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Protein

Ketohexokinase

Gene

KHK

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

Functioni

Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate.1 Publication

Catalytic activityi

ATP + D-fructose = ADP + D-fructose 1-phosphate.1 Publication

Enzyme regulationi

Requires potassium. Inhibition by ADP.

Kineticsi

kcat is 7.6 sec(-1).1 Publication

  1. KM=0.8 mM for D-fructose (at 25 degrees Celsius)1 Publication
  2. KM=0.15 mM for Mg-ATP (at 25 degrees Celsius)1 Publication

    Pathway:ifructose metabolism

    This protein is involved in the pathway fructose metabolism, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway fructose metabolism and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151D-fructose
    Binding sitei41 – 411D-fructose; via amide nitrogen
    Binding sitei42 – 421D-fructose
    Binding sitei45 – 451D-fructose
    Binding sitei108 – 1081ATP
    Binding sitei258 – 2581D-fructose

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi255 – 2584ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • fructokinase activity Source: UniProtKB
    • ketohexokinase activity Source: MGI

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06437-MONOMER.
    BRENDAi2.7.1.3. 2681.
    ReactomeiREACT_1571. Fructose catabolism.
    REACT_355167. Essential fructosuria.
    SABIO-RKP50053.
    UniPathwayiUPA00202.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KetohexokinaseImported (EC:2.7.1.31 Publication)
    Alternative name(s):
    Hepatic fructokinase
    Gene namesi
    Name:KHKImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6315. KHK.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: LIFEdb
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Involvement in diseasei

    Fructosuria (FRUCT)2 Publications

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

    Disease descriptionBenign defect of intermediary metabolism.

    See also OMIM:229800
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → R in FRUCT; loss of ketohexokinase function; insoluble. 2 Publications
    VAR_006072
    Natural varianti43 – 431A → T in FRUCT; no effect on ketohexokinase function; decreases enzyme activity but no effect in substrate affinity; decreases thermal stability. 2 Publications
    VAR_006073

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi229800. phenotype.
    Orphaneti2056. Essential fructosuria.
    PharmGKBiPA30095.

    Polymorphism and mutation databases

    BioMutaiKHK.
    DMDMi1730044.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298KetohexokinasePRO_0000080088Add
    BLAST

    Proteomic databases

    MaxQBiP50053.
    PaxDbiP50053.
    PRIDEiP50053.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00029488.

    PTM databases

    PhosphoSiteiP50053.

    Expressioni

    Tissue specificityi

    Most abundant in liver, kidney, gut, spleen and pancreas. Low levels also found in adrenal, muscle, brain and eye.1 Publication

    Gene expression databases

    BgeeiP50053.
    CleanExiHS_KHK.
    ExpressionAtlasiP50053. baseline and differential.
    GenevisibleiP50053. HS.

    Organism-specific databases

    HPAiHPA007040.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LHX9Q9NQ693EBI-1053974,EBI-10175218

    Protein-protein interaction databases

    BioGridi109996. 12 interactions.
    IntActiP50053. 1 interaction.
    STRINGi9606.ENSP00000260598.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106Combined sources
    Beta strandi13 – 2210Combined sources
    Beta strandi29 – 313Combined sources
    Beta strandi33 – 419Combined sources
    Helixi42 – 5312Combined sources
    Beta strandi57 – 637Combined sources
    Helixi67 – 7812Combined sources
    Beta strandi86 – 883Combined sources
    Beta strandi90 – 923Combined sources
    Beta strandi96 – 1027Combined sources
    Turni103 – 1053Combined sources
    Beta strandi108 – 1136Combined sources
    Helixi122 – 1265Combined sources
    Helixi130 – 1323Combined sources
    Beta strandi133 – 1397Combined sources
    Helixi143 – 15715Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi167 – 1726Combined sources
    Helixi177 – 1848Combined sources
    Beta strandi185 – 1917Combined sources
    Helixi193 – 1986Combined sources
    Helixi204 – 2118Combined sources
    Helixi212 – 2143Combined sources
    Beta strandi220 – 2245Combined sources
    Helixi226 – 2283Combined sources
    Beta strandi230 – 2334Combined sources
    Beta strandi239 – 2424Combined sources
    Helixi256 – 26914Combined sources
    Helixi274 – 28916Combined sources
    Beta strandi291 – 2944Combined sources
    Helixi295 – 2973Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLZX-ray1.85A/B/C/D5-298[»]
    2HQQX-ray1.86A1-298[»]
    2HW1X-ray2.10A1-298[»]
    3B3LX-ray2.90A/B/C/D1-298[»]
    3NBVX-ray2.30A/B5-298[»]
    3NBWX-ray2.34A/B5-298[»]
    3NC2X-ray2.50A/B5-298[»]
    3NC9X-ray2.40A/B5-298[»]
    3NCAX-ray2.60A/B5-298[»]
    3Q92X-ray2.80A/B5-298[»]
    3QA2X-ray2.52A/B5-298[»]
    3QAIX-ray2.70A/B5-298[»]
    3RO4X-ray2.60A/B5-298[»]
    ProteinModelPortaliP50053.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50053.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carbohydrate kinase PfkB family.Curated

