dbPTM

PLAK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLAK_HUMAN
UniProt AC	P14923
Protein Name	Junction plakoglobin
Gene Name	JUP
Organism	Homo sapiens (Human).
Sequence Length	745
Subcellular Localization	Cell junction, adherens junction . Cell junction, desmosome . Cytoplasm, cytoskeleton . Membrane Peripheral membrane protein . Cytoplasmic in a soluble and membrane-associated form.
Protein Description	Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity)..
Protein Sequence	MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEVMNLME -------CCCCCCCC	8.70	22223895
14	Phosphorylation	MEQPIKVTEWQQTYT CCCCEEEEEEEEEEE	26.89	21945579
14	O-linked_Glycosylation	MEQPIKVTEWQQTYT CCCCEEEEEEEEEEE	26.89	28510447
19	Phosphorylation	KVTEWQQTYTYDSGI EEEEEEEEEECCCCC	11.61	21945579
20	Phosphorylation	VTEWQQTYTYDSGIH EEEEEEEEECCCCCC	10.04	21945579
21	Phosphorylation	TEWQQTYTYDSGIHS EEEEEEEECCCCCCC	25.00	21945579
22	Phosphorylation	EWQQTYTYDSGIHSG EEEEEEECCCCCCCC	9.56	21945579
24	Phosphorylation	QQTYTYDSGIHSGAN EEEEECCCCCCCCCC	29.27	21945579
28	Phosphorylation	TYDSGIHSGANTCVP ECCCCCCCCCCCCCC	37.37	21945579
32	Phosphorylation	GIHSGANTCVPSVSS CCCCCCCCCCCCCCC	17.85	21945579
36	Phosphorylation	GANTCVPSVSSKGIM CCCCCCCCCCCCCCC	17.77	21945579
38	Phosphorylation	NTCVPSVSSKGIMEE CCCCCCCCCCCCCCC	30.58	21945579
39	Phosphorylation	TCVPSVSSKGIMEED CCCCCCCCCCCCCCH	32.52	21945579
40	Ubiquitination	CVPSVSSKGIMEEDE CCCCCCCCCCCCCHH	44.97	21906983
53	Phosphorylation	DEACGRQYTLKKTTT HHHCCCEEEEEEEEE	16.81	21945579
54	Phosphorylation	EACGRQYTLKKTTTY HHCCCEEEEEEEEEE	24.62	21945579
56	Ubiquitination	CGRQYTLKKTTTYTQ CCCEEEEEEEEEECC	40.03	-
57	Ubiquitination	GRQYTLKKTTTYTQG CCEEEEEEEEEECCC	54.97	-
58	Phosphorylation	RQYTLKKTTTYTQGV CEEEEEEEEEECCCC	23.84	21945579
59	Phosphorylation	QYTLKKTTTYTQGVP EEEEEEEEEECCCCC	27.04	21945579
60	Phosphorylation	YTLKKTTTYTQGVPP EEEEEEEEECCCCCC	29.78	21945579
61	Phosphorylation	TLKKTTTYTQGVPPS EEEEEEEECCCCCCC	8.58	21945579
62	Phosphorylation	LKKTTTYTQGVPPSQ EEEEEEECCCCCCCC	19.43	21945579
68	Phosphorylation	YTQGVPPSQGDLEYQ ECCCCCCCCCCCHHH	40.50	21945579
74	Phosphorylation	PSQGDLEYQMSTTAR CCCCCCHHHHHHHHH	19.47	21945579
77	Phosphorylation	GDLEYQMSTTARAKR CCCHHHHHHHHHHHH	13.69	21945579
78	Phosphorylation	DLEYQMSTTARAKRV CCHHHHHHHHHHHHH	21.09	21945579
79	Phosphorylation	LEYQMSTTARAKRVR CHHHHHHHHHHHHHH	13.57	21945579
94	Phosphorylation	EAMCPGVSGEDSSLL HHHCCCCCCCCCHHE	42.24	28555341
98	Phosphorylation	PGVSGEDSSLLLATQ CCCCCCCCHHEEEEE	20.70	26657352
99	Phosphorylation	GVSGEDSSLLLATQV CCCCCCCHHEEEEEE	35.04	28857561
104	Phosphorylation	DSSLLLATQVEGQAT CCHHEEEEEEECCCC	32.87	28857561
120	Phosphorylation	LQRLAEPSQLLKSAI HHHHHCHHHHHHHHH	25.60	20068231
124	Ubiquitination	AEPSQLLKSAIVHLI HCHHHHHHHHHHHHH	46.57	21906983
125	Phosphorylation	EPSQLLKSAIVHLIN CHHHHHHHHHHHHHC	24.17	28152594
133	Phosphorylation	AIVHLINYQDDAELA HHHHHHCCCCHHHHH	13.31	28152594
