dbPTM

PDLI7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDLI7_HUMAN
UniProt AC	Q9NR12
Protein Name	PDZ and LIM domain protein 7
Gene Name	PDLIM7
Organism	Homo sapiens (Human).
Sequence Length	457
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By similarity)..
Protein Description	May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity)..
Protein Sequence	MDSFKVVLEGPAPWGFRLQGGKDFNVPLSISRLTPGGKAAQAGVAVGDWVLSIDGENAGSLTHIEAQNKIRACGERLSLGLSRAQPVQSKPQKASAPAADPPRYTFAPSVSLNKTARPFGAPPPADSAPQQNGQPLRPLVPDASKQRLMENTEDWRPRPGTGQSRSFRILAHLTGTEFMQDPDEEHLKKSSQVPRTEAPAPASSTPQEPWPGPTAPSPTSRPPWAVDPAFAERYAPDKTSTVLTRHSQPATPTPLQSRTSIVQAAAGGVPGGGSNNGKTPVCHQCHKVIRGRYLVALGHAYHPEEFVCSQCGKVLEEGGFFEEKGAIFCPPCYDVRYAPSCAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYMEEGVPYCERDYEKMFGTKCHGCDFKIDAGDRFLEALGFSWHDTCFVCAICQINLEGKTFYSKKDRPLCKSHAFSHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Acetylation	---MDSFKVVLEGPA ---CCCEEEEEECCC	35.07	19818139
22	Ubiquitination	GFRLQGGKDFNVPLS CEEECCCCCCCCCEE	67.00	23000965
22	Malonylation	GFRLQGGKDFNVPLS CEEECCCCCCCCCEE	67.00	26320211
29	Phosphorylation	KDFNVPLSISRLTPG CCCCCCEEEEEECCC	16.67	22199227
31	Phosphorylation	FNVPLSISRLTPGGK CCCCEEEEEECCCCH	20.19	22199227
34	Phosphorylation	PLSISRLTPGGKAAQ CEEEEEECCCCHHHH	20.83	22199227
52	Phosphorylation	AVGDWVLSIDGENAG EECCEEEEECCCCCC	14.71	28348404
60	Phosphorylation	IDGENAGSLTHIEAQ ECCCCCCCCCHHHHH	27.90	26657352
62	Phosphorylation	GENAGSLTHIEAQNK CCCCCCCCHHHHHHH	23.62	26657352
78	Phosphorylation	RACGERLSLGLSRAQ HHHHHHHHHCCCCCC	26.98	30266825
82	Phosphorylation	ERLSLGLSRAQPVQS HHHHHCCCCCCCCCC	24.62	24732914
89	Phosphorylation	SRAQPVQSKPQKASA CCCCCCCCCCCCCCC	46.68	-
89	O-linked_Glycosylation	SRAQPVQSKPQKASA CCCCCCCCCCCCCCC	46.68	20068230
89	O-linked_Glycosylation	SRAQPVQSKPQKASA CCCCCCCCCCCCCCC	46.68	30059200
90	Ubiquitination	RAQPVQSKPQKASAP CCCCCCCCCCCCCCC	34.08	23000965
95	O-linked_Glycosylation	QSKPQKASAPAADPP CCCCCCCCCCCCCCC	41.65	30059200
95	Phosphorylation	QSKPQKASAPAADPP CCCCCCCCCCCCCCC	41.65	21945579
96 (in isoform 2)	Phosphorylation	-	11.56	26657352
103	Asymmetric dimethylarginine	APAADPPRYTFAPSV CCCCCCCCCEECCCC	48.81	-
103	Methylation	APAADPPRYTFAPSV CCCCCCCCCEECCCC	48.81	24129315
104	Phosphorylation	PAADPPRYTFAPSVS CCCCCCCCEECCCCC	16.39	21945579
105	Phosphorylation	AADPPRYTFAPSVSL CCCCCCCEECCCCCC	18.01	21945579
105	O-linked_Glycosylation	AADPPRYTFAPSVSL CCCCCCCEECCCCCC	18.01	30059200
109	Phosphorylation	PRYTFAPSVSLNKTA CCCEECCCCCCCCCC	22.40	21945579
111	Phosphorylation	YTFAPSVSLNKTARP CEECCCCCCCCCCCC	30.48	23401153
114	Ubiquitination	APSVSLNKTARPFGA CCCCCCCCCCCCCCC	49.18	23000965
117	Methylation	VSLNKTARPFGAPPP CCCCCCCCCCCCCCC	32.10	115486907
137	Methylation	QQNGQPLRPLVPDAS CCCCCCCCCCCCCHH	29.23	115368691
144	Phosphorylation	RPLVPDASKQRLMEN CCCCCCHHHHHHHHC	36.38	27251275
