dbPTM

PDLI4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDLI4_HUMAN
UniProt AC	P50479
Protein Name	PDZ and LIM domain protein 4
Gene Name	PDLIM4
Organism	Homo sapiens (Human).
Sequence Length	330
Subcellular Localization	Isoform 1: Cytoplasm, cytoskeleton . Nucleus . Cytoplasm . Cytoplasm, perinuclear region . Cell projection, lamellipodium . Cell projection, dendritic spine . Early endosome membrane Peripheral membrane protein Cytoplasmic side . Recycling endosome me
Protein Description	Isoform 1: 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. [PubMed: 19307596 Involved in reorganization of the actin cytoskeleton]
Protein Sequence	MPHSVTLRGPSPWGFRLVGGRDFSAPLTISRVHAGSKAALAALCPGDLIQAINGESTELMTHLEAQNRIKGCHDHLTLSVSRPEGRSWPSAPDDSKAQAHRIHIDPEIQDGSPTTSRRPSGTGTGPEDGRPSLGSPYGQPPRFPVPHNGSSEATLPAQMSTLHVSPPPSADPARGLPRSRDCRVDLGSEVYRMLREPAEPVAAEPKQSGSFRYLQGMLEAGEGGDWPGPGGPRNLKPTASKLGAPLSGLQGLPECTRCGHGIVGTIVKARDKLYHPECFMCSDCGLNLKQRGYFFLDERLYCESHAKARVKPPEGYDVVAVYPNAKVELV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPHSVTLRGPS ----CCCCEEECCCC	15.78	29514088
6	Phosphorylation	--MPHSVTLRGPSPW --CCCCEEECCCCCC	17.47	24719451
8	Methylation	MPHSVTLRGPSPWGF CCCCEEECCCCCCCE	45.68	83108549
11	Phosphorylation	SVTLRGPSPWGFRLV CEEECCCCCCCEEEE	35.79	22617229
21	Methylation	GFRLVGGRDFSAPLT CEEEECCCCCCCCEE	35.55	115491241
36	Phosphorylation	ISRVHAGSKAALAAL EEEECCCCHHHHHHH	21.65	-
79	Phosphorylation	CHDHLTLSVSRPEGR CCCCEEEEEECCCCC	16.89	24719451
81	Phosphorylation	DHLTLSVSRPEGRSW CCEEEEEECCCCCCC	38.45	24719451
87	Phosphorylation	VSRPEGRSWPSAPDD EECCCCCCCCCCCCC	54.95	24719451
112	Phosphorylation	DPEIQDGSPTTSRRP CCCCCCCCCCCCCCC	27.62	22617229
114	Phosphorylation	EIQDGSPTTSRRPSG CCCCCCCCCCCCCCC	38.82	23927012
115	Phosphorylation	IQDGSPTTSRRPSGT CCCCCCCCCCCCCCC	24.50	23927012
116	Phosphorylation	QDGSPTTSRRPSGTG CCCCCCCCCCCCCCC	28.86	23927012
120	Phosphorylation	PTTSRRPSGTGTGPE CCCCCCCCCCCCCCC	47.37	30266825
122	Phosphorylation	TSRRPSGTGTGPEDG CCCCCCCCCCCCCCC	35.59	30266825
124	Phosphorylation	RRPSGTGTGPEDGRP CCCCCCCCCCCCCCC	49.77	30266825
132	Phosphorylation	GPEDGRPSLGSPYGQ CCCCCCCCCCCCCCC	43.96	30266825
135	Phosphorylation	DGRPSLGSPYGQPPR CCCCCCCCCCCCCCC	21.90	30266825
137	Phosphorylation	RPSLGSPYGQPPRFP CCCCCCCCCCCCCCC	30.04	30266825
150	Phosphorylation	FPVPHNGSSEATLPA CCCCCCCCCCCCCCC	30.26	23927012
151	Phosphorylation	PVPHNGSSEATLPAQ CCCCCCCCCCCCCCE	32.42	23927012
154	Phosphorylation	HNGSSEATLPAQMST CCCCCCCCCCCEEEE	29.26	23927012
160	Phosphorylation	ATLPAQMSTLHVSPP CCCCCEEEEEECCCC	18.75	23927012
161	Phosphorylation	TLPAQMSTLHVSPPP CCCCEEEEEECCCCC	18.62	26657352
165	Phosphorylation	QMSTLHVSPPPSADP EEEEEECCCCCCCCC	22.42	26657352
169	Phosphorylation	LHVSPPPSADPARGL EECCCCCCCCCCCCC	51.59	23186163
188	Phosphorylation	DCRVDLGSEVYRMLR CCCCCCCHHHHHHHC	31.05	26356563
191	Phosphorylation	VDLGSEVYRMLREPA CCCCHHHHHHHCCCC	6.05	25884760
208	Phosphorylation	VAAEPKQSGSFRYLQ CCCCCCCCCCCHHHH	42.40	26437602
210	Phosphorylation	AEPKQSGSFRYLQGM CCCCCCCCCHHHHHH	16.28	26437602
238	Phosphorylation	GPRNLKPTASKLGAP CCCCCCCCHHHHCCC	41.81	27251275
240	Phosphorylation	RNLKPTASKLGAPLS CCCCCCHHHHCCCCC	30.78	27251275
241	Ubiquitination	NLKPTASKLGAPLSG CCCCCHHHHCCCCCC	48.77	-
247	Phosphorylation	SKLGAPLSGLQGLPE HHHCCCCCCCCCCCC	36.08	27251275
265	Phosphorylation	CGHGIVGTIVKARDK CCCCCHHHHEECCCC	16.23	23312004
293	Phosphorylation	LNLKQRGYFFLDERL CCHHHCCEEEECCCE	8.05	25884760
316	Phosphorylation	RVKPPEGYDVVAVYP CCCCCCCCCEEEECC	12.14	25394399

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
Oops, there are no upstream regulatory protein records of PDLI4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDLI4_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RBPMS_HUMAN	RBPMS	physical	16189514

Drug and Disease Associations

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

Regulatory Network of PDLI4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	19369195 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316, AND MASSSPECTROMETRY.	19534553 [Abstract]