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Protein

Arylsulfatase B

Gene

ARSB

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

Functioni

Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Enzyme regulationi

Inhibited by ethanol (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Calcium
Metal bindingi54 – 541Calcium
Metal bindingi91 – 911Calcium; via 3-oxoalanine1 Publication
Binding sitei145 – 1451SubstrateBy similarity
Active sitei147 – 1471
Binding sitei242 – 2421SubstrateBy similarity
Metal bindingi300 – 3001Calcium
Metal bindingi301 – 3011Calcium
Binding sitei318 – 3181SubstrateBy similarity

GO - Molecular functioni

  • arylsulfatase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • N-acetylgalactosamine-4-sulfatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03665-MONOMER.
BRENDAi3.1.6.12. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_120888. CS/DS degradation.
REACT_121036. The activation of arylsulfatases.
REACT_147719. MPS VI - Maroteaux-Lamy syndrome.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase B (EC:3.1.6.12)
Short name:
ASB
Alternative name(s):
N-acetylgalactosamine-4-sulfatase
Short name:
G4S
Gene namesi
Name:ARSB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:714. ARSB.

Subcellular locationi

  • Lysosome
  • Cell surface By similarity

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • lysosomal lumen Source: Reactome
  • lysosome Source: ProtInc
  • mitochondrion Source: Ensembl
  • rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 6 (MPS6)10 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:253200
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651S → F in MPS6; intermediate form. 1 Publication
VAR_019017
Natural varianti86 – 861Missing in MPS6; severe form; low protein levels and activity. 1 Publication
VAR_019018
Natural varianti92 – 921T → M in MPS6; mild form. 1 Publication
VAR_007294
Natural varianti95 – 951R → Q in MPS6; mild/severe form. 1 Publication
VAR_007295
Natural varianti116 – 1161P → H in MPS6; severe form. 1 Publication
VAR_019019
Natural varianti117 – 1171C → R in MPS6; severe form. 1 Publication
VAR_007296
Natural varianti137 – 1371G → V in MPS6; intermediate form. 1 Publication
VAR_007297
Natural varianti142 – 1421M → I in MPS6. 1 Publication
VAR_019020
Natural varianti144 – 1441G → R in MPS6; severe form; severe reduction of activity. 1 Publication
VAR_019021
Natural varianti146 – 1461W → L in MPS6. 1 Publication
VAR_019022
Natural varianti146 – 1461W → R in MPS6. 1 Publication
VAR_019023
Natural varianti146 – 1461W → S in MPS6. 1 Publication
VAR_019024
Natural varianti152 – 1521R → W in MPS6; intermediate form. 1 Publication
VAR_007298
Natural varianti160 – 1601R → Q in MPS6; intermediate form. 1 Publication
VAR_007299
Natural varianti192 – 1921C → R in MPS6; mild form; severe reduction of activity. 3 Publications
VAR_019025
Natural varianti210 – 2101Y → C in MPS6; mild/intermediate. 2 Publications
VAR_007300
Natural varianti236 – 2361L → P in MPS6; mild form. 2 Publications
VAR_007301
Natural varianti239 – 2391Q → R in MPS6. 2 Publications
VAR_019026
Natural varianti302 – 3021G → R in MPS6; severe form. 1 Publication
VAR_007302
Natural varianti312 – 3121W → C in MPS6; severe form; low protein levels and activity. 1 Publication
VAR_019027
Natural varianti315 – 3151R → Q in MPS6; intermediate form. 2 Publications
VAR_019028
Natural varianti321 – 3211L → P in MPS6; intermediate form; severe reduction of activity. 2 Publications
VAR_019029
Natural varianti384 – 3841S → N in MPS6. 1 Publication
Corresponds to variant rs25414 [ dbSNP | Ensembl ].
VAR_019030
Natural varianti393 – 3931H → P in MPS6; mild/severe form. 1 Publication
VAR_007304
Natural varianti399 – 3991F → L in MPS6. 1 Publication
VAR_019031
Natural varianti405 – 4051C → Y in MPS6; mild form. 1 Publication
VAR_007305
Natural varianti484 – 4841R → G in MPS6. 1 Publication
Corresponds to variant rs201101343 [ dbSNP | Ensembl ].
VAR_019032
Natural varianti498 – 4981L → P in MPS6; mild/severe form. 1 Publication
VAR_007306
Natural varianti521 – 5211C → Y in MPS6; severe form; severe reduction of activity. 1 Publication
VAR_019033
Natural varianti531 – 5311P → R in MPS6; mild form. 1 Publication
VAR_019034
Multiple sulfatase deficiency (MSD)1 Publication

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.

