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Protein

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1

Gene

NDST1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 disaccharide 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. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=13.3 µM for K5 polysaccharide1 Publication
  2. KM=0.35 µM for N-acetylated HS-II1 Publication

    Pathway: heparan sulfate biosynthesis

    This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
    View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

    Pathway: heparin biosynthesis

    This protein is involved in the pathway heparin biosynthesis, which is part of Glycan metabolism.
    View all proteins of this organism that are known to be involved in the pathway heparin biosynthesis and in Glycan metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei614 – 6141For sulfotransferase activity
    Binding sitei712 – 7121PAPS1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi614 – 6185PAPS1 Publication
    Nucleotide bindingi833 – 8375PAPS1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Inflammatory response

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01001-MONOMER.
    ReactomeiREACT_121248. HS-GAG biosynthesis.
    SABIO-RKP52848.
    UniPathwayiUPA00756.
    UPA00862.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 (EC:2.8.2.8)
    Alternative name(s):
    Glucosaminyl N-deacetylase/N-sulfotransferase 1
    Short name:
    NDST-1
    N-heparan sulfate sulfotransferase 1
    Short name:
    N-HSST 1
    [Heparan sulfate]-glucosamine N-sulfotransferase 1
    Short name:
    HSNST 1
    Including the following 2 domains:
    Heparan sulfate N-deacetylase 1 (EC:3.-.-.-)
    Heparan sulfate N-sulfotransferase 1 (EC:2.8.2.-)
    Gene namesi
    Name:NDST1
    Synonyms:HSST, HSST1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7680. NDST1.

    Subcellular locationi

    • Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei18 – 3922Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini40 – 882843LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal recessive 46 (MRT46)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT46 manifestations include delayed psychomotor development apparent from infancy or early childhood, delayed or absent expressive speech, hypotonia, and therapy-responsive seizures in some patients. Behavioral abnormalities are variable and include aggression, self-injurious behavior, and sleep disturbances.

    See also OMIM:616116
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti611 – 6111G → S in MRT46. 1 Publication
    VAR_072646
    Natural varianti640 – 6401F → L in MRT46. 1 Publication
    VAR_072647
    Natural varianti642 – 6421E → D in MRT46. 1 Publication
    VAR_072648
    Natural varianti709 – 7091R → Q in MRT46. 1 Publication
    VAR_072649

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi614 – 6141K → A: Loss of sulfotransferase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi616116. phenotype.
    Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
    PharmGKBiPA31486.

    Polymorphism and mutation databases

    BioMutaiNDST1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 882882Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1PRO_0000085210Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi667 – 6671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi818 ↔ 8281 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP52848.
    PaxDbiP52848.
    PRIDEiP52848.

    PTM databases

    PhosphoSiteiP52848.

    Expressioni

    Tissue specificityi

    Widely expressed. Expression is most abundant in heart, liver and pancreas.

    Gene expression databases

    BgeeiP52848.
    CleanExiHS_NDST1.
    ExpressionAtlasiP52848. baseline and differential.
    GenevisibleiP52848. HS.

    Organism-specific databases

    HPAiHPA060532.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi109572. 6 interactions.
    STRINGi9606.ENSP00000261797.

