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Reviewed, UniProtKB/Swiss-Prot P52849 (NDST2_HUMAN)

Last modified November 3, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
    EC=2.8.2.8
Alternative name(s):
    Glucosaminyl N-deacetylase/N-sulfotransferase 2
      Short name=NDST-2
    N-heparan sulfate sulfotransferase 2
      Short name=N-HSST 2
Including the following 2 domains:
    1- Recommended name:
            Heparan sulfate N-deacetylase 2
              EC=3.-.-.-
    2- Recommended name:
            Heparan sulfate N-sulfotransferase 2
              EC=2.8.2.-
Gene names
Name: NDST2
Synonyms: HSST2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Ref.4 Ref.5 Ref.6

Catalytic activity

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

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Glycan metabolism; heparin biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Miscellaneous

The presence of 4 different heparan sulfate N-deacetylase/N-sulfotransferase enzymes in mammals, as well as differences in their enzyme activity suggest that some initiate heparan sulfate modification/sulfation reactions, whereas other later on fill in or extend already modified heparan sulfate sequences.

Sequence similarities

Belongs to the sulfotransferase 1 family. NDST subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4.7 µM for K5 polysaccharide

KM=0.76 µM for N-acetylated HS-II

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52849-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P52849-2)

The sequence of this isoform differs from the canonical sequence as follows:
     366-377: TEEEDAGDDMLL → ELIPLLLWHIIV
     378-883: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
PRO_0000085212

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Signal-anchor for type II membrane protein Potential
Topological domain40 – 883844Lumenal Potential
Nucleotide binding613 – 6175PAPS By similarity
Nucleotide binding832 – 8365PAPS By similarity
Region41 – 597557Heparan sulfate N-deacetylase 2
Region598 – 883286Heparan sulfate N-sulfotransferase 2

Sites

Active site6131For sulfotransferase activity By similarity
Binding site7111PAPS By similarity

Amino acid modifications

Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation7261N-linked (GlcNAc...) Potential
Glycosylation8021N-linked (GlcNAc...) Potential
Disulfide bond817 ↔ 827 By similarity

Natural variations

Alternative sequence366 – 37712TEEED…DDMLL → ELIPLLLWHIIV in isoform 2.
VSP_017403
Alternative sequence378 – 883506Missing in isoform 2.
VSP_017404

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 457166F8FCB403E1

FASTA883100,875
        10         20         30         40         50         60 
MLQLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSGGA 

        70         80         90        100        110        120 
AGPGPARPPV PPRPPRPPET ARTEPVVLVF VESAYSQLGQ EIVAILESSR FRYSTELAPG 

       130        140        150        160        170        180 
RGDMPTLTDN THGRYVLVIY ENLLKYVNLD AWSRELLDRY CVEYGVGIIG FFRAHEHSLL 

       190        200        210        220        230        240 
SAQLKGFPLF LHSNLGLRDY QVNPSAPLLH LTRPSRLEPG PLPGDDWTIF QSNHSTYEPV 

       250        260        270        280        290        300 
LLASLRPAEP AVPGPVLRRA RLPTVVQDLG LHDGIQRVLF GHGLSFWLHK LIFVDAVAYL 

       310        320        330        340        350        360 
TGKRLCLDLD RYILVDIDDI FVGKEGTRMK VADVEALLTT QNKLRTLVPN FTFNLGFSGK 

       370        380        390        400        410        420 
FYHTGTEEED AGDDMLLKHR KEFWWFPHMW SHMQPHLFHN RSVLADQMRL NKQFALEHGI 

       430        440        450        460        470        480 
PTDLGYAVAP HHSGVYPIHT QLYEAWKSVW GIQVTSTEEY PHLRPARYRR GFIHNGIMVL 

       490        500        510        520        530        540 
PRQTCGLFTH TIFYNEYPGG SRELDRSIRG GELFLTVLLN PISIFMTHLS NYGNDRLGLY 

       550        560        570        580        590        600 
TFESLVRFLQ CWTRLRLQTL PPVPLAQKYF ELFPQERSPL WQNPCDDKRH KDIWSKEKTC 

       610        620        630        640        650        660 
DRLPKFLIVG PQKTGTTAIH FFLSLHPAVT SSFPSPSTFE EIQFFNSPNY HKGIDWYMDF 