145	Methylation	PLVPDASKQRLMENT CCCCCHHHHHHHHCC	40.95	115486915
145	Ubiquitination	PLVPDASKQRLMENT CCCCCHHHHHHHHCC	40.95	23000965
152	Phosphorylation	KQRLMENTEDWRPRP HHHHHHCCCCCCCCC	23.24	27251275
161	Phosphorylation	DWRPRPGTGQSRSFR CCCCCCCCCCCCCEE	34.43	28857561
164	Phosphorylation	PRPGTGQSRSFRILA CCCCCCCCCCEEHHH	31.10	27251275
165	Methylation	RPGTGQSRSFRILAH CCCCCCCCCEEHHHH	31.74	115486899
166	Phosphorylation	PGTGQSRSFRILAHL CCCCCCCCEEHHHHH	24.91	-
174	Phosphorylation	FRILAHLTGTEFMQD EEHHHHHHCCCCCCC	31.99	28555341
176	Phosphorylation	ILAHLTGTEFMQDPD HHHHHHCCCCCCCCC	22.33	28555341
188	Acetylation	DPDEEHLKKSSQVPR CCCHHHHHHHCCCCC	53.14	26051181
194 (in isoform 6)	Phosphorylation	-	29.82	26437602
196	Phosphorylation	KSSQVPRTEAPAPAS HHCCCCCCCCCCCCC	30.35	24732914
200 (in isoform 6)	Phosphorylation	-	21.24	24719451
203	Phosphorylation	TEAPAPASSTPQEPW CCCCCCCCCCCCCCC	33.41	30206219
204	Ubiquitination	EAPAPASSTPQEPWP CCCCCCCCCCCCCCC	46.33	23000965
204	Phosphorylation	EAPAPASSTPQEPWP CCCCCCCCCCCCCCC	46.33	30206219
205	Phosphorylation	APAPASSTPQEPWPG CCCCCCCCCCCCCCC	26.88	21712546
214 (in isoform 6)	Phosphorylation	-	58.05	26437602
214	Phosphorylation	QEPWPGPTAPSPTSR CCCCCCCCCCCCCCC	58.05	21712546
217	Phosphorylation	WPGPTAPSPTSRPPW CCCCCCCCCCCCCCC	38.04	25159151
219	Phosphorylation	GPTAPSPTSRPPWAV CCCCCCCCCCCCCCC	41.53	30175587
220	Phosphorylation	PTAPSPTSRPPWAVD CCCCCCCCCCCCCCC	46.29	23898821
222 (in isoform 6)	Phosphorylation	-	28.66	26437602
234	Phosphorylation	DPAFAERYAPDKTST CHHHHHHHCCCCCCC	17.62	28152594
238	Malonylation	AERYAPDKTSTVLTR HHHHCCCCCCCEEEE	43.23	26320211
238	Sumoylation	AERYAPDKTSTVLTR HHHHCCCCCCCEEEE	43.23	-
238	Sumoylation	AERYAPDKTSTVLTR HHHHCCCCCCCEEEE	43.23	-
238	Ubiquitination	AERYAPDKTSTVLTR HHHHCCCCCCCEEEE	43.23	23000965
239	Phosphorylation	ERYAPDKTSTVLTRH HHHCCCCCCCEEEEC	36.69	28152594
239	O-linked_Glycosylation	ERYAPDKTSTVLTRH HHHCCCCCCCEEEEC	36.69	55821367
240	Phosphorylation	RYAPDKTSTVLTRHS HHCCCCCCCEEEECC	23.43	23403867
240	O-linked_Glycosylation	RYAPDKTSTVLTRHS HHCCCCCCCEEEECC	23.43	30059200
241	O-linked_Glycosylation	YAPDKTSTVLTRHSQ HCCCCCCCEEEECCC	25.43	11192479
241	Phosphorylation	YAPDKTSTVLTRHSQ HCCCCCCCEEEECCC	25.43	23403867
244	Phosphorylation	DKTSTVLTRHSQPAT CCCCCEEEECCCCCC	23.23	23403867
246	Ubiquitination	TSTVLTRHSQPATPT CCCEEEECCCCCCCC	26.08	21890473
247	Phosphorylation	STVLTRHSQPATPTP CCEEEECCCCCCCCC	34.27	25159151
251	Phosphorylation	TRHSQPATPTPLQSR EECCCCCCCCCCCCC	34.09	30266825
253	Phosphorylation	HSQPATPTPLQSRTS CCCCCCCCCCCCCCH	32.07	22617229
257	Phosphorylation	ATPTPLQSRTSIVQA CCCCCCCCCCHHHHH	45.25	23403867
259	Phosphorylation	PTPLQSRTSIVQAAA CCCCCCCCHHHHHHC	28.22	26657352
260	Phosphorylation	TPLQSRTSIVQAAAG CCCCCCCHHHHHHCC	21.47	23911959