    Phylogenomic databases

    eggNOGiCOG0524.
    GeneTreeiENSGT00390000007458.
    HOGENOMiHOG000212926.
    HOVERGENiHBG003335.
    InParanoidiP50053.
    KOiK00846.
    OMAiKCGLQGY.
    OrthoDBiEOG7K6PV6.
    PhylomeDBiP50053.
    TreeFamiTF323942.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    InterProiIPR011611. PfkB_dom.
    IPR029056. Ribokinase-like.
    [Graphical view]
    PfamiPF00294. PfkB. 1 hit.
    [Graphical view]
    SUPFAMiSSF53613. SSF53613. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    Isoform C1 Publication (identifier: P50053-1) [UniParc]FASTAAdd to basket

    Also known as: Central, hepatic/renal/intestinal1 Publication

    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
    MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTVL
    60 70 80 90 100
    SLLGAPCAFM GSMAPGHVAD FLVADFRRRG VDVSQVAWQS KGDTPSSCCI
    110 120 130 140 150
    INNSNGNRTI VLHDTSLPDV SATDFEKVDL TQFKWIHIEG RNASEQVKML
    160 170 180 190 200
    QRIDAHNTRQ PPEQKIRVSV EVEKPREELF QLFGYGDVVF VSKDVAKHLG
    210 220 230 240 250
    FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL HSDAFPPPRV
    260 270 280 290
    VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV
    Length:298
    Mass (Da):32,523
    Last modified:April 29, 2015 - v2
    Checksum:iBE77FC325CAC5721
    GO
    Isoform A1 Publication (identifier: P50053-2) [UniParc]FASTAAdd to basket

    Also known as: Peripheral1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         72-115: LVADFRRRGV...GNRTIVLHDT → VLDDLRRYSV...GSRTILYYDR

    Note: More widely distributed but with a low expression level. KM=7 mM for D-fructose (at 25 degrees Celsius). KM=036 mM for Mg-ATP (at 25 degrees Celsius). kcat is 6.9 sec(-1).1 Publication
    Show »
    Length:298
    Mass (Da):32,730
    Checksum:i1BA47BDC60C1B89F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → R in FRUCT; loss of ketohexokinase function; insoluble. 2 Publications
    VAR_006072
    Natural varianti43 – 431A → T in FRUCT; no effect on ketohexokinase function; decreases enzyme activity but no effect in substrate affinity; decreases thermal stability. 2 Publications
    VAR_006073
    Natural varianti49 – 491V → I.1 Publication
    Corresponds to variant rs2304681 [ dbSNP | Ensembl ].
    VAR_006074

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 11544LVADF…VLHDT → VLDDLRRYSVDLRYTVFQTT GSVPIATVIINEASGSRTIL YYDR in isoform A. CuratedVSP_004669Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X78678 mRNA. Translation: CAA55347.1.
    X78677 mRNA. Translation: CAA55346.1.
    CR456801 mRNA. Translation: CAG33082.1.
    AC013403 Genomic DNA. Translation: AAX93167.1.
    CH471053 Genomic DNA. Translation: EAX00643.1.
    BC006233 mRNA. Translation: AAH06233.1.
    Y09336 Genomic DNA. Translation: CAA70516.1.
    Y09341 Genomic DNA. Translation: CAA70522.1.
    Y09341 Genomic DNA. Translation: CAA70523.1.
    Y09340 Genomic DNA. Translation: CAA70521.1.
    AJ005168 Genomic DNA. Translation: CAA06409.1.
    CCDSiCCDS1734.1. [P50053-2]
    CCDS1735.1. [P50053-1]
    RefSeqiNP_000212.1. NM_000221.2. [P50053-2]
    NP_006479.1. NM_006488.2. [P50053-1]
    UniGeneiHs.567297.

