dbPTM

PAXI_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAXI_MOUSE
UniProt AC	Q8VI36
Protein Name	Paxillin
Gene Name	Pxn
Organism	Mus musculus (Mouse).
Sequence Length	591
Subcellular Localization	Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Cytoplasm, cell cortex . Colocalizes with integrins at the cell periphery. Colocalizes with PXN to membrane ruffles and the leading edge of migrating cells (By similarity).
Protein Description	Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion)..
Protein Sequence	MDDLDALLADLESTTSHISKRPVFLSEEPPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVLDPLDQWQPSGSRYAHQQPPSPLPVYSSSAKNSSASNTQDGVGSLCSRAGEEEHVYSFPNKQKSAEPSPTVMSSSLGSNLSELDRLLLELNAVQHSPPGFPADEAESSPPLPGALSPLYGIPENNTPLGGKAGPLVKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSSQQQTRISASSATRELDELMASLSDFKMQGLEQRVDGERPWAAGWPPSSRQSSPEGQDEGGFMAQGKTGSSSPPGGLSKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHSLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQSCFVKLFC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDLDALL -------CCHHHHHH	9.03	-
26	Phosphorylation	SKRPVFLSEEPPYSY HCCCEECCCCCCCCC	28.57	-
31	Phosphorylation	FLSEEPPYSYPTGNH ECCCCCCCCCCCCCC	31.39	20442405
32	Phosphorylation	LSEEPPYSYPTGNHT CCCCCCCCCCCCCCC	30.34	-
33	Phosphorylation	SEEPPYSYPTGNHTY CCCCCCCCCCCCCCE	10.04	22817900
39	Phosphorylation	SYPTGNHTYQEIAVP CCCCCCCCEEEEECC	30.79	-
40	Phosphorylation	YPTGNHTYQEIAVPP CCCCCCCEEEEECCC	9.15	22817900
76	Phosphorylation	WQPSGSRYAHQQPPS CCCCCCCCCCCCCCC	15.33	27087446
83	Phosphorylation	YAHQQPPSPLPVYSS CCCCCCCCCCCCCCC	45.83	27087446
88	Phosphorylation	PPSPLPVYSSSAKNS CCCCCCCCCCCCCCC	10.82	27742792
89	Phosphorylation	PSPLPVYSSSAKNSS CCCCCCCCCCCCCCC	20.32	25619855
90	Phosphorylation	SPLPVYSSSAKNSSA CCCCCCCCCCCCCCC	19.34	25619855
91	Phosphorylation	PLPVYSSSAKNSSAS CCCCCCCCCCCCCCC	37.00	25619855
95	Phosphorylation	YSSSAKNSSASNTQD CCCCCCCCCCCCCCC	26.95	27357545
96	Phosphorylation	SSSAKNSSASNTQDG CCCCCCCCCCCCCCC	45.14	28973931
106	Phosphorylation	NTQDGVGSLCSRAGE CCCCCHHHHHHHHCC	24.64	28973931
109	Phosphorylation	DGVGSLCSRAGEEEH CCHHHHHHHHCCCCC	30.38	20469934
118	Phosphorylation	AGEEEHVYSFPNKQK HCCCCCEEECCCCCC	13.40	27087446
119	Phosphorylation	GEEEHVYSFPNKQKS CCCCCEEECCCCCCC	32.89	26824392
125	Ubiquitination	YSFPNKQKSAEPSPT EECCCCCCCCCCCCC	53.92	-
126	Phosphorylation	SFPNKQKSAEPSPTV ECCCCCCCCCCCCCC	35.06	27087446
130	Phosphorylation	KQKSAEPSPTVMSSS CCCCCCCCCCCCCCC	25.38	27087446
132	Phosphorylation	KSAEPSPTVMSSSLG CCCCCCCCCCCCCCC	32.93	27087446
135	Phosphorylation	EPSPTVMSSSLGSNL CCCCCCCCCCCCCCH	16.67	27742792
136	Phosphorylation	PSPTVMSSSLGSNLS CCCCCCCCCCCCCHH	16.10	25521595
137	Phosphorylation	SPTVMSSSLGSNLSE CCCCCCCCCCCCHHH	29.46	25521595
140	Phosphorylation	VMSSSLGSNLSELDR CCCCCCCCCHHHHHH	39.63	27742792
143	Phosphorylation	SSLGSNLSELDRLLL CCCCCCHHHHHHHHH	40.12	25521595
158	Phosphorylation	ELNAVQHSPPGFPAD HHHCCCCCCCCCCCC	18.72	26239621
169	Phosphorylation	FPADEAESSPPLPGA CCCCCCCCCCCCCCC	56.01	26239621
170	Phosphorylation	PADEAESSPPLPGAL CCCCCCCCCCCCCCC	23.26	26239621
178	Phosphorylation	PPLPGALSPLYGIPE CCCCCCCCCCCCCCC	16.60	26239621
