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Protein

Kynurenine--oxoglutarate transaminase 3

Gene

Ccbl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).By similarity1 Publication

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.1 Publication
An L-cysteine-S-conjugate + H2O = RSH + NH3 + pyruvate.1 Publication
L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Enzyme regulationi

Kynurenine transamination is competitively inhibited by cysteine, glutamine, histidine, methionine, leucine, or phenylalanine.1 Publication

Kineticsi

  1. KM=0.7 mM for glutamine1 Publication
  2. KM=0.7 mM for histidine1 Publication
  3. KM=0.7 mM for cysteine1 Publication
  4. KM=0.9 mM for methionine1 Publication
  5. KM=1.1 mM for phenylalanine1 Publication
  6. KM=1.4 mM for asparagine1 Publication
  7. KM=1.5 mM for kynurenine1 Publication
  8. KM=7.1 mM for tryptophan1 Publication
  9. KM=3.0 mM for serine1 Publication
  10. KM=0.4 mM for glyoxylate1 Publication
  11. KM=0.6 mM for phenylpyruvate1 Publication

    pH dependencei

    Optimum pH is 9.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541Substrate
    Binding sitei72 – 721Substrate; via amide nitrogen
    Binding sitei219 – 2191Substrate
    Binding sitei430 – 4301Substrate

    GO - Molecular functioni

    • cysteine-S-conjugate beta-lyase activity Source: UniProtKB-EC
    • kynurenine-glyoxylate transaminase activity Source: UniProtKB
    • kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    • poly(A) RNA binding Source: MGI
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    • 2-oxoglutarate metabolic process Source: UniProtKB
    • biosynthetic process Source: InterPro
    • cellular amino acid metabolic process Source: UniProtKB
    • kynurenine metabolic process Source: UniProtKB
    • L-kynurenine metabolic process Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Lyase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.6.1.7. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynurenine--oxoglutarate transaminase 3 (EC:2.6.1.7)
    Alternative name(s):
    Cysteine-S-conjugate beta-lyase 2 (EC:4.4.1.13)
    Kynurenine aminotransferase III
    Short name:
    KATIII
    Kynurenine--glyoxylate transaminase (EC:2.6.1.63)
    Kynurenine--oxoglutarate transaminase III
    Gene namesi
    Name:Ccbl2
    Synonyms:Kat3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 3

    Organism-specific databases

    MGIiMGI:2677849. Ccbl2.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrion Source: MGI
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 455455Kynurenine--oxoglutarate transaminase 3PRO_0000287705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei117 – 1171N6-acetyllysine; alternateCombined sources
    Modified residuei117 – 1171N6-succinyllysine; alternateCombined sources
    Modified residuei281 – 2811N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ71RI9.
    MaxQBiQ71RI9.
    PaxDbiQ71RI9.
    PRIDEiQ71RI9.

    PTM databases

    iPTMnetiQ71RI9.
    PhosphoSiteiQ71RI9.

    Expressioni

    Tissue specificityi

    Widely expressed, with higher expression levels in liver, kidney, heart and neuroendocrine tissues.1 Publication

    Developmental stagei

    Expressed from postnatal day (PND) 7 and peaks in adult.1 Publication

    Gene expression databases

    BgeeiQ71RI9.
    CleanExiMM_CCBL2.
    ExpressionAtlasiQ71RI9. baseline and differential.
    GenevisibleiQ71RI9. MM.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    IntActiQ71RI9. 3 interactions.
    MINTiMINT-1854868.
    STRINGi10090.ENSMUSP00000041675.

