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Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 5

Gene

HS3ST5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and 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.1 Publication

Catalytic activityi

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei183PAPSBy similarity1
Binding sitei191PAPSBy similarity1
Binding sitei293PAPSBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi100 – 104PAPSBy similarity5
Nucleotide bindingi309 – 313PAPSBy similarity5

GO - Molecular functioni

  • [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Source: UniProtKB
  • 3'-phosphoadenosine 5'-phosphosulfate binding Source: UniProtKB

GO - Biological processi

  • glycosaminoglycan biosynthetic process Source: Reactome
  • heparan sulfate proteoglycan biosynthetic process, enzymatic modification Source: UniProtKB
  • negative regulation of coagulation Source: UniProtKB
  • protein sulfation Source: UniProtKB
  • regulation of viral entry into host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciZFISH:HS16520-MONOMER.
ReactomeiR-HSA-2022928. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparan sulfate glucosamine 3-O-sulfotransferase 5 (EC:2.8.2.23)
Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5
Short name:
3-OST-5
Short name:
Heparan sulfate 3-O-sulfotransferase 5
Short name:
h3-OST-5
Gene namesi
Name:HS3ST5
Synonyms:3OST5, HS3OST5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:19419. HS3ST5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini33 – 346LumenalSequence analysisAdd BLAST314

GO - Cellular componenti

  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi99R → A: Reduces enzyme activity by over 99%. 1 Publication1
Mutagenesisi104R → A: Reduces enzyme activity by 93%,. 1 Publication1
Mutagenesisi155K → A: Reduces enzyme activity by over 99%. 1 Publication1
Mutagenesisi195Q → A: Reduces enzyme activity by over 99%. 1 Publication1
Mutagenesisi309K → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi311R → A: Reduces enzyme activity by 98%. 1 Publication1

Organism-specific databases

DisGeNETi222537.
OpenTargetsiENSG00000249853.
PharmGKBiPA164741639.

Polymorphism and mutation databases

BioMutaiHS3ST5.
DMDMi61214369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000852221 – 346Heparan sulfate glucosamine 3-O-sulfotransferase 5Add BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi287N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi294 ↔ 304By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8IZT8.
PRIDEiQ8IZT8.

PTM databases

iPTMnetiQ8IZT8.
PhosphoSitePlusiQ8IZT8.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle and fetal brain, and also found in adult brain, spinal cord, cerebellum and colon.2 Publications

Gene expression databases

BgeeiENSG00000249853.
CleanExiHS_HS3ST5.
GenevisibleiQ8IZT8. HS.

Organism-specific databases

HPAiHPA021823.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000427888.

Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi92 – 97Combined sources6
Helixi103 – 110Combined sources8
Beta strandi116 – 118Combined sources3
Helixi129 – 133Combined sources5
Helixi136 – 140Combined sources5
Beta strandi151 – 155Combined sources5
Helixi157 – 160Combined sources4
Helixi165 – 172Combined sources8
Beta strandi177 – 182Combined sources6
Helixi185 – 202Combined sources18
Helixi210 – 214Combined sources5
Turni217 – 219Combined sources3
Helixi227 – 231Combined sources5
Helixi234 – 242Combined sources9
Helixi247 – 249Combined sources3
Beta strandi250 – 254Combined sources5
Helixi255 – 260Combined sources6
Helixi262 – 272Combined sources11
Helixi281 – 283Combined sources3
Beta strandi284 – 287Combined sources4
Turni288 – 291Combined sources4
Beta strandi292 – 296Combined sources5
Beta strandi298 – 300Combined sources3
Helixi318 – 339Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BD9X-ray2.30A88-346[»]
ProteinModelPortaliQ8IZT8.
SMRiQ8IZT8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IZT8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 128Substrate bindingBy similarity7
Regioni155 – 158Substrate bindingBy similarity4
Regioni226 – 227Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3704. Eukaryota.
ENOG410XS59. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ8IZT8.
KOiK08104.
OMAiGRTFNWP.
OrthoDBiEOG091G0CS5.
PhylomeDBiQ8IZT8.
TreeFamiTF350755.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8IZT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFKQQAWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPIEGRLGGA
60 70 80 90 100
RTQAEFPLRA LQFKRGLLHE FRKGNASKEQ VRLHDLVQQL PKAIIIGVRK
110 120 130 140 150
GGTRALLEML NLHPAVVKAS QEIHFFDNDE NYGKGIEWYR KKMPFSYPQQ
160 170 180 190 200
ITIEKSPAYF ITEEVPERIY KMNSSIKLLI IVREPTTRAI SDYTQVLEGK
210 220 230 240 250
ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER WLKYFPIEQF
260 270 280 290 300
HVVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII
310 320 330 340
FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP
Length:346
Mass (Da):40,408
Last modified:March 1, 2003 - v1
Checksum:iC763F70793FDB156
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052531247I → N.Corresponds to variant rs17793043dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503292 mRNA. Translation: AAN37737.1.
AK091074 mRNA. No translation available.
AK289907 mRNA. Translation: BAF82596.1.
CH471051 Genomic DNA. Translation: EAW48251.1.
BC093911 mRNA. Translation: AAH93911.1.
BC093913 mRNA. Translation: AAH93913.1.
CCDSiCCDS34517.1.
RefSeqiNP_705840.2. NM_153612.3.
XP_006715442.1. XM_006715379.2.
XP_011533890.1. XM_011535588.2.
XP_016865959.1. XM_017010470.1.
XP_016865960.1. XM_017010471.1.
XP_016865961.1. XM_017010472.1.
XP_016865962.1. XM_017010473.1.
XP_016865963.1. XM_017010474.1.
UniGeneiHs.645477.