181	Phosphorylation	PGALSPLYGIPENNT CCCCCCCCCCCCCCC	19.18	26239621
216	Phosphorylation	GLEDVRPSVESLLDE CHHHHCHHHHHHHHH	28.14	26239621
219	Phosphorylation	DVRPSVESLLDELES HHCHHHHHHHHHHHH	31.88	26239621
226	Phosphorylation	SLLDELESSVPSPVP HHHHHHHHCCCCCCC	49.62	26239621
227	Phosphorylation	LLDELESSVPSPVPA HHHHHHHCCCCCCCE	28.77	26239621
230	Phosphorylation	ELESSVPSPVPAITV HHHHCCCCCCCEEEE	36.05	26239621
236	Phosphorylation	PSPVPAITVNQGEMS CCCCCEEEECCCCCC	18.60	26239621
243	Phosphorylation	TVNQGEMSSPQRVTS EECCCCCCCCCCCCC	34.27	26239621
244	Phosphorylation	VNQGEMSSPQRVTSS ECCCCCCCCCCCCCH	24.60	26239621
249	Phosphorylation	MSSPQRVTSSQQQTR CCCCCCCCCHHHHHH	25.50	26643407
250	Phosphorylation	SSPQRVTSSQQQTRI CCCCCCCCHHHHHHH	24.24	26824392
251	Phosphorylation	SPQRVTSSQQQTRIS CCCCCCCHHHHHHHC	23.73	24899341
255	Phosphorylation	VTSSQQQTRISASSA CCCHHHHHHHCCHHH	26.15	26239621
258	Phosphorylation	SQQQTRISASSATRE HHHHHHHCCHHHHHH	20.86	27087446
260	Phosphorylation	QQTRISASSATRELD HHHHHCCHHHHHHHH	17.45	27087446
261	Phosphorylation	QTRISASSATRELDE HHHHCCHHHHHHHHH	33.12	27087446
263	Phosphorylation	RISASSATRELDELM HHCCHHHHHHHHHHH	26.99	26239621
272	Phosphorylation	ELDELMASLSDFKMQ HHHHHHHHHHHHHHC	17.91	26824392
272 (in isoform 2)	Phosphorylation	-	17.91	29514104
274	Phosphorylation	DELMASLSDFKMQGL HHHHHHHHHHHHCCH	38.21	28066266
288 (in isoform 2)	Phosphorylation	-	51.62	29514104
302	Phosphorylation	WPPSSRQSSPEGQDE CCCCCCCCCCCCCCC	46.91	23737553
303	Phosphorylation	PPSSRQSSPEGQDEG CCCCCCCCCCCCCCC	20.73	25521595
318	Phosphorylation	GFMAQGKTGSSSPPG CCCCCCCCCCCCCCC	49.47	27087446
320	Phosphorylation	MAQGKTGSSSPPGGL CCCCCCCCCCCCCCC	32.64	21082442
321	Phosphorylation	AQGKTGSSSPPGGLS CCCCCCCCCCCCCCC	48.48	22942356
322	Phosphorylation	QGKTGSSSPPGGLSK CCCCCCCCCCCCCCC	36.49	27087446
328	Phosphorylation	SSPPGGLSKPGSQLD CCCCCCCCCCHHHHH	39.83	22942356
332	Phosphorylation	GGLSKPGSQLDSMLG CCCCCCHHHHHHHHH	35.78	22942356
336	Phosphorylation	KPGSQLDSMLGSLQS CCHHHHHHHHHHHHH	25.21	22942356
340	Phosphorylation	QLDSMLGSLQSDLNK HHHHHHHHHHHHHHH	21.19	26824392
343	Phosphorylation	SMLGSLQSDLNKLGV HHHHHHHHHHHHHCH	49.73	25619855
363	Ubiquitination	GVCGACKKPIAGQVV CCCCCCCCCCCCCEE	41.35	-
371	Phosphorylation	PIAGQVVTAMGKTWH CCCCCEEECCCCCCC	16.45	25367039
376	Phosphorylation	VVTAMGKTWHPEHFV EEECCCCCCCCHHCE	24.23	25367039
385	Phosphorylation	HPEHFVCTHCQEEIG CCHHCEECCCCHHHC	22.00	25367039
393	Phosphorylation	HCQEEIGSRNFFERD CCCHHHCCCCCCCCC	29.70	25367039
407	Ubiquitination	DGQPYCEKDYHSLFS CCCCCCCCCHHHCCC	61.09	-
409	Phosphorylation	QPYCEKDYHSLFSPR CCCCCCCHHHCCCCC	12.36	17242355
414	Phosphorylation	KDYHSLFSPRCYYCN CCHHHCCCCCEEEEC	19.41	23984901
466	Ubiquitination	DGKAYCRKDYFDMFA CCCEEECHHHHHHCC	53.90	-
468	Phosphorylation	KAYCRKDYFDMFAPK CEEECHHHHHHCCCC	12.43	19060867
533	Phosphorylation	HYHERRGSLCSGCQK EEECCCCCCCCCCCC	25.13	28507225
535	Glutathionylation	HERRGSLCSGCQKPI ECCCCCCCCCCCCCC	3.35	24333276
538	Glutathionylation	RGSLCSGCQKPITGR CCCCCCCCCCCCCHH	2.43	24333276
540	Ubiquitination	SLCSGCQKPITGRCI CCCCCCCCCCCHHHH	42.33	-
543	Phosphorylation	SGCQKPITGRCITAM CCCCCCCCHHHHHHH	27.40	25266776
572	Phosphorylation	LKQLNKGTFKEQNDK HHHHCCCCCCCCCCC	32.89	20388733

