ARSA_HUMAN - dbPTM
ARSA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARSA_HUMAN
UniProt AC P15289
Protein Name Arylsulfatase A
Gene Name ARSA
Organism Homo sapiens (Human).
Sequence Length 507
Subcellular Localization Endoplasmic reticulum . Lysosome .
Protein Description Hydrolyzes cerebroside sulfate..
Protein Sequence MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA
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
693-oxoalanine (Cys)FYVPVSLCTPSRAAL
EEEEHHHCCCCHHHH		4.02-
69OxidationFYVPVSLCTPSRAAL
EEEEHHHCCCCHHHH		4.029342345
158N-linked_GlycosylationHDQGPCQNLTCFPPA
CCCCCCCCCEECCCC		43.99UniProtKB CARBOHYD
160N-linked_GlycosylationQGPCQNLTCFPPATP
CCCCCCCEECCCCCC		21.4619159218
160N-linked_GlycosylationQGPCQNLTCFPPATP
CCCCCCCEECCCCCC		21.4619159218
184N-linked_GlycosylationVPIPLLANLSVEAQP
CCCCEEECCCEECCC		32.5812888274
186N-linked_GlycosylationIPLLANLSVEAQPPW
CCEEECCCEECCCCC		20.0912888274
186N-linked_GlycosylationIPLLANLSVEAQPPW
CCEEECCCEECCCCC		20.0912888274
237PhosphorylationYPQFSGQSFAERSGR
CCCCCCCCHHHHHCC		29.9226091039
291MethylationPETMRMSRGGCSGLL
HHHEEECCCCCCCCE		35.86-
293MethylationTMRMSRGGCSGLLRC
HEEECCCCCCCCEEC		10.99-
350N-linked_GlycosylationLAGAPLPNVTLDGFD
HCCCCCCCCEECCCC		47.2719159218
352N-linked_GlycosylationGAPLPNVTLDGFDLS
CCCCCCCEECCCCCC		26.2719159218
352N-linked_GlycosylationGAPLPNVTLDGFDLS
CCCCCCCEECCCCCC		26.2719159218
409O-linked_GlycosylationGSAHSDTTADPACHA
CCCCCCCCCCHHCCC		33.77OGP
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 ARSA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARSA_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 ARSA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARSA_HUMANARSAphysical
9521684
CETN2_HUMANCETN2physical
21988832
PPIC_HUMANPPICphysical
21988832
PCH2_HUMANTRIP13physical
25416956
SUMF1_HUMANSUMF1physical
26186194
GALNS_HUMANGALNSphysical
26186194
MESD_HUMANMESDC2physical
26186194
ZBT43_HUMANZBTB43physical
26186194
PDIA5_HUMANPDIA5physical
26186194
PPOX_HUMANPPOXphysical
26186194
GFPT2_HUMANGFPT2physical
26186194
PCH2_HUMANTRIP13physical
21516116
SUMF1_HUMANSUMF1physical
28514442
ZBT43_HUMANZBTB43physical
28514442
GALNS_HUMANGALNSphysical
28514442
MESD_HUMANMESDC2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
250100Leukodystrophy metachromatic (MLD)
272200Multiple sulfatase deficiency (MSD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARSA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of a covalent intermediate of endogenous humanarylsulfatase A.";
Chruszcz M., Laidler P., Monkiewicz M., Ortlund E., Lebioda L.,Lewinski K.;
J. Inorg. Biochem. 96:386-392(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 19-507, SUBUNIT,GLYCOSYLATION AT ASN-158 AND ASN-184, ACTIVE SITE, ENZYME REGULATION,CALCIUM-BINDING, AND COFACTOR.
"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-158 AND ASN-350, AND MASSSPECTROMETRY.

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