P15848 (ARSB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Mucopolysaccharidosis 6 (MPS6) [MIM:253200]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 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: The protein represented in this entry is involved in disease pathogenesis. 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.10 Ref.11
Sequence similarities	Belongs to the sulfatase family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Ichthyosis Leukodystrophy Metachromatic leukodystrophy Mucopolysaccharidosis
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	autophagy Inferred from electronic annotation. Source: Compara carbohydrate metabolic process Traceable author statement. Source: Reactome central nervous system development Inferred from electronic annotation. Source: Compara chondroitin sulfate catabolic process Traceable author statement. Source: Reactome glycosphingolipid metabolic process Traceable author statement. Source: Reactome lysosomal transport Traceable author statement Ref.1. Source: ProtInc lysosome organization Traceable author statement Ref.14. Source: ProtInc phospholipid metabolic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to pH Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara endoplasmic reticulum lumen Traceable author statement. Source: Reactome lysosomal lumen Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara rough endoplasmic reticulum Inferred from electronic annotation. Source: Compara
Molecular_function	N-acetylgalactosamine-4-sulfatase activity Traceable author statement. Source: Reactome arylsulfatase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P15848-1)

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.

Isoform 2 (identifier: P15848-2)

The sequence of this isoform differs from the canonical sequence as follows:
     405-533: CPRNSMAPAK...KATGVWGPWM → YWPECSLLL

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 36

36

Or 38 Potential

Chain

37 – 533

497

Arylsulfatase B

PRO_0000033421

Sites

Active site

147

1

Metal binding

53

1

Calcium

Metal binding

54

1

Calcium

Metal binding

91

1

Calcium; via 3-oxoalanine Ref.10

Metal binding

300

1

Calcium

Metal binding

301

1

Calcium

Binding site

145

1

Substrate By similarity

Binding site

242

1

Substrate By similarity

Binding site

318

1

Substrate By similarity

Amino acid modifications

Modified residue

91

1

3-oxoalanine (Cys)

Glycosylation

188

1

N-linked (GlcNAc...) Potential

Glycosylation

279

1

N-linked (GlcNAc...)

Glycosylation

291

1

N-linked (GlcNAc...) Probable

Glycosylation

366

1

N-linked (GlcNAc...) Ref.12

Glycosylation

426

1

N-linked (GlcNAc...)

Glycosylation

458

1

N-linked (GlcNAc...) Potential

Disulfide bond

117 ↔ 521

Disulfide bond

121 ↔ 155

Disulfide bond

181 ↔ 192

Disulfide bond

405 ↔ 447

Natural variations

Alternative sequence

405 – 533

129

CPRNS…WGPWM → YWPECSLLL in isoform 2.