Disease descriptionA 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.

See also OMIM:272200

Keywords - Diseasei

Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy, Mucopolysaccharidosis

Organism-specific databases

MIMi253200. phenotype.
272200. phenotype.
Orphaneti276212. Mucopolysaccharidosis type 6, rapidly progressing.
276223. Mucopolysaccharidosis type 6, slowly progressing.
PharmGKBiPA25006.

Polymorphism and mutation databases

BioMutaiARSB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Or 38Sequence AnalysisAdd
BLAST
Chaini37 – 533497Arylsulfatase BPRO_0000033421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 9113-oxoalanine (Cys)1 Publication
Disulfide bondi117 ↔ 521
Disulfide bondi121 ↔ 155
Disulfide bondi181 ↔ 192
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)
Glycosylationi291 – 2911N-linked (GlcNAc...)Curated
Glycosylationi366 – 3661N-linked (GlcNAc...)1 Publication
Disulfide bondi405 ↔ 447
Glycosylationi426 – 4261N-linked (GlcNAc...)
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP15848.
PaxDbiP15848.
PRIDEiP15848.

PTM databases

PhosphoSiteiP15848.

Expressioni

Gene expression databases

BgeeiP15848.
CleanExiHS_ARSB.
ExpressionAtlasiP15848. baseline and differential.
GenevisibleiP15848. HS.

Organism-specific databases

HPAiHPA037770.
HPA037771.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi106904. 7 interactions.
IntActiP15848. 2 interactions.
STRINGi9606.ENSP00000264914.

