CHSTC_HUMAN - dbPTM
CHSTC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHSTC_HUMAN
UniProt AC Q9NRB3
Protein Name Carbohydrate sulfotransferase 12
Gene Name CHST12
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor..
Protein Sequence MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDRELTADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQQAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKRVMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTKFLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSFANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDRQLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
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
72UbiquitinationDVDEFLDKFLSAGVK
CHHHHHHHHHHHCCC
50.80-
75PhosphorylationEFLDKFLSAGVKQSD
HHHHHHHHHCCCHHH
26.55-
79UbiquitinationKFLSAGVKQSDLPRK
HHHHHCCCHHHCCCC
43.07-
86UbiquitinationKQSDLPRKETEQPPA
CHHHCCCCCCCCCCC
68.03-
88O-linked_GlycosylationSDLPRKETEQPPAPG
HHCCCCCCCCCCCCC
42.8555828457
96PhosphorylationEQPPAPGSMEESVRG
CCCCCCCCHHHHHCC
23.2024505115
97SulfoxidationQPPAPGSMEESVRGY
CCCCCCCHHHHHCCC
9.0821406390
107PhosphorylationSVRGYDWSPRDARRS
HHCCCCCCHHHHCCC
13.7324719451
134N-linked_GlycosylationVLRGFCANSSLAFPT
HHHHHHCCCCCCCCC
33.06UniProtKB CARBOHYD
142UbiquitinationSSLAFPTKERAFDDI
CCCCCCCCCCCCCCC
45.50-
172UbiquitinationAIYCYVPKVACTNWK
EEEEEECHHHCCCCE
32.21-
209N-linked_GlycosylationIPREHVHNASAHLTF
CCHHHHCCCHHHHHH
34.21UniProtKB CARBOHYD
240UbiquitinationVKLKKYTKFLFVRDP
HHHHHCCEEEEECCH
36.66-
253PhosphorylationDPFVRLISAFRSKFE
CHHHHHHHHHHHHCC
26.4124719451
258UbiquitinationLISAFRSKFELENEE
HHHHHHHHCCCCCHH
38.30-
280N-linked_GlycosylationPMLRLYANHTSLPAS
HHHHHHCCCCCCCHH
25.97UniProtKB CARBOHYD
282PhosphorylationLRLYANHTSLPASAR
HHHHCCCCCCCHHHH
31.5922210691
283PhosphorylationRLYANHTSLPASARE
HHHCCCCCCCHHHHH
25.4622210691
370N-linked_GlycosylationRFPPSYRNRTASSWE
CCCHHHCCCCCCCCC
37.10UniProtKB CARBOHYD
396PhosphorylationRQQLYKLYEADFVLF
HHHHHHHHHCCEEEE
12.62-
405PhosphorylationADFVLFGYPKPENLL
CCEEEECCCCHHHHC
10.76-

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 CHSTC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHSTC_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 CHSTC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UGGG1_HUMANUGGT1physical
17353931
ATP23_HUMANXRCC6BP1physical
28514442
RMND1_HUMANRMND1physical
28514442
FBX2_HUMANFBXO2physical
28514442
PON2_HUMANPON2physical
28514442
SSRP1_HUMANSSRP1physical
28514442
MD2L2_HUMANMAD2L2physical
28514442
SE1L1_HUMANSEL1Lphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHSTC_HUMAN

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Related Literatures of Post-Translational Modification

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