCCCC	29.81	27097102
60	Phosphorylation	IISIFSSTEKGSKKK EEECCCCCCCCCCCC	40.28	27097102
62	Acetylation	SIFSSTEKGSKKKEK ECCCCCCCCCCCCCC	69.44	-
64	Phosphorylation	FSSTEKGSKKKEKER CCCCCCCCCCCCCCC	52.98	28432305
128	Acetylation	QAVLDVLKFYDSNTV HHHHHHHHHCCCCCC	41.55	-
130	Phosphorylation	VLDVLKFYDSNTVKQ HHHHHHHCCCCCCEE	19.51	22673903
132	Phosphorylation	DVLKFYDSNTVKQKY HHHHHCCCCCCEEEE	24.03	29779826
134	Phosphorylation	LKFYDSNTVKQKYLS HHHCCCCCCEEEEEC	32.79	30417516
139	Phosphorylation	SNTVKQKYLSFTPPE CCCCEEEEECCCCCC	12.70	27097102
141	Phosphorylation	TVKQKYLSFTPPEKD CCEEEEECCCCCCCC	24.80	28689409
143	Phosphorylation	KQKYLSFTPPEKDGF EEEEECCCCCCCCCC	34.26	28689409
152	Phosphorylation	PEKDGFPSGTPALNT CCCCCCCCCCCCCCC	53.70	29779826
154	Phosphorylation	KDGFPSGTPALNTKG CCCCCCCCCCCCCCC	15.10	27097102
159	Phosphorylation	SGTPALNTKGSETSA CCCCCCCCCCCCCEE	37.32	27097102
162	Phosphorylation	PALNTKGSETSAVVT CCCCCCCCCCEEEEE	38.98	27097102
164	Phosphorylation	LNTKGSETSAVVTEE CCCCCCCCEEEEECC	24.55	27097102
165	Phosphorylation	NTKGSETSAVVTEED CCCCCCCEEEEECCC	18.27	27097102
169	Phosphorylation	SETSAVVTEEDDDDE CCCEEEEECCCCCCC	27.36	27097102
192	Phosphorylation	PRPDHTKSIYTRSVI CCCCCCCCCCCCCCC	23.22	23984901
194	Phosphorylation	PDHTKSIYTRSVIDP CCCCCCCCCCCCCCC	11.82	23984901
195	Phosphorylation	DHTKSIYTRSVIDPI CCCCCCCCCCCCCCC	18.13	23984901
197	Phosphorylation	TKSIYTRSVIDPIPA CCCCCCCCCCCCCCC	18.67	28689409
209	Phosphorylation	IPAPVGDSNVDSGAK CCCCCCCCCCCCCCC	32.59	22108457
213	Phosphorylation	VGDSNVDSGAKSSDK CCCCCCCCCCCCCHH	36.05	28689409
217	Phosphorylation	NVDSGAKSSDKQKKK CCCCCCCCCHHHHHH	43.14	25575281
218	Phosphorylation	VDSGAKSSDKQKKKA CCCCCCCCHHHHHHC	48.39	28689409
226	Acetylation	DKQKKKAKMTDEEIM HHHHHHCCCCHHHHH	51.73	22902405
241	Phosphorylation	EKLRTIVSIGDPKKK HHHHHHHCCCCCCCC	19.60	23984901
370	Ubiquitination	QVIHRDIKSDNVLLG CCEECCCCCCCEEEC	56.92	-
401	Phosphorylation	TPEQSKRSTMVGTPY CHHHHCCCCCCCCCC	25.29	21738781
402	Phosphorylation	PEQSKRSTMVGTPYW HHHHCCCCCCCCCCC	21.65	22669945
474	Methylation	EKLSPIFRDFLNRCL HHCCHHHHHHHHHHH	34.19	18962139
479	Methylation	IFRDFLNRCLEMDVE HHHHHHHHHHHCCHH	28.66	26494511
488	Methylation	LEMDVEKRGSAKELL HHCCHHHCCCHHHHH	30.69	26494517
507	Phosphorylation	LKLAKPLSSLTPLIL HHHHHCHHHHHHHHH	31.65	23984901
508	Phosphorylation	KLAKPLSSLTPLILA HHHHCHHHHHHHHHH	43.90	23984901
510	Phosphorylation	AKPLSSLTPLILAAK HHCHHHHHHHHHHHH	20.28	23984901

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 PAK2_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
402	T	Phosphorylation		-
Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate (By similarity).

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 PAK2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAK2_RAT	Pak2	physical	7592896
MBP_RAT	Mbp	physical	7592896
CDC42_RAT	Cdc42	physical	7592896

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PAK2_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139; SER-141 ANDTHR-143, AND MASS SPECTROMETRY.	16641100 [Abstract]
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASSSPECTROMETRY.	16396499 [Abstract]

show