274	Phosphorylation	GGVPGGGSNNGKTPV CCCCCCCCCCCCCCC	30.32	26657352
278	Acetylation	GGGSNNGKTPVCHQC CCCCCCCCCCCCHHH	52.35	25953088
279	Phosphorylation	GGSNNGKTPVCHQCH CCCCCCCCCCCHHHH	23.50	24732914
287	Acetylation	PVCHQCHKVIRGRYL CCCHHHHHHHCCCEE	47.16	26051181
293	Phosphorylation	HKVIRGRYLVALGHA HHHHCCCEEEECCCC	14.35	28152594
301	Ubiquitination	LVALGHAYHPEEFVC EEECCCCCCHHHHEC	16.54	21890473
301	Phosphorylation	LVALGHAYHPEEFVC EEECCCCCCHHHHEC	16.54	27642862
338	Phosphorylation	PCYDVRYAPSCAKCK CCCCEEECCCHHHCC	4.48	32645325
340	Phosphorylation	YDVRYAPSCAKCKKK CCEEECCCHHHCCHH	20.66	30631047
347	Malonylation	SCAKCKKKITGEIMH CHHHCCHHHHHHHHH	30.87	26320211
349	Phosphorylation	AKCKKKITGEIMHAL HHCCHHHHHHHHHHH	37.33	21712546
360	Ubiquitination	MHALKMTWHVHCFTC HHHHHCCEEEEEHHH	6.49	21890473
366	Phosphorylation	TWHVHCFTCAACKTP CEEEEEHHHHHCCCC	13.46	28348404
372	Phosphorylation	FTCAACKTPIRNRAF HHHHHCCCCCCCCEE	24.67	24719451
381	Sulfoxidation	IRNRAFYMEEGVPYC CCCCEEEHHCCCCCC	2.82	30846556
392	Phosphorylation	VPYCERDYEKMFGTK CCCCCCHHHHHHCCC	24.54	27642862
394	Ubiquitination	YCERDYEKMFGTKCH CCCCHHHHHHCCCCC	33.04	21890473
394	Malonylation	YCERDYEKMFGTKCH CCCCHHHHHHCCCCC	33.04	26320211
394	Acetylation	YCERDYEKMFGTKCH CCCCHHHHHHCCCCC	33.04	26051181
416	Ubiquitination	AGDRFLEALGFSWHD CCHHHHHHHCCCCCH	18.35	32015554
450	Malonylation	KKDRPLCKSHAFSHV CCCCCCHHHCCCCCC	53.62	26320211
450	Ubiquitination	KKDRPLCKSHAFSHV CCCCCCHHHCCCCCC	53.62	32015554
451	Phosphorylation	KDRPLCKSHAFSHV- CCCCCHHHCCCCCC-	21.03	20068231
455	Phosphorylation	LCKSHAFSHV----- CHHHCCCCCC-----	24.91	20068231

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 PDLI7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDLI7_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 PDLI7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSMF1_HUMAN	PSMF1	physical	16189514
PAK5_HUMAN	PAK7	physical	16189514
ENKD1_HUMAN	ENKD1	physical	16189514
WWP2_HUMAN	WWP2	physical	16189514
AP5B1_HUMAN	AP5B1	physical	16189514
CC185_HUMAN	CCDC185	physical	16189514
FND11_HUMAN	C20orf195	physical	16189514
TPM2_HUMAN	TPM2	physical	10359609
RET_HUMAN	RET	physical	12176011
ZMY11_HUMAN	ZMYND11	physical	16382137
SMUF1_HUMAN	SMURF1	physical	16611643
MDM2_HUMAN	MDM2	physical	21060154
P53_HUMAN	TP53	physical	21060154
NR2C2_HUMAN	NR2C2	physical	16446357
TAB2_HUMAN	TAB2	physical	16446357
TRAF6_HUMAN	TRAF6	physical	16446357
TRAF2_HUMAN	TRAF2	physical	21864338
TRAF3_HUMAN	TRAF3	physical	21864338
ZMY11_HUMAN	ZMYND11	physical	20732415
ZMY11_HUMAN	ZMYND11	physical	19379743
TRADD_HUMAN	TRADD	physical	19379743
3BP2_HUMAN	SH3BP2	physical	21988832
CSN5_HUMAN	COPS5	physical	24078030
CBLC_HUMAN	CBLC	physical	24466333
WWP2_HUMAN	WWP2	physical	25416956
HBB_HUMAN	HBB	physical	26186194
ACTG_HUMAN	ACTG1	physical	26496610
ACTN4_HUMAN	ACTN4	physical	26496610