       670        680        690        700        710        720 
FPVPSNASTD FLFEKSATYF DSEVVPRRGA ALLPRAKIIT VLTNPADRAY SWYQHQRAHG 

       730        740        750        760        770        780 
DPVALNYTFY QVISASSQTP LALRSLQNRC LVPGYYSTHL QRWLTYYPSG QLLIVDGQEL 

       790        800        810        820        830        840 
RTNPAASMES IQKFLGITPF LNYTRTLRFD DDKGFWCQGL EGGKTRCLGR SKGRRYPDMD 

       850        860        870        880 
TESRLFLTDF FRNHNLELSK LLSRLGQPVP SWLREELQHS SLG

« Hide

Isoform 2.

Checksum: C4831C3D2752087C
Show »

FASTA37742,093

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References

« Hide 'large scale' references
[1]"cDNA cloning, genomic organization and chromosomal localization of human heparan glucosaminyl N-deacetylase/N-sulphotransferase-2."
Humphries D.E., Lanciotti J., Karlinsky J.B.
Biochem. J. 332:303-307(1998) [PubMed: 9601056] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Ovary.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-377 (ISOFORM 2).
Tissue: Brain.
[4]"Overexpression of different isoforms of glucosaminyl N-deacetylase/N-sulfotransferase results in distinct heparan sulfate N-sulfation patterns."
Pikas D.S., Eriksson I., Kjellen L.
Biochemistry 39:4552-4558(2000) [PubMed: 10758005] [Abstract]
Cited for: FUNCTION.
[5]"Antibody-based assay for N-deacetylase activity of heparan sulfate/heparin N-deacetylase/N-sulfotransferase (NDST): novel characteristics of NDST-1 and -2."
van den Born J., Pikas D.S., Pisa B.J., Eriksson I., Kjellen L., Berden J.H.M.
Glycobiology 13:1-10(2003) [PubMed: 12634318] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Characterization of the N-deacetylase domain from the heparan sulfate N-deacetylase/N-sulfotransferase 2."
Duncan M.B., Liu M., Fox C., Liu J.
Biochem. Biophys. Res. Commun. 339:1232-1237(2006) [PubMed: 16343444] [Abstract]
Cited for: FUNCTION.

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Web resources

GGDB

GlycoGene database

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Cross-references

Sequence databases

U36601 mRNA. Translation: AAC27120.1.
AF042084 Genomic DNA. Translation: AAB97086.1.
BC035711 mRNA. Translation: AAH35711.1.
BC110588 mRNA. Translation: AAI10589.1.
BC110589 mRNA. Translation: AAI10590.1.
AB208870 mRNA. Translation: BAD92107.1.
IPIIPI00005600.
IPI00737119.
RefSeqNP_003626.1.
UniGeneHs.654758

3D structure databases

HSSPHSSP built from PDB template 1NST based on UniProtKB P52848.
ModBaseSearch...

Protein-protein interaction databases

STRINGP52849.

Proteomic databases

PRIDEP52849.

Genome annotation databases

EnsemblENST00000299641; ENSP00000299641; ENSG00000166507; Homo sapiens. [Genome view]
ENST00000309979; ENSP00000310657; ENSG00000166507; Homo sapiens. [Genome view]
ENST00000426473; ENSP00000401772; ENSG00000166507; Homo sapiens. [Genome view]
ENST00000429742; ENSP00000392733; ENSG00000166507; Homo sapiens. [Genome view]
GeneID8509.
KEGGhsa:8509.
UCSCuc001jvk.1. human.

Organism-specific databases

CTD8509.
GeneCardsGC10M075231.
H-InvDBHIX0025947.
HGNCHGNC:7681. NDST2.
MIM603268. gene.
PharmGKBPA31487.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP52849.
HOVERGENP52849.
OMAFLQCWTR.

Enzyme and pathway databases

BRENDA2.8.2.8. 247.

Gene expression databases

ArrayExpressP52849.
BgeeP52849.
CleanExHS_NDST2.
GenevestigatorP52849.
GermOnlineENSG00000166507. Homo sapiens.

Family and domain databases

InterProIPR000863. Sulfotransferase.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio31847.
SOURCESearch...

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Entry information

Entry nameNDST2_HUMAN
AccessionPrimary (citable) accession number: P52849
Secondary accession number(s): Q2TB32, Q59H89
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 3, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents