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Q9Y663

- HS3SA_HUMAN

UniProt

Q9Y663 - HS3SA_HUMAN

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Protein
Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
Gene
HS3ST3A1, 3OST3A1, HS3ST3A, UNQ2551/PRO6180
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 an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in 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. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.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 sitei166 – 1661Substrate
Binding sitei243 – 2431PAPS
Binding sitei251 – 2511PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665PAPS
Nucleotide bindingi368 – 3725PAPS

GO - Molecular functioni

  1. [heparan sulfate]-glucosamine 3-sulfotransferase 3 activity Source: UniProtKB-EC
  2. sulfotransferase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan biosynthetic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS07937-MONOMER.
ReactomeiREACT_121248. HS-GAG biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 (EC:2.8.2.30)
Alternative name(s):
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1
Short name:
3-OST-3A
Short name:
Heparan sulfate 3-O-sulfotransferase 3A1
Short name:
h3-OST-3A
Gene namesi
Synonyms:3OST3A1, HS3ST3A
ORF Names:UNQ2551/PRO6180
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:5196. HS3ST3A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei25 – 4319Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini44 – 406363Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611K → A: 99.6% loss of enzymatic activity. 1 Publication
Mutagenesisi162 – 1621K → A: 99.6% loss of enzymatic activity; no HSV1 entry activity. 2 Publications
Mutagenesisi166 – 1661R → E: 99.8% loss of enzymatic activity. 1 Publication
Mutagenesisi170 – 1701E → Q: 17% loss of enzymatic activity. 1 Publication
Mutagenesisi173 – 1731R → S: 44.1% loss of enzymatic activity. 1 Publication
Mutagenesisi182 – 1821G → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi184 – 1841E → Q: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi186 – 1861H → F: Abolishes enzymatic activity. 1 Publication
Mutagenesisi189 – 1891D → N: 99.1% loss of enzymatic activity. 1 Publication
Mutagenesisi190 – 1901R → E: 32% loss of enzymatic activity. 1 Publication
Mutagenesisi194 – 1941K → A: 99.5% loss of enzymatic activity. 1 Publication
Mutagenesisi215 – 2151K → A: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi218 – 2181S → A: 23.3% loss of enzymatic activity. 1 Publication
Mutagenesisi224 – 2241E → Q: 47.6% loss of enzymatic activity. 1 Publication
Mutagenesisi255 – 2551Q → A: 99.6% loss of enzymatic activity. 1 Publication
Mutagenesisi259 – 2591K → A: 48.3% loss of enzymatic activity. 1 Publication
Mutagenesisi288 – 2881I → A: 65% loss of enzymatic activity. 1 Publication
Mutagenesisi293 – 2931K → A: 33.6% loss of enzymatic activity. 1 Publication
Mutagenesisi362 – 3621H → A: No effect on enzymatic activity. 1 Publication
Mutagenesisi365 – 3651G → A: 43% loss of enzymatic activity. 1 Publication
Mutagenesisi366 – 3661K → A: 99.8% loss of enzymatic activity. 1 Publication
Mutagenesisi368 – 3681K → A: 99.9% loss of enzymatic activity. 1 Publication
Mutagenesisi370 – 3701R → E: 99.2% loss of enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA29469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
PRO_0000085217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi273 – 2731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi344 – 3441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi351 ↔ 3631 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y663.
PRIDEiQ9Y663.

PTM databases

PhosphoSiteiQ9Y663.

Expressioni

Tissue specificityi

Ubiquitous. Most abundant in heart and placenta, followed by liver and kidney.1 Publication

Gene expression databases

ArrayExpressiQ9Y663.
BgeeiQ9Y663.
CleanExiHS_HS3ST3A1.
GenevestigatoriQ9Y663.

Interactioni

Protein-protein interaction databases

BioGridi115280. 1 interaction.
STRINGi9606.ENSP00000284110.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 1479
Beta strandi154 – 1596
Helixi165 – 1728
Beta strandi178 – 1803
Turni187 – 1904
Helixi192 – 1943
Helixi195 – 2028
Beta strandi211 – 2155
Helixi217 – 2215
Helixi225 – 2328
Beta strandi237 – 2426
Helixi245 – 25915
Helixi266 – 2705
Helixi284 – 2874
Helixi291 – 2988
Turni299 – 3013
Helixi304 – 3063
Beta strandi307 – 3115
Helixi312 – 3176
Helixi319 – 33012
Helixi338 – 3403
Beta strandi341 – 3444
Turni345 – 3484
Beta strandi349 – 3546
Helixi377 – 39822

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T8TX-ray1.85A/B139-406[»]
1T8UX-ray1.95A/B139-406[»]
ProteinModelPortaliQ9Y663.
SMRiQ9Y663. Positions 139-406.

Miscellaneous databases

EvolutionaryTraceiQ9Y663.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1907Substrate binding
Regioni215 – 2184Substrate binding
Regioni255 – 2595Substrate binding
Regioni283 – 2842Substrate binding
Regioni367 – 3704Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG73846.
HOGENOMiHOG000036663.
HOVERGENiHBG053377.
InParanoidiQ9Y663.
KOiK07809.
OMAiSGERLIM.
OrthoDBiEOG7PS1GM.
PhylomeDBiQ9Y663.
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.

