PDLI2_MOUSE - dbPTM
PDLI2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDLI2_MOUSE
UniProt AC Q8R1G6
Protein Name PDZ and LIM domain protein 2
Gene Name Pdlim2
Organism Mus musculus (Mouse).
Sequence Length 349
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Localizes at the cytoskeleton. Colocalizes with beta-1 integrin (ITGB1) and alpha-actinin but not with paxillin (PXN) (By similarity)..
Protein Description Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity (By similarity)..
Protein Sequence MALTVDVAGPAPWGFRISGGRDFHTPIIVTKVTERGKAEAADLRPGDIIVAINGQSAENMLHAEAQSKIRQSASPLRLQLDRSQTASPGQTNGEGSLEVLATRFQGSLRTHRDSQSSQRSACFSPVSLSPRPCSPFSTPPPTSPVALSKEDMIGCSFQSLTHSPGLAAAHHLTYPGHPTSQQAGHSSPSDSAVRVLLHSPGRPSSPRFSSLDLEEDSEVFKMLQENRQGRAAPRQSSSFRLLQEALEAEERGGTPAFVPSSLSSQASLPTSRALATPPKLHTCEKCSVNISNQAVRIQEGRYRHPGCYTCADCGLNLKMRGHFWVGNELYCEKHARQRYSMPGTLNSRA
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
72PhosphorylationAQSKIRQSASPLRLQ
HHHHHHHCCCCCEEE		22.3623984901
74PhosphorylationSKIRQSASPLRLQLD
HHHHHCCCCCEEEEE		29.7026060331
83PhosphorylationLRLQLDRSQTASPGQ
CEEEEECCCCCCCCC		31.3926239621
85PhosphorylationLQLDRSQTASPGQTN
EEEECCCCCCCCCCC		30.2827566939
87PhosphorylationLDRSQTASPGQTNGE
EECCCCCCCCCCCCC		32.7126824392
91PhosphorylationQTASPGQTNGEGSLE
CCCCCCCCCCCCHHH		51.6225266776
96PhosphorylationGQTNGEGSLEVLATR
CCCCCCCHHHHHHEE		19.6325266776
102PhosphorylationGSLEVLATRFQGSLR
CHHHHHHEEEHHHCC		28.0530635358
107PhosphorylationLATRFQGSLRTHRDS
HHEEEHHHCCCCCCC		12.1424453211
110PhosphorylationRFQGSLRTHRDSQSS
EEHHHCCCCCCCCCC		26.9328576409
114PhosphorylationSLRTHRDSQSSQRSA
HCCCCCCCCCCCCEE		31.7319367708
116PhosphorylationRTHRDSQSSQRSACF
CCCCCCCCCCCEECC		32.1825266776
120PhosphorylationDSQSSQRSACFSPVS
CCCCCCCEECCCCCC		23.0426745281
124PhosphorylationSQRSACFSPVSLSPR
CCCEECCCCCCCCCC		25.0321082442
127PhosphorylationSACFSPVSLSPRPCS
EECCCCCCCCCCCCC		26.8921082442
129PhosphorylationCFSPVSLSPRPCSPF
CCCCCCCCCCCCCCC		16.0321082442
134PhosphorylationSLSPRPCSPFSTPPP
CCCCCCCCCCCCCCC		31.4921082442
137PhosphorylationPRPCSPFSTPPPTSP
CCCCCCCCCCCCCCC		43.3121082442
138PhosphorylationRPCSPFSTPPPTSPV
CCCCCCCCCCCCCCC		39.9521082442
142PhosphorylationPFSTPPPTSPVALSK
CCCCCCCCCCCCCCH		51.9821082442
143PhosphorylationFSTPPPTSPVALSKE
CCCCCCCCCCCCCHH		24.1321082442
148PhosphorylationPTSPVALSKEDMIGC
CCCCCCCCHHHHCCC		25.0221082442
156PhosphorylationKEDMIGCSFQSLTHS
HHHHCCCCHHHCCCC		22.5526060331
159PhosphorylationMIGCSFQSLTHSPGL
HCCCCHHHCCCCCCC		32.9726060331
161PhosphorylationGCSFQSLTHSPGLAA
CCCHHHCCCCCCCHH		26.0926060331
163PhosphorylationSFQSLTHSPGLAAAH
CHHHCCCCCCCHHHH		18.5426060331
173PhosphorylationLAAAHHLTYPGHPTS
CHHHHCCCCCCCCCH		24.2626060331
174PhosphorylationAAAHHLTYPGHPTSQ
HHHHCCCCCCCCCHH		17.3626060331
179PhosphorylationLTYPGHPTSQQAGHS
CCCCCCCCHHCCCCC		33.2325338131
180PhosphorylationTYPGHPTSQQAGHSS
CCCCCCCHHCCCCCC		25.4226060331
186PhosphorylationTSQQAGHSSPSDSAV
CHHCCCCCCCCCCHH		42.9226060331
187PhosphorylationSQQAGHSSPSDSAVR
HHCCCCCCCCCCHHH		23.8121183079
189PhosphorylationQAGHSSPSDSAVRVL
CCCCCCCCCCHHHHH		46.2626060331
191PhosphorylationGHSSPSDSAVRVLLH
CCCCCCCCHHHHHHC		32.7626060331
199PhosphorylationAVRVLLHSPGRPSSP
HHHHHHCCCCCCCCC		29.0827087446
204PhosphorylationLHSPGRPSSPRFSSL
HCCCCCCCCCCCCCC		52.1726824392
205PhosphorylationHSPGRPSSPRFSSLD
CCCCCCCCCCCCCCC		23.8327087446
209PhosphorylationRPSSPRFSSLDLEED
CCCCCCCCCCCHHHC		31.1321082442
210PhosphorylationPSSPRFSSLDLEEDS
CCCCCCCCCCHHHCH		24.1626824392
236PhosphorylationGRAAPRQSSSFRLLQ
CCCCCCCCHHHHHHH		29.2721183079
237PhosphorylationRAAPRQSSSFRLLQE
CCCCCCCHHHHHHHH		25.7623984901
238PhosphorylationAAPRQSSSFRLLQEA
CCCCCCHHHHHHHHH		21.4521183079
254PhosphorylationEAEERGGTPAFVPSS
HHHHCCCCCCCCCCC		17.8026239621
263PhosphorylationAFVPSSLSSQASLPT
CCCCCCCCCCCCCCC		23.50-
267PhosphorylationSSLSSQASLPTSRAL
CCCCCCCCCCCCCCC		27.5225266776
270PhosphorylationSSQASLPTSRALATP
CCCCCCCCCCCCCCC		35.8229176673
271PhosphorylationSQASLPTSRALATPP
CCCCCCCCCCCCCCC		17.3929176673
276PhosphorylationPTSRALATPPKLHTC
CCCCCCCCCCCCCCC		40.7626824392
331GlutathionylationWVGNELYCEKHARQR
EECCEEEEHHHHHHH		9.8024333276
344PhosphorylationQRYSMPGTLNSRA--
HHCCCCCCCCCCC--		19.5229514104
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
137SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDLI2_MOUSE !!
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 PDLI2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
17468759
UB2D1_MOUSEUbe2d1physical
20889505
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDLI2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-199 AND SER-205, ANDMASS SPECTROMETRY.
"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-199, AND MASSSPECTROMETRY.

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