PPAL_HUMAN - dbPTM
PPAL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPAL_HUMAN
UniProt AC P11117
Protein Name Lysosomal acid phosphatase
Gene Name ACP2
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Lysosome membrane
Single-pass membrane protein
Lumenal side . Lysosome lumen. The soluble form arises by proteolytic processing of the membrane-bound form.
Protein Description
Protein Sequence MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEEWPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAGLFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESSRNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSFRFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVYNGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLRLTEPVVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGEDHA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
46PhosphorylationLYRHGDRSPVKTYPK
HHHCCCCCCCCCCCC
38.4930576142
50PhosphorylationGDRSPVKTYPKDPYQ
CCCCCCCCCCCCCCC
45.3430576142
53UbiquitinationSPVKTYPKDPYQEEE
CCCCCCCCCCCCCCC
62.00-
92N-linked_GlycosylationQRYHGFLNTSYHRQE
HHHHCCCCCCCCCEE
25.3919159218
133N-linked_GlycosylationGMQRFNPNISWQPIP
CCCCCCCCCCCCCCC
41.8719159218
143O-linked_GlycosylationWQPIPVHTVPITEDR
CCCCCCEEEECCCCC
28.36OGP
153UbiquitinationITEDRLLKFPLGPCP
CCCCCCCCCCCCCCC
49.91-
162PhosphorylationPLGPCPRYEQLQNET
CCCCCCCHHHHHHHC
7.9930576142
167N-linked_GlycosylationPRYEQLQNETRQTPE
CCHHHHHHHCCCCHH
62.2919159218
175PhosphorylationETRQTPEYQNESSRN
HCCCCHHHCCHHHHH
20.1730576142
177N-linked_GlycosylationRQTPEYQNESSRNAQ
CCCHHHCCHHHHHHH
50.6619159218
179PhosphorylationTPEYQNESSRNAQFL
CHHHCCHHHHHHHHH
41.9930576142
180PhosphorylationPEYQNESSRNAQFLD
HHHCCHHHHHHHHHH
24.3130576142
191N-linked_GlycosylationQFLDMVANETGLTDL
HHHHHHHHHCCCCCC
35.633056714
2362-HydroxyisobutyrylationMQRLSRLKDFSFRFL
HHHHHHHHHHHHHHH
56.47-
239PhosphorylationLSRLKDFSFRFLFGI
HHHHHHHHHHHHHHH
26.1624719451
267N-linked_GlycosylationLLAQIRKNLTLMATT
HHHHHHHCCEEEEEC
28.5419159218
269PhosphorylationAQIRKNLTLMATTSQ
HHHHHCCEEEEECCC
24.7129978859
273PhosphorylationKNLTLMATTSQLPKL
HCCEEEEECCCCCCC
17.0229978859
274PhosphorylationNLTLMATTSQLPKLL
CCEEEEECCCCCCCH
12.6329978859
275PhosphorylationLTLMATTSQLPKLLV
CEEEEECCCCCCCHH
25.9324706070
322N-linked_GlycosylationLYQEDSGNFSVEMYF
EEECCCCCEEEEEEE
29.943056714
331N-linked_GlycosylationSVEMYFRNESDKAPW
EEEEEEECCCCCCCC
43.1319159218

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 PPAL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPAL_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 PPAL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UCRI_HUMANUQCRFS1physical
22939629

Drug and Disease Associations
Kegg Disease
H01113 Acid phosphatase deficiency
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 PPAL_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-92; ASN-133; ASN-167;ASN-177; ASN-267 AND ASN-331, AND MASS SPECTROMETRY.

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