Q9Y663-1 [UniParc]FASTAAdd to Basket

« Hide

MAPPGPASAL STSAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCQTLS    50
GPVVGLSGGG EEAGAPGGGV LAGGPRELAV WPAAAQRKRL LQLPQWRRRR 100
PPAPRDDGEE AAWEEESPGL SGGPGGSGAG STVAEAPPGT LALLLDEGSK 150
QLPQAIIIGV KKGGTRALLE FLRVHPDVRA VGAEPHFFDR SYDKGLAWYR 200
DLMPRTLDGQ ITMEKTPSYF VTREAPARIS AMSKDTKLIV VVRDPVTRAI 250
SDYTQTLSKR PDIPTFESLT FKNRTAGLID TSWSAIQIGI YAKHLEHWLR 300
HFPIRQMLFV SGERLISDPA GELGRVQDFL GLKRIITDKH FYFNKTKGFP 350
CLKKAEGSSR PHCLGKTKGR THPEIDREVV RRLREFYRPF NLKFYQMTGH 400
DFGWDG 406
Length:406
Mass (Da):44,900
Last modified:November 1, 1999 - v1
Checksum:i57B6A0ABC897577A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF105376 mRNA. Translation: AAD30208.1.
AY358838 mRNA. Translation: AAQ89197.1.
AK292047 mRNA. Translation: BAF84736.1.
CH471108 Genomic DNA. Translation: EAW89959.1.
BC044647 mRNA. Translation: AAH44647.1.
CCDSiCCDS11165.1.
RefSeqiNP_006033.1. NM_006042.1.
UniGeneiHs.462270.

Genome annotation databases

EnsembliENST00000284110; ENSP00000284110; ENSG00000153976.
GeneIDi9955.
KEGGihsa:9955.
UCSCiuc002gob.1. human.

Polymorphism databases

DMDMi61214551.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF105376 mRNA. Translation: AAD30208.1 .
AY358838 mRNA. Translation: AAQ89197.1 .
AK292047 mRNA. Translation: BAF84736.1 .
CH471108 Genomic DNA. Translation: EAW89959.1 .
BC044647 mRNA. Translation: AAH44647.1 .
CCDSi CCDS11165.1.
RefSeqi NP_006033.1. NM_006042.1.
UniGenei Hs.462270.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T8T X-ray 1.85 A/B 139-406 [» ]
1T8U X-ray 1.95 A/B 139-406 [» ]
ProteinModelPortali Q9Y663.
SMRi Q9Y663. Positions 139-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115280. 1 interaction.
STRINGi 9606.ENSP00000284110.

PTM databases

PhosphoSitei Q9Y663.

Polymorphism databases

DMDMi 61214551.

Proteomic databases

PaxDbi Q9Y663.
PRIDEi Q9Y663.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284110 ; ENSP00000284110 ; ENSG00000153976 .
GeneIDi 9955.
KEGGi hsa:9955.
UCSCi uc002gob.1. human.

Organism-specific databases

CTDi 9955.
GeneCardsi GC17M013339.
HGNCi HGNC:5196. HS3ST3A1.
MIMi 604057. gene.
neXtProti NX_Q9Y663.
PharmGKBi PA29469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73846.
HOGENOMi HOG000036663.
HOVERGENi HBG053377.
InParanoidi Q9Y663.
KOi K07809.
OMAi SGERLIM.
OrthoDBi EOG7PS1GM.
PhylomeDBi Q9Y663.
TreeFami TF350755.

Enzyme and pathway databases

BioCyci MetaCyc:HS07937-MONOMER.
Reactomei REACT_121248. HS-GAG biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q9Y663.
GeneWikii HS3ST3A1.
GenomeRNAii 9955.
NextBioi 37564.
PROi Q9Y663.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y663.
Bgeei Q9Y663.
CleanExi HS_HS3ST3A1.
Genevestigatori Q9Y663.

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. "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cDNAs and identification of distinct genomic loci."
    Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G., Jenkins N.A., Rosenberg R.D.
    J. Biol. Chem. 274:5170-5184(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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: Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry."
    Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D., Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.
    Cell 99:13-22(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HSV-1 ENTRY, MUTAGENESIS OF LYS-162.
  7. "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities."
    Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M.S., Rosenberg R.D.
    J. Biol. Chem. 274:5185-5192(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues."
    Liu J., Shriver Z., Blaiklock P., Yoshida K., Sasisekharan R., Rosenberg R.D.
    J. Biol. Chem. 274:38155-38162(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1."
    Moon A.F., Edavettal S.C., Krahn J.M., Munoz E.M., Negishi M., Linhardt R.J., Liu J., Pedersen L.C.
    J. Biol. Chem. 279:45185-45193(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 139-406 IN A TERNARY COMPLEX WITH PAPS AND A TETRASACCHARIDE, DISULFIDE BOND, BINDING SITES, MUTAGENESIS OF LYS-161; LYS-162; ARG-166; GLU-170; ARG-173; GLY-182; GLU-184; HIS-186; ASP-189; ARG-190; LYS-194; LYS-215; SER-218; GLU-224; GLN-255; LYS-259; ILE-288; LYS-293; HIS-362; GLY-365; LYS-366; LYS-368 AND ARG-370.

Entry informationi

Entry nameiHS3SA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y663
Secondary accession number(s): A8K7N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 111 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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