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P15848

- ARSB_HUMAN

UniProt

P15848 - ARSB_HUMAN

Protein

Arylsulfatase B

Gene

ARSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.

    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

    1. arylsulfatase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. N-acetylgalactosamine-4-sulfatase activity Source: Reactome

    GO - Biological processi

    1. autophagy Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. cellular protein metabolic process Source: Reactome
    4. central nervous system development Source: Ensembl
    5. chondroitin sulfate catabolic process Source: Reactome
    6. chondroitin sulfate metabolic process Source: Reactome
    7. glycosaminoglycan metabolic process Source: Reactome
    8. glycosphingolipid metabolic process Source: Reactome
    9. lysosomal transport Source: ProtInc
    10. lysosome organization Source: ProtInc
    11. post-translational protein modification Source: Reactome
    12. response to estrogen Source: Ensembl
    13. response to methylmercury Source: Ensembl
    14. response to nutrient Source: Ensembl
    15. response to pH Source: Ensembl
    16. small molecule metabolic process Source: Reactome
    17. sphingolipid metabolic process Source: Reactome

    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.

    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:714. ARSB.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: Ensembl
    4. lysosomal lumen Source: Reactome
    5. lysosome Source: ProtInc
    6. mitochondrion Source: Ensembl
    7. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    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.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [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.1 Publication
    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.

    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.

    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)
    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).

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP15848.
    PaxDbiP15848.
    PRIDEiP15848.

    PTM databases

    PhosphoSiteiP15848.

    Expressioni

    Gene expression databases

    ArrayExpressiP15848.
    BgeeiP15848.
    CleanExiHS_ARSB.
    GenevestigatoriP15848.

    Organism-specific databases

    HPAiHPA037770.
    HPA037771.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi106904. 3 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 – 549
    Helixi61 – 633
    Helixi70 – 778
    Beta strandi79 – 824
    Helixi93 – 1008
    Helixi104 – 1074
    Helixi129 – 1357
    Beta strandi139 – 1446
    Helixi153 – 1553
    Helixi157 – 1593
    Beta strandi163 – 1675
    Beta strandi169 – 1713
    Turni175 – 1773
    Beta strandi179 – 1846
    Turni185 – 1884
    Beta strandi189 – 1946
    Helixi211 – 22414
    Beta strandi232 – 2376
    Beta strandi242 – 2443
    Helixi249 – 2513
    Helixi253 – 2553
    Helixi261 – 28626
    Helixi290 – 2923
    Beta strandi293 – 3019
    Helixi305 – 3073
    Beta strandi320 – 3223
    Helixi323 – 3264
    Beta strandi330 – 3334
    Beta strandi341 – 3444
    Helixi350 – 3523
    Helixi353 – 3608
    Helixi377 – 3826
    Beta strandi390 – 3967
    Beta strandi429 – 4357
    Beta strandi438 – 4436
    Turni454 – 4563
    Beta strandi472 – 4765
    Turni477 – 4793
    Turni488 – 4903
    Helixi492 – 50716
    Helixi519 – 5213
    Turni524 – 5263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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. Align

    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

    MGPRGAASLP RGPGPRRLLL PVVLPLLLLL LLAPPGSGAG ASRPPHLVFL    50
    LADDLGWNDV GFHGSRIRTP HLDALAAGGV LLDNYYTQPL CTPSRSQLLT 100
    GRYQIRTGLQ HQIIWPCQPS CVPLDEKLLP QLLKEAGYTT HMVGKWHLGM 150
    YRKECLPTRR GFDTYFGYLL GSEDYYSHER CTLIDALNVT RCALDFRDGE 200
    EVATGYKNMY STNIFTKRAI ALITNHPPEK PLFLYLALQS VHEPLQVPEE 250
    YLKPYDFIQD KNRHHYAGMV SLMDEAVGNV TAALKSSGLW NNTVFIFSTD 300
    NGGQTLAGGN NWPLRGRKWS LWEGGVRGVG FVASPLLKQK GVKNRELIHI 350
    SDWLPTLVKL ARGHTNGTKP LDGFDVWKTI SEGSPSPRIE LLHNIDPNFV 400
    DSSPCPRNSM APAKDDSSLP EYSAFNTSVH AAIRHGNWKL LTGYPGCGYW 450
    FPPPSQYNVS EIPSSDPPTK TLWLFDIDRD PEERHDLSRE YPHIVTKLLS 500
    RLQFYHKHSV PVYFPAQDPR CDPKATGVWG PWM 533
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4043.1. [P15848-1 ]
    CCDS43334.1. [P15848-2 ]
    PIRi S35990. KJHUAB.
    RefSeqi NP_000037.2. NM_000046.3. [P15848-1 ]
    NP_942002.1. NM_198709.2. [P15848-2 ]
    UniGenei Hs.149103.
    Hs.604199.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FSU X-ray 2.50 A 42-533 [» ]
    ProteinModelPortali P15848.
    SMRi P15848. Positions 42-533.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106904. 3 interactions.
    IntActi P15848. 2 interactions.
    STRINGi 9606.ENSP00000264914.

    Chemistry

    ChEMBLi CHEMBL2399.

    PTM databases

    PhosphoSitei P15848.

    Proteomic databases

    MaxQBi P15848.
    PaxDbi P15848.
    PRIDEi P15848.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264914 ; ENSP00000264914 ; ENSG00000113273 . [P15848-1 ]
    ENST00000396151 ; ENSP00000379455 ; ENSG00000113273 . [P15848-2 ]
    ENST00000565165 ; ENSP00000456339 ; ENSG00000113273 . [P15848-2 ]
    GeneIDi 411.
    KEGGi hsa:411.
    UCSCi uc003kfq.3. human. [P15848-1 ]
    uc003kfr.4. human. [P15848-2 ]

    Organism-specific databases

    CTDi 411.
    GeneCardsi GC05M078108.
    HGNCi HGNC:714. ARSB.
    HPAi HPA037770.
    HPA037771.
    MIMi 253200. phenotype.
    272200. phenotype.
    611542. gene.
    neXtProti NX_P15848.
    Orphaneti 276212. Mucopolysaccharidosis type 6, rapidly progressing.
    276223. Mucopolysaccharidosis type 6, slowly progressing.
    PharmGKBi PA25006.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3119.
    HOGENOMi HOG000135354.
    HOVERGENi HBG004282.
    InParanoidi P15848.
    KOi K01135.
    OMAi QKGVKNR.
    OrthoDBi EOG7MKW5Q.
    PhylomeDBi P15848.
    TreeFami TF314186.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03665-MONOMER.
    BRENDAi 3.1.6.12. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_120888. CS/DS degradation.
    REACT_121036. The activation of arylsulfatases.

    Miscellaneous databases

    EvolutionaryTracei P15848.
    GenomeRNAii 411.
    NextBioi 1737.
    PROi P15848.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15848.
    Bgeei P15848.
    CleanExi HS_ARSB.
    Genevestigatori P15848.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view ]
    Pfami PF00884. Sulfatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    13. 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. 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.

    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: October 1, 2014
    This is version 152 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