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Protein

Heparan-sulfate 6-O-sulfotransferase 2

Gene

hs6st2

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Required for muscle development and angiogenesis.2 Publications

Catalytic activityi

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 6-sulfate.

GO - Molecular functioni

  1. heparan sulfate 6-O-sulfotransferase activity Source: ZFIN

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. embryonic eye morphogenesis Source: ZFIN
  3. metabolic process Source: GOC
  4. muscle organ development Source: UniProtKB-KW
  5. patterning of blood vessels Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Transferase

Keywords - Biological processi

Angiogenesis, Differentiation, Myogenesis

Enzyme and pathway databases

ReactomeiREACT_328124. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparan-sulfate 6-O-sulfotransferase 2 (EC:2.8.2.-)
Short name:
HS 6-OST-2
Short name:
HS6ST-2
Gene namesi
Name:hs6st2
Synonyms:hs6st
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 14

Organism-specific databases

ZFINiZDB-GENE-030909-14. hs6st2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini31 – 468438LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Morpholino knockdown results in defects in the branching morphogenesis of the caudal vein and defects in somite specification with impaired muscle differentiation.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Heparan-sulfate 6-O-sulfotransferase 2PRO_0000190808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Expressed ubiquitously during gastrulation. During early somitogenesis, strong expression in head and presumptive brain. During mid-somitogenesis, strong expression in eye, hindbrain and somitic boundaries and weak expression in tail bud. During late somitogenesis, strong expression in eye, hindbrain, branchial arch primordia, spinal cord and ventral medial somites. At 24 hours post-fertilization (hpf), strong expression throughout the head, with expression receeding from the trunk spinal cord, ventral medial somites and somitic boundaries; expressed in cells surrounding vascular structures of the dorsal aorta and caudal vein in the tail. At 36 hpf, expressed in lens, optic stalk, hindbrain and pectoral fin. At 48 hpf, expressed in eye, brain, otic vesicle and branchial arches.3 Publications

Developmental stagei

Expressed both maternally and zygotically throughout the cleavage, gastrulation and somitogenesis stages.2 Publications

Gene expression databases

BgeeiQ800H9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 11275'-phosphosulfate-bindingSequence Analysis
Regioni197 – 20593'-phosphate bindingSequence Analysis

Sequence similaritiesi

Belongs to the sulfotransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG302961.
GeneTreeiENSGT00390000013468.
HOGENOMiHOG000007772.
HOVERGENiHBG083012.
InParanoidiQ800H9.
KOiK08102.
OMAiKRNLRGM.
OrthoDBiEOG75MVW3.
PhylomeDBiQ800H9.
TreeFamiTF312835.

Family and domain databases

InterProiIPR010635. Heparan_SO4-6-sulfoTrfase.
IPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12812. PTHR12812. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q800H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGKSNYSRL LIALLMILFF GGIVLQYICS TSDWQLLHLA SLSSRLGSRA
60 70 80 90 100
PGDRLNGAGA GDPYSSEDGA LVRFVPRFNF TTKDLSRAVD FHIKGDDVIV
110 120 130 140 150
FLHIQKTGGT TFGRHLVRNI QLERPCECHA GQKKCTCYRP GKRDTWLFSR
160 170 180 190 200
FSTGWSCGLH ADWTELTNCV PSFMSNRESQ ERRMTPSRNY YYITILRDPV
210 220 230 240 250
WRYLSEWRHV QRGATWKASK HMCDGRLPTL TELPSCYPGD DWSGCSLEEF
260 270 280 290 300
MVCPYNLANN RQTRMLADLS LVGCYNLTVM SENQRWAMLL ESAKRNLRNM
310 320 330 340 350
AFFGLTEYQR KTQYLFEHTF RLSFIAPFTQ LNGTRAASVE VEPETQRRIR
360 370 380 390 400
ELNQWDVELY EYARDLFLQR FQFARQQERR EARQRRIQER RKLRAKVKSW
410 420 430 440 450
LGVTGKAVFK PTKEPPMTEQ SPAFAEEKQA DAERTLESET EGQVEENWLE
460
EDDGEIMLDY LENVEQWR
Length:468
Mass (Da):54,605
Last modified:March 6, 2007 - v2
Checksum:i7E6771A7C818FF0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061K → R in AAH45453 (Ref. 4) Curated
Sequence conflicti241 – 2411D → G in AAH45453 (Ref. 4) Curated
Sequence conflicti434 – 4341R → Q in CAD44529 (PubMed:12782624).Curated
Sequence conflicti434 – 4341R → Q in AAT80868 (PubMed:16009360).Curated
Sequence conflicti434 – 4341R → Q in ABH11457 (PubMed:17075883).Curated
Sequence conflicti461 – 4611L → S in CAD44529 (PubMed:12782624).Curated
Sequence conflicti461 – 4611L → S in AAT80868 (PubMed:16009360).Curated
Sequence conflicti461 – 4611L → S in ABH11457 (PubMed:17075883).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ505990 mRNA. Translation: CAD44529.1.
AY575769 mRNA. Translation: AAT80868.1.
DQ812995 mRNA. Translation: ABH11457.1.
BC045453 mRNA. Translation: AAH45453.1.
BC065683 mRNA. Translation: AAH65683.1.
RefSeqiNP_919402.1. NM_194421.1.
UniGeneiDr.77382.

