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P15586

- GNS_HUMAN

UniProt

P15586 - GNS_HUMAN

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Protein

N-acetylglucosamine-6-sulfatase

Gene

GNS

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

Functioni

Catalytic activityi

Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.

Cofactori

Binds 1 calcium ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551CalciumBy similarity
Metal bindingi56 – 561CalciumBy similarity
Metal bindingi91 – 911Calcium; via 3-oxoalanineBy similarity
Metal bindingi326 – 3261CalciumBy similarity
Metal bindingi327 – 3271CalciumBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. N-acetylglucosamine-6-sulfatase activity Source: ProtInc
  3. sulfuric ester hydrolase activity Source: MGI

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan catabolic process Source: ProtInc
  3. glycosaminoglycan metabolic process Source: Reactome
  4. keratan sulfate catabolic process Source: Reactome
  5. keratan sulfate metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06046-MONOMER.
BRENDAi3.1.6.14. 2681.
ReactomeiREACT_121313. Keratan sulfate degradation.
REACT_19287. Lysosome Vesicle Biogenesis.
SABIO-RKP15586.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-6-sulfatase (EC:3.1.6.14)
Alternative name(s):
Glucosamine-6-sulfatase
Short name:
G6S
Gene namesi
Name:GNS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4422. GNS.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3D (MPS3D) [MIM:252940]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941S → I in MPS3D. 1 Publication
VAR_064070
Natural varianti304 – 3063Missing in MPS3D. 1 Publication
VAR_064071
Natural varianti340 – 3401K → R in MPS3D. 1 Publication
VAR_064072
Natural varianti418 – 4181G → E in MPS3D. 1 Publication
VAR_064073

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

MIMi252940. phenotype.
Orphaneti79272. Sanfilippo syndrome type D.
PharmGKBiPA28802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Add
BLAST
Chaini37 – 552516N-acetylglucosamine-6-sulfatasePRO_0000033413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 9113-oxoalanine (Cys)By similarity
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi183 – 1831N-linked (GlcNAc...)2 Publications
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi387 – 3871N-linked (GlcNAc...)1 Publication
Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi422 – 4221N-linked (GlcNAc...)2 Publications
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The form A (78 kDa) is processed by internal peptidase cleavage to a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP15586.
PaxDbiP15586.
PeptideAtlasiP15586.
PRIDEiP15586.

PTM databases

PhosphoSiteiP15586.

Expressioni

Gene expression databases

BgeeiP15586.
CleanExiHS_GNS.
ExpressionAtlasiP15586. baseline and differential.
GenevestigatoriP15586.

Organism-specific databases

HPAiCAB026011.
HPA013695.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1752200,EBI-389883

Protein-protein interaction databases

BioGridi109061. 21 interactions.
IntActiP15586. 7 interactions.
STRINGi9606.ENSP00000258145.

Structurei

3D structure databases

ProteinModelPortaliP15586.
SMRiP15586. Positions 46-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00400000022041.
HOGENOMiHOG000169239.
HOVERGENiHBG005840.
InParanoidiP15586.
KOiK01137.
OrthoDBiEOG75QR3Q.
PhylomeDBiP15586.
TreeFamiTF313545.

Family and domain databases

Gene3Di3.40.720.10. 3 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR012251. GlcNAc_6-SO4ase.
IPR015981. GlcNAc_6-SO4ase_euk.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PANTHERiPTHR10342:SF212. PTHR10342:SF212. 1 hit.
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
PIRSFiPIRSF036666. G6S. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15586-1) [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
MRLLPLAPGR LRRGSPRHLP SCSPALLLLV LGGCLGVFGV AAGTRRPNVV
60 70 80 90 100
LLLTDDQDEV LGGMTPLKKT KALIGEMGMT FSSAYVPSAL CCPSRASILT
110 120 130 140 150
GKYPHNHHVV NNTLEGNCSS KSWQKIQEPN TFPAILRSMC GYQTFFAGKY
160 170 180 190 200
LNEYGAPDAG GLEHVPLGWS YWYALEKNSK YYNYTLSING KARKHGENYS
210 220 230 240 250
VDYLTDVLAN VSLDFLDYKS NFEPFFMMIA TPAPHSPWTA APQYQKAFQN
260 270 280 290 300
VFAPRNKNFN IHGTNKHWLI RQAKTPMTNS SIQFLDNAFR KRWQTLLSVD
310 320 330 340 350
DLVEKLVKRL EFTGELNNTY IFYTSDNGYH TGQFSLPIDK RQLYEFDIKV
360 370 380 390 400
PLLVRGPGIK PNQTSKMLVA NIDLGPTILD IAGYDLNKTQ MDGMSLLPIL
410 420 430 440 450
RGASNLTWRS DVLVEYQGEG RNVTDPTCPS LSPGVSQCFP DCVCEDAYNN
460 470 480 490 500
TYACVRTMSA LWNLQYCEFD DQEVFVEVYN LTADPDQITN IAKTIDPELL
510 520 530 540 550
GKMNYRLMML QSCSGPTCRT PGVFDPGYRF DPRLMFSNRG SVRTRRFSKH

LL
Length:552
Mass (Da):62,082
Last modified:April 1, 1993 - v3
Checksum:i85094043F6E64468
GO
Isoform 2 (identifier: P15586-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-84: Missing.

Note: No experimental confirmation available.

