Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heparan sulfate 2-O-sulfotransferase 1

Gene

HS2ST1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1401 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

ReactomeiR-GGA-2022928. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparan sulfate 2-O-sulfotransferase 1 (EC:2.8.2.-)
Short name:
cHS2ST
Gene namesi
Name:HS2ST1
Synonyms:HS2ST
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 8

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini29 – 356LumenalSequence analysisAdd BLAST328

GO - Cellular componenti

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80R → A: Less than 10% activity toward polysaccharide substrates. 1 Publication1
Mutagenesisi94Y → A: Preferentially transfers sulfates to IdoA units. 1 Publication1
Mutagenesisi106H → A: Preferentially transfers sulfates to IdoA units. 1 Publication1
Mutagenesisi140H → A: Complete loss of activity; when associated with Ala-142. 1 Publication1
Mutagenesisi142H → A: Complete loss of activity; when associated with Ala-140. 1 Publication1
Mutagenesisi189R → A: Only transfers sulfates to GlcA moieties within the polysaccharide. 1 Publication1
Mutagenesisi288R → A: Less than 10% activity toward polysaccharide substrates. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002076771 – 356Heparan sulfate 2-O-sulfotransferase 1Add BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi108N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi201 ↔ 2091 Publication
Disulfide bondi222 ↔ 2281 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ76KB1.

Expressioni

Tissue specificityi

Expressed in heart, limb, head and trunk. At stages 20 and 24, it is expressed in the most regions of the first and second pharyngeal arche. In both wing and leg buds, it is detected at the overlying ectoderm and mesenchyme throughout stages 21, 23 and 24.1 Publication

Gene expression databases

ExpressionAtlasiQ76KB1. baseline.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

DIPiDIP-48642N.
STRINGi9031.ENSGALP00000010096.

Structurei

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi75 – 78Combined sources4
Beta strandi82 – 85Combined sources4
Helixi86 – 100Combined sources15
Beta strandi103 – 107Combined sources5
Helixi110 – 112Combined sources3
Helixi118 – 130Combined sources13
Helixi132 – 134Combined sources3
Beta strandi136 – 142Combined sources7
Helixi148 – 151Combined sources4
Beta strandi158 – 163Combined sources6
Helixi166 – 179Combined sources14
Beta strandi181 – 184Combined sources4
Helixi198 – 203Combined sources6
Helixi211 – 213Combined sources3
Helixi217 – 222Combined sources6
Helixi226 – 229Combined sources4
Helixi234 – 246Combined sources13
Beta strandi248 – 253Combined sources6
Helixi254 – 256Combined sources3
Helixi257 – 267Combined sources11
Helixi269 – 272Combined sources4
Helixi275 – 280Combined sources6
Beta strandi290 – 292Combined sources3
Helixi298 – 304Combined sources7
Helixi308 – 329Combined sources22
Beta strandi332 – 335Combined sources4
Beta strandi338 – 341Combined sources4
Beta strandi348 – 352Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F5FX-ray2.65A69-356[»]
4NDZX-ray3.45A/B/C/D/E/F69-356[»]
ProteinModelPortaliQ76KB1.
SMRiQ76KB1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ76KB1.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 3 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3922. Eukaryota.
ENOG410XTA1. LUCA.
HOGENOMiHOG000220833.
HOVERGENiHBG053202.
InParanoidiQ76KB1.
KOiK02513.
PhylomeDBiQ76KB1.
TreeFamiTF315238.

Family and domain databases

InterProiView protein in InterPro
IPR007734. Heparan_SO4_2-O-STrfase.
IPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
PANTHERiPTHR12129. PTHR12129. 1 hit.
PfamiView protein in Pfam
PF03567. Sulfotransfer_2. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q76KB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLRIMLPP KLQLLAVLVF GVAVLFLENQ IQKLEESRGK LERAIARHEV
60 70 80 90 100
REIEQRHTAD GPRQEVALDE EDDVVIIYNR VPKTASTSFT NIAYDLCAKN
110 120 130 140 150
RYHVLHINTT KNNPVMSLQD QVRFVKNVTS WKEMKPGFYH GHVSYLDFAK
160 170 180 190 200
FGVKKKPIYI NVIRDPIERL VSYYYFLRFG DDYRPGLRRR KQGDKKTFDE
210 220 230 240 250
CVAAGGSDCA PEKLWLQIPF FCGHSSECWN VGSRWALEQA KYNLINEYFL
260 270 280 290 300
VGVTEELEDF IMLLEAALPR FFRGATELYR TGKKSHLRKT TEKKLPTKET
310 320 330 340 350
IAKLQQSEIW KMENEFYEFA LEQFQFVRAH AVREKDGELY ILAQNFFYEK

IYPKSN
Length:356
Mass (Da):41,702
Last modified:July 5, 2004 - v1
Checksum:iD19F4F276DDDBFA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093516 mRNA. Translation: BAD00706.1.
RefSeqiNP_989812.1. NM_204481.1.
UniGeneiGga.9290.

Genome annotation databases

EnsembliENSGALT00000044504; ENSGALP00000042738; ENSGALG00000028423.
GeneIDi395140.
KEGGigga:395140.

Similar proteinsi

Entry informationi

Entry nameiHS2ST_CHICK
AccessioniPrimary (citable) accession number: Q76KB1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 10, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families