dbPTM

PDLI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDLI1_HUMAN
UniProt AC	O00151
Protein Name	PDZ and LIM domain protein 1
Gene Name	PDLIM1
Organism	Homo sapiens (Human).
Sequence Length	329
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, myofibril, sarcomere, Z line . Associates with actin stress fibers.
Protein Description	Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton. [PubMed: 10861853 Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity]
Protein Sequence	MTTQQIDLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAALANLCIGDVITAIDGENTSNMTHLEAQNRIKGCTDNLTLTVARSEHKVWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPASSTTARVITNQYNNPAGLYSSENISNFNNALESKTAASGVEANSRPLDHAQPPSSLVIDKESEVYKMLQEKQELNEPPKQSTSFLVLQEILESEEKGDPNKPSGFRSVKAPVTKVAASIGNAQKLPMCDKCGTGIVGVFVKLRDRHRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHARERVTPPEGYEVVTVFPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTTQQIDLQ ------CCCEEEECC	33.06	22814378
2	Phosphorylation	------MTTQQIDLQ ------CCCEEEECC	33.06	28857561
3	Phosphorylation	-----MTTQQIDLQG -----CCCEEEECCC	19.71	28857561
22	Acetylation	GFRLVGGKDFEQPLA CEEEECCCCCCCCEE	54.00	26051181
22	Ubiquitination	GFRLVGGKDFEQPLA CEEEECCCCCCCCEE	54.00	21890473
22	2-Hydroxyisobutyrylation	GFRLVGGKDFEQPLA CEEEECCCCCCCCEE	54.00	-
31	Phosphorylation	FEQPLAISRVTPGSK CCCCEEEEEECCCCH	18.32	20068231
34	Phosphorylation	PLAISRVTPGSKAAL CEEEEEECCCCHHHH	22.33	22199227
37	Phosphorylation	ISRVTPGSKAALANL EEEECCCCHHHHHHH	21.96	26270265
61	Sulfoxidation	DGENTSNMTHLEAQN CCCCCCCCCHHHHHH	2.21	30846556
71	Ubiquitination	LEAQNRIKGCTDNLT HHHHHHHCCCCCCEE	44.70	-
71	Malonylation	LEAQNRIKGCTDNLT HHHHHHHCCCCCCEE	44.70	26320211
71	Acetylation	LEAQNRIKGCTDNLT HHHHHHHCCCCCCEE	44.70	26051181
73	Glutathionylation	AQNRIKGCTDNLTLT HHHHHCCCCCCEEEE	3.52	22555962
73	S-nitrosylation	AQNRIKGCTDNLTLT HHHHHCCCCCCEEEE	3.52	22178444
78	Phosphorylation	KGCTDNLTLTVARSE CCCCCCEEEEEECCC	27.00	27251275
80	Phosphorylation	CTDNLTLTVARSEHK CCCCEEEEEECCCCC	13.59	27251275
84	Phosphorylation	LTLTVARSEHKVWSP EEEEEECCCCCEECC	34.02	25106551
87	Methylation	TVARSEHKVWSPLVT EEECCCCCEECCEEC	41.15	-
87	Ubiquitination	TVARSEHKVWSPLVT EEECCCCCEECCEEC	41.15	-
90	Phosphorylation	RSEHKVWSPLVTEEG CCCCCEECCEECCCC	16.02	19664994
94	O-linked_Glycosylation	KVWSPLVTEEGKRHP CEECCEECCCCCCCC	35.68	55821493
94	Phosphorylation	KVWSPLVTEEGKRHP CEECCEECCCCCCCC	35.68	23927012
98	Malonylation	PLVTEEGKRHPYKMN CEECCCCCCCCCCCC	51.30	26320211
98	2-Hydroxyisobutyrylation	PLVTEEGKRHPYKMN CEECCCCCCCCCCCC	51.30	-
98	Acetylation	PLVTEEGKRHPYKMN CEECCCCCCCCCCCC	51.30	25953088
98	Ubiquitination	PLVTEEGKRHPYKMN CEECCCCCCCCCCCC	51.30	-
102	Phosphorylation	EEGKRHPYKMNLASE CCCCCCCCCCCCCCC	19.42	27259358
104	Sulfoxidation	GKRHPYKMNLASEPQ CCCCCCCCCCCCCCC	4.02	30846556
108	O-linked_Glycosylation	PYKMNLASEPQEVLH CCCCCCCCCCCEEEE	53.64	30059200
