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Q3UHN9

- NDST1_MOUSE

UniProt

Q3UHN9 - NDST1_MOUSE

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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

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
Complete GO annotation...

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 apparatus Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

MaxQBiQ3UHN9.
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.
GeneTreeiENSGT00760000119023.
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

        10         20         30         40         50
MPALACLRRL CRHLSPQAVL FLLFVFCLFS VFVSAYYLYG WNRGLEPSAD
60 70 80 90 100
ASESDCGDPP PVAPSRLLPI KPVQAVAPSR 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 TQNELRTHIP
360 370 380 390 400
NFTFNLGYSG KFFHTGTDAE DAGDDLLLSY VKEFWWFPHM WSHMQPHLFH
410 420 430 440 450
NQSVLAEQMA LNKKFAVEHG IPTDMGYAVA PHHSGVYPVH VQLYEAWKQV
460 470 480 490 500
WGIRVTSTEE 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 AALLPKAKIL
710 720 730 740 750
SILINPADRA YSWYQHQRAH DDPVALKYTF HEVITAGPDA SSKLRALQNR
760 770 780 790 800
CLVPGWYATH IERWLSAFHA NQILVLDGKL LRTEPAKVMD TVQKFLGVTS
810 820 830 840 850
TVDYHKTLAF DPKKGFWCQL LEGGKTKCLG KSKGRKYPEM DLDSRAFLKD
860 870 880
YFRDHNIELS KLLYKMGQTL PTWLREDLQN TR
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

MaxQBi Q3UHN9.
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 ENSGT00760000119023.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 89 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