dbPTM

LGMN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LGMN_HUMAN
UniProt AC	Q99538
Protein Name	Legumain
Gene Name	LGMN
Organism	Homo sapiens (Human).
Sequence Length	433
Subcellular Localization	Lysosome.
Protein Description	Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system..
Protein Sequence	MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTNDLEESRQLTEEIQRHLDARHLIEKSVRKIVSLLAASEAEVEQLLSERAPLTGHSCYPEALLHFRTHCFNWHSPTYEYALRHLYVLVNLCEKPYPLHRIKLSMDHVCLGHY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	O-linked_Glycosylation	WKVAVFLSVALGIGA HHHHHHHHHHHCCCC	8.22	23301498
91	N-linked_Glycosylation	GIVINRPNGTDVYQG CEEEECCCCCCCCCC	63.86	23776206
125	Ubiquitination	RGDAEAVKGIGSGKV HCCHHHHCCCCCCCE	52.43	21906983
125	Ubiquitination	RGDAEAVKGIGSGKV HCCHHHHCCCCCCCE	52.43	21906983
129	Phosphorylation	EAVKGIGSGKVLKSG HHHCCCCCCCEECCC	33.26	-
131	Ubiquitination	VKGIGSGKVLKSGPQ HCCCCCCCEECCCCC	46.20	-
167	N-linked_Glycosylation	DLHVKDLNETIHYMY CCCCCCHHHHHHHHH	55.27	23776206
185	Phosphorylation	MYRKMVFYIEACESG HHHHEEEEEEECCCC	6.09	-
224	Ubiquitination	YACYYDEKRSTYLGD CEEEEECCCCEECCC	49.07	-
224	Ubiquitination	YACYYDEKRSTYLGD CEEEEECCCCEECCC	49.07	-
226	Phosphorylation	CYYDEKRSTYLGDWY EEEECCCCEECCCCE	32.26	-
253	Ubiquitination	LTKETLHKQYHLVKS HHHHHHHHHHCHHHC	56.52	-
263	N-linked_Glycosylation	HLVKSHTNTSHVMQY CHHHCCCCCHHHHEE	33.87	23776206
272	N-linked_Glycosylation	SHVMQYGNKTISTMK HHHHEECCEEEEHHH	33.10	23776206
274	Phosphorylation	VMQYGNKTISTMKVM HHEECCEEEEHHHHH	24.94	-
276	Phosphorylation	QYGNKTISTMKVMQF EECCEEEEHHHHHHH	27.90	-
277	Phosphorylation	YGNKTISTMKVMQFQ ECCEEEEHHHHHHHC	19.70	-
287	Acetylation	VMQFQGMKRKASSPV HHHHCCCCCCCCCCC	58.53	11924495
289	Ubiquitination	QFQGMKRKASSPVPL HHCCCCCCCCCCCCC	47.29	-
305	O-linked_Glycosylation	PVTHLDLTPSPDVPL CCCCCCCCCCCCCCH	22.76	OGP
307	O-linked_Glycosylation	THLDLTPSPDVPLTI CCCCCCCCCCCCHHH	28.62	OGP
316	Ubiquitination	DVPLTIMKRKLMNTN CCCHHHHHHCCCCCC	42.40	21906983
316	Ubiquitination	DVPLTIMKRKLMNTN CCCHHHHHHCCCCCC	42.40	21906983
316	2-Hydroxyisobutyrylation	DVPLTIMKRKLMNTN CCCHHHHHHCCCCCC	42.40	-
318	Ubiquitination	PLTIMKRKLMNTNDL CHHHHHHCCCCCCCH	46.71	21906983
318	Ubiquitination	PLTIMKRKLMNTNDL CHHHHHHCCCCCCCH	46.71	21906983
322	Phosphorylation	MKRKLMNTNDLEESR HHHCCCCCCCHHHHH	19.02	30257219
342	Ubiquitination	IQRHLDARHLIEKSV HHHHHHHHHHHHHHH	25.47	-
347	Ubiquitination	DARHLIEKSVRKIVS HHHHHHHHHHHHHHH	47.45	-
351	Ubiquitination	LIEKSVRKIVSLLAA HHHHHHHHHHHHHHC	45.35	-
406	Phosphorylation	EYALRHLYVLVNLCE HHHHHHHHHHHHHCC	5.89	20068231
414	Ubiquitination	VLVNLCEKPYPLHRI HHHHHCCCCCCCCCE	49.18	-

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
226	S	Phosphorylation	Kinase	SRPK2	P78362	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:24610907

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF6_HUMAN	TRAF6	physical	24610907
U17L2_HUMAN	USP17L2	physical	24610907
PDIA5_HUMAN	PDIA5	physical	26186194
ATG7_HUMAN	ATG7	physical	26186194
HNRH2_HUMAN	HNRNPH2	physical	26344197
PDIA5_HUMAN	PDIA5	physical	28514442
ATG7_HUMAN	ATG7	physical	28514442

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 LGMN_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-91 AND ASN-167, AND MASSSPECTROMETRY.	19159218 [Abstract]