dbPTM

PTPRJ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTPRJ_HUMAN
UniProt AC	Q12913
Protein Name	Receptor-type tyrosine-protein phosphatase eta
Gene Name	PTPRJ
Organism	Homo sapiens (Human).
Sequence Length	1337
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Cell projection, ruffle membrane. Cell junction. After T-cell stimulation, it is temporarily excluded from immunological synapses.
Protein Description	Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling..
Protein Sequence	MKPAAREARLPPRSPGLRWALPLLLLLLRLGQILCAGGTPSPIPDPSVATVATGENGITQISSTAESFHKQNGTGTPQVETNTSEDGESSGANDSLRTPEQGSNGTDGASQKTPSSTGPSPVFDIKAVSISPTNVILTWKSNDTAASEYKYVVKHKMENEKTITVVHQPWCNITGLRPATSYVFSITPGIGNETWGDPRVIKVITEPIPVSDLRVALTGVRKAALSWSNGNGTASCRVLLESIGSHEELTQDSRLQVNISGLKPGVQYNINPYLLQSNKTKGDPLGTEGGLDASNTERSRAGSPTAPVHDESLVGPVDPSSGQQSRDTEVLLVGLEPGTRYNATVYSQAANGTEGQPQAIEFRTNAIQVFDVTAVNISATSLTLIWKVSDNESSSNYTYKIHVAGETDSSNLNVSEPRAVIPGLRSSTFYNITVCPVLGDIEGTPGFLQVHTPPVPVSDFRVTVVSTTEIGLAWSSHDAESFQMHITQEGAGNSRVEITTNQSIIIGGLFPGTKYCFEIVPKGPNGTEGASRTVCNRTVPSAVFDIHVVYVTTTEMWLDWKSPDGASEYVYHLVIESKHGSNHTSTYDKAITLQGLIPGTLYNITISPEVDHVWGDPNSTAQYTRPSNVSNIDVSTNTTAATLSWQNFDDASPTYSYCLLIEKAGNSSNATQVVTDIGITDATVTELIPGSSYTVEIFAQVGDGIKSLEPGRKSFCTDPASMASFDCEVVPKEPALVLKWTCPPGANAGFELEVSSGAWNNATHLESCSSENGTEYRTEVTYLNFSTSYNISITTVSCGKMAAPTRNTCTTGITDPPPPDGSPNITSVSHNSVKVKFSGFEASHGPIKAYAVILTTGEAGHPSADVLKYTYEDFKKGASDTYVTYLIRTEEKGRSQSLSEVLKYEIDVGNESTTLGYYNGKLEPLGSYRACVAGFTNITFHPQNKGLIDGAESYVSFSRYSDAVSLPQDPGVICGAVFGCIFGALVIVTVGGFIFWRKKRKDAKNNEVSFSQIKPKKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLVGISQPKYAAELAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIIMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEIVLPEWTIRDFTVKNIQTSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQSPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIVRSQKDSKVDLIYQNTTAMTIYENLAPVTTFGKTNGYIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
64	O-linked_Glycosylation	GITQISSTAESFHKQ CEEEEHHHHHHHHHH	27.88	OGP
72	N-linked_Glycosylation	AESFHKQNGTGTPQV HHHHHHHCCCCCCCE	55.59	UniProtKB CARBOHYD
74	O-linked_Glycosylation	SFHKQNGTGTPQVET HHHHHCCCCCCCEEE	45.49	OGP
82	N-linked_Glycosylation	GTPQVETNTSEDGES CCCCEEEECCCCCCC	28.27	UniProtKB CARBOHYD
84	Phosphorylation	PQVETNTSEDGESSG CCEEEECCCCCCCCC	35.44	29759185
93	N-linked_Glycosylation	DGESSGANDSLRTPE CCCCCCCCCCCCCCC	42.82	UniProtKB CARBOHYD
104	N-linked_Glycosylation	RTPEQGSNGTDGASQ CCCCCCCCCCCCCCC	65.30	17660510
142	N-linked_Glycosylation	VILTWKSNDTAASEY EEEEEECCCCCHHHH	47.10	17660510
