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Protein

Carbohydrate sulfotransferase 2

Gene

CHST2

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

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.1 Publication

Kineticsi

  1. KM=3.9 µM for PAPS1 Publication
  2. KM=1.4 mM for BetaBnO-GlcNAc1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei152 – 1521Not glycosylated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 1797PAPSCurated
    Nucleotide bindingi332 – 3409PAPSCurated

    GO - Molecular functioni

    • N-acetylglucosamine 6-O-sulfotransferase activity Source: UniProtKB
    • sulfotransferase activity Source: ProtInc

    GO - Biological processi

    • carbohydrate metabolic process Source: Reactome
    • glycosaminoglycan metabolic process Source: Reactome
    • inflammatory response Source: ProtInc
    • keratan sulfate biosynthetic process Source: Reactome
    • keratan sulfate metabolic process Source: Reactome
    • multicellular organismal development Source: ProtInc
    • N-acetylglucosamine metabolic process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • sulfur compound metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    SABIO-RKQ9Y4C5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 2 (EC:2.8.2.-)
    Alternative name(s):
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2
    Short name:
    GST-2
    N-acetylglucosamine 6-O-sulfotransferase 1
    Short name:
    GlcNAc6ST-1
    Short name:
    Gn6ST-1
    Gene namesi
    Name:CHST2
    Synonyms:GN6ST
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1970. CHST2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5454CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei55 – 7521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini76 – 530455LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • Golgi membrane Source: Reactome
    • integral component of membrane Source: UniProtKB-KW
    • intrinsic component of Golgi membrane Source: UniProtKB
    • trans-Golgi network Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591C → S: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39. 1 Publication
    Mutagenesisi86 – 861C → S: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12. 1 Publication
    Mutagenesisi174 – 1741R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi296 – 2961R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi304 – 3041K → A: Loss of function. 1 Publication
    Mutagenesisi332 – 3321R → A: Loss of function. 1 Publication
    Mutagenesisi341 – 3411R → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi457 – 4571N → A: Reduced localization in the Golgi. 1 Publication
    Mutagenesisi475 – 4751N → A: Unable to sulfate the sialyl Lewis X tetrasaccharide. 1 Publication
    Mutagenesisi518 – 5181K → A: Has weak or no effect. 1 Publication
    Mutagenesisi519 – 5191D → A: Has weak or no effect. 1 Publication
    Mutagenesisi520 – 5201L → A: Has weak or no effect. 1 Publication
    Mutagenesisi521 – 5211S → A: No effect. 1 Publication
    Mutagenesisi522 – 5221K → A: No effect. 1 Publication
    Mutagenesisi523 – 5231T → A: Has weak or no effect. 1 Publication
    Mutagenesisi524 – 5241L → A or T: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi525 – 5251L → A: Induces a strong decrease in enzyme activity. 1 Publication
    Mutagenesisi525 – 5251L → T: Has weak or no effect. 1 Publication
    Mutagenesisi526 – 5261R → A: Has weak or no effect. 1 Publication
    Mutagenesisi527 – 5271K → A: No effect. 1 Publication
    Mutagenesisi528 – 5281P → A: Has weak or no effect. 1 Publication
    Mutagenesisi529 – 5291R → A: No effect. 1 Publication
    Mutagenesisi530 – 5301L → A or T: Induces a strong decrease in enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26502.

    Polymorphism and mutation databases

    BioMutaiCHST2.
    DMDMi61212252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530Carbohydrate sulfotransferase 2PRO_0000085186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi243 – 2431N-linked (GlcNAc...)1 Publication
    Glycosylationi457 – 4571N-linked (GlcNAc...)1 Publication
    Glycosylationi475 – 4751N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Glycosylation at Asn-475 is required for catalytic activity.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Y4C5.
    PRIDEiQ9Y4C5.

