CHSTA_HUMAN - dbPTM
CHSTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHSTA_HUMAN
UniProt AC O43529
Protein Name Carbohydrate sulfotransferase 10
Gene Name CHST10
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis..
Protein Sequence MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDVYSAKQEFLFLTTMPEVRKLPEEKHIPEELKPTGKELPDSQLVQPLVYMERLELIRNVCRDDALKNLSHTPVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSDAEIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRRNRTETRGIQFEDFVRYLGDPNHRWLDLQFGDHIIHWVTYVELCAPCEIMYSVIGHHETLEDDAPYILKEAGIDHLVSYPTIPPGITVYNRTKVEHYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN
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
30UbiquitinationKFITLTFKDPDVYSA
HHHHEECCCCCHHCC
64.2233845483
45O-linked_GlycosylationKQEFLFLTTMPEVRK
CCEEEEEECCHHHHC
17.45OGP
66PhosphorylationIPEELKPTGKELPDS
CCHHHCCCCCCCCHH
60.3424719451
66O-linked_GlycosylationIPEELKPTGKELPDS
CCHHHCCCCCCCCHH
60.3455831019
81PhosphorylationQLVQPLVYMERLELI
HCCHHHHHHHHHHHH
10.8424719451
98UbiquitinationVCRDDALKNLSHTPV
HCCHHHHHCCCCCCC
58.5229967540
99N-linked_GlycosylationCRDDALKNLSHTPVS
CCHHHHHCCCCCCCH
47.85UniProtKB CARBOHYD
101PhosphorylationDDALKNLSHTPVSKF
HHHHHCCCCCCCHHH
34.4123532336
103PhosphorylationALKNLSHTPVSKFVL
HHHCCCCCCCHHHHH
23.2423532336
128UbiquitinationILFCQTPKVGNTQWK
EEEECCCCCCCCCCE
67.19-
177UbiquitinationFSDAEIQKRLKTYFK
CCHHHHHHHHHHHHH
66.42-
228N-linked_GlycosylationIIRKYRRNRTETRGI
HHHHHHCCCCCCCCC
46.34UniProtKB CARBOHYD
316N-linked_GlycosylationPPGITVYNRTKVEHY
CCCEEEECCCCEEEE
40.59UniProtKB CARBOHYD
328PhosphorylationEHYFLGISKRDIRRL
EEEECCCCHHHHHHH
21.60-
348PhosphorylationGDFKLFGYQKPDFLL
CCEEECCCCCCCCCC
13.1622817900
350UbiquitinationFKLFGYQKPDFLLN-
EEECCCCCCCCCCC-
37.76-

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 CHSTA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHSTA_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 CHSTA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSF1_HUMANHSF1physical
21988832
PON2_HUMANPON2physical
26186194
PPM1A_HUMANPPM1Aphysical
26186194
H6ST2_HUMANHS6ST2physical
26186194
NPTX1_HUMANNPTX1physical
26186194
PARL_HUMANPARLphysical
26186194
DPB1_HUMANHLA-DPB1physical
26186194
SGPP1_HUMANSGPP1physical
26186194
PARL_HUMANPARLphysical
28514442
NPTX1_HUMANNPTX1physical
28514442
PON2_HUMANPON2physical
28514442
PPM1A_HUMANPPM1Aphysical
28514442
SGPP1_HUMANSGPP1physical
28514442
S22AI_HUMANSLC22A18physical
28514442
B4GA1_HUMANB4GAT1physical
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 CHSTA_HUMAN

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Related Literatures of Post-Translational Modification

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