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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei151 – 1511PAPS1 Publication
Binding sitei159 – 1591PAPS1 Publication
Binding sitei259 – 2591PAPS1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 725PAPS1 Publication
Nucleotide bindingi274 – 2785PAPS1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671R → E or A: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi68 – 681K → A: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi72 – 721R → A or E: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi76 – 761E → A or Q: Strongly decreases the enzymatic activity. 1 Publication
Mutagenesisi88 – 881E → A: Decreases the enzymatic activity. 1 Publication
Mutagenesisi89 – 891N → A or D: Decreases the enzymatic activity. 1 Publication
Mutagenesisi90 – 901E → Q or A: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi92 – 921H → F or A: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi95 – 951D → A or N: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi96 – 961W → A or F: Decreases the enzymatic activity. 1 Publication
Mutagenesisi98 – 981E → A: Decreases the enzymatic activity. 1 Publication
Mutagenesisi123 – 1231K → A: Abolishes the enzymatic activity. 1 Publication
Mutagenesisi132 – 1321K → A: Decreases the enzymatic activity. 1 Publication
Mutagenesisi163 – 1631Q → A: Strongly decreases the enzymatic activity. 1 Publication
Mutagenesisi197 – 1971R → A: Weakly decrease the enzymatic activity. 1 Publication
Mutagenesisi271 – 2711H → A: No effect. 1 Publication
Mutagenesisi271 – 2711H → F: Decreases the enzymatic activity. 1 Publication
Mutagenesisi273 – 2731S → A: Weakly decrease the enzymatic activity. 1 Publication
Mutagenesisi274 – 2741K → A: Strongly decrease the enzymatic activity. 1 Publication
Mutagenesisi276 – 2761R → A: Abolishes the enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 311291Heparan sulfate glucosamine 3-O-sulfotransferase 1PRO_0000033452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi260 ↔ 2691 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO35310.
PaxDbiO35310.
PRIDEiO35310.

PTM databases

PhosphoSiteiO35310.

Expressioni

Gene expression databases

BgeeiO35310.
ExpressionAtlasiO35310. baseline and differential.
GenevisibleiO35310. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051055.

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 634Combined sources
Helixi71 – 788Combined sources
Beta strandi84 – 863Combined sources
Turni93 – 953Combined sources
Helixi97 – 1004Combined sources
Helixi104 – 1096Combined sources
Beta strandi119 – 1235Combined sources
Helixi125 – 1273Combined sources
Helixi133 – 1408Combined sources
Beta strandi145 – 1506Combined sources
Helixi153 – 17018Combined sources
Helixi178 – 1825Combined sources
Helixi193 – 1975Combined sources
Helixi200 – 2089Combined sources
Helixi213 – 2153Combined sources
Beta strandi216 – 2205Combined sources
Helixi221 – 2266Combined sources
Helixi228 – 23811Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 2534Combined sources
Turni254 – 2574Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi266 – 2683Combined sources
Helixi283 – 30422Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKJX-ray2.50A/B/C48-311[»]
3UANX-ray1.84A/B48-311[»]
ProteinModelPortaliO35310.
SMRiO35310. Positions 54-311.
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.
OrthoDBiEOG7PS1GM.
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.
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.
UniGeneiMm.12559.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKJX-ray2.50A/B/C48-311[»]
3UANX-ray1.84A/B48-311[»]
ProteinModelPortaliO35310.
SMRiO35310. Positions 54-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051055.

PTM databases

PhosphoSiteiO35310.

Proteomic databases

MaxQBiO35310.
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.
OrthoDBiEOG7PS1GM.
PhylomeDBiO35310.
TreeFamiTF350755.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO35310.
NextBioi288320.
PROiO35310.
SOURCEiSearch...

Gene expression databases

BgeeiO35310.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase."
    Shworak N.W., Liu J., Fritze L.M.S., Schwartz J.J., Zhang L., Logeart D., Rosenberg R.D.
    J. Biol. Chem. 272:28008-28019(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    Strain: C3H/An.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. "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].
    Strain: 129.
    Tissue: Mammary tumor.
  4. "Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III."
    Hernaiz M., Liu J., Rosenberg R.D., Linhardt R.J.
    Biochem. Biophys. Res. Commun. 276:292-297(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Crystal structure and mutational analysis of heparan sulfate 3-O-sulfotransferase isoform 1."
    Edavettal S.C., Lee K.A., Negishi M., Linhardt R.J., Liu J., Pedersen L.C.
    J. Biol. Chem. 279:25789-25797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 74-311 IN COMPLEX WITH PAPS, DISULFIDE BOND, BINDING SITES, MUTAGENESIS OF ARG-67; LYS-68; ARG-72; GLU-76; GLU-88; ASN-89; GLU-90; HIS-92; ASP-95; TRP-96; GLU-98; LYS-123; LYS-132; GLN-163; ARG-197; HIS-271; SER-273; LYS-274 AND ARG-276.

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: January 20, 2016
This is version 115 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.