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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

HSD17B10

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

Functioni

Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. Catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD).3 Publications

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.
Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.

Kineticsi

  1. KM=25.7 µM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)1 Publication
  2. KM=85.2 µM for beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  3. KM=41 µM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  4. KM=5 µM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  5. KM=219 µM for isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  6. KM=36.4 µM for chenodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  7. KM=1.7 µM for dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)1 Publication
  8. KM=30.6 µM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)1 Publication
  9. KM=42.3 µM for NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.3 for the dehydrogenase reaction at 25 degrees Celsius, and 7.0 for the reductase reaction at 25 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei155Substrate1
    Active sitei168Proton acceptor1
    Binding sitei172NAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 41NAD1 PublicationAdd BLAST30

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01071-MONOMER.
    ZFISH:HS01071-MONOMER.
    BRENDAi1.1.1.178. 2681.
    1.1.1.35. 2681.
    ReactomeiR-HSA-6785470. tRNA processing in the mitochondrion.
    R-HSA-6787450. tRNA modification in the mitochondrion.
    R-HSA-70895. Branched-chain amino acid catabolism.
    R-HSA-8868766. rRNA processing in the mitochondrion.
    SABIO-RKQ99714.

    Chemistry databases

    SwissLipidsiSLP:000000787.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.35)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.51)
    Short name:
    17-beta-HSD 10
    3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.178)
    3-hydroxyacyl-CoA dehydrogenase type II
    Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
    Mitochondrial ribonuclease P protein 2
    Short name:
    Mitochondrial RNase P protein 2
    Short chain dehydrogenase/reductase family 5C member 1
    Short-chain type dehydrogenase/reductase XH98G2
    Type II HADH
    Gene namesi
    Name:HSD17B10
    Synonyms:ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4800. HSD17B10.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: ProtInc
    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    • plasma membrane Source: ProtInc
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBD deficiency)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder that leads to neurological abnormalities, including psychomotor retardation and, in virtually all patients, loss of mental and motor skills.
    See also OMIM:300438
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_015987122L → V in MHBD deficiency. 1 PublicationCorresponds to variant rs28935476dbSNPEnsembl.1
    Natural variantiVAR_015988130R → C in MHBD deficiency. 2 PublicationsCorresponds to variant rs28935475dbSNPEnsembl.1
    Natural variantiVAR_032093247N → S in MHBD deficiency; intermediate enzyme activity. 1 PublicationCorresponds to variant rs122461163dbSNPEnsembl.1
    Mental retardation, X-linked, syndromic, 10 (MRXS10)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXS10 patients manifest mild mental retardation, choreoathetosis and abnormal behavior.
    See also OMIM:300220
    Mental retardation, X-linked 17 (MRX17)1 Publication
    The gene represented in this entry is involved in disease pathogenesis. A chromosomal microduplication involving HSD17B10 and HUWE1 has been found in patients with mental retardation.
    Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
    See also OMIM:300705

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    DisGeNETi3028.
    MalaCardsiHSD17B10.
    MIMi300220. phenotype.
    300438. phenotype.
    300705. phenotype.
    OpenTargetsiENSG00000072506.
    Orphaneti85295. HSD10 disease, atypical type.
    391428. HSD10 disease, infantile type.
    391457. HSD10 disease, neonatal type.
    PharmGKBiPA162391638.

    Chemistry databases

    ChEMBLiCHEMBL4159.

    Polymorphism and mutation databases

    BioMutaiHSD17B10.
    DMDMi2492759.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000548102 – 2613-hydroxyacyl-CoA dehydrogenase type-2Add BLAST260

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei53N6-acetyllysine; alternateBy similarity1
    Modified residuei53N6-succinyllysine; alternateBy similarity1
    Modified residuei69N6-acetyllysineBy similarity1
    Modified residuei99N6-acetyllysineBy similarity1
    Modified residuei105N6-acetyllysineBy similarity1
    Modified residuei212N6-acetyllysine; alternateBy similarity1
    Modified residuei212N6-succinyllysine; alternateBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ99714.
    MaxQBiQ99714.
    PaxDbiQ99714.
    PeptideAtlasiQ99714.
    PRIDEiQ99714.
    TopDownProteomicsiQ99714-1. [Q99714-1]
    Q99714-2. [Q99714-2]

    2D gel databases

    REPRODUCTION-2DPAGEIPI00017726.
    Q99714.
    UCD-2DPAGEQ99714.

    PTM databases

    iPTMnetiQ99714.
    PhosphoSitePlusiQ99714.
    SwissPalmiQ99714.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in normal tissues but is overexpressed in neurons affected in AD.1 Publication

    Gene expression databases

    BgeeiENSG00000072506.
    CleanExiHS_HSD17B10.
    ExpressionAtlasiQ99714. baseline and differential.
    GenevisibleiQ99714. HS.

