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Protein

Arylsulfatase K

Gene

ARSK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401CalciumBy similarity
Metal bindingi80 – 801Calcium; via 3-oxoalanineBy similarity
Binding sitei128 – 1281SubstrateBy similarity
Binding sitei251 – 2511SubstrateBy similarity
Metal bindingi313 – 3131CalciumBy similarity
Metal bindingi314 – 3141CalciumBy similarity

GO - Molecular functioni

  • arylsulfatase activity Source: HGNC
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase K (EC:3.1.6.-)
Short name:
ASK
Alternative name(s):
Telethon sulfatase
Gene namesi
Name:ARSK
Synonyms:TSULF
ORF Names:UNQ630/PRO1246
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:25239. ARSK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485311.

Polymorphism and mutation databases

BioMutaiARSK.
DMDMi74738157.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 536514Arylsulfatase KPRO_0000042219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 8013-oxoalanine (Cys)By similarity
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence analysis
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi498 – 4981N-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.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6UWY0.
PaxDbiQ6UWY0.
PRIDEiQ6UWY0.

PTM databases

iPTMnetiQ6UWY0.
PhosphoSiteiQ6UWY0.

Expressioni

Gene expression databases

BgeeiQ6UWY0.
CleanExiHS_ARSK.
ExpressionAtlasiQ6UWY0. baseline and differential.
GenevisibleiQ6UWY0. HS.

Organism-specific databases

HPAiHPA042384.

Interactioni

Protein-protein interaction databases

BioGridi127507. 25 interactions.
STRINGi9606.ENSP00000369346.

Structurei

3D structure databases

ProteinModelPortaliQ6UWY0.
SMRiQ6UWY0. Positions 33-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00730000110906.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ6UWY0.
KOiK12376.
OMAiRDWQNTD.
OrthoDBiEOG75B853.
PhylomeDBiQ6UWY0.
TreeFamiTF313545.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UWY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLWVSVVA ALALAVLAPG AGEQRRRAAK APNVVLVVSD SFDGRLTFHP
60 70 80 90 100
GSQVVKLPFI NFMKTRGTSF LNAYTNSPIC CPSRAAMWSG LFTHLTESWN
110 120 130 140 150
NFKGLDPNYT TWMDVMERHG YRTQKFGKLD YTSGHHSISN RVEAWTRDVA
160 170 180 190 200
FLLRQEGRPM VNLIRNRTKV RVMERDWQNT DKAVNWLRKE AINYTEPFVI
210 220 230 240 250
YLGLNLPHPY PSPSSGENFG SSTFHTSLYW LEKVSHDAIK IPKWSPLSEM
260 270 280 290 300
HPVDYYSSYT KNCTGRFTKK EIKNIRAFYY AMCAETDAML GEIILALHQL
310 320 330 340 350
DLLQKTIVIY SSDHGELAME HRQFYKMSMY EASAHVPLLM MGPGIKAGLQ
360 370 380 390 400
VSNVVSLVDI YPTMLDIAGI PLPQNLSGYS LLPLSSETFK NEHKVKNLHP
410 420 430 440 450
PWILSEFHGC NVNASTYMLR TNHWKYIAYS DGASILPQLF DLSSDPDELT
460 470 480 490 500
NVAVKFPEIT YSLDQKLHSI INYPKVSASV HQYNKEQFIK WKQSIGQNYS
510 520 530
NVIANLRWHQ DWQKEPRKYE NAIDQWLKTH MNPRAV
Length:536
Mass (Da):61,450
Last modified:July 5, 2004 - v1
Checksum:i5A6D1B0FD8FCF386
GO

Sequence cautioni

The sequence AAH36047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801S → P in CAD38634 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti525 – 5251Q → R.1 Publication
Corresponds to variant rs17084927 [ dbSNP | Ensembl ].
VAR_052516

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY875939 mRNA. Translation: AAW66667.1.
AY358596 mRNA. Translation: AAQ88959.1.
AK303855 mRNA. Translation: BAG64796.1.
BC036047 mRNA. Translation: AAH36047.1. Different initiation.
BC130329 mRNA. Translation: AAI30330.1.
AL832711 mRNA. Translation: CAD38634.1.
CCDSiCCDS4073.1.
RefSeqiNP_937793.1. NM_198150.2.
UniGeneiHs.585051.

Genome annotation databases

EnsembliENST00000380009; ENSP00000369346; ENSG00000164291.
GeneIDi153642.
KEGGihsa:153642.
UCSCiuc003kld.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY875939 mRNA. Translation: AAW66667.1.
AY358596 mRNA. Translation: AAQ88959.1.
AK303855 mRNA. Translation: BAG64796.1.
BC036047 mRNA. Translation: AAH36047.1. Different initiation.
BC130329 mRNA. Translation: AAI30330.1.
AL832711 mRNA. Translation: CAD38634.1.
CCDSiCCDS4073.1.
RefSeqiNP_937793.1. NM_198150.2.
UniGeneiHs.585051.

3D structure databases

ProteinModelPortaliQ6UWY0.
SMRiQ6UWY0. Positions 33-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127507. 25 interactions.
STRINGi9606.ENSP00000369346.

PTM databases

iPTMnetiQ6UWY0.
PhosphoSiteiQ6UWY0.

Polymorphism and mutation databases

BioMutaiARSK.
DMDMi74738157.

Proteomic databases

MaxQBiQ6UWY0.
PaxDbiQ6UWY0.
PRIDEiQ6UWY0.

Protocols and materials databases

DNASUi153642.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380009; ENSP00000369346; ENSG00000164291.
GeneIDi153642.
KEGGihsa:153642.
UCSCiuc003kld.4. human.

Organism-specific databases

CTDi153642.
GeneCardsiARSK.
HGNCiHGNC:25239. ARSK.
HPAiHPA042384.
MIMi610011. gene.
neXtProtiNX_Q6UWY0.
PharmGKBiPA143485311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00730000110906.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ6UWY0.
KOiK12376.
OMAiRDWQNTD.
OrthoDBiEOG75B853.
PhylomeDBiQ6UWY0.
TreeFamiTF313545.

Enzyme and pathway databases

ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Miscellaneous databases

GenomeRNAii153642.
PROiQ6UWY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UWY0.
CleanExiHS_ARSK.
ExpressionAtlasiQ6UWY0. baseline and differential.
GenevisibleiQ6UWY0. HS.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship."
    Sardiello M., Annunziata I., Roma G., Ballabio A.
    Hum. Mol. Genet. 14:3203-3217(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and initial characterization of three novel human sulfatases."
    Obaya A.J.
    Gene 372:110-117(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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], VARIANT ARG-525.
    Tissue: Trachea.
  5. "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].
    Tissue: Brain and Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-536.
    Tissue: Heart.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiARSK_HUMAN
AccessioniPrimary (citable) accession number: Q6UWY0
Secondary accession number(s): A2BDE3
, B4E1I4, Q3ZCW3, Q8N3Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 102 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

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.