dbPTM

PAXI_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAXI_RAT
UniProt AC	Q66H76
Protein Name	Paxillin
Gene Name	Pxn
Organism	Rattus norvegicus (Rat).
Sequence Length	586
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	MDDLDALLADLESTTSHISKRPVFLSEEPPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVLDPLDQWQPSGSRYAHQQPPSPSPIYSSSTKNSSASNPQDSVGSLCSRAGEEEHVYSFPNKQKSAEPSPTVMSSSLGSNLSELDRLLLELNAVQRSPSGFSAGMVSVQASREPLGSWGTEGRAIILSPFFQDEAESSPPLPGALSPLYGVPESNNLLGGKAGPLMKEKPKRNGGRGLEDVRPSVESLLDELENSVPSPVPAITVNQGEMSSPQRVTSSQQQTRISASSATRELDELMASLSDFKFMAQGKTGSSSPPGGLSKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHSLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQSCFLKLFC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDLDALL -------CCHHHHHH	9.03	-
31	Phosphorylation	FLSEEPPYSYPTGNH ECCCCCCCCCCCCCC	31.39	17395594
76	Phosphorylation	WQPSGSRYAHQQPPS CCCCCCCCCCCCCCC	15.33	27097102
83	Phosphorylation	YAHQQPPSPSPIYSS CCCCCCCCCCCCCCC	44.70	23712012
85	Phosphorylation	HQQPPSPSPIYSSST CCCCCCCCCCCCCCC	28.41	27097102
88	Phosphorylation	PPSPSPIYSSSTKNS CCCCCCCCCCCCCCC	13.09	27097102
89	Phosphorylation	PSPSPIYSSSTKNSS CCCCCCCCCCCCCCC	20.66	27097102
90	Phosphorylation	SPSPIYSSSTKNSSA CCCCCCCCCCCCCCC	25.67	27097102
91	Phosphorylation	PSPIYSSSTKNSSAS CCCCCCCCCCCCCCC	37.14	27097102
92	Phosphorylation	SPIYSSSTKNSSASN CCCCCCCCCCCCCCC	35.87	27097102
95	Phosphorylation	YSSSTKNSSASNPQD CCCCCCCCCCCCCCC	28.92	25575281
96	Phosphorylation	SSSTKNSSASNPQDS CCCCCCCCCCCCCCC	45.14	22108457
98	Phosphorylation	STKNSSASNPQDSVG CCCCCCCCCCCCCHH	51.49	22108457
103	Phosphorylation	SASNPQDSVGSLCSR CCCCCCCCHHHHHHH	24.11	25575281
106	Phosphorylation	NPQDSVGSLCSRAGE CCCCCHHHHHHHHCC	24.85	27097102
109	Phosphorylation	DSVGSLCSRAGEEEH CCHHHHHHHHCCCCC	30.38	16641100
118	Phosphorylation	AGEEEHVYSFPNKQK HCCCCCEEECCCCCC	13.40	15308668
119	Phosphorylation	GEEEHVYSFPNKQKS CCCCCEEECCCCCCC	32.89	27097102
126	Phosphorylation	SFPNKQKSAEPSPTV ECCCCCCCCCCCCCC	35.06	29779826
130	Phosphorylation	KQKSAEPSPTVMSSS CCCCCCCCCCCCCCC	25.38	23712012
132	Phosphorylation	KSAEPSPTVMSSSLG CCCCCCCCCCCCCCC	32.93	29779826
135	Phosphorylation	EPSPTVMSSSLGSNL CCCCCCCCCCCCCCH	16.67	27097102
136	Phosphorylation	PSPTVMSSSLGSNLS CCCCCCCCCCCCCHH	16.10	27097102
137	Phosphorylation	SPTVMSSSLGSNLSE CCCCCCCCCCCCHHH	29.46	21738781
140	Phosphorylation	VMSSSLGSNLSELDR CCCCCCCCCHHHHHH	39.63	27097102
143	Phosphorylation	SSLGSNLSELDRLLL CCCCCCHHHHHHHHH	40.12	27097102
207	Phosphorylation	PPLPGALSPLYGVPE CCCCCCCCCCCCCCC	16.60	28689409
210	Phosphorylation	PGALSPLYGVPESNN CCCCCCCCCCCCCCC	21.33	-
256	Phosphorylation	LLDELENSVPSPVPA HHHHHHHCCCCCCCC	26.48	22673903
259	Phosphorylation	ELENSVPSPVPAITV HHHHCCCCCCCCEEE	36.05	22673903
272	Phosphorylation	TVNQGEMSSPQRVTS EECCCCCCCCCCCCC	34.27	22673903
