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Q3UHN9

- NDST1_MOUSE

UniProt

Q3UHN9 - NDST1_MOUSE

Protein

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1

Gene

Ndst1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    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.6 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi614 – 6185PAPSBy similarity
    Nucleotide bindingi833 – 8375PAPSBy similarity

    GO - Molecular functioni

    1. [heparan sulfate]-glucosamine N-sulfotransferase activity Source: MGI
    2. deacetylase activity Source: MGI
    3. sulfotransferase activity Source: MGI

    GO - Biological processi

    1. embryonic neurocranium morphogenesis Source: MGI
    2. embryonic viscerocranium morphogenesis Source: MGI
    3. fibroblast growth factor receptor signaling pathway Source: MGI
    4. forebrain development Source: MGI
    5. glycosaminoglycan metabolic process Source: MGI
    6. heparan sulfate proteoglycan biosynthetic process Source: UniProtKB-UniPathway
    7. heparin biosynthetic process Source: UniProtKB-UniPathway
    8. inflammatory response Source: UniProtKB-KW
    9. MAPK cascade Source: MGI
    10. midbrain development Source: MGI
    11. organ morphogenesis Source: MGI
    12. polysaccharide biosynthetic process Source: MGI
    13. protein deacetylation Source: MGI
    14. protein sulfation Source: MGI
    15. respiratory gaseous exchange Source: MGI
    16. smoothened signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_198654. HS-GAG biosynthesis.
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:104719. Ndst1.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice survive until birth but are cyanotic and die neonatally in a condition resembling respiratory distress syndrome. In addition, a minor proportion of mice embryos die during the embryonic period. Mutant mice display cerebral hypoplasia and craniofacial defects, disturbed Ca2+ kinetics in myotubes. They also display deficiencies L-selectin and chemokine-mediated neutrophil trafficking during inflammatory responses.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi486 – 4861C → W: Loss of deacetylase activity but does not affect sulfotransferase activity. 1 Publication
    Mutagenesisi614 – 6141K → A: Loss of sulfotransferase activity but does not affect deacetylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 882882Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1PRO_0000225655Add
    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 ↔ 828By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ3UHN9.
    PRIDEiQ3UHN9.

    PTM databases

    PhosphoSiteiQ3UHN9.

    Expressioni

    Tissue specificityi

    Widely expressed in adult and throughout development.1 Publication

    Gene expression databases

    BgeeiQ3UHN9.
    GenevestigatoriQ3UHN9.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    DIPiDIP-29859N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3UHN9.
    SMRiQ3UHN9. Positions 579-879.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 882844LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00740000115140.
    HOGENOMiHOG000008010.
    HOVERGENiHBG082011.
    InParanoidiQ3UHN9.
    KOiK02576.
    OMAiTNTIDYH.
    OrthoDBiEOG7FXZXJ.
    PhylomeDBiQ3UHN9.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3UHN9-1) [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

    MPALACLRRL CRHLSPQAVL FLLFVFCLFS VFVSAYYLYG WNRGLEPSAD    50
    ASESDCGDPP PVAPSRLLPI KPVQAVAPSR TDPLVLVFVE SLYSQLGQEV 100
    VAILESSRFK YRTEIAPGKG DMPTLTDKGR GRFALIIYEN ILKYVNLDAW 150
    NRELLDKYCV AYGVGIIGFF KANENSLLSA QLKGFPLFLH SNLGLKDCSI 200
    NPKSPLLYVT RPSEVEKGVL PGEDWTVFQS NHSTYEPVLL AKTRSSESIP 250
    HLGADAGLHA ALHATVVQDL GLHDGIQRVL FGNNLNFWLH KLVFVDAVAF 300
    LTGKRLSLPL DRYILVDIDD IFVGKEGTRM KVEDVKALFD TQNELRTHIP 350
    NFTFNLGYSG KFFHTGTDAE DAGDDLLLSY VKEFWWFPHM WSHMQPHLFH 400
    NQSVLAEQMA LNKKFAVEHG IPTDMGYAVA PHHSGVYPVH VQLYEAWKQV 450
    WGIRVTSTEE YPHLKPARYR RGFIHNGIMV LPRQTCGLFT HTIFYNEYPG 500
    GSSELDKIIN GGELFLTVLL NPISIFMTHL SNYGNDRLGL YTFKHLVRFL 550
    HSWTNLRLQT LPPVQLAQKY FQIFSEEKDP LWQDPCEDKR HKDIWSKEKT 600
    CDRFPKLLII GPQKTGTTAL YLFLGMHPDL SSNYPSSETF EEIQFFNGHN 650
    YHKGIDWYME FFPIPSNTTS DFYFEKSANY FDSEVAPRRA AALLPKAKIL 700
    SILINPADRA YSWYQHQRAH DDPVALKYTF HEVITAGPDA SSKLRALQNR 750
    CLVPGWYATH IERWLSAFHA NQILVLDGKL LRTEPAKVMD TVQKFLGVTS 800
    TVDYHKTLAF DPKKGFWCQL LEGGKTKCLG KSKGRKYPEM DLDSRAFLKD 850
    YFRDHNIELS KLLYKMGQTL PTWLREDLQN TR 882
    Length:882
    Mass (Da):100,726
    Last modified:March 7, 2006 - v2
    Checksum:i8BE300ABCB8E648D
    GO
    Isoform 2 (identifier: Q3UHN9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         480-495: VLPRQTCGLFTHTIFY → RLGDTEVKNPDKSLTS
         496-882: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:495
    Mass (Da):55,731
    Checksum:i7023F8CAA85F2344
    GO
    Isoform 3 (identifier: Q3UHN9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-185: KYVNLDAWNR...SLLSAQLKGF → SISCHSSSVL...EGFEPGPARV
         186-882: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:185
    Mass (Da):20,078
    Checksum:i4877F728103F7FCB
    GO