    Structurei

    Secondary structure

    1
    455
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 463Combined sources
    Helixi53 – 564Combined sources
    Helixi57 – 626Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi70 – 723Combined sources
    Helixi80 – 9011Combined sources
    Helixi93 – 964Combined sources
    Helixi105 – 11915Combined sources
    Turni125 – 1273Combined sources
    Beta strandi128 – 1336Combined sources
    Helixi134 – 14613Combined sources
    Beta strandi152 – 1587Combined sources
    Helixi163 – 1697Combined sources
    Beta strandi173 – 1786Combined sources
    Helixi191 – 1933Combined sources
    Helixi198 – 2025Combined sources
    Beta strandi209 – 2179Combined sources
    Turni219 – 2213Combined sources
    Helixi227 – 24014Combined sources
    Beta strandi243 – 2475Combined sources
    Turni249 – 2524Combined sources
    Helixi263 – 2653Combined sources
    Turni267 – 2693Combined sources
    Helixi270 – 2723Combined sources
    Beta strandi273 – 2786Combined sources
    Helixi279 – 2824Combined sources
    Helixi286 – 2883Combined sources
    Beta strandi291 – 2944Combined sources
    Helixi297 – 30812Combined sources
    Turni309 – 3113Combined sources
    Helixi316 – 33015Combined sources
    Turni331 – 3344Combined sources
    Beta strandi335 – 3384Combined sources
    Helixi339 – 35921Combined sources
    Turni360 – 3623Combined sources
    Beta strandi364 – 3674Combined sources
    Beta strandi369 – 3779Combined sources
    Helixi379 – 3813Combined sources
    Helixi394 – 40613Combined sources
    Beta strandi407 – 4093Combined sources
    Helixi413 – 4164Combined sources
    Turni419 – 4213Combined sources
    Helixi422 – 4254Combined sources
    Beta strandi428 – 4325Combined sources
    Helixi437 – 44812Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZJGX-ray3.00A/B42-451[»]
    3E2FX-ray2.59A/B42-451[»]
    3E2YX-ray2.26A/B42-451[»]
    3E2ZX-ray2.81A/B42-451[»]
    ProteinModelPortaliQ71RI9.
    SMRiQ71RI9. Positions 42-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG0257. Eukaryota.
    COG0436. LUCA.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000223045.
    HOVERGENiHBG008391.
    InParanoidiQ71RI9.
    KOiK00816.
    OMAiARKVHDF.
    OrthoDBiEOG76DTSB.
    TreeFamiTF352342.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    Isoform 1 (identifier: Q71RI9-1) [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
    MLLAQRRLIS LGCRSKPIKT IYSSSKVLGL CTSAKMALKF KNAKRIEGLD
    60 70 80 90 100
    SNVWVEFTKL AADPSVVNLG QGFPDISPPS YVKEELSKAA FIDNMNQYTR
    110 120 130 140 150
    GFGHPALVKA LSCLYGKIYQ RQIDPNEEIL VAVGAYGSLF NSIQGLVDPG
    160 170 180 190 200
    DEVIIMVPFY DCYEPMVRMA GAVPVFIPLR SKPTDGMKWT SSDWTFDPRE
    210 220 230 240 250
    LESKFSSKTK AIILNTPHNP LGKVYTRQEL QVIADLCVKH DTLCISDEVY
    260 270 280 290 300
    EWLVYTGHTH VKIATLPGMW ERTITIGSAG KTFSVTGWKL GWSIGPAHLI
    310 320 330 340 350
    KHLQTVQQNS FYTCATPLQA ALAEAFWIDI KRMDDPECYF NSLPKELEVK
    360 370 380 390 400
    RDRMVRLLNS VGLKPIVPDG GYFIIADVSS LGADLSDMNS DEPYDYKFVK
    410 420 430 440 450
    WMTKHKKLTA IPVSAFCDSK SKPHFEKLVR FCFIKKDSTL DAAEEIFRAW

    NSQKS
    Length:455
    Mass (Da):51,126
    Last modified:July 5, 2004 - v1
    Checksum:i94FA35EC67121EF2
    GO
    Isoform 2 (identifier: Q71RI9-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: Missing.