108	Phosphorylation	PYKMNLASEPQEVLH CCCCCCCCCCCEEEE	53.64	20068231
118	Phosphorylation	QEVLHIGSAHNRSAM CEEEECCCCCCCCCC	26.25	23401153
123	Phosphorylation	IGSAHNRSAMPFTAS CCCCCCCCCCCCCCC	33.95	23927012
125	Sulfoxidation	SAHNRSAMPFTASPA CCCCCCCCCCCCCCC	2.71	21406390
128	O-linked_Glycosylation	NRSAMPFTASPASST CCCCCCCCCCCCCCC	21.98	30059200
128	Phosphorylation	NRSAMPFTASPASST CCCCCCCCCCCCCCC	21.98	23927012
130	Phosphorylation	SAMPFTASPASSTTA CCCCCCCCCCCCCCE	20.24	23927012
133	Phosphorylation	PFTASPASSTTARVI CCCCCCCCCCCEEEE	31.44	23927012
134	O-linked_Glycosylation	FTASPASSTTARVIT CCCCCCCCCCEEEEE	31.70	30059200
134	Phosphorylation	FTASPASSTTARVIT CCCCCCCCCCEEEEE	31.70	23927012
135	O-linked_Glycosylation	TASPASSTTARVITN CCCCCCCCCEEEEEC	23.21	OGP
135	Phosphorylation	TASPASSTTARVITN CCCCCCCCCEEEEEC	23.21	23927012
136	O-linked_Glycosylation	ASPASSTTARVITNQ CCCCCCCCEEEEECC	17.89	OGP
136	Phosphorylation	ASPASSTTARVITNQ CCCCCCCCEEEEECC	17.89	23927012
141	Phosphorylation	STTARVITNQYNNPA CCCEEEEECCCCCCC	17.26	21945579
144	Phosphorylation	ARVITNQYNNPAGLY EEEEECCCCCCCCCC	20.98	21945579
151	Phosphorylation	YNNPAGLYSSENISN CCCCCCCCCCCCHHH	14.83	21945579
152	Phosphorylation	NNPAGLYSSENISNF CCCCCCCCCCCHHHH	35.90	21945579
153	Phosphorylation	NPAGLYSSENISNFN CCCCCCCCCCHHHHH	22.55	21945579
157	Phosphorylation	LYSSENISNFNNALE CCCCCCHHHHHHHHH	47.12	21945579
167	Phosphorylation	NNALESKTAASGVEA HHHHHHHHHHCCCCC	36.41	28857561
170	Phosphorylation	LESKTAASGVEANSR HHHHHHHCCCCCCCC	40.69	28857561
176	Phosphorylation	ASGVEANSRPLDHAQ HCCCCCCCCCCCCCC	42.18	28857561
186	Phosphorylation	LDHAQPPSSLVIDKE CCCCCCCCCEEEECH	42.88	17287340
187	Phosphorylation	DHAQPPSSLVIDKES CCCCCCCCEEEECHH	32.22	17287340
192	Acetylation	PSSLVIDKESEVYKM CCCEEEECHHHHHHH	52.60	26051181
192	2-Hydroxyisobutyrylation	PSSLVIDKESEVYKM CCCEEEECHHHHHHH	52.60	-
192	Ubiquitination	PSSLVIDKESEVYKM CCCEEEECHHHHHHH	52.60	-
194	Phosphorylation	SLVIDKESEVYKMLQ CEEEECHHHHHHHHH	37.80	29978859
197	Phosphorylation	IDKESEVYKMLQEKQ EECHHHHHHHHHHHH	6.14	25394399
198	2-Hydroxyisobutyrylation	DKESEVYKMLQEKQE ECHHHHHHHHHHHHH	38.01	-
198	Ubiquitination	DKESEVYKMLQEKQE ECHHHHHHHHHHHHH	38.01	-
203	Ubiquitination	VYKMLQEKQELNEPP HHHHHHHHHHHCCCC	35.79	-
203	2-Hydroxyisobutyrylation	VYKMLQEKQELNEPP HHHHHHHHHHHCCCC	35.79	-
211	Ubiquitination	QELNEPPKQSTSFLV HHHCCCCCCCHHHHH	68.54	-
213	Phosphorylation	LNEPPKQSTSFLVLQ HCCCCCCCHHHHHHH	31.95	28450419
214	Phosphorylation	NEPPKQSTSFLVLQE CCCCCCCHHHHHHHH	22.47	28450419
215	Phosphorylation	EPPKQSTSFLVLQEI CCCCCCHHHHHHHHH	23.10	28102081
233	Ubiquitination	EEKGDPNKPSGFRSV HHCCCCCCCCCCCCC	46.04	-
233	Acetylation	EEKGDPNKPSGFRSV HHCCCCCCCCCCCCC	46.04	26051181
235	Phosphorylation	KGDPNKPSGFRSVKA CCCCCCCCCCCCCCC	52.77	25056879
239	Phosphorylation	NKPSGFRSVKAPVTK CCCCCCCCCCCCHHH	26.21	25056879
241	Ubiquitination	PSGFRSVKAPVTKVA CCCCCCCCCCHHHHH	48.49	-