Genome annotation databases

EnsembliENSDART00000002250; ENSDARP00000022497; ENSDARG00000012025.
GeneIDi378450.
KEGGidre:378450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ505990 mRNA. Translation: CAD44529.1.
AY575769 mRNA. Translation: AAT80868.1.
DQ812995 mRNA. Translation: ABH11457.1.
BC045453 mRNA. Translation: AAH45453.1.
BC065683 mRNA. Translation: AAH65683.1.
RefSeqiNP_919402.1. NM_194421.1.
UniGeneiDr.77382.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000002250; ENSDARP00000022497; ENSDARG00000012025.
GeneIDi378450.
KEGGidre:378450.

Organism-specific databases

CTDi90161.
ZFINiZDB-GENE-030909-14. hs6st2.

Phylogenomic databases

eggNOGiNOG302961.
GeneTreeiENSGT00390000013468.
HOGENOMiHOG000007772.
HOVERGENiHBG083012.
InParanoidiQ800H9.
KOiK08102.
OMAiKRNLRGM.
OrthoDBiEOG75MVW3.
PhylomeDBiQ800H9.
TreeFamiTF312835.

Enzyme and pathway databases

ReactomeiREACT_328124. HS-GAG biosynthesis.

Miscellaneous databases

NextBioi20813773.

Gene expression databases

BgeeiQ800H9.

Family and domain databases

InterProiIPR010635. Heparan_SO4-6-sulfoTrfase.
IPR027417. P-loop_NTPase.
IPR005331. Sulfotransferase.
[Graphical view]
PANTHERiPTHR12812. PTHR12812. 1 hit.
PfamiPF03567. Sulfotransfer_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Heparan sulfate 6-o-sulfotransferase is essential for muscle development in zebrafish."
    Bink R.J., Habuhi H., Lele Z., Dolk E., Joore J., Rauch G.-J., Geisler R., Wilson S.W., de Hertog J., Kimata K., Zivkovic D.
    J. Biol. Chem. 278:31118-31127(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  2. "A unique role for 6-O sulfation modification in zebrafish vascular development."
    Chen E., Stringer S.E., Rusch M.A., Selleck S.B., Ekker S.C.
    Dev. Biol. 284:364-376(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  3. "Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: II. The 6-O-sulfotransferase family."
    Cadwallader A.B., Yost H.J.
    Dev. Dyn. 235:3432-3437(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  4. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.
    Tissue: Embryo.

Entry informationi

Entry nameiH6ST2_DANRE
AccessioniPrimary (citable) accession number: Q800H9
Secondary accession number(s): A0MGZ6, Q6P0B4, Q7ZVQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 6, 2007
Last modified: April 1, 2015
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.