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P15848 (ARSB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arylsulfatase B

Short name=ASB
EC=3.1.6.12
Alternative name(s):
N-acetylgalactosamine-4-sulfatase
Short name=G4S
Gene names
Name:ARSB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Subcellular location

Lysosome.

Post-translational modification

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. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD).

Involvement in disease

Defects in ARSB are the cause of mucopolysaccharidosis type 6 (MPS6) [MIM:253200]; also known as Maroteaux-Lamy syndrome. MPS6 is an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22

Arylsulfatase B activity is defective in multiple sulfatase deficiency (MSD) [MIM:272200]. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Note=Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys-91 that is not converted to 3-oxoalanine. Ref.7 Ref.8

Sequence similarities

Belongs to the sulfatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636Or 38 Potential
Chain37 – 533497Arylsulfatase B
PRO_0000033421

Sites

Active site1471
Metal binding531Calcium
Metal binding541Calcium
Metal binding911Calcium; via 3-oxoalanine Ref.7
Metal binding3001Calcium
Metal binding3011Calcium
Binding site1451Substrate By similarity
Binding site2421Substrate By similarity
Binding site3181Substrate By similarity

Amino acid modifications

Modified residue9113-oxoalanine (Cys)
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...)
Glycosylation2911N-linked (GlcNAc...) Probable
Glycosylation3661N-linked (GlcNAc...) Ref.9
Glycosylation4261N-linked (GlcNAc...)
Glycosylation4581N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 521
Disulfide bond121 ↔ 155
Disulfide bond181 ↔ 192
Disulfide bond405 ↔ 447

Natural variations

Natural variant651S → F in MPS6; intermediate form. Ref.19
VAR_019017
Natural variant861Missing in MPS6; severe form; low protein levels and activity.
VAR_019018
Natural variant921T → M in MPS6; mild form. Ref.16
VAR_007294
Natural variant951R → Q in MPS6; mild/severe form. Ref.16
VAR_007295
Natural variant1161P → H in MPS6; severe form. Ref.19
VAR_019019
Natural variant1171C → R in MPS6; severe form. Ref.12
VAR_007296
Natural variant1371G → V in MPS6; intermediate form. Ref.11
VAR_007297
Natural variant1421M → I in MPS6. Ref.15
VAR_019020
Natural variant1441G → R in MPS6; severe form; severe reduction of activity. Ref.13
VAR_019021
Natural variant1461W → L in MPS6. Ref.15
VAR_019022
Natural variant1461W → R in MPS6. Ref.15
VAR_019023
Natural variant1461W → S in MPS6. Ref.15
VAR_019024
Natural variant1521R → W in MPS6; intermediate form. Ref.14
VAR_007298
Natural variant1601R → Q in MPS6; intermediate form. Ref.14
VAR_007299
Natural variant1921C → R in MPS6; mild form; severe reduction of activity. Ref.13 Ref.20 Ref.21
VAR_019025
Natural variant2101Y → C in MPS6; mild/intermediate. Ref.16 Ref.22
VAR_007300
Natural variant2361L → P in MPS6; mild form. Ref.12 Ref.22
VAR_007301
Natural variant2391Q → R in MPS6. Ref.20 Ref.21
VAR_019026
Natural variant3021G → R in MPS6; severe form. Ref.17
VAR_007302
Natural variant3121W → C in MPS6; severe form; low protein levels and activity. Ref.22
VAR_019027
Natural variant3151R → Q in MPS6; intermediate form. Ref.19 Ref.22
VAR_019028
Natural variant3211L → P in MPS6; intermediate form; severe reduction of activity. Ref.13 Ref.22
VAR_019029
Natural variant3581V → L.
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].
VAR_061883
Natural variant3581V → M. Ref.3 Ref.4 Ref.18 Ref.19 Ref.21 Ref.22
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].
VAR_016061
Natural variant3761V → M. Ref.11 Ref.22
Corresponds to variant rs17220759 [ dbSNP | Ensembl ].
VAR_007303
Natural variant3841S → N in MPS6. Ref.22
Corresponds to variant rs25414 [ dbSNP | Ensembl ].
VAR_019030
Natural variant3931H → P in MPS6; mild/severe form. Ref.16
VAR_007304
Natural variant3991F → L in MPS6. Ref.21
VAR_019031
Natural variant4051C → Y in MPS6; mild form. Ref.12
VAR_007305
Natural variant4841R → G in MPS6. Ref.22
VAR_019032
Natural variant4981L → P in MPS6; mild/severe form. Ref.16
VAR_007306
Natural variant5211C → Y in MPS6; severe form; severe reduction of activity. Ref.13
VAR_019033
Natural variant5311P → R in MPS6; mild form. Ref.19
VAR_019034

