ARSG_HUMAN - dbPTM
ARSG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARSG_HUMAN
UniProt AC Q96EG1
Protein Name Arylsulfatase G
Gene Name ARSG
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Lysosome . Previously observed endoplasmic reticulum localization is most likely due to folding/maturation problems for overexpressed proteins.
Protein Description Displays arylsulfatase activity at acidic pH with pseudosubstrates, such as p-nitrocatechol sulfate and also, but with lower activity, p-nitrophenyl sulfate and 4-methylumbelliferyl sulfate..
Protein Sequence MGWLFLKVLLAGVSFSGFLYPLVDFCISGKTRGQKPNFVIILADDMGWGDLGANWAETKDTANLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTRNFAVTSVGGLPLNETTLAEVLQQAGYVTGIIGKWHLGHHGSYHPNFRGFDYYFGIPYSHDMGCTDTPGYNHPPCPACPQGDGPSRNLQRDCYTDVALPLYENLNIVEQPVNLSSLAQKYAEKATQFIQRASTSGRPFLLYVALAHMHVPLPVTQLPAAPRGRSLYGAGLWEMDSLVGQIKDKVDHTVKENTFLWFTGDNGPWAQKCELAGSVGPFTGFWQTRQGGSPAKQTTWEGGHRVPALAYWPGRVPVNVTSTALLSVLDIFPTVVALAQASLPQGRRFDGVDVSEVLFGRSQPGHRVLFHPNSGAAGEFGALQTVRLERYKAFYITGGARACDGSTGPELQHKFPLIFNLEDDTAEAVPLERGGAEYQAVLPEVRKVLADVLQDIANDNISSADYTQDPSVTPCCNPYQIACRCQAA
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
69PhosphorylationANLDKMASEGMRFVD
CCHHHHHHHCCCEEE
31.05-
843-oxoalanine (Cys)FHAAASTCSPSRASL
HHHHHCCCCHHHHHH
5.36-
84OxidationFHAAASTCSPSRASL
HHHHHCCCCHHHHHH
5.3618283100
93PhosphorylationPSRASLLTGRLGLRN
HHHHHHHHHCCCCCC
26.0821815630
110PhosphorylationTRNFAVTSVGGLPLN
CCCEEEEEECCCCCC
16.5022210691
117N-linked_GlycosylationSVGGLPLNETTLAEV
EECCCCCCHHCHHHH
42.50UniProtKB CARBOHYD
120PhosphorylationGLPLNETTLAEVLQQ
CCCCCHHCHHHHHHH
20.1422210691
196PhosphorylationRNLQRDCYTDVALPL
CCCCCHHHHCCHHHH
15.4021712546
204PhosphorylationTDVALPLYENLNIVE
HCCHHHHHCCCCCCC
10.7921712546
215N-linked_GlycosylationNIVEQPVNLSSLAQK
CCCCCCCCHHHHHHH
40.67UniProtKB CARBOHYD
218PhosphorylationEQPVNLSSLAQKYAE
CCCCCHHHHHHHHHH
30.7821712546
226UbiquitinationLAQKYAEKATQFIQR
HHHHHHHHHHHHHHH
48.87-
356N-linked_GlycosylationWPGRVPVNVTSTALL
CCCCCCCCCCHHHHH
25.86UniProtKB CARBOHYD
371O-linked_GlycosylationSVLDIFPTVVALAQA
HHHHHHHHHHHHHHC
19.50OGP
379PhosphorylationVVALAQASLPQGRRF
HHHHHHCCCCCCCCC
28.6224719451
451UbiquitinationTGPELQHKFPLIFNL
CCHHHHHCCCEEEEC
35.40-
497N-linked_GlycosylationLQDIANDNISSADYT
HHHHHCCCCCCCCCC
35.53UniProtKB CARBOHYD

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 ARSG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARSG_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 ARSG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMF1_HUMANSUMF1physical
28514442
YDJC_HUMANYDJCphysical
28514442
GSK3A_HUMANGSK3Aphysical
28514442
TM214_HUMANTMEM214physical
28514442
MESD_HUMANMESDC2physical
28514442
CTGE5_HUMANCTAGE5physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
DPH1_HUMANDPH1physical
28514442
IDE_HUMANIDEphysical
28514442
CGRF1_HUMANCGRRF1physical
28514442
GATA_HUMANQRSL1physical
28514442
TOR3A_HUMANTOR3Aphysical
28514442
FBX21_HUMANFBXO21physical
28514442
BACE2_HUMANBACE2physical
28514442
TBB8_HUMANTUBB8physical
28514442
SPCS1_HUMANSPCS1physical
28514442
CALX_HUMANCANXphysical
28514442
E2AK3_HUMANEIF2AK3physical
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 ARSG_HUMAN

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Related Literatures of Post-Translational Modification

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