172	N-linked_Glycosylation	VVHQPWCNITGLRPA EEECCCCCCCCCCCC	30.87	UniProtKB CARBOHYD
174	Phosphorylation	HQPWCNITGLRPATS ECCCCCCCCCCCCCE	19.03	24719451
192	N-linked_Glycosylation	SITPGIGNETWGDPR EECCCCCCCCCCCCE	41.42	UniProtKB CARBOHYD
226	Phosphorylation	GVRKAALSWSNGNGT HEEEEEEEECCCCCC	24.59	-
231	N-linked_Glycosylation	ALSWSNGNGTASCRV EEEECCCCCCCHHEE	49.22	UniProtKB CARBOHYD
233	Phosphorylation	SWSNGNGTASCRVLL EECCCCCCCHHEEEH	21.28	-
258	N-linked_Glycosylation	QDSRLQVNISGLKPG CCCCEEEECCCCCCC	15.11	UniProtKB CARBOHYD
278	N-linked_Glycosylation	NPYLLQSNKTKGDPL CHHHCCCCCCCCCCC	42.95	UniProtKB CARBOHYD
305	O-linked_Glycosylation	RSRAGSPTAPVHDES CCCCCCCCCCCCCCC	45.34	OGP
341	Phosphorylation	GLEPGTRYNATVYSQ EECCCCCEEEEEEEE	14.69	24043423
342	N-linked_Glycosylation	LEPGTRYNATVYSQA ECCCCCEEEEEEEEC	26.33	16335952
344	Phosphorylation	PGTRYNATVYSQAAN CCCCEEEEEEEECCC	19.15	24043423
346	Phosphorylation	TRYNATVYSQAANGT CCEEEEEEEECCCCC	7.24	24043423
347	Phosphorylation	RYNATVYSQAANGTE CEEEEEEEECCCCCC	14.70	24043423
351	N-linked_Glycosylation	TVYSQAANGTEGQPQ EEEEECCCCCCCCCE	62.02	16335952
376	N-linked_Glycosylation	VFDVTAVNISATSLT EEEEEEEEEEECEEE	21.74	UniProtKB CARBOHYD
391	N-linked_Glycosylation	LIWKVSDNESSSNYT EEEEEECCCCCCCEE	43.47	16335952
396	N-linked_Glycosylation	SDNESSSNYTYKIHV ECCCCCCCEEEEEEE	34.80	16335952
413	N-linked_Glycosylation	ETDSSNLNVSEPRAV CCCCCCCCCCCCCEE	39.25	17660510
431	N-linked_Glycosylation	LRSSTFYNITVCPVL CCCCCEEEEEEECCC	21.18	UniProtKB CARBOHYD
475	Phosphorylation	TEIGLAWSSHDAESF CEEEEEECCCCHHHE	16.52	24275569
499	Phosphorylation	GNSRVEITTNQSIII CCCCEEEEECCEEEE	13.24	28270605
500	Phosphorylation	NSRVEITTNQSIIIG CCCEEEEECCEEEEC	36.60	28270605
501	N-linked_Glycosylation	SRVEITTNQSIIIGG CCEEEEECCEEEECC	25.59	UniProtKB CARBOHYD
503	Phosphorylation	VEITTNQSIIIGGLF EEEEECCEEEECCCC	20.16	28270605
525	N-linked_Glycosylation	EIVPKGPNGTEGASR EEECCCCCCCCCCCC	77.88	17660510
536	N-linked_Glycosylation	GASRTVCNRTVPSAV CCCCEECCCCCCCCE	38.02	UniProtKB CARBOHYD
581	Phosphorylation	VIESKHGSNHTSTYD EEEECCCCCCCCCCH	25.76	29978859
582	N-linked_Glycosylation	IESKHGSNHTSTYDK EEECCCCCCCCCCHH	47.23	UniProtKB CARBOHYD
584	Phosphorylation	SKHGSNHTSTYDKAI ECCCCCCCCCCHHEE	27.32	29978859
585	Phosphorylation	KHGSNHTSTYDKAIT CCCCCCCCCCHHEEE	19.88	29978859
586	Phosphorylation	HGSNHTSTYDKAITL CCCCCCCCCHHEEEC	36.57	29978859
587	Phosphorylation	GSNHTSTYDKAITLQ CCCCCCCCHHEEECC	18.40	29978859
603	N-linked_Glycosylation	LIPGTLYNITISPEV CCCCCEEEEEECCCC	28.21	UniProtKB CARBOHYD