VSP_042721

Natural variant

65

1

S → F in MPS6; intermediate form. Ref.22

VAR_019017

Natural variant

86

1

Missing in MPS6; severe form; low protein levels and activity. Ref.25

VAR_019018

Natural variant

92

1

T → M in MPS6; mild form. Ref.19

VAR_007294

Natural variant

95

1

R → Q in MPS6; mild/severe form. Ref.19

VAR_007295

Natural variant

116

1

P → H in MPS6; severe form. Ref.22

VAR_019019

Natural variant

117

1

C → R in MPS6; severe form. Ref.15

VAR_007296

Natural variant

137

1

G → V in MPS6; intermediate form. Ref.14

VAR_007297

Natural variant

142

1

M → I in MPS6. Ref.18

VAR_019020

Natural variant

144

1

G → R in MPS6; severe form; severe reduction of activity. Ref.16

VAR_019021

Natural variant

146

1

W → L in MPS6. Ref.18

VAR_019022

Natural variant

146

1

W → R in MPS6. Ref.18

VAR_019023

Natural variant

146

1

W → S in MPS6. Ref.18

VAR_019024

Natural variant

152

1

R → W in MPS6; intermediate form. Ref.17

VAR_007298

Natural variant

160

1

R → Q in MPS6; intermediate form. Ref.17

VAR_007299

Natural variant

192

1

C → R in MPS6; mild form; severe reduction of activity. Ref.16 Ref.23 Ref.24

VAR_019025

Natural variant

210

1

Y → C in MPS6; mild/intermediate. Ref.19 Ref.25

VAR_007300

Natural variant

236

1

L → P in MPS6; mild form. Ref.15 Ref.25

VAR_007301

Natural variant

239

1

Q → R in MPS6. Ref.23 Ref.24

VAR_019026

Natural variant

302

1

G → R in MPS6; severe form. Ref.20

VAR_007302

Natural variant

312

1

W → C in MPS6; severe form; low protein levels and activity. Ref.25

VAR_019027

Natural variant

315

1

R → Q in MPS6; intermediate form. Ref.22 Ref.25

VAR_019028

Natural variant

321

1

L → P in MPS6; intermediate form; severe reduction of activity. Ref.16 Ref.25

VAR_019029

Natural variant

358

1

V → L.
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].

VAR_061883

Natural variant

358

1

V → M. Ref.3 Ref.4 Ref.21 Ref.22 Ref.24 Ref.25
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].

VAR_016061

Natural variant

376

1

V → M. Ref.14 Ref.25
Corresponds to variant rs17220759 [ dbSNP | Ensembl ].

VAR_007303

Natural variant

384

1

S → N in MPS6. Ref.25
Corresponds to variant rs25414 [ dbSNP | Ensembl ].

VAR_019030

Natural variant

393

1

H → P in MPS6; mild/severe form. Ref.19

VAR_007304

Natural variant

399

1

F → L in MPS6. Ref.24

VAR_019031

Natural variant

405

1

C → Y in MPS6; mild form. Ref.15

VAR_007305

Natural variant

484

1

R → G in MPS6. Ref.25

VAR_019032

Natural variant

498

1

L → P in MPS6; mild/severe form. Ref.19

VAR_007306

Natural variant

521

1

C → Y in MPS6; severe form; severe reduction of activity. Ref.16

VAR_019033

Natural variant

531

1

P → R in MPS6; mild form. Ref.22

VAR_019034

Experimental info

Sequence conflict

153

1

K → F AA sequence Ref.1

Sequence conflict

408 – 410

3

NSM → SPC AA sequence Ref.1

Secondary structure

1

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533

Helix Strand Turn

Details...

Beta strand

46 – 54

9

Helix

61 – 63

3

Helix

70 – 77

8

Beta strand

79 – 82

4

Helix

93 – 100

8

Helix

104 – 107

4

Helix

129 – 135

7

Beta strand

139 – 144

6

Helix

153 – 155

3

Helix

157 – 159

3

Beta strand

163 – 167

5

Beta strand

169 – 171

3

Turn

175 – 177

3

Beta strand

179 – 184

6

Turn

185 – 188

4

Beta strand

189 – 194

6

Helix

211 – 224

14

Beta strand

232 – 237

6

Beta strand

242 – 244

3

Helix

249 – 251

3

Helix

253 – 255

3

Helix

261 – 286

26

Helix

290 – 292

3

Beta strand

293 – 301

9

Helix

305 – 307

3

Beta strand

320 – 322

3

Helix

323 – 326

4

Beta strand

330 – 333

4

Beta strand

341 – 344

4

Helix

350 – 352

3

Helix

353 – 360

8

Helix

377 – 382

6

Beta strand

390 – 396

7

Beta strand

429 – 435

7

Beta strand

438 – 443

6

Turn

454 – 456

3

Beta strand

472 – 476

5

Turn

477 – 479

3

Turn

488 – 490

3

Helix

492 – 507

16

Helix

519 – 521

3

Turn

524 – 526

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 5983FB6911C4789A	FASTA	533	59,687
	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
	Isoform 2 [UniParc]. Checksum: A3B6A96052F3E839	FASTA	413	45,996
	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 ARGHTNGTKP LDGFDVWKTI SEGSPSPRIE LLHNIDPNFV DSSPYWPECS LLL