    Structurei

    Secondary structure

    1
    882
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi604 – 6096Combined sources
    Helixi617 – 6259Combined sources
    Beta strandi630 – 6323Combined sources
    Turni637 – 6393Combined sources
    Beta strandi646 – 6483Combined sources
    Helixi649 – 6535Combined sources
    Helixi655 – 6595Combined sources
    Beta strandi672 – 6765Combined sources
    Helixi679 – 6824Combined sources
    Helixi686 – 6938Combined sources
    Beta strandi698 – 7036Combined sources
    Helixi706 – 71914Combined sources
    Helixi723 – 7275Combined sources
    Helixi730 – 7345Combined sources
    Helixi742 – 75211Combined sources
    Helixi753 – 7553Combined sources
    Helixi757 – 7659Combined sources
    Helixi770 – 7723Combined sources
    Beta strandi773 – 7775Combined sources
    Helixi778 – 7836Combined sources
    Helixi785 – 79612Combined sources
    Helixi805 – 8073Combined sources
    Beta strandi808 – 8114Combined sources
    Turni812 – 8154Combined sources
    Beta strandi816 – 8205Combined sources
    Helixi842 – 86625Combined sources
    Helixi872 – 8787Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NSTX-ray2.30A558-882[»]
    ProteinModelPortaliP52848.
    SMRiP52848. Positions 579-879.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52848.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 598559Heparan sulfate N-deacetylase 1Add
    BLAST
    Regioni599 – 882284Heparan sulfate N-sulfotransferase 1Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG267831.
    GeneTreeiENSGT00760000119023.
    HOGENOMiHOG000008010.
    HOVERGENiHBG082011.
    InParanoidiP52848.
    KOiK02576.
    OMAiTNTIDYH.
    PhylomeDBiP52848.
    TreeFamiTF313193.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR021930. Heparan_SO4_deacetylase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF12062. HSNSD. 1 hit.
    PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P52848-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MPALACLRRL CRHVSPQAVL FLLFIFCLFS VFISAYYLYG WKRGLEPSAD
    60 70 80 90 100
    APEPDCGDPP PVAPSRLLPL KPVQAATPSR TDPLVLVFVE SLYSQLGQEV
    110 120 130 140 150
    VAILESSRFK YRTEIAPGKG DMPTLTDKGR GRFALIIYEN ILKYVNLDAW
    160 170 180 190 200
    NRELLDKYCV AYGVGIIGFF KANENSLLSA QLKGFPLFLH SNLGLKDCSI
    210 220 230 240 250
    NPKSPLLYVT RPSEVEKGVL PGEDWTVFQS NHSTYEPVLL AKTRSSESIP
    260 270 280 290 300
    HLGADAGLHA ALHATVVQDL GLHDGIQRVL FGNNLNFWLH KLVFVDAVAF
    310 320 330 340 350
    LTGKRLSLPL DRYILVDIDD IFVGKEGTRM KVEDVKALFD TQNELRAHIP
    360 370 380 390 400
    NFTFNLGYSG KFFHTGTNAE DAGDDLLLSY VKEFWWFPHM WSHMQPHLFH
    410 420 430 440 450
    NQSVLAEQMA LNKKFAVEHG IPTDMGYAVA PHHSGVYPVH VQLYEAWKQV
    460 470 480 490 500
    WSIRVTSTEE YPHLKPARYR RGFIHNGIMV LPRQTCGLFT HTIFYNEYPG
    510 520 530 540 550
    GSSELDKIIN GGELFLTVLL NPISIFMTHL SNYGNDRLGL YTFKHLVRFL
    560 570 580 590 600
    HSWTNLRLQT LPPVQLAQKY FQIFSEEKDP LWQDPCEDKR HKDIWSKEKT
    610 620 630 640 650
    CDRFPKLLII GPQKTGTTAL YLFLGMHPDL SSNYPSSETF EEIQFFNGHN
    660 670 680 690 700
    YHKGIDWYME FFPIPSNTTS DFYFEKSANY FDSEVAPRRA AALLPKAKVL
    710 720 730 740 750
    TILINPADRA YSWYQHQRAH DDPVALKYTF HEVITAGSDA SSKLRALQNR
    760 770 780 790 800
    CLVPGWYATH IERWLSAYHA NQILVLDGKL LRTEPAKVMD MVQKFLGVTN
    810 820 830 840 850
    TIDYHKTLAF DPKKGFWCQL LEGGKTKCLG KSKGRKYPEM DLDSRAFLKD
    860 870 880
    YYRDHNIELS KLLYKMGQTL PTWLREDLQN TR
    Length:882
    Mass (Da):100,868
    Last modified:October 1, 1996 - v1
    Checksum:iD4B716B84A0BF4C4
    GO
    Isoform 2 (identifier: P52848-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         523-556: ISIFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNL → VSAPQPMAAGEKGLLHSLSAADTGFLEPGKGGEA
         557-882: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:556
    Mass (Da):62,065
    Checksum:iC3D09802532B4D97
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 285FIFCL → QVVCQ in AAH12888 (PubMed:15489334).Curated
    Sequence conflicti60 – 601P → A in AAA67765 (Ref. 3) Curated
    Sequence conflicti364 – 3641H → Q in AAH12888 (PubMed:15489334).Curated
    Sequence conflicti689 – 6891R → G in AAA67765 (Ref. 3) Curated
    Sequence conflicti743 – 7431K → R in AAA67765 (Ref. 3) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti611 – 6111G → S in MRT46. 1 Publication
    VAR_072646
    Natural varianti640 – 6401F → L in MRT46. 1 Publication
    VAR_072647
    Natural varianti642 – 6421E → D in MRT46. 1 Publication
    VAR_072648
    Natural varianti709 – 7091R → Q in MRT46. 1 Publication
    VAR_072649

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei523 – 55634ISIFM…SWTNL → VSAPQPMAAGEKGLLHSLSA ADTGFLEPGKGGEA in isoform 2. 1 PublicationVSP_017397Add
    BLAST
    Alternative sequencei557 – 882326Missing in isoform 2. 1 PublicationVSP_017398Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18918 mRNA. Translation: AAA75281.1.
    U36600 mRNA. Translation: AAC27354.1.
    U17970 mRNA. Translation: AAA67765.1.
    BC012888 mRNA. Translation: AAH12888.1.
    CCDSiCCDS34277.1. [P52848-1]
    PIRiA57169.
    RefSeqiNP_001287992.1. NM_001301063.1.
    NP_001534.1. NM_001543.4. [P52848-1]
    XP_006714846.1. XM_006714783.1. [P52848-1]
    UniGeneiHs.222055.