618	N-linked_Glycosylation	DHVWGDPNSTAQYTR CCCCCCCCCCCEEEC	57.65	UniProtKB CARBOHYD
628	N-linked_Glycosylation	AQYTRPSNVSNIDVS CEEECCCCCCCEEEC	43.87	UniProtKB CARBOHYD
637	N-linked_Glycosylation	SNIDVSTNTTAATLS CCEEECCCCEEEEEE	28.11	UniProtKB CARBOHYD
666	N-linked_Glycosylation	LLIEKAGNSSNATQV EEEEECCCCCCCEEE	47.31	UniProtKB CARBOHYD
669	N-linked_Glycosylation	EKAGNSSNATQVVTD EECCCCCCCEEEEEE	46.99	UniProtKB CARBOHYD
761	N-linked_Glycosylation	VSSGAWNNATHLESC EECCCCCCCEEEECC	35.20	UniProtKB CARBOHYD
772	N-linked_Glycosylation	LESCSSENGTEYRTE EECCCCCCCCEEEEE	65.71	UniProtKB CARBOHYD
784	N-linked_Glycosylation	RTEVTYLNFSTSYNI EEEEEEEEEECEEEE	20.57	UniProtKB CARBOHYD
790	N-linked_Glycosylation	LNFSTSYNISITTVS EEEECEEEEEEEEEE	22.69	UniProtKB CARBOHYD
808	Phosphorylation	MAAPTRNTCTTGITD EECCCCCCCCCCCCC	14.13	22210691
814	Phosphorylation	NTCTTGITDPPPPDG CCCCCCCCCCCCCCC	43.74	22210691
824	N-linked_Glycosylation	PPPDGSPNITSVSHN CCCCCCCCCEEECCC	52.44	UniProtKB CARBOHYD
910	N-linked_Glycosylation	KYEIDVGNESTTLGY CEEEECCCCCEEEEE	39.64	UniProtKB CARBOHYD
937	N-linked_Glycosylation	ACVAGFTNITFHPQN EEEECEEEEEECCCC	29.10	19159218
1009	Phosphorylation	DAKNNEVSFSQIKPK CCCCCCCCHHHCCCC	17.01	28355574
1011	Phosphorylation	KNNEVSFSQIKPKKS CCCCCCHHHCCCCCC	24.40	28355574
1014	Ubiquitination	EVSFSQIKPKKSKLI CCCHHHCCCCCCCCE	43.05	-
1029	Phosphorylation	RVENFEAYFKKQQAD EEECHHHHHHHHHCC	14.56	27642862
1031	Acetylation	ENFEAYFKKQQADSN ECHHHHHHHHHCCCC	36.68	7431975
1031	Ubiquitination	ENFEAYFKKQQADSN ECHHHHHHHHHCCCC	36.68	-
1032	Ubiquitination	NFEAYFKKQQADSNC CHHHHHHHHHCCCCC	37.43	-
1045	Phosphorylation	NCGFAEEYEDLKLVG CCCCCHHHCCCEEEE	13.27	27642862
1049	Ubiquitination	AEEYEDLKLVGISQP CHHHCCCEEEECCCH	54.14	-
1057	Ubiquitination	LVGISQPKYAAELAE EEECCCHHHHHHHHH	39.63	-
1058	Phosphorylation	VGISQPKYAAELAEN EECCCHHHHHHHHHH	20.09	28674419
1071	Phosphorylation	ENRGKNRYNNVLPYD HHCCCCCCCCCCCCC	22.08	27642862
1077	Phosphorylation	RYNNVLPYDISRVKL CCCCCCCCCCEEEEE	23.03	29978859
1080	Phosphorylation	NVLPYDISRVKLSVQ CCCCCCCEEEEEEEE	28.29	29978859
1085	Phosphorylation	DISRVKLSVQTHSTD CCEEEEEEEECCCCC	13.37	27642862
1090	Phosphorylation	KLSVQTHSTDDYINA EEEEECCCCCCCCCC	36.60	27642862
1091	Phosphorylation	LSVQTHSTDDYINAN EEEECCCCCCCCCCC	25.86	-
1094	Phosphorylation	QTHSTDDYINANYMP ECCCCCCCCCCCCCC	10.01	27642862
1099	Phosphorylation	DDYINANYMPGYHSK CCCCCCCCCCCCCCC	11.41	27642862
1103	Phosphorylation	NANYMPGYHSKKDFI CCCCCCCCCCCCCEE	9.32	27642862
1105	Phosphorylation	NYMPGYHSKKDFIAT CCCCCCCCCCCEEEE	32.68	-