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [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. , 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 1), VARIANT MET-358. Tissue: Cerebellum.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Colon.
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
[9]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-55; 424-454 AND 466-483. Tissue: Placenta.
[10]	"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] [Europe PMC] [Abstract] Cited for: OXOALANINE AT CYS-91, MASS SPECTROMETRY, ABSENCE OF OXOALANINE IN MSD.
[11]	"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] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MSD.
[12]	"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-366, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[14]	"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] [Europe PMC] [Abstract] Cited for: VARIANT MPS6 VAL-137, VARIANT MET-376.
[15]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 ARG-117; PRO-236 AND TYR-405.
[16]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 ARG-144; ARG-192; PRO-321 AND TYR-521, CHARACTERIZATION OF VARIANTS MPS6.
[17]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 TRP-152 AND GLN-160.
[18]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 ILE-142; ARG-146; LEU-146 AND SER-146.
[19]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 MET-92; GLN-95; CYS-210; PRO-393 AND PRO-498.
[20]	"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] [Europe PMC] [Abstract] Cited for: VARIANT MPS-IV ARG-302.
[21]	"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. , 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] [Europe PMC] [Abstract] Cited for: VARIANT MET-358.
[22]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 PHE-65; HIS-116; GLN-315 AND ARG-531, VARIANT MET-358.
[23]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 ARG-192 AND ARG-239.
[24]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS MPS6 ARG-192; ARG-239 AND LEU-399, VARIANT MET-358.
[25]	"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] [Europe PMC] [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

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05225 mRNA. Translation: AAA51784.1.
M32373 mRNA. Translation: AAA51779.1.
X72735 , X72736, X72737, X72738, X72739, X72740, X72741, X72742 Genomic DNA. Translation: CAA51272.1.
AK314903 mRNA. Translation: BAG37417.1.
AC020937 Genomic DNA. No translation available.
AC025755 Genomic DNA. No translation available.
AC099485 Genomic DNA. No translation available.
AC114963 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95822.1.
BC029051 mRNA. Translation: AAH29051.1.
S57777 Genomic DNA. Translation: AAB19988.1.

IPI

IPI00306576.
IPI00413690.

PIR

KJHUAB. S35990.

RefSeq

NP_000037.2. NM_000046.3.
NP_942002.1. NM_198709.2.

UniGene

Hs.149103.
Hs.604199.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FSU	X-ray	2.50	A	42-533	[»]

ProteinModelPortal

P15848.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15848. 2 interactions.

STRING

9606.ENSP00000264914.

PTM databases

PhosphoSite

P15848.

Polymorphism databases

DMDM

114223.

Proteomic databases

PaxDb

P15848.

PRIDE

P15848.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264914; ENSP00000264914; ENSG00000113273.
ENST00000396151; ENSP00000379455; ENSG00000113273.
ENST00000565165; ENSP00000456339; ENSG00000113273.

GeneID

411.

KEGG

hsa:411.

UCSC

uc003kfq.3. human.

Organism-specific databases

CTD

411.

GeneCards

GC05M078108.

HGNC

HGNC:714. ARSB.

HPA

HPA037770.
HPA037771.

MIM

253200. phenotype.
272200. phenotype.
611542. gene.

neXtProt

NX_P15848.

Orphanet

276212. Mucopolysaccharidosis type 6, rapidly progressing.
276223. Mucopolysaccharidosis type 6, slowly progressing.

PharmGKB

PA25006.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3119.

HOGENOM

HOG000135354.

HOVERGEN

HBG004282.

InParanoid

P15848.

KO

K01135.

OMA

WLFDIDR.

OrthoDB

EOG4DV5M0.

PhylomeDB

P15848.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03665-MONOMER.

BRENDA

3.1.6.12. 2681.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

P15848.

Bgee

P15848.

CleanEx

HS_ARSB.

Genevestigator

P15848.

GermOnline

ENSG00000113273. Homo sapiens.

Family and domain databases

Gene3D

3.40.720.10. 1 hit.

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]

Pfam

PF00884. Sulfatase. 1 hit.
[Graphical view]

SUPFAM

SSF53649. Alkaline_phosphatase_core. 1 hit.

PROSITE

PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2399.

EvolutionaryTrace

P15848.

GenomeRNAi

411.

NextBio

1737.

SOURCE

Search...

Entry information

Entry name

ARSB_HUMAN

Accession

Primary (citable) accession number: P15848
Secondary accession number(s): B2RC20, Q8N322, Q9UDI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.