dbPTM

IGJ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IGJ_HUMAN
UniProt AC	P01591
Protein Name	Immunoglobulin J chain
Gene Name	JCHAIN {ECO:0000312\|HGNC:HGNC:5713}
Organism	Homo sapiens (Human).
Sequence Length	159
Subcellular Localization	Secreted .
Protein Description	Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component..
Protein Sequence	MKNHLLFWGVLAVFIKAVHVKAQEDERIVLVDNKCKCARITSRIIRSSEDPNEDIVERNIRIIVPLNNRENISDPTSPLRTRFVYHLSDLCKKCDPTEVELDNQIVTATQSNICDEDSATETCYTYDRNKCYTAVVPLVYGGETKMVETALTPDACYPD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Ubiquitination	GVLAVFIKAVHVKAQ HHHHHHHHHHHHCCC	32.65	22817900
21	Ubiquitination	FIKAVHVKAQEDERI HHHHHHHCCCCCCCE	29.49	22817900
23	Pyrrolidone_carboxylic_acid	KAVHVKAQEDERIVL HHHHHCCCCCCCEEE	53.62	-
23	Pyrrolidone_carboxylic_acid	KAVHVKAQEDERIVL HHHHHCCCCCCCEEE	53.62	407930
23	Pyrrolidone_carboxylic_acid	KAVHVKAQEDERIVL HHHHHCCCCCCCEEE	53.62	407930
34	Ubiquitination	RIVLVDNKCKCARIT CEEEECCCCHHHHHH	30.52	22817900
36	Ubiquitination	VLVDNKCKCARITSR EEECCCCHHHHHHHH	32.32	22817900
41	Phosphorylation	KCKCARITSRIIRSS CCHHHHHHHHHHHCC	13.34	24719451
47	Phosphorylation	ITSRIIRSSEDPNED HHHHHHHCCCCCCHH	27.89	24719451
48	Phosphorylation	TSRIIRSSEDPNEDI HHHHHHCCCCCCHHH	35.85	23911959
71	N-linked_Glycosylation	VPLNNRENISDPTSP EECCCCCCCCCCCCH	35.51	15084671
71	N-linked_Glycosylation	VPLNNRENISDPTSP EECCCCCCCCCCCCH	35.51	15084671
73	Phosphorylation	LNNRENISDPTSPLR CCCCCCCCCCCCHHH	49.47	29083192
76	Phosphorylation	RENISDPTSPLRTRF CCCCCCCCCHHHHHH	48.22	29083192
77	Phosphorylation	ENISDPTSPLRTRFV CCCCCCCCHHHHHHH	27.59	29083192
88	Phosphorylation	TRFVYHLSDLCKKCD HHHHHHHHHHHHHCC	18.41	27080861
92	Ubiquitination	YHLSDLCKKCDPTEV HHHHHHHHHCCCCEE	64.83	22817900
93	Ubiquitination	HLSDLCKKCDPTEVE HHHHHHHHCCCCEEE	42.76	22817900
97	O-linked_Glycosylation	LCKKCDPTEVELDNQ HHHHCCCCEEECCCE	39.14	OGP
109	O-linked_Glycosylation	DNQIVTATQSNICDE CCEEEEEECCCCCCC	24.14	OGP
130	Ubiquitination	CYTYDRNKCYTAVVP EEECCCCCEEEEEEE	29.52	22817900
145	Ubiquitination	LVYGGETKMVETALT EEECCCCCEEEEECC	36.32	-

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 IGJ_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IGJ_HUMAN !!

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 IGJ_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-71, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.	18780401 [Abstract]
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.	16740002 [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-71, AND MASS SPECTROMETRY.	16335952 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.	15084671 [Abstract]