Show »
Length:532
Mass (Da):59,989
Checksum:i8D6E2305AB5BBF85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521F → C in BAD97204. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941S → I in MPS3D. 1 Publication
VAR_064070
Natural varianti304 – 3063Missing in MPS3D. 1 Publication
VAR_064071
Natural varianti340 – 3401K → R in MPS3D. 1 Publication
VAR_064072
Natural varianti418 – 4181G → E in MPS3D. 1 Publication
VAR_064073
Natural varianti550 – 5501H → Q.
Corresponds to variant rs2230292 [ dbSNP | Ensembl ].
VAR_064074

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 8420Missing in isoform 2. 1 PublicationVSP_056486Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12173 mRNA. Translation: CAA78164.1.
AK302443 mRNA. Translation: BAG63740.1.
AK223484 mRNA. Translation: BAD97204.1.
AC025262 Genomic DNA. No translation available.
BC012482 mRNA. Translation: AAH12482.1.
CCDSiCCDS8970.1. [P15586-1]
PIRiS27164. KJHUGU.
RefSeqiNP_002067.1. NM_002076.3.
UniGeneiHs.334534.

Genome annotation databases

EnsembliENST00000258145; ENSP00000258145; ENSG00000135677. [P15586-1]
ENST00000542058; ENSP00000444819; ENSG00000135677. [P15586-2]
GeneIDi2799.
KEGGihsa:2799.
UCSCiuc001ssg.4. human. [P15586-1]

Polymorphism databases

DMDMi232126.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12173 mRNA. Translation: CAA78164.1 .
AK302443 mRNA. Translation: BAG63740.1 .
AK223484 mRNA. Translation: BAD97204.1 .
AC025262 Genomic DNA. No translation available.
BC012482 mRNA. Translation: AAH12482.1 .
CCDSi CCDS8970.1. [P15586-1 ]
PIRi S27164. KJHUGU.
RefSeqi NP_002067.1. NM_002076.3.
UniGenei Hs.334534.

3D structure databases

ProteinModelPortali P15586.
SMRi P15586. Positions 46-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109061. 21 interactions.
IntActi P15586. 7 interactions.
STRINGi 9606.ENSP00000258145.

PTM databases

PhosphoSitei P15586.

Polymorphism databases

DMDMi 232126.

Proteomic databases

MaxQBi P15586.
PaxDbi P15586.
PeptideAtlasi P15586.
PRIDEi P15586.

Protocols and materials databases

DNASUi 2799.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258145 ; ENSP00000258145 ; ENSG00000135677 . [P15586-1 ]
ENST00000542058 ; ENSP00000444819 ; ENSG00000135677 . [P15586-2 ]
GeneIDi 2799.
KEGGi hsa:2799.
UCSCi uc001ssg.4. human. [P15586-1 ]

Organism-specific databases

CTDi 2799.
GeneCardsi GC12M065107.
H-InvDB HIX0010785.
HGNCi HGNC:4422. GNS.
HPAi CAB026011.
HPA013695.
MIMi 252940. phenotype.
607664. gene.
neXtProti NX_P15586.
Orphaneti 79272. Sanfilippo syndrome type D.
PharmGKBi PA28802.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00400000022041.
HOGENOMi HOG000169239.
HOVERGENi HBG005840.
InParanoidi P15586.
KOi K01137.
OrthoDBi EOG75QR3Q.
PhylomeDBi P15586.
TreeFami TF313545.

Enzyme and pathway databases

BioCyci MetaCyc:HS06046-MONOMER.
BRENDAi 3.1.6.14. 2681.
Reactomei REACT_121313. Keratan sulfate degradation.
REACT_19287. Lysosome Vesicle Biogenesis.
SABIO-RK P15586.

Miscellaneous databases

ChiTaRSi GNS. human.
GenomeRNAii 2799.
NextBioi 11033.
PROi P15586.
SOURCEi Search...

Gene expression databases

Bgeei P15586.
CleanExi HS_GNS.
ExpressionAtlasi P15586. baseline and differential.
Genevestigatori P15586.

Family and domain databases

Gene3Di 3.40.720.10. 3 hits.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR012251. GlcNAc_6-SO4ase.
IPR015981. GlcNAc_6-SO4ase_euk.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
PANTHERi PTHR10342:SF212. PTHR10342:SF212. 1 hit.
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036666. G6S. 1 hit.
SUPFAMi SSF53649. SSF53649. 2 hits.
PROSITEi PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases."
    Robertson D.A., Freeman C., Morris C.P., Hopwood J.J.
    Biochem. J. 288:539-544(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-422.
    Tissue: Endothelial cell.
  2. "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] (ISOFORM 2).
    Tissue: Testis.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Urinary bladder.
  6. "Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase."
    Robertson D.A., Freeman C., Nelson P.V., Morris C.P., Hopwood J.J.
    Biochem. Biophys. Res. Commun. 157:218-224(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-552 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  7. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-183 AND ASN-279.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-183; ASN-317; ASN-387 AND ASN-422.
    Tissue: Liver.
  9. "Genomic basis of mucopolysaccharidosis type IIID (MIM 252940) revealed by sequencing of GNS encoding N-acetylglucosamine-6-sulfatase."
    Mok A., Cao H., Hegele R.A.
    Genomics 81:1-5(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MPS3D.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANTS MPS3D ILE-94; 304-GLU--LEU-306 DEL; ARG-340 AND GLU-418.

Entry informationi

Entry nameiGNS_HUMAN
AccessioniPrimary (citable) accession number: P15586
Secondary accession number(s): B4DYH8, Q53F05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 139 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3