Structurei

Secondary structure

1
533
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 549Combined sources
Helixi61 – 633Combined sources
Helixi70 – 778Combined sources
Beta strandi79 – 824Combined sources
Helixi93 – 1008Combined sources
Helixi104 – 1074Combined sources
Helixi129 – 1357Combined sources
Beta strandi139 – 1446Combined sources
Helixi153 – 1553Combined sources
Helixi157 – 1593Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi169 – 1713Combined sources
Turni175 – 1773Combined sources
Beta strandi179 – 1846Combined sources
Turni185 – 1884Combined sources
Beta strandi189 – 1946Combined sources
Helixi211 – 22414Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi242 – 2443Combined sources
Helixi249 – 2513Combined sources
Helixi253 – 2553Combined sources
Helixi261 – 28626Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 3019Combined sources
Helixi305 – 3073Combined sources
Beta strandi320 – 3223Combined sources
Helixi323 – 3264Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi341 – 3444Combined sources
Helixi350 – 3523Combined sources
Helixi353 – 3608Combined sources
Helixi377 – 3826Combined sources
Beta strandi390 – 3967Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi438 – 4436Combined sources
Turni454 – 4563Combined sources
Beta strandi472 – 4765Combined sources
Turni477 – 4793Combined sources
Turni488 – 4903Combined sources
Helixi492 – 50716Combined sources
Helixi519 – 5213Combined sources
Turni524 – 5263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSUX-ray2.50A42-533[»]
ProteinModelPortaliP15848.
SMRiP15848. Positions 42-533.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15848.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiP15848.
KOiK01135.
OMAiQKGVKNR.
OrthoDBiEOG7MKW5Q.
PhylomeDBiP15848.
TreeFamiTF314186.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: P15848-1) [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
MGPRGAASLP RGPGPRRLLL PVVLPLLLLL LLAPPGSGAG ASRPPHLVFL
60 70 80 90 100
LADDLGWNDV GFHGSRIRTP HLDALAAGGV LLDNYYTQPL CTPSRSQLLT
110 120 130 140 150
GRYQIRTGLQ HQIIWPCQPS CVPLDEKLLP QLLKEAGYTT HMVGKWHLGM
160 170 180 190 200
YRKECLPTRR GFDTYFGYLL GSEDYYSHER CTLIDALNVT RCALDFRDGE
210 220 230 240 250
EVATGYKNMY STNIFTKRAI ALITNHPPEK PLFLYLALQS VHEPLQVPEE
260 270 280 290 300
YLKPYDFIQD KNRHHYAGMV SLMDEAVGNV TAALKSSGLW NNTVFIFSTD
310 320 330 340 350
NGGQTLAGGN NWPLRGRKWS LWEGGVRGVG FVASPLLKQK GVKNRELIHI
360 370 380 390 400
SDWLPTLVKL ARGHTNGTKP LDGFDVWKTI SEGSPSPRIE LLHNIDPNFV
410 420 430 440 450
DSSPCPRNSM APAKDDSSLP EYSAFNTSVH AAIRHGNWKL LTGYPGCGYW
460 470 480 490 500
FPPPSQYNVS EIPSSDPPTK TLWLFDIDRD PEERHDLSRE YPHIVTKLLS
510 520 530
RLQFYHKHSV PVYFPAQDPR CDPKATGVWG PWM
Length:533
Mass (Da):59,687
Last modified:April 1, 1990 - v1
Checksum:i5983FB6911C4789A
GO
Isoform 2 (identifier: P15848-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:413
Mass (Da):45,996
Checksum:iA3B6A96052F3E839
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531K → F AA sequence (PubMed:2303452).Curated
Sequence conflicti408 – 4103NSM → SPC AA sequence (PubMed:2303452).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651S → F in MPS6; intermediate form. 1 Publication
VAR_019017
Natural varianti86 – 861Missing in MPS6; severe form; low protein levels and activity. 1 Publication
VAR_019018
Natural varianti92 – 921T → M in MPS6; mild form. 1 Publication
VAR_007294
Natural varianti95 – 951R → Q in MPS6; mild/severe form. 1 Publication
VAR_007295
Natural varianti116 – 1161P → H in MPS6; severe form. 1 Publication
VAR_019019
Natural varianti117 – 1171C → R in MPS6; severe form. 1 Publication
VAR_007296
Natural varianti137 – 1371G → V in MPS6; intermediate form. 1 Publication
VAR_007297
Natural varianti142 – 1421M → I in MPS6. 1 Publication
VAR_019020
Natural varianti144 – 1441G → R in MPS6; severe form; severe reduction of activity. 1 Publication
VAR_019021
Natural varianti146 – 1461W → L in MPS6. 1 Publication
VAR_019022
Natural varianti146 – 1461W → R in MPS6. 1 Publication
VAR_019023
Natural varianti146 – 1461W → S in MPS6. 1 Publication
VAR_019024
Natural varianti152 – 1521R → W in MPS6; intermediate form. 1 Publication
VAR_007298
Natural varianti160 – 1601R → Q in MPS6; intermediate form. 1 Publication
VAR_007299
Natural varianti192 – 1921C → R in MPS6; mild form; severe reduction of activity. 3 Publications
VAR_019025
Natural varianti210 – 2101Y → C in MPS6; mild/intermediate. 2 Publications
VAR_007300
Natural varianti236 – 2361L → P in MPS6; mild form. 2 Publications
VAR_007301
Natural varianti239 – 2391Q → R in MPS6. 2 Publications
VAR_019026
Natural varianti302 – 3021G → R in MPS6; severe form. 1 Publication
VAR_007302
Natural varianti312 – 3121W → C in MPS6; severe form; low protein levels and activity. 1 Publication
VAR_019027
Natural varianti315 – 3151R → Q in MPS6; intermediate form. 2 Publications
VAR_019028
Natural varianti321 – 3211L → P in MPS6; intermediate form; severe reduction of activity. 2 Publications
VAR_019029
Natural varianti358 – 3581V → L.
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].
VAR_061883
Natural varianti358 – 3581V → M.6 Publications
Corresponds to variant rs1065757 [ dbSNP | Ensembl ].
VAR_016061
Natural varianti376 – 3761V → M.2 Publications
Corresponds to variant rs17220759 [ dbSNP | Ensembl ].
VAR_007303
Natural varianti384 – 3841S → N in MPS6. 1 Publication
Corresponds to variant rs25414 [ dbSNP | Ensembl ].
VAR_019030
Natural varianti393 – 3931H → P in MPS6; mild/severe form. 1 Publication
VAR_007304
Natural varianti399 – 3991F → L in MPS6. 1 Publication
VAR_019031
Natural varianti405 – 4051C → Y in MPS6; mild form. 1 Publication
VAR_007305
Natural varianti484 – 4841R → G in MPS6. 1 Publication
Corresponds to variant rs201101343 [ dbSNP | Ensembl ].
VAR_019032
Natural varianti498 – 4981L → P in MPS6; mild/severe form. 1 Publication
VAR_007306
Natural varianti521 – 5211C → Y in MPS6; severe form; severe reduction of activity. 1 Publication
VAR_019033
Natural varianti531 – 5311P → R in MPS6; mild form. 1 Publication
VAR_019034