Genome annotation databases

EnsembliENST00000312719; ENSP00000427888; ENSG00000249853.
ENST00000411826; ENSP00000440332; ENSG00000249853.
GeneIDi222537.
KEGGihsa:222537.
UCSCiuc003pwg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503292 mRNA. Translation: AAN37737.1.
AK091074 mRNA. No translation available.
AK289907 mRNA. Translation: BAF82596.1.
CH471051 Genomic DNA. Translation: EAW48251.1.
BC093911 mRNA. Translation: AAH93911.1.
BC093913 mRNA. Translation: AAH93913.1.
CCDSiCCDS34517.1.
RefSeqiNP_705840.2. NM_153612.3.
XP_006715442.1. XM_006715379.2.
XP_011533890.1. XM_011535588.2.
XP_016865959.1. XM_017010470.1.
XP_016865960.1. XM_017010471.1.
XP_016865961.1. XM_017010472.1.
XP_016865962.1. XM_017010473.1.
XP_016865963.1. XM_017010474.1.
UniGeneiHs.645477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BD9X-ray2.30A88-346[»]
ProteinModelPortaliQ8IZT8.
SMRiQ8IZT8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000427888.

PTM databases

iPTMnetiQ8IZT8.
PhosphoSitePlusiQ8IZT8.

Polymorphism and mutation databases

BioMutaiHS3ST5.
DMDMi61214369.

Proteomic databases

PaxDbiQ8IZT8.
PRIDEiQ8IZT8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312719; ENSP00000427888; ENSG00000249853.
ENST00000411826; ENSP00000440332; ENSG00000249853.
GeneIDi222537.
KEGGihsa:222537.
UCSCiuc003pwg.4. human.

Organism-specific databases

CTDi222537.
DisGeNETi222537.
GeneCardsiHS3ST5.
HGNCiHGNC:19419. HS3ST5.
HPAiHPA021823.
MIMi609407. gene.
neXtProtiNX_Q8IZT8.
OpenTargetsiENSG00000249853.
PharmGKBiPA164741639.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3704. Eukaryota.
ENOG410XS59. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ8IZT8.
KOiK08104.
OMAiGRTFNWP.
OrthoDBiEOG091G0CS5.
PhylomeDBiQ8IZT8.
TreeFamiTF350755.

Enzyme and pathway databases

BioCyciZFISH:HS16520-MONOMER.
ReactomeiR-HSA-2022928. HS-GAG biosynthesis.

Miscellaneous databases

EvolutionaryTraceiQ8IZT8.
GenomeRNAii222537.
PROiQ8IZT8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000249853.
CleanExiHS_HS3ST5.
GenevisibleiQ8IZT8. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHS3S5_HUMAN
AccessioniPrimary (citable) accession number: Q8IZT8
Secondary accession number(s): A8K1J2, Q52LI2, Q8N285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.