273	Phosphorylation	VNQGEMSSPQRVTSS ECCCCCCCCCCCCCH	24.60	22673903
278	Phosphorylation	MSSPQRVTSSQQQTR CCCCCCCCCHHHHHH	25.50	23984901
279	Phosphorylation	SSPQRVTSSQQQTRI CCCCCCCCHHHHHHH	24.24	23984901
280	Phosphorylation	SPQRVTSSQQQTRIS CCCCCCCHHHHHHHC	23.73	23984901
284	Phosphorylation	VTSSQQQTRISASSA CCCHHHHHHHCCHHH	26.15	23984901
287	Phosphorylation	SQQQTRISASSATRE HHHHHHHCCHHHHHH	20.86	29779826
289	Phosphorylation	QQTRISASSATRELD HHHHHCCHHHHHHHH	17.45	25403869
290	Phosphorylation	QTRISASSATRELDE HHHHCCHHHHHHHHH	33.12	25403869
292	Phosphorylation	RISASSATRELDELM HHCCHHHHHHHHHHH	26.99	25403869
301	Phosphorylation	ELDELMASLSDFKFM HHHHHHHHHCHHHHH	17.91	23984901
303	Phosphorylation	DELMASLSDFKFMAQ HHHHHHHCHHHHHHC	38.21	30181290
313	Phosphorylation	KFMAQGKTGSSSPPG HHHHCCCCCCCCCCC	49.47	21738781
315	Phosphorylation	MAQGKTGSSSPPGGL HHCCCCCCCCCCCCC	32.64	27097102
316	Phosphorylation	AQGKTGSSSPPGGLS HCCCCCCCCCCCCCC	48.48	27097102
317	Phosphorylation	QGKTGSSSPPGGLSK CCCCCCCCCCCCCCC	36.49	23712012
323	Phosphorylation	SSPPGGLSKPGSQLD CCCCCCCCCCHHHHH	39.83	27097102
327	Phosphorylation	GGLSKPGSQLDSMLG CCCCCCHHHHHHHHH	35.78	27097102
331	Phosphorylation	KPGSQLDSMLGSLQS CCHHHHHHHHHHHHH	25.21	27097102
335	Phosphorylation	QLDSMLGSLQSDLNK HHHHHHHHHHHHHHH	21.19	27097102
338	Phosphorylation	SMLGSLQSDLNKLGV HHHHHHHHHHHHHCH	49.73	16641100
528	Phosphorylation	HYHERRGSLCSGCQK EEECCCCCCCCCCCC	25.13	23984901
531	Phosphorylation	ERRGSLCSGCQKPIT CCCCCCCCCCCCCCC	48.15	25575281

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	PTK2	Q05397	GPS
31	Y	Phosphorylation	Kinase	PTK2B	P70600	GPS
31	Y	Phosphorylation	Kinase	PTK6	-	Uniprot
83	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
118	Y	Phosphorylation	Kinase	PTK2B	P70600	GPS
118	Y	Phosphorylation	Kinase	PTK6	-	Uniprot
126	S	Phosphorylation	Kinase	GSK3A	P18265	PSP
126	S	Phosphorylation	Kinase	GSK3B	P18266	PSP
130	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
130	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
273	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Rnf5	Q5M807	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
273	S	Phosphorylation	-
Phosphorylation at Ser-273 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation (By similarity).
279	S	Phosphorylation	-
Phosphorylation at Ser-279 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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ILK_RAT	Ilk	physical	11304546

Drug and Disease Associations

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

Regulatory Network of PAXI_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 SER-106 AND SER-109, ANDMASS SPECTROMETRY.	16641100 [Abstract]

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