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei405 – 533129CPRNS…WGPWM → YWPECSLLL in isoform 2. 1 PublicationVSP_042721Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4043.1. [P15848-1]
CCDS43334.1. [P15848-2]
PIRiS35990. KJHUAB.
RefSeqiNP_000037.2. NM_000046.3. [P15848-1]
NP_942002.1. NM_198709.2. [P15848-2]
UniGeneiHs.149103.
Hs.604199.

Genome annotation databases

EnsembliENST00000264914; ENSP00000264914; ENSG00000113273. [P15848-1]
ENST00000396151; ENSP00000379455; ENSG00000113273. [P15848-2]
ENST00000565165; ENSP00000456339; ENSG00000113273. [P15848-2]
GeneIDi411.
KEGGihsa:411.
UCSCiuc003kfq.3. human. [P15848-1]
uc003kfr.4. human. [P15848-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4043.1. [P15848-1]
CCDS43334.1. [P15848-2]
PIRiS35990. KJHUAB.
RefSeqiNP_000037.2. NM_000046.3. [P15848-1]
NP_942002.1. NM_198709.2. [P15848-2]
UniGeneiHs.149103.
Hs.604199.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSUX-ray2.50A42-533[»]
ProteinModelPortaliP15848.
SMRiP15848. Positions 42-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106904. 7 interactions.
IntActiP15848. 2 interactions.
STRINGi9606.ENSP00000264914.

Chemistry

ChEMBLiCHEMBL2399.

PTM databases

PhosphoSiteiP15848.

Polymorphism and mutation databases

BioMutaiARSB.

Proteomic databases

MaxQBiP15848.
PaxDbiP15848.
PRIDEiP15848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264914; ENSP00000264914; ENSG00000113273. [P15848-1]
ENST00000396151; ENSP00000379455; ENSG00000113273. [P15848-2]
ENST00000565165; ENSP00000456339; ENSG00000113273. [P15848-2]
GeneIDi411.
KEGGihsa:411.
UCSCiuc003kfq.3. human. [P15848-1]
uc003kfr.4. human. [P15848-2]

Organism-specific databases

CTDi411.
GeneCardsiGC05M078108.
HGNCiHGNC:714. ARSB.
HPAiHPA037770.
HPA037771.
MIMi253200. phenotype.
272200. phenotype.
611542. gene.
neXtProtiNX_P15848.
Orphaneti276212. Mucopolysaccharidosis type 6, rapidly progressing.
276223. Mucopolysaccharidosis type 6, slowly progressing.
PharmGKBiPA25006.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiP15848.
KOiK01135.
OMAiQKGVKNR.
OrthoDBiEOG7MKW5Q.
PhylomeDBiP15848.
TreeFamiTF314186.

Enzyme and pathway databases

BioCyciMetaCyc:HS03665-MONOMER.
BRENDAi3.1.6.12. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_120888. CS/DS degradation.
REACT_121036. The activation of arylsulfatases.
REACT_147719. MPS VI - Maroteaux-Lamy syndrome.

Miscellaneous databases

ChiTaRSiARSB. human.
EvolutionaryTraceiP15848.
GenomeRNAii411.
NextBioi1737.
PROiP15848.
SOURCEiSearch...

Gene expression databases

BgeeiP15848.
CleanExiHS_ARSB.
ExpressionAtlasiP15848. baseline and differential.
GenevisibleiP15848. HS.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY, ABSENCE OF OXOALANINE IN MSD.
  11. Cited for: INVOLVEMENT IN MSD.
  12. "Arylsulfatase B regulates colonic epithelial cell migration by effects on MMP9 expression and RhoA activation."
    Bhattacharyya S., Tobacman J.K.
    Clin. Exp. Metastasis 26:535-545(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "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.
    Tissue: Liver.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. Cited for: VARIANT MET-358.
  23. "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.
  24. "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.
  25. "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.
  26. "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.

Entry informationi

Entry nameiARSB_HUMAN
AccessioniPrimary (citable) accession number: P15848
Secondary accession number(s): B2RC20, Q8N322, Q9UDI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 24, 2015
This is version 161 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.