141	Phosphorylation	QDDAELATRALPELT CCHHHHHHHHHHHHH	29.15	22817900
149	Ubiquitination	RALPELTKLLNDEDP HHHHHHHHHCCCCCC	64.70	21906983
160	Phosphorylation	DEDPVVVTKAAMIVN CCCCHHHHHHHHHHH	11.89	-
161	Ubiquitination	EDPVVVTKAAMIVNQ CCCHHHHHHHHHHHH	23.65	21906983
170	Phosphorylation	AMIVNQLSKKEASRR HHHHHHHCHHHHHHH	31.73	20860994
171	Ubiquitination	MIVNQLSKKEASRRA HHHHHHCHHHHHHHH	64.32	-
175	Phosphorylation	QLSKKEASRRALMGS HHCHHHHHHHHHCCC	24.32	29514088
182	Phosphorylation	SRRALMGSPQLVAAV HHHHHCCCHHHHHHH	8.77	26846344
193	Sulfoxidation	VAAVVRTMQNTSDLD HHHHHHHHCCCCCCH	1.71	28183972
196	Phosphorylation	VVRTMQNTSDLDTAR HHHHHCCCCCCHHHH	13.51	28258704
197	Phosphorylation	VRTMQNTSDLDTARC HHHHCCCCCCHHHHH	43.66	27251275
201	Phosphorylation	QNTSDLDTARCTTSI CCCCCCHHHHHHHHH	24.25	28258704
224	Ubiquitination	EGLLAIFKSGGIPAL CCHHHHHHCCCHHHH	41.92	21906983
272	Ubiquitination	RLADGLQKMVPLLNK HHHHHHHHHHHHHCC	47.08	-
279	Ubiquitination	KMVPLLNKNNPKFLA HHHHHHCCCCCCEEE	59.06	-
322	Phosphorylation	LVQIMRNYSYEKLLW HHHHHHHCCHHHHHH	11.41	29978859
323	Phosphorylation	VQIMRNYSYEKLLWT HHHHHHCCHHHHHHH	30.30	29978859
324	Phosphorylation	QIMRNYSYEKLLWTT HHHHHCCHHHHHHHH	13.51	29978859
326	Ubiquitination	MRNYSYEKLLWTTSR HHHCCHHHHHHHHHH	40.42	-
326	Acetylation	MRNYSYEKLLWTTSR HHHCCHHHHHHHHHH	40.42	25825284
336	Acetylation	WTTSRVLKVLSVCPS HHHHHHHHHHHCCCC	37.97	26051181
336	Ubiquitination	WTTSRVLKVLSVCPS HHHHHHHHHHHCCCC	37.97	-
345	Ubiquitination	LSVCPSNKPAIVEAG HHCCCCCCCEEEEEC	39.91	-
359	Ubiquitination	GGMQALGKHLTSNSP CHHHHHHHHHCCCCH	35.97	-
385	Ubiquitination	NLSDVATKQEGLESV HHHHHCHHHHHHHHH	36.29	21906983
401	Phosphorylation	KILVNQLSVDDVNVL HHHHHCCCCCCEEEE	17.46	23090842
409	Phosphorylation	VDDVNVLTCATGTLS CCCEEEEEECCCCHH	8.87	23090842
412	Phosphorylation	VNVLTCATGTLSNLT EEEEEECCCCHHCCE	32.61	23090842
414	Phosphorylation	VLTCATGTLSNLTCN EEEECCCCHHCCEEC	23.74	23090842
424	Ubiquitination	NLTCNNSKNKTLVTQ CCEECCCCCCEEEEC	65.67	-
426	Ubiquitination	TCNNSKNKTLVTQNS EECCCCCCEEEECCH	47.15	-
427	Phosphorylation	CNNSKNKTLVTQNSG ECCCCCCEEEECCHH	35.54	25867546
430	Phosphorylation	SKNKTLVTQNSGVEA CCCCEEEECCHHHHH	25.75	22817900
433	Phosphorylation	KTLVTQNSGVEALIH CEEEECCHHHHHHHH	34.10	25867546
448	Acetylation	AILRAGDKDDITEPA HHHHCCCCCCCCHHH	57.28	26051181
448	Ubiquitination	AILRAGDKDDITEPA HHHHCCCCCCCCHHH	57.28	-
452	Phosphorylation	AGDKDDITEPAVCAL CCCCCCCCHHHHHHH	42.80	22210691
463	Phosphorylation	VCALRHLTSRHPEAE HHHHHHHHHCCCHHH	20.00	22817900
475	Phosphorylation	EAEMAQNSVRLNYGI HHHHHHHHHHHHCCH	9.13	22210691
480	Phosphorylation	QNSVRLNYGIPAIVK HHHHHHHCCHHHHHH	22.48	27273156
499	Ubiquitination	PNQWPLVKATIGLIR CCCCHHHHHHHHHHH	47.71	21906983
533	Ubiquitination	RLVQLLVKAHQDAQR HHHHHHHHHCHHHHH	39.87	-
546	Phosphorylation	QRHVAAGTQQPYTDG HHHHHCCCCCCCCCC	21.21	21945579
550	Phosphorylation	AAGTQQPYTDGVRME HCCCCCCCCCCCCHH	17.08	21945579
551	Phosphorylation	AGTQQPYTDGVRMEE CCCCCCCCCCCCHHH	32.72	21945579
