HS3SB_HUMAN - dbPTM
HS3SB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS3SB_HUMAN
UniProt AC Q9Y662
Protein Name Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
Gene Name HS3ST3B1
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate..
Protein Sequence MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPGLLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPDSPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKGLAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERLISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEIDREVVRRLREFYRPFNLKFYQMTGHDFGWD
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
6Phosphorylation--MGQRLSGGRSCLD
--CCCCCCCCCCCCC
41.2029083192
10PhosphorylationQRLSGGRSCLDVPGR
CCCCCCCCCCCCCCC
23.4729083192
79O-linked_GlycosylationHDPPALATAPDGTPP
CCCCCCCCCCCCCCC
39.3055831641
84O-linked_GlycosylationLATAPDGTPPRLPFR
CCCCCCCCCCCCCCC
37.1855831647
96O-linked_GlycosylationPFRAPPATPLASGKE
CCCCCCCCCCCCCHH
25.30OGP
132PhosphorylationISSFFSGSGSKQLPQ
CHHHCCCCCCCCCCE
38.40-
134PhosphorylationSFFSGSGSKQLPQAI
HHCCCCCCCCCCEEE
20.94-
191PhosphorylationYRDLMPRTLDGQITM
HHHHCCCCCCCCEEE
24.2727251275
197PhosphorylationRTLDGQITMEKTPSY
CCCCCCEEEEECCCC
16.0527251275
200AcetylationDGQITMEKTPSYFVT
CCCEEEEECCCCEEE
55.7230589383
201PhosphorylationGQITMEKTPSYFVTR
CCEEEEECCCCEEEC
12.2627251275
203PhosphorylationITMEKTPSYFVTREA
EEEEECCCCEEECCC
36.1129116813
207PhosphorylationKTPSYFVTREAPARI
ECCCCEEECCCCHHH
16.9429116813
232PhosphorylationVVVRDPVTRAISDYT
EEECCHHHHHHHHHH
21.5524670416
258N-linked_GlycosylationFESLTFKNRTAGLID
CCCCCCCCCCCCCEE
42.20UniProtKB CARBOHYD
266PhosphorylationRTAGLIDTSWSAIQI
CCCCCEECCCHHHHH
25.7128387310
267PhosphorylationTAGLIDTSWSAIQIG
CCCCEECCCHHHHHH
18.4528387310
269PhosphorylationGLIDTSWSAIQIGIY
CCEECCCHHHHHHHH
18.4322468782
276PhosphorylationSAIQIGIYAKHLEHW
HHHHHHHHHHHHHHH
12.3722468782
324AcetylationLKRIITDKHFYFNKT
CCEEEECCCCCCCCC
27.287365175
329N-linked_GlycosylationTDKHFYFNKTKGFPC
ECCCCCCCCCCCCCC
39.44UniProtKB 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 HS3SB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS3SB_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 HS3SB_HUMAN !!

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

Oops, there are no PPI records of HS3SB_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HS3SB_HUMAN

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Related Literatures of Post-Translational Modification

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