    Organism-specific databases

    HPAiHPA001432.

    Interactioni

    Subunit structurei

    Homotetramer (By similarity). Interacts with MRPP1/TRMT10C and MRPP3/KIAA0391.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050674EBI-79964,EBI-77613
    TRMT10CQ7L0Y34EBI-79964,EBI-2107046

    Protein-protein interaction databases

    BioGridi109278. 243 interactors.
    IntActiQ99714. 26 interactors.
    MINTiMINT-3059664.
    STRINGi9606.ENSP00000168216.

    Structurei

    Secondary structure

    1261
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi12 – 16Combined sources5
    Turni17 – 19Combined sources3
    Helixi21 – 32Combined sources12
    Beta strandi36 – 41Combined sources6
    Helixi47 – 54Combined sources8
    Beta strandi58 – 62Combined sources5
    Helixi68 – 82Combined sources15
    Beta strandi87 – 90Combined sources4
    Beta strandi100 – 102Combined sources3
    Turni103 – 106Combined sources4
    Helixi111 – 121Combined sources11
    Helixi123 – 136Combined sources14
    Beta strandi148 – 153Combined sources6
    Helixi157 – 160Combined sources4
    Helixi166 – 186Combined sources21
    Helixi187 – 189Combined sources3
    Beta strandi191 – 198Combined sources8
    Helixi204 – 208Combined sources5
    Helixi216 – 219Combined sources4
    Beta strandi222 – 224Combined sources3
    Helixi230 – 242Combined sources13
    Beta strandi250 – 254Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F67model-A1-261[»]
    1SO8X-ray2.30A1-261[»]
    1U7TX-ray2.00A/B/C/D1-261[»]
    2O23X-ray1.20A/B1-261[»]
    ProteinModelPortaliQ99714.
    SMRiQ99714.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99714.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1199. Eukaryota.
    ENOG410XNNW. LUCA.
    GeneTreeiENSGT00760000118868.
    HOVERGENiHBG002145.
    InParanoidiQ99714.
    KOiK08683.
    OMAiLMGLVNC.
    OrthoDBiEOG091G0G9O.
    PhylomeDBiQ99714.
    TreeFamiTF354307.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 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. AlignAdd to basket

    Isoform 1 (identifier: Q99714-1) [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
    MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ
    60 70 80 90 100
    AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT
    110 120 130 140 150
    YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI
    160 170 180 190 200
    INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL
    210 220 230 240 250
    FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV
    260
    IRLDGAIRMQ P
    Length:261
    Mass (Da):26,923
    Last modified:January 23, 2007 - v3
    Checksum:i9E74F242E3E6FEF1
    GO
    Isoform 2 (identifier: Q99714-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-199: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:252
    Mass (Da):25,984
    Checksum:iF36BB71070CE872D
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_015987122L → V in MHBD deficiency. 1 PublicationCorresponds to variant rs28935476dbSNPEnsembl.1
    Natural variantiVAR_015988130R → C in MHBD deficiency. 2 PublicationsCorresponds to variant rs28935475dbSNPEnsembl.1
    Natural variantiVAR_032093247N → S in MHBD deficiency; intermediate enzyme activity. 1 PublicationCorresponds to variant rs122461163dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_007830191 – 199Missing in isoform 2. 1 Publication9

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U96132 mRNA. Translation: AAC51812.1.
    U73514 mRNA. Translation: AAB68958.1.
    AF069134 mRNA. Translation: AAC39900.1.
    AF035555 mRNA. Translation: AAC15902.1.
    AF037438 Genomic DNA. Translation: AAC16419.1.
    CR456723 mRNA. Translation: CAG33004.1.
    Z97054 Genomic DNA. Translation: CAI42652.1.
    Z97054 Genomic DNA. Translation: CAI42653.1.
    CH471154 Genomic DNA. Translation: EAW93157.1.
    CH471154 Genomic DNA. Translation: EAW93158.1.
    BC000372 mRNA. Translation: AAH00372.1.
    BC008708 mRNA. Translation: AAH08708.1.
    AY092415 mRNA. Translation: AAM18189.1.
    CCDSiCCDS14354.1. [Q99714-1]
    CCDS35300.1. [Q99714-2]
    RefSeqiNP_001032900.1. NM_001037811.2. [Q99714-2]
    NP_004484.1. NM_004493.2. [Q99714-1]
    UniGeneiHs.171280.

