HS2ST_HUMAN - dbPTM
HS2ST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS2ST_HUMAN
UniProt AC Q7LGA3
Protein Name Heparan sulfate 2-O-sulfotransferase 1
Gene Name HS2ST1
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 the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand-binding interactions and signaling processes. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues (By similarity)..
Protein Sequence MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRSKLERAIARHEVREIEQRHTMDGPRQDATLDEEEDMVIIYNRVPKTASTSFTNIAYDLCAKNKYHVLHINTTKNNPVMSLQDQVRFVKNITSWKEMKPGFYHGHVSYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATELYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
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
58O-linked_GlycosylationREIEQRHTMDGPRQD
HHHHHHHCCCCCCCC
21.10OGP
78PhosphorylationEEDMVIIYNRVPKTA
CCCEEEEECCCCCCC
5.9322817900
101UbiquitinationYDLCAKNKYHVLHIN
HHHHHCCCEEEEEEE
35.71-
102PhosphorylationDLCAKNKYHVLHINT
HHHHCCCEEEEEEEC
13.4222210691
108N-linked_GlycosylationKYHVLHINTTKNNPV
CEEEEEEECCCCCCC
30.83UniProtKB CARBOHYD
109PhosphorylationYHVLHINTTKNNPVM
EEEEEEECCCCCCCC
38.2522210691
110PhosphorylationHVLHINTTKNNPVMS
EEEEEECCCCCCCCC
27.5622210691
123MethylationMSLQDQVRFVKNITS
CCHHHHHHHHHHHCC
25.6324410261
123DimethylationMSLQDQVRFVKNITS
CCHHHHHHHHHHHCC
25.63-
126UbiquitinationQDQVRFVKNITSWKE
HHHHHHHHHHCCHHH
39.66-
127N-linked_GlycosylationDQVRFVKNITSWKEM
HHHHHHHHHCCHHHC
37.15UniProtKB CARBOHYD
164MethylationPIYINVIRDPIERLV
CEEEEEECCHHHHHH
39.09115479677
183PhosphorylationFLRFGDDYRPGLRRR
HHHCCCCCCCCCCCC
24.36-
298UbiquitinationTEKKLPTKQTIAKLQ
CCCCCCCHHHHHHHH
43.4329967540
303UbiquitinationPTKQTIAKLQQSDIW
CCHHHHHHHHHHHHH
42.8729967540
340PhosphorylationREKDGDLYILAQNFF
ECCCCCEEEEEECCH
9.9122817900
348PhosphorylationILAQNFFYEKIYPKS
EEEECCHHHHHCCCC
16.5122817900

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 HS2ST_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS2ST_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 HS2ST_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT12A_HUMANATP12Aphysical
26186194
NMNA3_HUMANNMNAT3physical
26186194
DIAP3_HUMANDIAPH3physical
26186194
CKAP4_HUMANCKAP4physical
26186194
1A02_HUMANHLA-Aphysical
26186194
1A03_HUMANHLA-Aphysical
26186194
1A01_HUMANHLA-Aphysical
26186194
1A26_HUMANHLA-Aphysical
26186194
TBC23_HUMANTBC1D23physical
26186194
DYM_HUMANDYMphysical
26186194
PIGU_HUMANPIGUphysical
26186194
NMNA3_HUMANNMNAT3physical
28514442
SOGA3_HUMANSOGA3physical
28514442
TBC23_HUMANTBC1D23physical
28514442
DIAP3_HUMANDIAPH3physical
28514442
USP9Y_HUMANUSP9Yphysical
28514442
AT12A_HUMANATP12Aphysical
28514442
DYM_HUMANDYMphysical
28514442
CKAP4_HUMANCKAP4physical
28514442
CTR1_HUMANSLC7A1physical
28514442
A4_HUMANAPPphysical
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 HS2ST_HUMAN

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Related Literatures of Post-Translational Modification

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