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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831PAPSBy similarity
Binding sitei191 – 1911PAPSBy similarity
Binding sitei293 – 2931PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1045PAPSBy similarity
Nucleotide bindingi309 – 3135PAPSBy similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_121248. 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
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:19419. HS3ST5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 346314LumenalSequence AnalysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991R → A: Reduces enzyme activity by over 99%. 1 Publication
Mutagenesisi104 – 1041R → A: Reduces enzyme activity by 93%,. 1 Publication
Mutagenesisi155 – 1551K → A: Reduces enzyme activity by over 99%. 1 Publication
Mutagenesisi195 – 1951Q → A: Reduces enzyme activity by over 99%. 1 Publication
Mutagenesisi309 – 3091K → A: Loss of enzyme activity. 1 Publication
Mutagenesisi311 – 3111R → A: Reduces enzyme activity by 98%. 1 Publication

Organism-specific databases

PharmGKBiPA164741639.

Polymorphism and mutation databases

BioMutaiHS3ST5.
DMDMi61214369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Heparan sulfate glucosamine 3-O-sulfotransferase 5PRO_0000085222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi294 ↔ 304By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8IZT8.
PeptideAtlasiQ8IZT8.
PRIDEiQ8IZT8.

PTM databases

PhosphoSiteiQ8IZT8.

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

BgeeiQ8IZT8.
CleanExiHS_HS3ST5.
GenevestigatoriQ8IZT8.

Organism-specific databases

HPAiHPA021823.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000387653.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 976Combined sources
Helixi103 – 1108Combined sources
Beta strandi116 – 1183Combined sources
Helixi129 – 1335Combined sources
Helixi136 – 1405Combined sources
Beta strandi151 – 1555Combined sources
Helixi157 – 1604Combined sources
Helixi165 – 1728Combined sources
Beta strandi177 – 1826Combined sources
Helixi185 – 20218Combined sources
Helixi210 – 2145Combined sources
Turni217 – 2193Combined sources
Helixi227 – 2315Combined sources
Helixi234 – 2429Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 2545Combined sources
Helixi255 – 2606Combined sources
Helixi262 – 27211Combined sources
Helixi281 – 2833Combined sources
Beta strandi284 – 2874Combined sources
Turni288 – 2914Combined sources
Beta strandi292 – 2965Combined sources
Beta strandi298 – 3003Combined sources
Helixi318 – 33922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BD9X-ray2.30A88-346[»]
ProteinModelPortaliQ8IZT8.
SMRiQ8IZT8. Positions 87-346.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IZT8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1287Substrate bindingBy similarity
Regioni155 – 1584Substrate bindingBy similarity
Regioni226 – 2272Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282030.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ8IZT8.
KOiK08104.
OMAiGRTFNWP.
OrthoDBiEOG7PS1GM.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471I → N.
Corresponds to variant rs17793043 [ dbSNP | Ensembl ].
VAR_052531

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.
UniGeneiHs.645477.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

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.
UniGeneiHs.645477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BD9X-ray2.30A88-346[»]
ProteinModelPortaliQ8IZT8.
SMRiQ8IZT8. Positions 87-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000387653.

PTM databases

PhosphoSiteiQ8IZT8.

Polymorphism and mutation databases

BioMutaiHS3ST5.
DMDMi61214369.

Proteomic databases

PaxDbiQ8IZT8.
PeptideAtlasiQ8IZT8.
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.
GeneCardsiGC06M114376.
HGNCiHGNC:19419. HS3ST5.
HPAiHPA021823.
MIMi609407. gene.
neXtProtiNX_Q8IZT8.
PharmGKBiPA164741639.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282030.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ8IZT8.
KOiK08104.
OMAiGRTFNWP.
OrthoDBiEOG7PS1GM.
PhylomeDBiQ8IZT8.
TreeFamiTF350755.

Enzyme and pathway databases

ReactomeiREACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

EvolutionaryTraceiQ8IZT8.
GenomeRNAii222537.
NextBioi91615.
PROiQ8IZT8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IZT8.
CleanExiHS_HS3ST5.
GenevestigatoriQ8IZT8.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1."
    Xia G., Chen J., Tiwari V., Ju W., Li J.-P., Malmstroem A., Shukla D., Liu J.
    J. Biol. Chem. 277:37912-37919(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, FUNCTION IN HSV-1 ENTRY.
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus and Corpus callosum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Characterization of a heparan sulfate 3-O-sulfotransferase-5, an enzyme synthesizing a tetrasulfated disaccharide."
    Mochizuki H., Yoshida K., Gotoh M., Sugioka S., Kikuchi N., Kwon Y.-D., Tawada A., Maeyama K., Inaba N., Hiruma T., Kimata K., Narimatsu H.
    J. Biol. Chem. 278:26780-26787(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  6. "The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5."
    Duncan M.B., Chen J., Krise J.P., Liu J.
    Biochim. Biophys. Acta 1671:34-43(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Engineering sulfotransferases to modify heparan sulfate."
    Xu D., Moon A.F., Song D., Pedersen L.C., Liu J.
    Nat. Chem. Biol. 4:200-202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-346 IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-99; ARG-104; LYS-155; GLN-195; LYS-309 AND ARG-311.

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: May 27, 2015
This is version 112 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

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.