    Sequence cautioni

    The sequence BAE41527.1 differs from that shown. Reason: Frameshift at position 185.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091F → S in BAE27818. (PubMed:16141072)Curated
    Sequence conflicti789 – 7891M → V in AAC17228. (PubMed:9565617)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 18543KYVNL…QLKGF → SISCHSSSVLQTVKGKSAAG PFAQPGRKTGHVPEGFEPGP ARV in isoform 3. 1 PublicationVSP_017399Add
    BLAST
    Alternative sequencei186 – 882697Missing in isoform 3. 1 PublicationVSP_017400Add
    BLAST
    Alternative sequencei480 – 49516VLPRQ…HTIFY → RLGDTEVKNPDKSLTS in isoform 2. 1 PublicationVSP_017401Add
    BLAST
    Alternative sequencei496 – 882387Missing in isoform 2. 1 PublicationVSP_017402Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049894 mRNA. Translation: AAC17228.1.
    AF074926 mRNA. Translation: AAD15980.1.
    AK035642 mRNA. Translation: BAC29136.1.
    AK147282 mRNA. Translation: BAE27818.1.
    AK170041 mRNA. Translation: BAE41527.1. Frameshift.
    AK171013 mRNA. Translation: BAE42184.1.
    BC066098 mRNA. Translation: AAH66098.1.
    BC079561 mRNA. Translation: AAH79561.1.
    CCDSiCCDS37834.1. [Q3UHN9-1]
    RefSeqiNP_032332.2. NM_008306.4. [Q3UHN9-1]
    XP_006525730.1. XM_006525667.1. [Q3UHN9-1]
    XP_006525731.1. XM_006525668.1. [Q3UHN9-1]
    XP_006525732.1. XM_006525669.1. [Q3UHN9-1]
    XP_006525733.1. XM_006525670.1. [Q3UHN9-1]
    XP_006525734.1. XM_006525671.1. [Q3UHN9-1]
    XP_006525735.1. XM_006525672.1. [Q3UHN9-1]
    UniGeneiMm.181862.
    Mm.486185.

    Genome annotation databases

    EnsembliENSMUST00000169273; ENSMUSP00000126623; ENSMUSG00000054008. [Q3UHN9-1]
    GeneIDi15531.
    KEGGimmu:15531.
    UCSCiuc008fat.1. mouse. [Q3UHN9-1]
    uc008fav.1. mouse. [Q3UHN9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049894 mRNA. Translation: AAC17228.1 .
    AF074926 mRNA. Translation: AAD15980.1 .
    AK035642 mRNA. Translation: BAC29136.1 .
    AK147282 mRNA. Translation: BAE27818.1 .
    AK170041 mRNA. Translation: BAE41527.1 . Frameshift.
    AK171013 mRNA. Translation: BAE42184.1 .
    BC066098 mRNA. Translation: AAH66098.1 .
    BC079561 mRNA. Translation: AAH79561.1 .
    CCDSi CCDS37834.1. [Q3UHN9-1 ]
    RefSeqi NP_032332.2. NM_008306.4. [Q3UHN9-1 ]
    XP_006525730.1. XM_006525667.1. [Q3UHN9-1 ]
    XP_006525731.1. XM_006525668.1. [Q3UHN9-1 ]
    XP_006525732.1. XM_006525669.1. [Q3UHN9-1 ]
    XP_006525733.1. XM_006525670.1. [Q3UHN9-1 ]
    XP_006525734.1. XM_006525671.1. [Q3UHN9-1 ]
    XP_006525735.1. XM_006525672.1. [Q3UHN9-1 ]
    UniGenei Mm.181862.
    Mm.486185.

