dbPTM

PDLI4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDLI4_MOUSE
UniProt AC	P70271
Protein Name	PDZ and LIM domain protein 4
Gene Name	Pdlim4
Organism	Mus musculus (Mouse).
Sequence Length	330
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, dendritic spine . Early endosome membrane Peripheral membrane protein Cytoplasmic side . Recycling endosome membrane Peripheral membrane protein Cytoplasmic side . Nucleus . Cytoplasm, perinuclear region
Protein Description	Suppresses SRC activation by recognizing and binding to active SRC and facilitating PTPN13-mediated dephosphorylation of SRC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from this protein allowing the initiation of a new SRC inactivation cycle. Involved in reorganization of the actin cytoskeleton (By similarity). In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the affinity of ACTN1 to F-actin (filamentous actin), and promotes formation of actin stress fibers. Involved in regulation of the synaptic AMPA receptor transport in dendritic spines of hippocampal pyramidal neurons directing the receptors toward an insertion at the postsynaptic membrane. Links endosomal surface-internalized GRIA1-containing AMPA receptors to the alpha-actinin/actin cytoskeleton. Increases AMPA receptor-mediated excitatory postsynaptic currents in neurons (By similarity)..
Protein Sequence	MTHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSVSRPENKNWPSAPDDKAQAHRIHIDPESQDCSPATSRRSSVSGISLEDNRSGLGSPYGQPPRLPVPHNGSSNEATLPAQMSALHVSPPTSADTARVLPRNRDCRVDLGSEVYRMLREPAEPTASEPKQSGSFRYLQGMLEAGEGGDRPGSGGPRNLKPAASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCENHAKARVKPPEGYDVVAVYPNAKVELV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTHSVTLRG ------CCEEEEECC	23.90	26643407
4	Phosphorylation	----MTHSVTLRGPS ----CCEEEEECCCC	13.97	24719451
6	Phosphorylation	--MTHSVTLRGPSPW --CCEEEEECCCCCC	17.47	26643407
11	Phosphorylation	SVTLRGPSPWGFRLV EEEECCCCCCCEEEE	35.79	24899341
107	Phosphorylation	RIHIDPESQDCSPAT EEECCCCCCCCCCCC	36.39	27087446
111	Phosphorylation	DPESQDCSPATSRRS CCCCCCCCCCCCCCC	26.34	25521595
114	Phosphorylation	SQDCSPATSRRSSVS CCCCCCCCCCCCCCC	26.59	27742792
115	Phosphorylation	QDCSPATSRRSSVSG CCCCCCCCCCCCCCC	28.01	25521595
118	Phosphorylation	SPATSRRSSVSGISL CCCCCCCCCCCCEEC	33.70	25521595
119	Phosphorylation	PATSRRSSVSGISLE CCCCCCCCCCCEECC	20.63	25521595
121	Phosphorylation	TSRRSSVSGISLEDN CCCCCCCCCEECCCC	32.15	24925903
124	Phosphorylation	RSSVSGISLEDNRSG CCCCCCEECCCCCCC	29.27	24925903
130	Phosphorylation	ISLEDNRSGLGSPYG EECCCCCCCCCCCCC	44.62	27180971
134	Phosphorylation	DNRSGLGSPYGQPPR CCCCCCCCCCCCCCC	21.71	27180971
136	Phosphorylation	RSGLGSPYGQPPRLP CCCCCCCCCCCCCCC	30.04	29472430
160	Phosphorylation	ATLPAQMSALHVSPP CCCCCCHHCCCCCCC	18.65	26643407
165	Phosphorylation	QMSALHVSPPTSADT CHHCCCCCCCCCCCH	17.89	26643407
168	Phosphorylation	ALHVSPPTSADTARV CCCCCCCCCCCHHCC	39.67	26643407
169	Phosphorylation	LHVSPPTSADTARVL CCCCCCCCCCHHCCC	29.89	26643407
172	Phosphorylation	SPPTSADTARVLPRN CCCCCCCHHCCCCCC	18.97	26643407
191	Phosphorylation	VDLGSEVYRMLREPA CCCCHHHHHHHCCCC	6.05	22817900
229	Phosphorylation	EGGDRPGSGGPRNLK CCCCCCCCCCCCCCH	43.17	24899341
265	Phosphorylation	CGHGIVGTIVKARDK CCCCCHHHHEECCCC	16.23	24719451
316	Phosphorylation	RVKPPEGYDVVAVYP CCCCCCCCCEEEECC	12.14	-

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
119	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
119	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDLI4_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 PDLI4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SSBP3_MOUSE	Ssbp3	physical	20211142
ZBTB9_MOUSE	Zbtb9	physical	20211142

Drug and Disease Associations

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

Regulatory Network of PDLI4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-111 AND SER-119, ANDMASS SPECTROMETRY.	19367708 [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-111; SER-118; SER-119AND SER-124, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASSSPECTROMETRY.	16452087 [Abstract]