    PTM databases

    PhosphoSiteiQ9Y4C5.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes.3 Publications

    Inductioni

    Up-regulated upon cytokine activation.1 Publication

    Gene expression databases

    BgeeiQ9Y4C5.
    CleanExiHS_CHST2.
    ExpressionAtlasiQ9Y4C5. baseline and differential.
    GenevisibleiQ9Y4C5. HS.

    Organism-specific databases

    HPAiHPA013313.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307911.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4C5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG67451.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9Y4C5.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9Y4C5.
    TreeFamiTF342871.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

    Isoform 1 (identifier: Q9Y4C5-1) [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
    MSRSPQRALP PGALPRLLQA APAAAPRALL PQWPRRPGRR WPASPLGMKV
    60 70 80 90 100
    FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAAGAAG
    110 120 130 140 150
    GSWGRPGPPP AGPPRAHARL DLRTPYRPPA AAVGAAPAAA AGMAGVAAPP
    160 170 180 190 200
    GNGTRGTGGV GDKRQLVYVF TTWRSGSSFF GELFNQNPEV FFLYEPVWHV
    210 220 230 240 250
    WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG GRNLTTLGIF
    260 270 280 290 300
    GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT
    310 320 330 340 350
    LVIKGVRVFD VAVLAPLLRD PALDLKVIHL VRDPRAVASS RIRSRHGLIR
    360 370 380 390 400
    ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGVGGPADYH ALGAMEVICN
    410 420 430 440 450
    SMAKTLQTAL QPPDWLQGHY LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE
    460 470 480 490 500
    MEQFALNMTS GSGSSSKPFV VSARNATQAA NAWRTALTFQ QIKQVEEFCY
    510 520 530
    QPMAVLGYER VNSPEEVKDL SKTLLRKPRL
    Length:530
    Mass (Da):57,857
    Last modified:March 1, 2003 - v2
    Checksum:iA82CA227B9D5651B
    GO
    Isoform 2 (identifier: Q9Y4C5-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-47: Missing.

    Note: Higher levels of expression compared to isoform 1 when expressed in HeLa cells. Exhibits similar intracellular GlcNAc-6-O-sulfation activity.
    Show »
    Length:483
    Mass (Da):52,787
    Checksum:iE27797D44931BA18
    GO

    Sequence cautioni

    The sequence BAA34265.2 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAB16886.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAB16887.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81A → V in BAB16887 (PubMed:11042394).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 2. CuratedVSP_018887Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2. Different initiation.
    AB014680 mRNA. Translation: BAA34266.2.
    AF083066 mRNA. Translation: AAD20981.1.
    AB021124 mRNA. Translation: BAB16886.1. Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1.
    CH471052 Genomic DNA. Translation: EAW78953.1.
    BC105010 mRNA. Translation: AAI05011.1.
    BC105012 mRNA. Translation: AAI05013.1.
    CCDSiCCDS3129.1. [Q9Y4C5-1]
    RefSeqiNP_004258.2. NM_004267.4. [Q9Y4C5-1]
    UniGeneiHs.529249.
    Hs.8786.

    Genome annotation databases

    EnsembliENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
    GeneIDi9435.
    KEGGihsa:9435.
    UCSCiuc003evm.3. human. [Q9Y4C5-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB014679 mRNA. Translation: BAA34265.2. Different initiation.
    AB014680 mRNA. Translation: BAA34266.2.
    AF083066 mRNA. Translation: AAD20981.1.
    AB021124 mRNA. Translation: BAB16886.1. Different initiation.
    AB021125 Genomic DNA. Translation: BAB16887.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW78952.1.
    CH471052 Genomic DNA. Translation: EAW78953.1.
    BC105010 mRNA. Translation: AAI05011.1.
    BC105012 mRNA. Translation: AAI05013.1.
    CCDSiCCDS3129.1. [Q9Y4C5-1]
    RefSeqiNP_004258.2. NM_004267.4. [Q9Y4C5-1]
    UniGeneiHs.529249.
    Hs.8786.

    3D structure databases

    ProteinModelPortaliQ9Y4C5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000307911.

    PTM databases

    PhosphoSiteiQ9Y4C5.