    3D structure databases

    ProteinModelPortali Q3UHN9.
    SMRi Q3UHN9. Positions 579-879.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29859N.

    PTM databases

    PhosphoSitei Q3UHN9.

    Proteomic databases

    PaxDbi Q3UHN9.
    PRIDEi Q3UHN9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169273 ; ENSMUSP00000126623 ; ENSMUSG00000054008 . [Q3UHN9-1 ]
    GeneIDi 15531.
    KEGGi mmu:15531.
    UCSCi uc008fat.1. mouse. [Q3UHN9-1 ]
    uc008fav.1. mouse. [Q3UHN9-2 ]

    Organism-specific databases

    CTDi 3340.
    MGIi MGI:104719. Ndst1.

    Phylogenomic databases

    eggNOGi NOG267831.
    GeneTreei ENSGT00740000115140.
    HOGENOMi HOG000008010.
    HOVERGENi HBG082011.
    InParanoidi Q3UHN9.
    KOi K02576.
    OMAi TNTIDYH.
    OrthoDBi EOG7FXZXJ.
    PhylomeDBi Q3UHN9.
    TreeFami TF313193.

    Enzyme and pathway databases

    UniPathwayi UPA00756 .
    UPA00862 .
    Reactomei REACT_198654. HS-GAG biosynthesis.

    Miscellaneous databases

    ChiTaRSi NDST1. mouse.
    NextBioi 288464.
    PROi Q3UHN9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UHN9.
    Genevestigatori Q3UHN9.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR021930. Heparan_SO4_deacetylase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF12062. HSNSD. 1 hit.
    PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and expression in mouse of two heparan sulfate glucosaminyl N-deacetylase/N-sulfotransferase genes."
      Kusche-Gullberg M., Eriksson I., Pikas D.S., Kjellen L.
      J. Biol. Chem. 273:11902-11907(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Leaden X A1.
      Tissue: Liver.
    2. "Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4."
      Aikawa J., Grobe K., Tsujimoto M., Esko J.D.
      J. Biol. Chem. 276:5876-5882(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Lung.
    3. "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] (ISOFORMS 1; 2 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Urinary bladder.
    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].
      Strain: C57BL/6J.
      Tissue: Brain.
    5. "Targeted disruption of NDST-1 gene leads to pulmonary hypoplasia and neonatal respiratory distress in mice."
      Fan G., Xiao L., Cheng L., Wang X., Sun B., Hu G.
      FEBS Lett. 467:7-11(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Defective heparan sulfate biosynthesis and neonatal lethality in mice lacking N-deacetylase/N-sulfotransferase-1."
      Ringvall M., Ledin J., Holmborn K., van Kuppevelt T., Ellin F., Eriksson I., Olofsson A.M., Kjellen L., Forsberg E.
      J. Biol. Chem. 275:25926-25930(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Distinct effects on heparan sulfate structure by different active site mutations in NDST-1."
      Bengtsson J., Eriksson I., Kjellen L.
      Biochemistry 42:2110-2115(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-486 AND LYS-614.
    8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "Cerebral hypoplasia and craniofacial defects in mice lacking heparan sulfate Ndst1 gene function."
      Grobe K., Inatani M., Pallerla S.R., Castagnola J., Yamaguchi Y., Esko J.D.
      Development 132:3777-3786(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    10. "Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses."
      Wang L., Fuster M., Sriramarao P., Esko J.D.
      Nat. Immunol. 6:902-910(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiNDST1_MOUSE
    AccessioniPrimary (citable) accession number: Q3UHN9
    Secondary accession number(s): O70353
    , Q3TBX3, Q3TDS3, Q8BZE5, Q9R206
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The presence of 4 different NDST 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3