Experimental info

Sequence conflict1531K → F AA sequence Ref.1
Sequence conflict408 – 4103NSM → SPC AA sequence Ref.1

Secondary structure

............................................................................... 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15848 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5983FB6911C4789A

FASTA53359,687
        10         20         30         40         50         60 
MGPRGAASLP RGPGPRRLLL PVVLPLLLLL LLAPPGSGAG ASRPPHLVFL LADDLGWNDV 

        70         80         90        100        110        120 
GFHGSRIRTP HLDALAAGGV LLDNYYTQPL CTPSRSQLLT GRYQIRTGLQ HQIIWPCQPS 

       130        140        150        160        170        180 
CVPLDEKLLP QLLKEAGYTT HMVGKWHLGM YRKECLPTRR GFDTYFGYLL GSEDYYSHER 

       190        200        210        220        230        240 
CTLIDALNVT RCALDFRDGE EVATGYKNMY STNIFTKRAI ALITNHPPEK PLFLYLALQS 

       250        260        270        280        290        300 
VHEPLQVPEE YLKPYDFIQD KNRHHYAGMV SLMDEAVGNV TAALKSSGLW NNTVFIFSTD 

       310        320        330        340        350        360 
NGGQTLAGGN NWPLRGRKWS LWEGGVRGVG FVASPLLKQK GVKNRELIHI SDWLPTLVKL 

       370        380        390        400        410        420 
ARGHTNGTKP LDGFDVWKTI SEGSPSPRIE LLHNIDPNFV DSSPCPRNSM APAKDDSSLP 

       430        440        450        460        470        480 
EYSAFNTSVH AAIRHGNWKL LTGYPGCGYW FPPPSQYNVS EIPSSDPPTK TLWLFDIDRD 