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
31	Y	Phosphorylation	Kinase	PTK2B	Q9QVP9	GPS
31	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
31	Y	Phosphorylation	Kinase	SRC	P05480	PSP
83	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
83	S	Phosphorylation	Kinase	ERK-SUBFAMILY	-	GPS
118	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
118	Y	Phosphorylation	Kinase	SRC	P05480	PSP
126	S	Phosphorylation	Kinase	GSK3A	Q2NL51	PSP
130	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
244	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
250	S	Phosphorylation	Kinase	SLK	Q9H2G2	PSP
250	S	Phosphorylation	Kinase	SLK	O54988	PSP
572	T	Phosphorylation	Kinase	PRKCD	P28867	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Rnf5	O35445	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
244	S	Phosphorylation	-
Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation (By similarity).
250	S	Phosphorylation	-
Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (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 PAXI_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABL1_MOUSE	Abl1	physical	9603926
GIT1_MOUSE	Git1	physical	12153727
ARHG7_MOUSE	Arhgef7	physical	12153727
CBL_MOUSE	Cbl	physical	8641358
MK01_MOUSE	Mapk1	physical	14636584
SRC_MOUSE	Src	physical	14636584
LIMK1_MOUSE	Limk1	physical	15023529
CRK_MOUSE	Crk	physical	14636584
MP2K1_MOUSE	Map2k1	physical	14636584
RAF1_MOUSE	Raf1	physical	14636584

Drug and Disease Associations

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

Regulatory Network of PAXI_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-83; TYR-88 AND TYR-118,AND MASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.	19367708 [Abstract]

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