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Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 1

Gene

Hs3st1

Organism
Mus musculus (Mouse)
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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei151PAPS1 Publication1
Binding sitei159PAPS1 Publication1
Binding sitei259PAPS1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi68 – 72PAPS1 Publication5
Nucleotide bindingi274 – 278PAPS1 Publication5

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.2.23. 3474.
ReactomeiR-MMU-2022928. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparan sulfate glucosamine 3-O-sulfotransferase 1 (EC:2.8.2.23)
Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1
Short name:
Heparan sulfate 3-O-sulfotransferase 1
Gene namesi
Name:Hs3st1
Synonyms:3ost, 3ost1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1201606. Hs3st1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67R → E or A: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi68K → A: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi72R → A or E: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi76E → A or Q: Strongly decreases the enzymatic activity. 1 Publication1
Mutagenesisi88E → A: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi89N → A or D: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi90E → Q or A: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi92H → F or A: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi95D → A or N: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi96W → A or F: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi98E → A: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi123K → A: Abolishes the enzymatic activity. 1 Publication1
Mutagenesisi132K → A: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi163Q → A: Strongly decreases the enzymatic activity. 1 Publication1
Mutagenesisi197R → A: Weakly decrease the enzymatic activity. 1 Publication1
Mutagenesisi271H → A: No effect. 1 Publication1
Mutagenesisi271H → F: Decreases the enzymatic activity. 1 Publication1
Mutagenesisi273S → A: Weakly decrease the enzymatic activity. 1 Publication1
Mutagenesisi274K → A: Strongly decrease the enzymatic activity. 1 Publication1
Mutagenesisi276R → A: Abolishes the enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000003345221 – 311Heparan sulfate glucosamine 3-O-sulfotransferase 1Add BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi196N-linked (GlcNAc...)Sequence analysis1
Glycosylationi246N-linked (GlcNAc...)Sequence analysis1
Glycosylationi253N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi260 ↔ 2691 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO35310.
PRIDEiO35310.

PTM databases

PhosphoSitePlusiO35310.

Expressioni

Gene expression databases

BgeeiENSMUSG00000051022.
ExpressionAtlasiO35310. baseline and differential.
GenevisibleiO35310. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051055.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 63Combined sources4
Helixi71 – 78Combined sources8
Beta strandi84 – 86Combined sources3
Turni93 – 95Combined sources3
Helixi97 – 100Combined sources4
Helixi104 – 109Combined sources6
Beta strandi119 – 123Combined sources5
Helixi125 – 127Combined sources3
Helixi133 – 140Combined sources8
Beta strandi145 – 150Combined sources6
Helixi153 – 170Combined sources18
Helixi178 – 182Combined sources5
Helixi193 – 197Combined sources5
Helixi200 – 208Combined sources9
Helixi213 – 215Combined sources3
Beta strandi216 – 220Combined sources5
Helixi221 – 226Combined sources6
Helixi228 – 238Combined sources11
Helixi247 – 249Combined sources3
Beta strandi250 – 253Combined sources4
Turni254 – 257Combined sources4
Beta strandi258 – 263Combined sources6
Beta strandi266 – 268Combined sources3
Helixi283 – 304Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VKJX-ray2.50A/B/C48-311[»]
3UANX-ray1.84A/B48-311[»]
ProteinModelPortaliO35310.
SMRiO35310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35310.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3704. Eukaryota.
ENOG410XS59. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiO35310.
KOiK01024.
OMAiFHEPNKK.
OrthoDBiEOG091G0CS5.
PhylomeDBiO35310.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLLLGAVL LVAQPQLVHS HPAAPGPGLK QQELLRKVII LPEDTGEGTA
60 70 80 90 100
SNGSTQQLPQ TIIIGVRKGG TRALLEMLSL HPDVAAAENE VHFFDWEEHY
110 120 130 140 150
SQGLGWYLTQ MPFSSPHQLT VEKTPAYFTS PKVPERIHSM NPTIRLLLIL
160 170 180 190 200
RDPSERVLSD YTQVLYNHLQ KHKPYPPIED LLMRDGRLNL DYKALNRSLY
210 220 230 240 250
HAHMLNWLRF FPLGHIHIVD GDRLIRDPFP EIQKVERFLK LSPQINASNF
260 270 280 290 300
YFNKTKGFYC LRDSGKDRCL HESKGRAHPQ VDPKLLDKLH EYFHEPNKKF
310
FKLVGRTFDW H
Length:311
Mass (Da):35,899
Last modified:January 1, 1998 - v1
Checksum:i7DCFAC494C838FD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019385 mRNA. Translation: AAB84387.1.
AK087753 mRNA. Translation: BAC39991.1.
BC009133 mRNA. Translation: AAH09133.1.
CCDSiCCDS19257.1.
RefSeqiNP_034604.1. NM_010474.2.
XP_017176175.1. XM_017320686.1.
UniGeneiMm.12559.

Genome annotation databases

EnsembliENSMUST00000053116; ENSMUSP00000051055; ENSMUSG00000051022.
ENSMUST00000117944; ENSMUSP00000113919; ENSMUSG00000051022.
GeneIDi15476.
KEGGimmu:15476.
UCSCiuc008xgy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019385 mRNA. Translation: AAB84387.1.
AK087753 mRNA. Translation: BAC39991.1.
BC009133 mRNA. Translation: AAH09133.1.
CCDSiCCDS19257.1.
RefSeqiNP_034604.1. NM_010474.2.
XP_017176175.1. XM_017320686.1.
UniGeneiMm.12559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VKJX-ray2.50A/B/C48-311[»]
3UANX-ray1.84A/B48-311[»]
ProteinModelPortaliO35310.
SMRiO35310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051055.

PTM databases

PhosphoSitePlusiO35310.

Proteomic databases

PaxDbiO35310.
PRIDEiO35310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053116; ENSMUSP00000051055; ENSMUSG00000051022.
ENSMUST00000117944; ENSMUSP00000113919; ENSMUSG00000051022.
GeneIDi15476.
KEGGimmu:15476.
UCSCiuc008xgy.2. mouse.

Organism-specific databases

CTDi9957.
MGIiMGI:1201606. Hs3st1.

Phylogenomic databases

eggNOGiKOG3704. Eukaryota.
ENOG410XS59. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiO35310.
KOiK01024.
OMAiFHEPNKK.
OrthoDBiEOG091G0CS5.
PhylomeDBiO35310.
TreeFamiTF350755.

Enzyme and pathway databases

BRENDAi2.8.2.23. 3474.
ReactomeiR-MMU-2022928. HS-GAG biosynthesis.

Miscellaneous databases

EvolutionaryTraceiO35310.
PROiO35310.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000051022.
ExpressionAtlasiO35310. baseline and differential.
GenevisibleiO35310. MM.

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 nameiHS3S1_MOUSE
AccessioniPrimary (citable) accession number: O35310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.