1133	Phosphorylation	MVWEKNVYAIIMLTK HHHHHHHHEEEEHHH	11.07	24719451
1139	Phosphorylation	VYAIIMLTKCVEQGR HHEEEEHHHHHHHCC	12.67	24719451
1192	Phosphorylation	KNIQTSESHPLRQFH EECCCCCCCCCCEEE	30.12	27732954
1201	Phosphorylation	PLRQFHFTSWPDHGV CCCEEEECCCCCCCC	22.70	20068231
1202	Phosphorylation	LRQFHFTSWPDHGVP CCEEEECCCCCCCCC	35.35	20068231
1211	Phosphorylation	PDHGVPDTTDLLINF CCCCCCCCHHHHHHH	19.01	20068231
1212	Phosphorylation	DHGVPDTTDLLINFR CCCCCCCHHHHHHHH	31.84	20068231
1225	Phosphorylation	FRYLVRDYMKQSPPE HHHHHHHHHHHCCCC	8.82	-
1257	Phosphorylation	IAIDRLIYQIENENT EEEEEEEEECCCCCE	14.18	27174698
1264	Phosphorylation	YQIENENTVDVYGIV EECCCCCEEEEEEEE	16.35	27174698
1268	Phosphorylation	NENTVDVYGIVYDLR CCCEEEEEEEEEEEE	9.18	27174698
1272	Phosphorylation	VDVYGIVYDLRMHRP EEEEEEEEEEECCCC	13.82	27174698
1306	Ubiquitination	VRSQKDSKVDLIYQN HHCCCCCCCEEEEEC	50.32	-
1311	Phosphorylation	DSKVDLIYQNTTAMT CCCCEEEEECCCCCE	11.74	27259358
1314	Phosphorylation	VDLIYQNTTAMTIYE CEEEEECCCCCEEEE	10.62	26356563
1315	Phosphorylation	DLIYQNTTAMTIYEN EEEEECCCCCEEEEC	23.21	28060719
1318	Phosphorylation	YQNTTAMTIYENLAP EECCCCCEEEECCCC	20.24	26356563
1320	Phosphorylation	NTTAMTIYENLAPVT CCCCCEEEECCCCCC	6.92	26356563

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
1311	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1311	Y	Phosphorylation	Kinase	SRC	P12931	PSP
1320	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1320	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF9	Q86YJ5	PMID:19457934

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTND1_HUMAN	CTNND1	physical	12370829
CTNB1_HUMAN	CTNNB1	physical	12370829
SDCB1_HUMAN	SDCBP	physical	12403354
PLCG1_HUMAN	PLCG1	physical	11259588
LAT_HUMAN	LAT	physical	11259588
EGFR_HUMAN	EGFR	physical	19836242
PTPRJ_HUMAN	PTPRJ	physical	19167335
BAP1_HUMAN	BAP1	physical	25640309
CASC3_HUMAN	CASC3	physical	25640309
CP17A_HUMAN	CYP17A1	physical	25640309
ESIP1_HUMAN	EPSTI1	physical	25640309
HXC6_HUMAN	HOXC6	physical	25640309
KLK7_HUMAN	KLK7	physical	25640309
KLK9_HUMAN	KLK9	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
PRD14_HUMAN	PRDM14	physical	25640309
TRI25_HUMAN	TRIM25	physical	25640309
RINT1_HUMAN	RINT1	physical	27880917
CS025_HUMAN	C19orf25	physical	27880917
CAPON_HUMAN	NOS1AP	physical	27880917
CA226_HUMAN	C1orf226	physical	27880917
RFIP1_HUMAN	RAB11FIP1	physical	27880917

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 PTPRJ_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 ANDASN-396, AND MASS SPECTROMETRY.	16335952 [Abstract]