    Genome annotation databases

    EnsembliENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]
    ENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]
    GeneIDi3028.
    KEGGihsa:3028.
    UCSCiuc004dsl.2. human. [Q99714-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U96132 mRNA. Translation: AAC51812.1.
    U73514 mRNA. Translation: AAB68958.1.
    AF069134 mRNA. Translation: AAC39900.1.
    AF035555 mRNA. Translation: AAC15902.1.
    AF037438 Genomic DNA. Translation: AAC16419.1.
    CR456723 mRNA. Translation: CAG33004.1.
    Z97054 Genomic DNA. Translation: CAI42652.1.
    Z97054 Genomic DNA. Translation: CAI42653.1.
    CH471154 Genomic DNA. Translation: EAW93157.1.
    CH471154 Genomic DNA. Translation: EAW93158.1.
    BC000372 mRNA. Translation: AAH00372.1.
    BC008708 mRNA. Translation: AAH08708.1.
    AY092415 mRNA. Translation: AAM18189.1.
    CCDSiCCDS14354.1. [Q99714-1]
    CCDS35300.1. [Q99714-2]
    RefSeqiNP_001032900.1. NM_001037811.2. [Q99714-2]
    NP_004484.1. NM_004493.2. [Q99714-1]
    UniGeneiHs.171280.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1F67model-A1-261[»]
    1SO8X-ray2.30A1-261[»]
    1U7TX-ray2.00A/B/C/D1-261[»]
    2O23X-ray1.20A/B1-261[»]
    ProteinModelPortaliQ99714.
    SMRiQ99714.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109278. 243 interactors.
    IntActiQ99714. 26 interactors.
    MINTiMINT-3059664.
    STRINGi9606.ENSP00000168216.

    Chemistry databases

    ChEMBLiCHEMBL4159.
    SwissLipidsiSLP:000000787.

    PTM databases

    iPTMnetiQ99714.
    PhosphoSitePlusiQ99714.
    SwissPalmiQ99714.

    Polymorphism and mutation databases

    BioMutaiHSD17B10.
    DMDMi2492759.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00017726.
    Q99714.
    UCD-2DPAGEQ99714.

    Proteomic databases

    EPDiQ99714.
    MaxQBiQ99714.
    PaxDbiQ99714.
    PeptideAtlasiQ99714.
    PRIDEiQ99714.
    TopDownProteomicsiQ99714-1. [Q99714-1]
    Q99714-2. [Q99714-2]

    Protocols and materials databases

    DNASUi3028.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]
    ENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]
    GeneIDi3028.
    KEGGihsa:3028.
    UCSCiuc004dsl.2. human. [Q99714-1]

    Organism-specific databases

    CTDi3028.
    DisGeNETi3028.
    GeneCardsiHSD17B10.
    HGNCiHGNC:4800. HSD17B10.
    HPAiHPA001432.
    MalaCardsiHSD17B10.
    MIMi300220. phenotype.
    300256. gene.
    300438. phenotype.
    300705. phenotype.
    neXtProtiNX_Q99714.
    OpenTargetsiENSG00000072506.
    Orphaneti85295. HSD10 disease, atypical type.
    391428. HSD10 disease, infantile type.
    391457. HSD10 disease, neonatal type.
    PharmGKBiPA162391638.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1199. Eukaryota.
    ENOG410XNNW. LUCA.
    GeneTreeiENSGT00760000118868.
    HOVERGENiHBG002145.
    InParanoidiQ99714.
    KOiK08683.
    OMAiLMGLVNC.
    OrthoDBiEOG091G0G9O.
    PhylomeDBiQ99714.
    TreeFamiTF354307.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01071-MONOMER.
    ZFISH:HS01071-MONOMER.
    BRENDAi1.1.1.178. 2681.
    1.1.1.35. 2681.
    ReactomeiR-HSA-6785470. tRNA processing in the mitochondrion.
    R-HSA-6787450. tRNA modification in the mitochondrion.
    R-HSA-70895. Branched-chain amino acid catabolism.
    R-HSA-8868766. rRNA processing in the mitochondrion.
    SABIO-RKQ99714.

    Miscellaneous databases

    ChiTaRSiHSD17B10. human.
    EvolutionaryTraceiQ99714.
    GeneWikiiHSD17B10.
    GenomeRNAii3028.
    PROiQ99714.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000072506.
    CleanExiHS_HSD17B10.
    ExpressionAtlasiQ99714. baseline and differential.
    GenevisibleiQ99714. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHCD2_HUMAN
    AccessioniPrimary (citable) accession number: Q99714
    Secondary accession number(s): Q5H927
    , Q6IBS9, Q8TCV9, Q96HD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 188 of the entry and version 3 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 X
      Human chromosome X: 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

    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.