dbPTM

IDUA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IDUA_HUMAN
UniProt AC	P35475
Protein Name	Alpha-L-iduronidase
Gene Name	IDUA
Organism	Homo sapiens (Human).
Sequence Length	653
Subcellular Localization	Lysosome.
Protein Description
Protein Sequence	MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
110	N-linked_Glycosylation	TGRGLSYNFTHLDGY CCCCCEEECEEHHHH	31.78	24036510
158	Phosphorylation	EWKDLVSSLARRYIG HHHHHHHHHHHHHHH	20.69	24719451
190	N-linked_Glycosylation	PDHHDFDNVSMTMQG CCCCCCCCCCEEHHH	27.96	UniProtKB CARBOHYD
336	N-linked_Glycosylation	HQNLLLANTTSAFPY CCCEEECCCCCCCCC	43.81	UniProtKB CARBOHYD
372	N-linked_Glycosylation	LTARFQVNNTRPPHV EEEEEEECCCCCCCC	33.11	24036510
415	N-linked_Glycosylation	AGTVLDSNHTVGVLA CCCCCCCCCCEEEEE	34.22	24036510
451	N-linked_Glycosylation	DDTRAHPNRSVAVTL CCCCCCCCCEEEEEE	38.70	23959878
475	Phosphorylation	GLVYVTRYLDNGLCS CEEEEEEECCCCCCC	14.72	-

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 IDUA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
372	N	Glycosylation		24036510
N-glycosylation at Asn-372 contributes to substrate binding and is required for full enzymatic activity.

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 IDUA_HUMAN !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607014	Mucopolysaccharidosis 1H (MPS1H)
607015	Mucopolysaccharidosis 1H/S (MPS1H/S)
607016	Mucopolysaccharidosis 1S (MPS1S)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IDUA_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-110, AND MASSSPECTROMETRY.	19159218 [Abstract]