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Q8IZT8

- HS3S5_HUMAN

UniProt

Q8IZT8 - HS3S5_HUMAN

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Protein

Heparan sulfate glucosamine 3-O-sulfotransferase 5

Gene

HS3ST5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Source: UniProtKB
  2. 3'-phosphoadenosine 5'-phosphosulfate binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan biosynthetic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. heparan sulfate proteoglycan biosynthetic process, enzymatic modification Source: UniProtKB
  5. negative regulation of coagulation Source: UniProtKB
  6. protein sulfation Source: UniProtKB
  7. regulation of viral entry into host cell Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:19419. HS3ST5.

Subcellular locationi

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. 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.

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 – 976
Helixi103 – 1108
Beta strandi116 – 1183
Helixi129 – 1335
Helixi136 – 1405
Beta strandi151 – 1555
Helixi157 – 1604
Helixi165 – 1728
Beta strandi177 – 1826
Helixi185 – 20218
Helixi210 – 2145
Turni217 – 2193
Helixi227 – 2315
Helixi234 – 2429
Helixi247 – 2493
Beta strandi250 – 2545
Helixi255 – 2606
Helixi262 – 27211
Helixi281 – 2833
Beta strandi284 – 2874
Turni288 – 2914
Beta strandi292 – 2965
Beta strandi298 – 3003
Helixi318 – 33922

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8IZT8.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini33 – 346314LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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:
EMBL
GenBank
DDBJ
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_006715379.1.
UniGeneiHs.645477.

Genome annotation databases

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

Polymorphism databases

DMDMi61214369.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34517.1.
RefSeqi NP_705840.2. NM_153612.3.
XP_006715442.1. XM_006715379.1.
UniGenei Hs.645477.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BD9 X-ray 2.30 A 88-346 [» ]
ProteinModelPortali Q8IZT8.
SMRi Q8IZT8. Positions 87-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000387653.

PTM databases

PhosphoSitei Q8IZT8.

Polymorphism databases

DMDMi 61214369.

Proteomic databases

PaxDbi Q8IZT8.
PeptideAtlasi Q8IZT8.
PRIDEi Q8IZT8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312719 ; ENSP00000427888 ; ENSG00000249853 .
ENST00000411826 ; ENSP00000440332 ; ENSG00000249853 .
GeneIDi 222537.
KEGGi hsa:222537.
UCSCi uc003pwg.4. human.

Organism-specific databases

CTDi 222537.
GeneCardsi GC06M114376.
HGNCi HGNC:19419. HS3ST5.
HPAi HPA021823.
MIMi 609407. gene.
neXtProti NX_Q8IZT8.
PharmGKBi PA164741639.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282030.
GeneTreei ENSGT00760000119023.
HOGENOMi HOG000036663.
HOVERGENi HBG053377.
InParanoidi Q8IZT8.
KOi K08104.
OMAi GRTFNWP.
OrthoDBi EOG7PS1GM.
PhylomeDBi Q8IZT8.
TreeFami TF350755.

Enzyme and pathway databases

Reactomei REACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q8IZT8.
GenomeRNAii 222537.
NextBioi 91615.
PROi Q8IZT8.
SOURCEi Search...

Gene expression databases

Bgeei Q8IZT8.
CleanExi HS_HS3ST5.
Genevestigatori Q8IZT8.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 107 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