    Genome annotation databases

    EnsembliENST00000261797; ENSP00000261797; ENSG00000070614. [P52848-1]
    GeneIDi3340.
    KEGGihsa:3340.
    UCSCiuc003lsk.4. human. [P52848-1]
    uc003lsl.3. human. [P52848-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18918 mRNA. Translation: AAA75281.1.
    U36600 mRNA. Translation: AAC27354.1.
    U17970 mRNA. Translation: AAA67765.1.
    BC012888 mRNA. Translation: AAH12888.1.
    CCDSiCCDS34277.1. [P52848-1]
    PIRiA57169.
    RefSeqiNP_001287992.1. NM_001301063.1.
    NP_001534.1. NM_001543.4. [P52848-1]
    XP_006714846.1. XM_006714783.1. [P52848-1]
    UniGeneiHs.222055.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NSTX-ray2.30A558-882[»]
    ProteinModelPortaliP52848.
    SMRiP52848. Positions 579-879.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109572. 6 interactions.
    STRINGi9606.ENSP00000261797.

    PTM databases

    PhosphoSiteiP52848.

    Polymorphism and mutation databases

    BioMutaiNDST1.

    Proteomic databases

    MaxQBiP52848.
    PaxDbiP52848.
    PRIDEiP52848.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000261797; ENSP00000261797; ENSG00000070614. [P52848-1]
    GeneIDi3340.
    KEGGihsa:3340.
    UCSCiuc003lsk.4. human. [P52848-1]
    uc003lsl.3. human. [P52848-2]

    Organism-specific databases

    CTDi3340.
    GeneCardsiGC05P149881.
    HGNCiHGNC:7680. NDST1.
    HPAiHPA060532.
    MIMi600853. gene.
    616116. phenotype.
    neXtProtiNX_P52848.
    Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
    PharmGKBiPA31486.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG267831.
    GeneTreeiENSGT00760000119023.
    HOGENOMiHOG000008010.
    HOVERGENiHBG082011.
    InParanoidiP52848.
    KOiK02576.
    OMAiTNTIDYH.
    PhylomeDBiP52848.
    TreeFamiTF313193.

    Enzyme and pathway databases

    UniPathwayiUPA00756.
    UPA00862.
    BioCyciMetaCyc:HS01001-MONOMER.
    ReactomeiREACT_121248. HS-GAG biosynthesis.
    SABIO-RKP52848.

    Miscellaneous databases

    ChiTaRSiNDST1. human.
    EvolutionaryTraceiP52848.
    GeneWikiiNDST1.
    GenomeRNAii3340.
    NextBioi13220.
    PROiP52848.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP52848.
    CleanExiHS_NDST1.
    ExpressionAtlasiP52848. baseline and differential.
    GenevisibleiP52848. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR021930. Heparan_SO4_deacetylase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF12062. HSNSD. 1 hit.
    PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of the human heparan sulfate-N-deacetylase/N-sulfotransferase gene from the Treacher Collins syndrome candidate region at 5q32-q33.1."
      Dixon J., Loftus S.K., Gladwin A.J., Scambler P.J., Wasmuth J.J., Dixon M.J.
      Genomics 26:239-244(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Localization of human heparan glucosaminyl N-deacetylase/N-sulphotransferase to the trans-Golgi network."
      Humphries D.E., Sullivan B.M., Aleixo M.D., Stow J.L.
      Biochem. J. 325:351-357(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Umbilical vein endothelial cell.
    3. Labell T.L., Milewicz D.J., Bonadio J., Edelhoff S., Disteche C.M., Byers P.H.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    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] (ISOFORM 2).
      Tissue: Lung.
    5. "A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase."
      Sueyoshi T., Kakuta Y., Pedersen L.C., Wall F.E., Pedersen L.G., Negishi M.
      FEBS Lett. 433:211-214(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-614.
    6. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/N-sulfotransferase 1."
      Kakuta Y., Sueyoshi T., Negishi M., Pedersen L.C.
      J. Biol. Chem. 274:10673-10676(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 579-882 IN COMPLEX WITH PAP, DISULFIDE BOND.
    9. Cited for: INVOLVEMENT IN MRT46, VARIANTS MRT46 SER-611; LEU-640; ASP-642 AND GLN-709.

    Entry informationi

    Entry nameiNDST1_HUMAN
    AccessioniPrimary (citable) accession number: P52848
    Secondary accession number(s): Q96E57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: June 24, 2015
    This is version 141 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

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.