    Polymorphism and mutation databases

    BioMutaiCHST2.
    DMDMi61212252.

    Proteomic databases

    PaxDbiQ9Y4C5.
    PRIDEiQ9Y4C5.

    Protocols and materials databases

    DNASUi9435.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000309575; ENSP00000307911; ENSG00000175040. [Q9Y4C5-1]
    GeneIDi9435.
    KEGGihsa:9435.
    UCSCiuc003evm.3. human. [Q9Y4C5-1]

    Organism-specific databases

    CTDi9435.
    GeneCardsiGC03P142838.
    HGNCiHGNC:1970. CHST2.
    HPAiHPA013313.
    MIMi603798. gene.
    neXtProtiNX_Q9Y4C5.
    PharmGKBiPA26502.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG67451.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9Y4C5.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9Y4C5.
    TreeFamiTF342871.

    Enzyme and pathway databases

    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    SABIO-RKQ9Y4C5.

    Miscellaneous databases

    ChiTaRSiCHST2. human.
    GeneWikiiCHST2.
    GenomeRNAii9435.
    NextBioi35332.
    PROiQ9Y4C5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y4C5.
    CleanExiHS_CHST2.
    ExpressionAtlasiQ9Y4C5. baseline and differential.
    GenevisibleiQ9Y4C5. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human N-acetylglucosamine-6-O-sulfotransferase involved in the biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal mapping, and expression in various organs and tumor cells."
      Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W., Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T., Nakagawara A., Kadomatsu K., Muramatsu T.
      J. Biochem. 124:670-678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Uchimura K., Muramatsu H., Muramatsu T.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial cells: cDNA cloning, expression, and chromosomal localization."
      Li X., Tedder T.F.
      Genomics 55:345-347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Umbilical vein endothelial cell.
    4. "Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to b-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence."
      Sakaguchi H., Kitagawa H., Sugahara K.
      Biochim. Biophys. Acta 1523:269-276(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. "CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin."
      Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.
      J. Leukoc. Biol. 69:565-574(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    8. "Characterization and mutagenesis of Gal/GlcNAc-6-O-sulfotransferases."
      Grunwell J.R., Rath V.L., Rasmussen J., Cabrilo Z., Bertozzi C.R.
      Biochemistry 41:15590-15600(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-174; ARG-296; LYS-304; ARG-332 AND ARG-341.
    9. "Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression."
      Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E., Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.
      J. Biol. Chem. 277:3979-3984(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    10. "Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis."
      de Graffenried C.L., Bertozzi C.R.
      J. Biol. Chem. 278:40282-40295(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1."
      Chen L., Ichihara-Tanaka K., Muramatsu T.
      J. Biochem. 136:659-664(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-518; ASP-519; LEU-520; SER-521; LYS-522; THR-523; LEU-524; LEU-525; ARG-526; LYS-527; PRO-528; ARG-529 AND LEU-530.
    12. "The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity."
      de Graffenried C.L., Bertozzi C.R.
      J. Biol. Chem. 279:40035-40043(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF CYS-59 AND CYS-86.
    13. "Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1."
      Desko M.M., Gross D.A., Kohler J.J.
      Glycobiology 19:1068-1077(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-243; ASN-457 AND ASN-475, ABSENCE OF GLYCOSYLATION AT ASN-152, MUTAGENESIS OF ASN-457 AND ASN-475.
    14. "Expression of long-form N-acetylglucosamine-6-O-sulfotransferase 1 in human high endothelial venules."
      Fujiwara M., Kobayashi M., Hoshino H., Uchimura K., Nakada T., Masumoto J., Sakai Y., Fukuda M., Nakayama J.
      J. Histochem. Cytochem. 60:397-407(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, ALTERNATIVE INITIATION.

    Entry informationi

    Entry nameiCHST2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4C5
    Secondary accession number(s): D3DNG5
    , Q2M370, Q9GZN5, Q9UED5, Q9Y6F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2003
    Last modified: June 24, 2015
    This is version 114 of the entry and version 2 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. 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.