ACTN1_HUMAN	ACTN1	physical	26496610
AP2A1_HUMAN	AP2A1	physical	26496610
VATA_HUMAN	ATP6V1A	physical	26496610
CALL3_HUMAN	CALML3	physical	26496610
CAZA2_HUMAN	CAPZA2	physical	26496610
CAPZB_HUMAN	CAPZB	physical	26496610
AP2M1_HUMAN	AP2M1	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
CLH1_HUMAN	CLTC	physical	26496610
CBPM_HUMAN	CPM	physical	26496610
EPS15_HUMAN	EPS15	physical	26496610
FLNA_HUMAN	FLNA	physical	26496610
GNAI2_HUMAN	GNAI2	physical	26496610
GBB1_HUMAN	GNB1	physical	26496610
ABLM1_HUMAN	ABLIM1	physical	26496610
MYO1B_HUMAN	MYO1B	physical	26496610
MYH9_HUMAN	MYH9	physical	26496610
MYL6_HUMAN	MYL6	physical	26496610
MYO1E_HUMAN	MYO1E	physical	26496610
MYO5A_HUMAN	MYO5A	physical	26496610
PLEC_HUMAN	PLEC	physical	26496610
SOAT1_HUMAN	SOAT1	physical	26496610
DHSO_HUMAN	SORD	physical	26496610
SPTN1_HUMAN	SPTAN1	physical	26496610
SPTB2_HUMAN	SPTBN1	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
ELOB_HUMAN	TCEB2	physical	26496610
TMOD1_HUMAN	TMOD1	physical	26496610
TPM1_HUMAN	TPM1	physical	26496610
TPM2_HUMAN	TPM2	physical	26496610
TPM3_HUMAN	TPM3	physical	26496610
TPM4_HUMAN	TPM4	physical	26496610
SYVC_HUMAN	VARS	physical	26496610
YES_HUMAN	YES1	physical	26496610
LUZP1_HUMAN	LUZP1	physical	26496610
ARPC4_HUMAN	ARPC4	physical	26496610
ARPC3_HUMAN	ARPC3	physical	26496610
ARP3_HUMAN	ACTR3	physical	26496610
ARPC2_HUMAN	ARPC2	physical	26496610
ML12A_HUMAN	MYL12A	physical	26496610
AKAP2_HUMAN	AKAP2	physical	26496610
SYNPO_HUMAN	SYNPO	physical	26496610
CE162_HUMAN	CEP162	physical	26496610
PALLD_HUMAN	PALLD	physical	26496610
MPRIP_HUMAN	MPRIP	physical	26496610
COBL_HUMAN	COBL	physical	26496610
CYTSA_HUMAN	SPECC1L	physical	26496610
RAI14_HUMAN	RAI14	physical	26496610
REPI1_HUMAN	REPIN1	physical	26496610
BMP2K_HUMAN	BMP2K	physical	26496610
MYO5C_HUMAN	MYO5C	physical	26496610
QSER1_HUMAN	QSER1	physical	26496610
ARP5L_HUMAN	ARPC5L	physical	26496610
MISP_HUMAN	MISP	physical	26496610
ACTT1_HUMAN	ACTRT1	physical	26496610
MYL6B_HUMAN	MYL6B	physical	26496610
TPRN_HUMAN	TPRN	physical	26496610
RNF31_HUMAN	RNF31	physical	27903798
HOIL1_HUMAN	RBCK1	physical	27903798
SHRPN_HUMAN	SHARPIN	physical	27903798
PTN14_HUMAN	PTPN14	physical	28514442
PDLI5_HUMAN	PDLIM5	physical	28514442
ZBT10_HUMAN	ZBTB10	physical	28514442
SLN12_HUMAN	SLFN12	physical	28514442
LPP_HUMAN	LPP	physical	28514442
BAG3_HUMAN	BAG3	physical	28514442
TRIP6_HUMAN	TRIP6	physical	28514442
LIMD1_HUMAN	LIMD1	physical	28514442
TPC10_HUMAN	TRAPPC10	physical	27173435
M21D2_HUMAN	MB21D2	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 PDLI7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-247 AND THR-251, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, AND MASSSPECTROMETRY.	18220336 [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 THR-251, AND MASSSPECTROMETRY.	17924679 [Abstract]