564	Phosphorylation	EEIVEGCTGALHILA HHHHCHHCCHHHHHH	36.02	20068231
595	Phosphorylation	LFVQLLYSSVENIQR HHHHHHHHCHHHHHH	28.07	24719451
596	Phosphorylation	FVQLLYSSVENIQRV HHHHHHHCHHHHHHH	21.64	22817900
641	Phosphorylation	LHSRNEGTATYAAAV HHHCCCCHHHHHHHH	15.06	21945579
643	Phosphorylation	SRNEGTATYAAAVLF HCCCCHHHHHHHHHH	17.33	21945579
644	Phosphorylation	RNEGTATYAAAVLFR CCCCHHHHHHHHHHH	7.56	21945579
660	Phosphorylation	SEDKNPDYRKRVSVE HCCCCCCHHHHHHHH	21.20	25394399
664	Phosphorylation	NPDYRKRVSVELTNS CCCHHHHHHHHHHHH	9.37	17081983
665	Phosphorylation	PDYRKRVSVELTNSL CCHHHHHHHHHHHHH	17.57	22167270
669	Phosphorylation	KRVSVELTNSLFKHD HHHHHHHHHHHHHCC	14.84	22167270
671	Phosphorylation	VSVELTNSLFKHDPA HHHHHHHHHHHCCHH	29.92	23927012
701	Phosphorylation	GDDMDATYRPMYSSD CCCCCCCCCCCCCCC	17.91	22817900
724	Phosphorylation	HMDMDGDYPIDTYSD CCCCCCCCCCCCCCC	13.97	22817900
728	Phosphorylation	DGDYPIDTYSDGLRP CCCCCCCCCCCCCCC	26.16	24275569
729	Phosphorylation	GDYPIDTYSDGLRPP CCCCCCCCCCCCCCC	10.87	22817900
730	Phosphorylation	DYPIDTYSDGLRPPY CCCCCCCCCCCCCCC	27.56	10902626

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
133	Y	Phosphorylation	Kinase	FYN	P06241	PSP
550	Y	Phosphorylation	Kinase	FER	P16591	PSP
550	Y	Phosphorylation	Kinase	FYN	P06241	PSP
644	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NTAQ1_HUMAN	WDYHV1	physical	16189514
RIBC2_HUMAN	RIBC2	physical	16189514
IKBE_HUMAN	NFKBIE	physical	16189514
CNBP1_HUMAN	CTNNBIP1	physical	16189514
CTNA1_HUMAN	CTNNA1	physical	9762469
APC_HUMAN	APC	physical	8074697
CADH1_HUMAN	CDH1	physical	8074697
ERBB2_HUMAN	ERBB2	physical	7702605
DESP_HUMAN	DSP	physical	9348293
DSG2_HUMAN	DSG2	physical	10769205
DSG2_HUMAN	DSG2	physical	8749329
CTNA1_HUMAN	CTNNA1	physical	9110993
CADH1_MOUSE	Cdh1	physical	12847106
DSC1_MOUSE	Dsc1	physical	12847106
DSG1A_MOUSE	Dsg1a	physical	12847106
DSC1_HUMAN	DSC1	physical	14673151
PLEC_HUMAN	PLEC	physical	22939629
PTH2_HUMAN	PTRH2	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
S2544_HUMAN	SLC25A44	physical	22939629
SYIM_HUMAN	IARS2	physical	22939629
CC130_HUMAN	CCDC130	physical	22365833
CTNA3_HUMAN	CTNNA3	physical	23718855
NFAC4_HUMAN	NFATC4	physical	21988832
CTNA1_HUMAN	CTNNA1	physical	25241761
APC_HUMAN	APC	physical	25241761
ERBB2_HUMAN	ERBB2	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761

Drug and Disease Associations

Kegg Disease
H00293	Arrhythmogenic right ventricular cardiomyopathy (ARVC)
H00669	Naxos disease and Carvajal syndrome
OMIM Disease
601214	Naxos disease (NXD)
611528	Arrhythmogenic right ventricular dysplasia, familial, 12 (ARVD12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLAK_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, ANDMASS SPECTROMETRY.	17081983 [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-660, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-660, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASSSPECTROMETRY.	15951569 [Abstract]