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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	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.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	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	lysosomal transport Traceable author statement. Source: ProtInc lysosome organization Traceable author statement. Source: ProtInc
Cellular component	lysosome Traceable author statement. Source: ProtInc
Molecular function	N-acetylgalactosamine-4-sulfatase activity Inferred from electronic annotation. Source: EC arylsulfatase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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.7

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.9

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

Natural variant

65

1

S → F in MPS6; intermediate form. Ref.19

VAR_019017

Natural variant

86

1

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

VAR_019018

Natural variant

92

1

T → M in MPS6; mild form. Ref.16

VAR_007294

Natural variant

95

1

R → Q in MPS6; mild/severe form. Ref.16

VAR_007295

Natural variant

116

1

P → H in MPS6; severe form. Ref.19

VAR_019019

Natural variant

117

1

C → R in MPS6; severe form. Ref.12

VAR_007296

Natural variant

137

1

G → V in MPS6; intermediate form. Ref.11

VAR_007297

Natural variant

142

1

M → I in MPS6. Ref.15

VAR_019020

Natural variant

144

1

G → R in MPS6; severe form; severe reduction of activity. Ref.13

VAR_019021

Natural variant

146

1

W → L in MPS6. Ref.15

VAR_019022

Natural variant

146

1

W → R in MPS6. Ref.15

VAR_019023

Natural variant

146

1

W → S in MPS6. Ref.15

VAR_019024

Natural variant

152

1

R → W in MPS6; intermediate form. Ref.14

VAR_007298

Natural variant

160

1

R → Q in MPS6; intermediate form. Ref.14

VAR_007299

Natural variant

192

1

C → R in MPS6; mild form; severe reduction of activity. Ref.13 Ref.20 Ref.21

VAR_019025

Natural variant

210

1

Y → C in MPS6; mild/intermediate. Ref.16 Ref.22

VAR_007300

Natural variant

236

1

L → P in MPS6; mild form. Ref.12 Ref.22

VAR_007301

Natural variant

239

1

Q → R in MPS6. Ref.20 Ref.21

VAR_019026

Natural variant

302

1

G → R in MPS6; severe form. Ref.17

VAR_007302

Natural variant

312

1

W → C in MPS6; severe form; low protein levels and activity. Ref.22

VAR_019027

Natural variant

315

1

R → Q in MPS6; intermediate form. Ref.19 Ref.22

VAR_019028

Natural variant

321

1

L → P in MPS6; intermediate form; severe reduction of activity. Ref.13 Ref.22

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.18 Ref.19 Ref.21 Ref.22
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].

VAR_016061

Natural variant

376

1

V → M. Ref.11 Ref.22
Corresponds to variant rs17220759 [ dbSNP | Ensembl ].

VAR_007303

Natural variant

384

1

S → N in MPS6. Ref.22
Corresponds to variant rs25414 [ dbSNP | Ensembl ].

VAR_019030

Natural variant

393

1

H → P in MPS6; mild/severe form. Ref.16

VAR_007304

Natural variant

399

1

F → L in MPS6. Ref.21

VAR_019031

Natural variant

405

1

C → Y in MPS6; mild form. Ref.12

VAR_007305

Natural variant

484

1

R → G in MPS6. Ref.22

VAR_019032

Natural variant

498

1

L → P in MPS6; mild/severe form. Ref.16

VAR_007306

Natural variant

521

1

C → Y in MPS6; severe form; severe reduction of activity. Ref.13

VAR_019033

Natural variant

531

1

P → R in MPS6; mild form. Ref.19

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)
	P15848 [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

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: 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. , 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. , 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

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.
S57777 Genomic DNA. Translation: AAB19988.1.

IPI

IPI00306576.

PIR

KJHUAB. S35990.

RefSeq

NP_000037.2. NM_000046.3.

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.

SMR

P15848. Positions 42-533.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15848. 2 interactions.

STRING

P15848.

Polymorphism databases

DMDM

114223.

Proteomic databases

PRIDE

P15848.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264914; ENSP00000264914; ENSG00000113273.
ENST00000341088; ENSP00000342327; ENSG00000113273.

GeneID

411.

KEGG

hsa:411.

UCSC

uc003kfq.1. human.

Organism-specific databases

CTD

411.

GeneCards

GC05M078108.

H-InvDB

HIX0018251.

HGNC

HGNC:714. ARSB.

HPA

HPA037770.
HPA037771.

MIM

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

neXtProt

NX_P15848.

Orphanet

583. Mucopolysaccharidosis type 6.
585. Multiple sulfatase deficiency.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12928.

GeneTree

ENSGT00560000077076.

HOGENOM

HBG651618.

HOVERGEN

HBG004282.

InParanoid

P15848.

OMA

RHDLSRE.

OrthoDB

EOG4DV5M0.

PhylomeDB

P15848.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03665-MONOMER.

BRENDA

3.1.6.12. 2681.

Gene expression databases

ArrayExpress

P15848.

Bgee

P15848.

CleanEx

HS_ARSB.

Genevestigator

P15848.

GermOnline

ENSG00000113273. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.720.10. Alk_phosphtse. 1 hit.

KO

K01135.

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

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Other

NextBio

1737.

SOURCE

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Entry information

Entry name

ARSB_HUMAN

Accession

Primary (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 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.