SPHM_HUMAN - dbPTM
SPHM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPHM_HUMAN
UniProt AC P51688
Protein Name N-sulphoglucosamine sulphohydrolase
Gene Name SGSH
Organism Homo sapiens (Human).
Sequence Length 502
Subcellular Localization Lysosome .
Protein Description Catalyzes a step in lysosomal heparan sulfate degradation..
Protein Sequence MSCPVPACCALLLVLGLCRARPRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENGSVLQVGRNITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFGNGESGMGRIPDWTPQAYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIHLTGRSLLPALEAEPLWATVFGSQSHHEVTMSYPMRSVQHRHFRLVHNLNFKMPFPIDQDFYVSPTFQDLLNRTTAGQPTGWYKDLRHYYYRARWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWETHDPWVCAPDGVLEEKLSPQCQPLHNEL
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
41N-linked_GlycosylationGFESGAYNNSAIATP
CCCCCCCCCCCCCCC
35.1312754519
703-oxoalanine (Cys)AFTSVSSCSPSRASL
CCCCHHHCCHHHHHH
5.59-
70OxidationAFTSVSSCSPSRASL
CCCCHHHCCHHHHHH
5.5924816101
89PhosphorylationPQHQNGMYGLHQDVH
CHHCCCCCCCCCCCC
20.2425627689
103UbiquitinationHHFNSFDKVRSLPLL
CCCCCHHHHHHHHHH
37.2221890473
123UbiquitinationVRTGIIGKKHVGPET
CCCCCCCCCCCCCCC
29.3332015554
142N-linked_GlycosylationDFAYTEENGSVLQVG
CEEEECCCCCEEEEC
41.63UniProtKB CARBOHYD
151N-linked_GlycosylationSVLQVGRNITRIKLL
CEEEECCCHHHHHHH
33.7724816101
174PhosphorylationDDRPFFLYVAFHDPH
CCCCEEEEEEECCCC
5.65-
240PhosphorylationRADLAAQYTTVGRMD
HHHHHHHHCCCCCCH
10.3129759185
241PhosphorylationADLAAQYTTVGRMDQ
HHHHHHHCCCCCCHH
11.70-
264N-linked_GlycosylationLRDAGVLNDTLVIFT
HHHCCCCCCEEEEEE
37.5012754519
264N-linked_GlycosylationLRDAGVLNDTLVIFT
HHHCCCCCCEEEEEE
37.5012754519
303UbiquitinationVSSPEHPKRWGQVSE
ECCCCCCCHHHCCHH
63.7921890473
330PhosphorylationLDWFSIPYPSYAIFG
HHHHCCCCCCEEECC
11.79-
332PhosphorylationWFSIPYPSYAIFGSK
HHCCCCCCEEECCCE
22.7323879269
333PhosphorylationFSIPYPSYAIFGSKT
HCCCCCCEEECCCEE
10.1423879269
407PhosphorylationQDFYVSPTFQDLLNR
CCEEECCHHHHHHHC
26.82-
413N-linked_GlycosylationPTFQDLLNRTTAGQP
CHHHHHHHCCCCCCC
46.6924816101
425UbiquitinationGQPTGWYKDLRHYYY
CCCCCHHHHHHHHHH
43.7221890473
448PhosphorylationRSRDPHETQNLATDP
CCCCHHHHCCCCCCH
21.5228851738
453PhosphorylationHETQNLATDPRFAQL
HHHCCCCCCHHHHHH
50.1028851738

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 SPHM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPHM_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 SPHM_HUMAN !!

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

Oops, there are no PPI records of SPHM_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
252900Mucopolysaccharidosis 3A (MPS3A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPHM_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-41 AND ASN-413, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-41 AND ASN-264.

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