       490        500        510        520        530 
PEERHDLSRE YPHIVTKLLS RLQFYHKHSV PVYFPAQDPR CDPKATGVWG PWM 

« Hide

References

« Hide 'large scale' references
[1]"Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B."
Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuehlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K.
J. Biol. Chem. 265:3374-3381(1990) [PubMed: 2303452] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-119; 135-158; 161-168; 286-295; 319-337; 379-387; 389-410; 440-450; 490-501; 508-520 AND 525-533.
Tissue: Placenta and Testis.
[2]"Human arylsulfatase B: MOPAC cloning, nucleotide sequence of a full-length cDNA, and regions of amino acid identity with arylsulfatases A and C."
Schuchman E.H., Jackson C.E., Desnick R.J.
Genomics 6:149-158(1990) [PubMed: 1968043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the human arylsulfatase B gene."
Modaressi S., Rupp K., von Figura K., Peters C.
Biol. Chem. Hoppe-Seyler 374:327-335(1993) [PubMed: 7687847] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-358.
[4]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-358.
Tissue: Cerebellum.
[5]"Human N-acetylgalactosamine-4-sulphatase: protein maturation and isolation of genomic clones."
Litjens T., Morris C.P., Gibson G.J., Beckmann K.R., Hopwood J.J.
Biochem. Int. 24:209-215(1991) [PubMed: 1930244] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
[6]"Components and proteolytic processing sites of arylsulfatase B from human placenta."
Kobayashi T., Honke K., Jin T., Gasa S., Miyazaki T., Makita A.
Biochim. Biophys. Acta 1159:243-247(1992) [PubMed: 1390929] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-55; 424-454 AND 466-483.
Tissue: Placenta.
[7]"A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency."
Schmidt B., Selmer T., Ingendoh A., von Figura K.
Cell 82:271-278(1995) [PubMed: 7628016] [Abstract]
Cited for: OXOALANINE AT CYS-91, MASS SPECTROMETRY, ABSENCE OF OXOALANINE IN MSD.
[8]"Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency."
Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I., Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G., Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M., Carrozzo R., Carella M., Ballabio A.
Hum. Mutat. 23:576-581(2004) [PubMed: 15146462] [Abstract]
Cited for: INVOLVEMENT IN MSD.
[9]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-366, MASS SPECTROMETRY.
Tissue: Liver.
[10]"Structure of a human lysosomal sulfatase."
Bond C.S., Clements P.R., Ashby S.J., Collyer C.A., Harrop S.J., Hopwood J.J., Guss J.M.
Structure 5:277-289(1997) [PubMed: 9032078] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[11]"Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B."
Wicker G., Prill V., Brooks D.A., Gibson G.J., Hopwood J.J., von Figura K., Peters C.
J. Biol. Chem. 266:21386-21391(1991) [PubMed: 1718978] [Abstract]
Cited for: VARIANT MPS6 VAL-137, VARIANT MET-376.
[12]"Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity."
Jin W.-D., Jackson C.E., Desnick R.J., Schuchman E.H.
Am. J. Hum. Genet. 50:795-800(1992) [PubMed: 1550123] [Abstract]
Cited for: VARIANTS MPS6 ARG-117; PRO-236 AND TYR-405.
[13]"Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes."
Isbrandt D., Arlt G., Brooks D.A., Hopwood J.J., von Figura K., Peters C.
Am. J. Hum. Genet. 54:454-463(1994) [PubMed: 8116615] [Abstract]
Cited for: VARIANTS MPS6 ARG-144; ARG-192; PRO-321 AND TYR-521, CHARACTERIZATION OF VARIANTS MPS6.
[14]"Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome)."
Voskoboeva E., Isbrandt D., von Figura K., Krasnopolskaya X., Peters C.
Hum. Genet. 93:259-264(1994) [PubMed: 8125475] [Abstract]
Cited for: VARIANTS MPS6 TRP-152 AND GLN-160.
[15]"N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI."
Simonaro C.M., Schuchman E.H.
Biochim. Biophys. Acta 1272:129-132(1995) [PubMed: 8541342] [Abstract]
Cited for: VARIANTS MPS6 ILE-142; ARG-146; LEU-146 AND SER-146.
[16]"Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS6 patients."
Litjens T., Brooks D.A., Peters C., Gibson G.J., Hopwood J.J.
Am. J. Hum. Genet. 58:1127-1134(1996) [PubMed: 8651289] [Abstract]
Cited for: VARIANTS MPS6 MET-92; GLN-95; CYS-210; PRO-393 AND PRO-498.
[17]"Two novel mutations of the arylsulfatase B gene in two Italian patients with severe form of mucopolysaccharidosis."
Villani G.R.D., Balzano N., Di Natale P.
Hum. Mutat. 11:410-410(1998) [PubMed: 10206678] [Abstract]
Cited for: VARIANT MPS-IV ARG-302.
[18]"Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome."
Wang D.G., Fan J.-B., Siao C.-J., Berno A., Young P., Sapolsky R., Ghandour G., Perkins N., Winchester E., Spencer J., Kruglyak L., Stein L., Hsie L., Topaloglou T., Hubbell E., Robinson E., Mittmann M., Morris M.S. expand/collapse author list , Shen N., Kilburn D., Rioux J., Nusbaum C., Rozen S., Hudson T.J., Lipshutz R., Chee M., Lander E.S.
Science 280:1077-1082(1998) [PubMed: 9582121] [Abstract]
Cited for: VARIANT MET-358.
[19]"Maroteaux-lamy syndrome: five novel mutations and their structural localization."
Villani G.R.D., Balzano N., Vitale D., Saviano M., Pavone V., Di Natale P.
Biochim. Biophys. Acta 1453:185-192(1999) [PubMed: 10036316] [Abstract]
Cited for: VARIANTS MPS6 PHE-65; HIS-116; GLN-315 AND ARG-531, VARIANT MET-358.
[20]"A novel mutation (Q239R) identified in a Taiwan Chinese patient with type VI mucopolysaccharidosis (Maroteaux-Lamy syndrome)."
Wu J.-Y., Yang C.-F., Lee C.-C., Chang J.-G., Tsai F.-J.
Hum. Mutat. 15:389-390(2000) [PubMed: 10738004] [Abstract]
Cited for: VARIANTS MPS6 ARG-192 AND ARG-239.
[21]"Mucopolysaccharidosis type VI: report of two Taiwanese patients and identification of one novel mutation."
Yang C.-F., Wu J.-Y., Lin S.-P., Tsai F.-J.
J. Formos. Med. Assoc. 100:820-823(2001) [PubMed: 11802522] [Abstract]
Cited for: VARIANTS MPS6 ARG-192; ARG-239 AND LEU-399, VARIANT MET-358.
[22]"Mutational analysis of mucopolysaccharidosis type VI patients undergoing a trial of enzyme replacement therapy."
Karageorgos L., Harmatz P., Simon J., Pollard A., Clements P.R., Brooks D.A., Hopwood J.J.
Hum. Mutat. 23:229-233(2004) [PubMed: 14974081] [Abstract]
Cited for: VARIANTS MPS6 TYR-86 DEL; CYS-210; PRO-236; CYS-312; GLN-315; PRO-321; ASN-384 AND GLY-484, VARIANTS MET-358 AND MET-376, CHARACTERIZATION OF VARIANTS MPS6 TYR-86 DEL AND CYS-312.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05225 mRNA. Translation: AAA51784.1.
M32373 mRNA. Translation: AAA51779.1.
X72735 expand/collapse EMBL AC list , X72736, X72737, X72738, X72739, X72740, X72741, X72742 Genomic DNA. Translation: CAA51272.1.
AK314903 mRNA. Translation: BAG37417.1.
S57777 Genomic DNA. Translation: AAB19988.1.
IPIIPI00306576.
PIRKJHUAB. S35990.
RefSeqNP_000037.2. NM_000046.3.
UniGeneHs.149103.
Hs.604199.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSUX-ray2.50A42-533[»]
ProteinModelPortalP15848.
SMRP15848. Positions 42-533.
ModBaseSearch...