    Genome annotation databases

    EnsembliENST00000260598; ENSP00000260598; ENSG00000138030.
    ENST00000260599; ENSP00000260599; ENSG00000138030. [P50053-2]
    GeneIDi3795.
    KEGGihsa:3795.
    UCSCiuc002ril.2. human. [P50053-1]
    uc002rim.2. human. [P50053-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X78678 mRNA. Translation: CAA55347.1.
    X78677 mRNA. Translation: CAA55346.1.
    CR456801 mRNA. Translation: CAG33082.1.
    AC013403 Genomic DNA. Translation: AAX93167.1.
    CH471053 Genomic DNA. Translation: EAX00643.1.
    BC006233 mRNA. Translation: AAH06233.1.
    Y09336 Genomic DNA. Translation: CAA70516.1.
    Y09341 Genomic DNA. Translation: CAA70522.1.
    Y09341 Genomic DNA. Translation: CAA70523.1.
    Y09340 Genomic DNA. Translation: CAA70521.1.
    AJ005168 Genomic DNA. Translation: CAA06409.1.
    CCDSiCCDS1734.1. [P50053-2]
    CCDS1735.1. [P50053-1]
    RefSeqiNP_000212.1. NM_000221.2. [P50053-2]
    NP_006479.1. NM_006488.2. [P50053-1]
    UniGeneiHs.567297.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLZX-ray1.85A/B/C/D5-298[»]
    2HQQX-ray1.86A1-298[»]
    2HW1X-ray2.10A1-298[»]
    3B3LX-ray2.90A/B/C/D1-298[»]
    3NBVX-ray2.30A/B5-298[»]
    3NBWX-ray2.34A/B5-298[»]
    3NC2X-ray2.50A/B5-298[»]
    3NC9X-ray2.40A/B5-298[»]
    3NCAX-ray2.60A/B5-298[»]
    3Q92X-ray2.80A/B5-298[»]
    3QA2X-ray2.52A/B5-298[»]
    3QAIX-ray2.70A/B5-298[»]
    3RO4X-ray2.60A/B5-298[»]
    ProteinModelPortaliP50053.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109996. 12 interactions.
    IntActiP50053. 1 interaction.
    STRINGi9606.ENSP00000260598.

    Chemistry

    BindingDBiP50053.
    ChEMBLiCHEMBL1275212.

    PTM databases

    PhosphoSiteiP50053.

    Polymorphism and mutation databases

    BioMutaiKHK.
    DMDMi1730044.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00029488.

    Proteomic databases

    MaxQBiP50053.
    PaxDbiP50053.
    PRIDEiP50053.

    Protocols and materials databases

    DNASUi3795.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000260598; ENSP00000260598; ENSG00000138030.
    ENST00000260599; ENSP00000260599; ENSG00000138030. [P50053-2]
    GeneIDi3795.
    KEGGihsa:3795.
    UCSCiuc002ril.2. human. [P50053-1]
    uc002rim.2. human. [P50053-2]

    Organism-specific databases

    CTDi3795.
    GeneCardsiGC02P027309.
    HGNCiHGNC:6315. KHK.
    HPAiHPA007040.
    MIMi229800. phenotype.
    614058. gene.
    neXtProtiNX_P50053.
    Orphaneti2056. Essential fructosuria.
    PharmGKBiPA30095.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0524.
    GeneTreeiENSGT00390000007458.
    HOGENOMiHOG000212926.
    HOVERGENiHBG003335.
    InParanoidiP50053.
    KOiK00846.
    OMAiKCGLQGY.
    OrthoDBiEOG7K6PV6.
    PhylomeDBiP50053.
    TreeFamiTF323942.

    Enzyme and pathway databases

    UniPathwayiUPA00202.
    BioCyciMetaCyc:HS06437-MONOMER.
    BRENDAi2.7.1.3. 2681.
    ReactomeiREACT_1571. Fructose catabolism.
    REACT_355167. Essential fructosuria.
    SABIO-RKP50053.

    Miscellaneous databases

    EvolutionaryTraceiP50053.
    GenomeRNAii3795.
    NextBioi14897.
    PROiP50053.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP50053.
    CleanExiHS_KHK.
    ExpressionAtlasiP50053. baseline and differential.
    GenevisibleiP50053. HS.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    InterProiIPR011611. PfkB_dom.
    IPR029056. Ribokinase-like.
    [Graphical view]
    PfamiPF00294. PfkB. 1 hit.
    [Graphical view]
    SUPFAMiSSF53613. SSF53613. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular basis of essential fructosuria: molecular cloning and mutational analysis of human ketohexokinase (fructokinase)."
      Bonthron D.T., Brady N., Donaldson I.A., Steinmann B.
      Hum. Mol. Genet. 3:1627-1631(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS FRUCT ARG-40 AND THR-43, VARIANT ILE-49.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Lung.
    6. "Structure and alternative splicing of the ketohexokinase gene."
      Hayward B.E., Bonthron D.T.
      Eur. J. Biochem. 257:85-91(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 AND 71-298, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Structures of alternatively spliced isoforms of human ketohexokinase."
      Trinh C.H., Asipu A., Bonthron D.T., Phillips S.E.
      Acta Crystallogr. D 65:201-211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FRUCTOSE AND AMP-PNP, X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF ISOFORM A, SUBUNIT, SUBSTRATE-BINDING SITES.
    9. "Properties of normal and mutant recombinant human ketohexokinases and implications for the pathogenesis of essential fructosuria."
      Asipu A., Hayward B.E., O'Reilly J., Bonthron D.T.
      Diabetes 52:2426-2432(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS FRUCT ARG-40 AND THR-43, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiKHK_HUMAN
    AccessioniPrimary (citable) accession number: P50053
    Secondary accession number(s): Q6IBK2
    , Q99532, Q9BRJ3, Q9UMN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 29, 2015
    Last modified: July 22, 2015
    This is version 148 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.