    Show »
    Length:420
    Mass (Da):47,321
    Checksum:iA6925006F7CE1C9C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 2. 2 PublicationsVSP_025605Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF363737 mRNA. Translation: AAQ15190.1.
    AK049569 mRNA. Translation: BAC33817.1.
    AK145623 mRNA. Translation: BAE26546.1.
    BC131942 mRNA. Translation: AAI31943.1.
    BC132615 mRNA. Translation: AAI32616.1.
    CCDSiCCDS17881.1. [Q71RI9-2]
    CCDS80040.1. [Q71RI9-1]
    RefSeqiNP_001280489.1. NM_001293560.1. [Q71RI9-1]
    NP_776124.1. NM_173763.4. [Q71RI9-2]
    XP_006501494.1. XM_006501431.2. [Q71RI9-2]
    XP_011238416.1. XM_011240114.1. [Q71RI9-2]
    UniGeneiMm.289643.

    Genome annotation databases

    EnsembliENSMUST00000044392; ENSMUSP00000041675; ENSMUSG00000040213. [Q71RI9-2]
    ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213. [Q71RI9-1]
    GeneIDi229905.
    KEGGimmu:229905.
    UCSCiuc008roz.2. mouse. [Q71RI9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF363737 mRNA. Translation: AAQ15190.1.
    AK049569 mRNA. Translation: BAC33817.1.
    AK145623 mRNA. Translation: BAE26546.1.
    BC131942 mRNA. Translation: AAI31943.1.
    BC132615 mRNA. Translation: AAI32616.1.
    CCDSiCCDS17881.1. [Q71RI9-2]
    CCDS80040.1. [Q71RI9-1]
    RefSeqiNP_001280489.1. NM_001293560.1. [Q71RI9-1]
    NP_776124.1. NM_173763.4. [Q71RI9-2]
    XP_006501494.1. XM_006501431.2. [Q71RI9-2]
    XP_011238416.1. XM_011240114.1. [Q71RI9-2]
    UniGeneiMm.289643.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZJGX-ray3.00A/B42-451[»]
    3E2FX-ray2.59A/B42-451[»]
    3E2YX-ray2.26A/B42-451[»]
    3E2ZX-ray2.81A/B42-451[»]
    ProteinModelPortaliQ71RI9.
    SMRiQ71RI9. Positions 42-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ71RI9. 3 interactions.
    MINTiMINT-1854868.
    STRINGi10090.ENSMUSP00000041675.

    PTM databases

    iPTMnetiQ71RI9.
    PhosphoSiteiQ71RI9.

    Proteomic databases

    EPDiQ71RI9.
    MaxQBiQ71RI9.
    PaxDbiQ71RI9.
    PRIDEiQ71RI9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000044392; ENSMUSP00000041675; ENSMUSG00000040213. [Q71RI9-2]
    ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213. [Q71RI9-1]
    GeneIDi229905.
    KEGGimmu:229905.
    UCSCiuc008roz.2. mouse. [Q71RI9-1]

    Organism-specific databases

    CTDi56267.
    MGIiMGI:2677849. Ccbl2.

    Phylogenomic databases

    eggNOGiKOG0257. Eukaryota.
    COG0436. LUCA.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000223045.
    HOVERGENiHBG008391.
    InParanoidiQ71RI9.
    KOiK00816.
    OMAiARKVHDF.
    OrthoDBiEOG76DTSB.
    TreeFamiTF352342.

    Enzyme and pathway databases

    BRENDAi2.6.1.7. 3474.

    Miscellaneous databases

    PROiQ71RI9.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ71RI9.
    CleanExiMM_CCBL2.
    ExpressionAtlasiQ71RI9. baseline and differential.
    GenevisibleiQ71RI9. MM.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family."
      Yu P., Li Z., Zhang L., Tagle D.A., Cai T.
      Gene 365:111-118(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: C57BL/6J.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
    3. "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: Brain.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen and Testis.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Biochemical and structural properties of mouse kynurenine aminotransferase III."
      Han Q., Robinson H., Cai T., Tagle D.A., Li J.
      Mol. Cell. Biol. 29:784-793(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 42-451 IN COMPLEXES WITH KYNURENINE AND GLUTAMINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiKAT3_MOUSE
    AccessioniPrimary (citable) accession number: Q71RI9
    Secondary accession number(s): Q8BJ84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: July 5, 2004
    Last modified: June 8, 2016
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.