PAXI_CHICK - dbPTM
PAXI_CHICK - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAXI_CHICK
UniProt AC P49024
Protein Name Paxillin
Gene Name PXN
Organism Gallus gallus (Chicken).
Sequence Length 559
Subcellular Localization Cytoplasm, cytoskeleton. Cell junction, focal adhesion.
Protein Description Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Binds in vitro to vinculin as well as to the SH3 domain of c-SRC and, when tyrosine phosphorylated, to the SH2 domain of v-CRK..
Protein Sequence MDDLDALLADLESTTSHISKRPVFLTEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVIDPLDQWQPSVSRYGHQQPQSQSPIYSSSAKSSSASVPRDGLSSPSPRASEEEHVYSFPNKQKSAEPSPTMTSTSLGSNLSELDRLLLELNAVQHNPPSGFSADEVSRSPSLPNVTGPHYVIPESSSSAGGKAAPPTKEKPKRNGGRGIEDVRPSVESLLDELESSVPSPVPAITVSQGEVSSPQRVNASQQQTRISASSATRELDELMASLSDFKFMAQGKAGGSSSPPSTTPKPGSQLDTMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGVFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFINGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC
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
29PhosphorylationPVFLTEETPYSYPTG
CEEECCCCCCCCCCC
22.69-
31PhosphorylationFLTEETPYSYPTGNH
EECCCCCCCCCCCCC
28.40-
40PhosphorylationYPTGNHTYQEIAVPP
CCCCCCEEEEEECCC
9.15-
76PhosphorylationWQPSVSRYGHQQPQS
CCCCHHHCCCCCCCC
16.08-
83PhosphorylationYGHQQPQSQSPIYSS
CCCCCCCCCCCCCCC
39.03-
85PhosphorylationHQQPQSQSPIYSSSA
CCCCCCCCCCCCCCC
20.6423106611
88PhosphorylationPQSQSPIYSSSAKSS
CCCCCCCCCCCCCCC
13.09-
89PhosphorylationQSQSPIYSSSAKSSS
CCCCCCCCCCCCCCC
20.66-
90PhosphorylationSQSPIYSSSAKSSSA
CCCCCCCCCCCCCCC
19.83-
91PhosphorylationQSPIYSSSAKSSSAS
CCCCCCCCCCCCCCC
33.50-
94PhosphorylationIYSSSAKSSSASVPR
CCCCCCCCCCCCCCC
29.28-
95PhosphorylationYSSSAKSSSASVPRD
CCCCCCCCCCCCCCC
29.26-
96PhosphorylationSSSAKSSSASVPRDG
CCCCCCCCCCCCCCC
31.49-
98PhosphorylationSAKSSSASVPRDGLS
CCCCCCCCCCCCCCC
34.30-
106PhosphorylationVPRDGLSSPSPRASE
CCCCCCCCCCCCCCC
34.14-
108PhosphorylationRDGLSSPSPRASEEE
CCCCCCCCCCCCCCC
29.03-
112PhosphorylationSSPSPRASEEEHVYS
CCCCCCCCCCCCCCC
46.98-
118PhosphorylationASEEEHVYSFPNKQK
CCCCCCCCCCCCCCC
13.4023106611
119PhosphorylationSEEEHVYSFPNKQKS
CCCCCCCCCCCCCCC
32.8923106611
126PhosphorylationSFPNKQKSAEPSPTM
CCCCCCCCCCCCCCC
35.0623106611
130PhosphorylationKQKSAEPSPTMTSTS
CCCCCCCCCCCCCCC
25.2223106611
132PhosphorylationKSAEPSPTMTSTSLG
CCCCCCCCCCCCCCC
37.1023106611
134PhosphorylationAEPSPTMTSTSLGSN
CCCCCCCCCCCCCCC
31.1923106611
135PhosphorylationEPSPTMTSTSLGSNL
CCCCCCCCCCCCCCH
12.7423106611
137PhosphorylationSPTMTSTSLGSNLSE
CCCCCCCCCCCCHHH
30.42-
143PhosphorylationTSLGSNLSELDRLLL
CCCCCCHHHHHHHHH
40.12-
164PhosphorylationHNPPSGFSADEVSRS
CCCCCCCCHHHHHCC
38.03-
171PhosphorylationSADEVSRSPSLPNVT
CHHHHHCCCCCCCCC
16.0123106611
173PhosphorylationDEVSRSPSLPNVTGP