241	Acetylation	PSGFRSVKAPVTKVA CCCCCCCCCCHHHHH	48.49	25953088
245	Phosphorylation	RSVKAPVTKVAASIG CCCCCCHHHHHHHHC	20.81	26074081
246	Acetylation	SVKAPVTKVAASIGN CCCCCHHHHHHHHCC	30.06	25953088
246	Ubiquitination	SVKAPVTKVAASIGN CCCCCHHHHHHHHCC	30.06	-
250	Phosphorylation	PVTKVAASIGNAQKL CHHHHHHHHCCHHCC	22.69	26657352
256	Ubiquitination	ASIGNAQKLPMCDKC HHHCCHHCCCCCCCC	52.74	-
262	2-Hydroxyisobutyrylation	QKLPMCDKCGTGIVG HCCCCCCCCCCCEEE	29.63	-
283	Glutathionylation	DRHRHPECYVCTDCG CCCCCCCEEEECCCC	3.48	22555962
284	Phosphorylation	RHRHPECYVCTDCGT CCCCCCEEEECCCCC	9.26	30108239
287	Phosphorylation	HPECYVCTDCGTNLK CCCEEEECCCCCCCE	25.04	30108239
291	Phosphorylation	YVCTDCGTNLKQKGH EEECCCCCCCEECCC	43.65	26657352
296	Acetylation	CGTNLKQKGHFFVED CCCCCEECCCEEECC	53.41	26051181
306	Phosphorylation	FFVEDQIYCEKHARE EEECCCEEEHHHHHH	6.74	28152594
309	Ubiquitination	EDQIYCEKHARERVT CCCEEEHHHHHHCCC	38.72	-
309	Acetylation	EDQIYCEKHARERVT CCCEEEHHHHHHCCC	38.72	25953088
316	Phosphorylation	KHARERVTPPEGYEV HHHHHCCCCCCCCEE	39.07	21945579
321	Nitration	RVTPPEGYEVVTVFP CCCCCCCCEEEEEEC	12.14	-
321	Phosphorylation	RVTPPEGYEVVTVFP CCCCCCCCEEEEEEC	12.14	21945579
325	Phosphorylation	PEGYEVVTVFPK--- CCCCEEEEEECC---	22.93	21945579
325	O-linked_Glycosylation	PEGYEVVTVFPK--- CCCCEEEEEECC---	22.93	30059200

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 PDLI1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDLI1_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 PDLI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STK35_HUMAN	STK35	physical	11973348
ACTN1_HUMAN	ACTN1	physical	10753915
ACTN4_HUMAN	ACTN4	physical	10753915
RNF12_HUMAN	RLIM	physical	19117995
PDLI1_HUMAN	PDLIM1	physical	19117995
ESR1_HUMAN	ESR1	physical	19117995
PNPT1_HUMAN	PNPT1	physical	22939629
ARI2_HUMAN	ARIH2	physical	22863883
HXK2_HUMAN	HK2	physical	22863883
NUBP1_HUMAN	NUBP1	physical	22863883
ACTN4_HUMAN	ACTN4	physical	26186194
ACTN1_HUMAN	ACTN1	physical	26186194
ACTN2_HUMAN	ACTN2	physical	26186194
ACTN3_HUMAN	ACTN3	physical	26186194
NUD12_HUMAN	NUDT12	physical	26186194
MOG1_HUMAN	RANGRF	physical	26186194
STMN1_HUMAN	STMN1	physical	26344197
ACTN3_HUMAN	ACTN3	physical	28514442
NUD12_HUMAN	NUDT12	physical	28514442
ACTN1_HUMAN	ACTN1	physical	28514442
ACTN2_HUMAN	ACTN2	physical	28514442
ACTN4_HUMAN	ACTN4	physical	28514442
GORS2_HUMAN	GORASP2	physical	27173435

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 PDLI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-187; SER-239AND TYR-321, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, AND MASSSPECTROMETRY.	17924679 [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-321, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144 AND TYR-151, ANDMASS SPECTROMETRY.	15592455 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	15144186 [Abstract]