Protein-protein interaction databases

IntActP15848. 2 interactions.
STRINGP15848.

Polymorphism databases

DMDM114223.

Proteomic databases

PRIDEP15848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264914; ENSP00000264914; ENSG00000113273.
ENST00000341088; ENSP00000342327; ENSG00000113273.
GeneID411.
KEGGhsa:411.
UCSCuc003kfq.1. human.

Organism-specific databases

CTD411.
GeneCardsGC05M078108.
H-InvDBHIX0018251.
HGNCHGNC:714. ARSB.
HPAHPA037770.
HPA037771.
MIM253200. phenotype.
272200. phenotype.
611542. gene.
neXtProtNX_P15848.
Orphanet583. Mucopolysaccharidosis type 6.
585. Multiple sulfatase deficiency.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12928.
GeneTreeENSGT00560000077076.
HOGENOMHBG651618.
HOVERGENHBG004282.
InParanoidP15848.
OMARHDLSRE.
OrthoDBEOG4DV5M0.
PhylomeDBP15848.

Enzyme and pathway databases

BioCycMetaCyc:HS03665-MONOMER.
BRENDA3.1.6.12. 2681.

Gene expression databases

ArrayExpressP15848.
BgeeP15848.
CleanExHS_ARSB.
GenevestigatorP15848.
GermOnlineENSG00000113273. Homo sapiens.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
KOK01135.
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio1737.
SOURCESearch...

Entry information

Entry nameARSB_HUMAN
AccessionPrimary (citable) accession number: P15848
Secondary accession number(s): B2RC20, Q9UDI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 25, 2012
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families