dbPTM

PAK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAK2_MOUSE
UniProt AC	Q8CIN4
Protein Name	Serine/threonine-protein kinase PAK 2
Gene Name	Pak2
Organism	Mus musculus (Mouse).
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	MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNTKGSETSAVVTEEDDDDEDAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSNVDSGAKSSDKQKKKAKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDNGELED ------CCCCCCCCC	39.52	26824392
2	Acetylation	------MSDNGELED ------CCCCCCCCC	39.52	-
19	Phosphorylation	PAPPVRMSSTIFSTG CCCCCEEECEEEECC	17.48	27180971
20	Phosphorylation	APPVRMSSTIFSTGG CCCCEEECEEEECCC	19.04	26824392
21	Phosphorylation	PPVRMSSTIFSTGGK CCCEEECEEEECCCC	20.80	23737553
24	Phosphorylation	RMSSTIFSTGGKDPL EEECEEEECCCCCCC	23.45	26160508
25	Phosphorylation	MSSTIFSTGGKDPLS EECEEEECCCCCCCC	38.92	26160508
32	Phosphorylation	TGGKDPLSANHSLKP CCCCCCCCCCCCCCC	32.20	18846507
36	Phosphorylation	DPLSANHSLKPLPSV CCCCCCCCCCCCCCC	37.58	22817900
38	Acetylation	LSANHSLKPLPSVPE CCCCCCCCCCCCCCC	47.74	23806337
42	Phosphorylation	HSLKPLPSVPEEKKP CCCCCCCCCCCCCCC	58.97	22817900
52	Acetylation	EEKKPRNKIISIFSG CCCCCCCCEEEEECC	42.57	23806337
52	Malonylation	EEKKPRNKIISIFSG CCCCCCCCEEEEECC	42.57	26320211
55	Phosphorylation	KPRNKIISIFSGTEK CCCCCEEEEECCCCC	22.51	26824392
58	Phosphorylation	NKIISIFSGTEKGSK CCEEEEECCCCCCCC	43.04	27180971
60	Phosphorylation	IISIFSGTEKGSKKK EEEEECCCCCCCCCC	33.07	28833060
62	Acetylation	SIFSGTEKGSKKKEK EEECCCCCCCCCCCC	69.21	23806337
64	Phosphorylation	FSGTEKGSKKKEKER ECCCCCCCCCCCCCC	52.98	26824392
75	Phosphorylation	EKERPEISPPSDFEH CCCCCCCCCCCHHCC	29.15	29899451
78	Phosphorylation	RPEISPPSDFEHTIH CCCCCCCCHHCCEEE	59.31	23608596
109	Phosphorylation	WARLLQTSNITKLEQ HHHHHHHCCHHHHHH	17.18	29514104
128	Acetylation	QAVLDVLKFYDSNTV HHHHHHHHHCCCCCC	41.55	-
130	Phosphorylation	VLDVLKFYDSNTVKQ HHHHHHHCCCCCCEE	19.51	28833060
132	Phosphorylation	DVLKFYDSNTVKQKY HHHHHCCCCCCEEEE	24.03	25521595
134	Phosphorylation	LKFYDSNTVKQKYLS HHHCCCCCCEEEEEC	32.79	23684622
136	Ubiquitination	FYDSNTVKQKYLSFT HCCCCCCEEEEECCC	38.75	22790023
139	Phosphorylation	SNTVKQKYLSFTPPE CCCCEEEEECCCCCC	12.70	25521595
141	Phosphorylation	TVKQKYLSFTPPEKD CCEEEEECCCCCCCC	24.80	27087446
143	Phosphorylation	KQKYLSFTPPEKDGF EEEEECCCCCCCCCC	34.26	25521595
152	Phosphorylation	PEKDGFPSGTPALNT CCCCCCCCCCCCCCC	53.70	25521595
154	Phosphorylation	KDGFPSGTPALNTKG CCCCCCCCCCCCCCC	15.10	25521595
159	Phosphorylation	SGTPALNTKGSETSA CCCCCCCCCCCCCEE	37.32	21082442
162	Phosphorylation	PALNTKGSETSAVVT CCCCCCCCCCEEEEE	38.98	25619855
164	Phosphorylation	LNTKGSETSAVVTEE CCCCCCCCEEEEECC	24.55	25619855
165	Phosphorylation	NTKGSETSAVVTEED CCCCCCCEEEEECCC	18.27	25619855
169	Phosphorylation	SETSAVVTEEDDDDE CCCEEEEECCCCCCC	27.36	25521595
190	Phosphorylation	IAPRPDHTKSIYTRS ECCCCCCCCCCCCCC	33.59	25619855
192	Phosphorylation	PRPDHTKSIYTRSVI CCCCCCCCCCCCCCC	23.22	27087446
194	Phosphorylation	PDHTKSIYTRSVIDP CCCCCCCCCCCCCCC	11.82	26643407
195	Phosphorylation	DHTKSIYTRSVIDPI CCCCCCCCCCCCCCC	18.13	26643407
197	Phosphorylation	TKSIYTRSVIDPIPA CCCCCCCCCCCCCCC	18.67	25521595
209	Phosphorylation	IPAPVGDSNVDSGAK CCCCCCCCCCCCCCC	32.59	25619855
213	Phosphorylation	VGDSNVDSGAKSSDK CCCCCCCCCCCCCHH	36.05	27087446
217	Phosphorylation	NVDSGAKSSDKQKKK CCCCCCCCCHHHHHH	43.14	23984901
218	Phosphorylation	VDSGAKSSDKQKKKA CCCCCCCCHHHHHHC	48.39	23984901
235	Ubiquitination	TDEEIMEKLRTIVSI CHHHHHHHHHHHHCC	26.37	22790023
241	Phosphorylation	EKLRTIVSIGDPKKK HHHHHHHCCCCCCCC	19.60	29514104
252	Phosphorylation	PKKKYTRYEKIGQGA CCCCEECEEECCCCC	17.49	22817900
370	Ubiquitination	QVIHRDIKSDNVLLG CCEECCCCCCCEEEC	56.92	22790023
381	Phosphorylation	VLLGMEGSVKLTDFG EEECCCCEEEEECCC	11.63	29176673
401	Phosphorylation	TPEQSKRSTMVGTPY CHHHHCCCCCCCCCC	25.29	25266776
402	Phosphorylation	PEQSKRSTMVGTPYW HHHHCCCCCCCCCCC	21.65	25521595
406	Phosphorylation	KRSTMVGTPYWMAPE CCCCCCCCCCCCCCH	11.20	22322096
408	Phosphorylation	STMVGTPYWMAPEVV CCCCCCCCCCCCHHH	13.98	29550500
474	Dimethylation	EKLSPIFRDFLNRCL HHCCHHHHHHHHHHH	34.19	-
474	Methylation	EKLSPIFRDFLNRCL HHCCHHHHHHHHHHH	34.19	18962133
490	Phosphorylation	MDVEKRGSAKELLQH CCHHHCCCHHHHHCC	39.95	-
504	Succinylation	HPFLKLAKPLSSLTP CHHHHHHHCHHHHHH	57.85	-
504	Acetylation	HPFLKLAKPLSSLTP CHHHHHHHCHHHHHH	57.85	-
517	Acetylation	TPLILAAKEAMKSNR HHHHHHHHHHHHHCC	40.16	22826441

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
20	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PAK2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PAK2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND THR-143, ANDMASS SPECTROMETRY.	17242355 [Abstract]

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