HHHHCCCCCCCCCCC
58.6723106611
182PhosphorylationPNVTGPHYVIPESSS
CCCCCCCEECCCCCC
11.83-
187PhosphorylationPHYVIPESSSSAGGK
CCEECCCCCCCCCCC
30.11-
188PhosphorylationHYVIPESSSSAGGKA
CEECCCCCCCCCCCC
27.01-
189PhosphorylationYVIPESSSSAGGKAA
EECCCCCCCCCCCCC
33.22-
190PhosphorylationVIPESSSSAGGKAAP
ECCCCCCCCCCCCCC
32.64-
199PhosphorylationGGKAAPPTKEKPKRN
CCCCCCCCCCCCCCC
51.26-
217PhosphorylationGIEDVRPSVESLLDE
CHHHHCHHHHHHHHH
28.14-
220PhosphorylationDVRPSVESLLDELES
HHCHHHHHHHHHHHH
31.88-
227PhosphorylationSLLDELESSVPSPVP
HHHHHHHHCCCCCCC
49.62-
228PhosphorylationLLDELESSVPSPVPA
HHHHHHHCCCCCCCE
28.77-
231PhosphorylationELESSVPSPVPAITV
HHHHCCCCCCCEEEE
36.05-
239PhosphorylationPVPAITVSQGEVSSP
CCCEEEEECCCCCCC
24.66-
245PhosphorylationVSQGEVSSPQRVNAS
EECCCCCCCCCCCHH
30.17-
259PhosphorylationSQQQTRISASSATRE
HHHHHHHCCHHHHHH
20.8623106611
262PhosphorylationQTRISASSATRELDE
HHHHCCHHHHHHHHH
33.12-
273PhosphorylationELDELMASLSDFKFM
HHHHHHHHHCCCCHH
17.91-
275PhosphorylationDELMASLSDFKFMAQ
HHHHHHHCCCCHHHC
38.21-
288PhosphorylationAQGKAGGSSSPPSTT
HCCCCCCCCCCCCCC
27.0723106611
289PhosphorylationQGKAGGSSSPPSTTP
CCCCCCCCCCCCCCC
50.5723106611
290PhosphorylationGKAGGSSSPPSTTPK
CCCCCCCCCCCCCCC
42.3923106611
295PhosphorylationSSSPPSTTPKPGSQL
CCCCCCCCCCCCCHH
33.38-
308PhosphorylationQLDTMLGSLQSDLNK
HHHHHHHHHHHHHHH
21.19-
344PhosphorylationVVTAMGKTWHPEHFV
EEECCCCCCCCHHCE
24.23-
361PhosphorylationHCQEEIGSRNFFERD
CCCHHHCCCCCCCCC
29.70-
377PhosphorylationQPYCEKDYHNLFSPR
CCCCCCCCHHCCCCC
12.04-
382PhosphorylationKDYHNLFSPRCYYCN
CCCHHCCCCCEEEEC
18.01-
398PhosphorylationPILDKVVTALDRTWH
HHHHHHHHHHHHCCC
25.21-
403PhosphorylationVVTALDRTWHPEHFF
HHHHHHHCCCHHHEE
28.00-
436PhosphorylationKAYCRKDYFDMFAPK
CEEECHHHHHHCCCC
12.43-
457PhosphorylationAILENYISALNTLWH
HHHHHHHHHHHHCCC
19.15-
481PhosphorylationFTPFINGSFFEHDGQ
CCCCCCCCCEEECCC
23.44-
501PhosphorylationHYHERRGSLCSGCQK
EEECCCCCCCCCCCC
25.13-
504PhosphorylationERRGSLCSGCQKPIT
CCCCCCCCCCCCCCC
48.15-
540PhosphorylationLKQLNKGTFKEQNDK
HHHHCCCCCCCCCCC
32.89-

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
31YPhosphorylationKinaseSRCP00523
PSP
40YPhosphorylationKinaseSRCP00523
PSP
88YPhosphorylationKinaseSRCP00523
PSP
118YPhosphorylationKinaseFAK1Q00944
Uniprot
118YPhosphorylationKinasePTK2Q05397
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAXI_CHICK !!

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_CHICK !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIRR_CHICKNUDT16L1physical
11805099
VINC_CHICKVCLphysical
7525621
FAK1_CHICKPTK2physical
7525621

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

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Related Literatures of Post-Translational Modification

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