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Protein

Histidine triad nucleotide-binding protein 2, mitochondrial

Gene

HINT2

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

Functioni

Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity.2 Publications

Kineticsi

  1. KM=128 µM for adenosine 5'-O-p-nitrophenylphosphoramidate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei136Purine nucleotide phosphoramidateBy similarity1
    Active sitei149Tele-AMP-histidine intermediate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi80 – 81Purine nucleotide phosphoramidateBy similarity2
    Nucleotide bindingi142 – 144Purine nucleotide phosphoramidateBy similarity3
    Nucleotide bindingi149 – 151Purine nucleotide phosphoramidateBy similarity3

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000137133-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine triad nucleotide-binding protein 2, mitochondrial (EC:3.-.-.-)
    Short name:
    HINT-2
    Alternative name(s):
    HINT-3
    HIT-17kDa
    PKCI-1-related HIT protein
    Gene namesi
    Name:HINT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:18344. HINT2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi149H → A: Loss of adenosine phosphoramidase activity. 1 Publication1

    Organism-specific databases

    DisGeNETi84681.
    OpenTargetsiENSG00000137133.
    PharmGKBiPA29287.

    Polymorphism and mutation databases

    BioMutaiHINT2.
    DMDMi51701612.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 17MitochondrionSequence analysisAdd BLAST17
    ChainiPRO_000010978618 – 163Histidine triad nucleotide-binding protein 2, mitochondrialAdd BLAST146

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei119N6-acetyllysineBy similarity1
    Modified residuei139N6-acetyllysineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9BX68.
    MaxQBiQ9BX68.
    PaxDbiQ9BX68.
    PeptideAtlasiQ9BX68.
    PRIDEiQ9BX68.
    TopDownProteomicsiQ9BX68.

    2D gel databases

    OGPiQ9BX68.

    PTM databases

    iPTMnetiQ9BX68.
    PhosphoSitePlusiQ9BX68.

    Expressioni

    Tissue specificityi

    High expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients.1 Publication

    Gene expression databases

    BgeeiENSG00000137133.
    CleanExiHS_HINT2.
    GenevisibleiQ9BX68. HS.

    Organism-specific databases

    HPAiHPA020961.
    HPA059109.

    Interactioni

    Protein-protein interaction databases

    BioGridi124200. 3 interactors.
    STRINGi9606.ENSP00000259667.

    Structurei

    Secondary structure

    1163
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi56 – 60Combined sources5
    Helixi65 – 67Combined sources3
    Beta strandi68 – 71Combined sources4
    Beta strandi73 – 79Combined sources7
    Beta strandi84 – 95Combined sources12
    Helixi100 – 102Combined sources3
    Helixi105 – 107Combined sources3
    Helixi108 – 124Combined sources17
    Beta strandi131 – 137Combined sources7
    Turni138 – 142Combined sources5
    Beta strandi145 – 147Combined sources3
    Beta strandi150 – 156Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4INCX-ray1.19A/B37-163[»]
    4INIX-ray1.65A/B37-163[»]
    4NJXX-ray2.83A/B/C/D1-163[»]
    4NJYX-ray1.32A1-163[»]
    4NJZX-ray2.40A/B/C/D1-163[»]
    4NK0X-ray2.02A/B1-163[»]
    ProteinModelPortaliQ9BX68.
    SMRiQ9BX68.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini55 – 163HITPROSITE-ProRule annotationAdd BLAST109

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi147 – 151Histidine triad motif5

    Sequence similaritiesi

    Belongs to the HINT family.Curated
    Contains 1 HIT domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG3275. Eukaryota.
    COG0537. LUCA.
    GeneTreeiENSGT00510000046448.
    HOGENOMiHOG000061064.
    HOVERGENiHBG051906.
    InParanoidiQ9BX68.
    OMAiNVAKQES.
    OrthoDBiEOG091G1001.
    PhylomeDBiQ9BX68.
    TreeFamiTF314862.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    [Graphical view]
    PANTHERiPTHR23089. PTHR23089. 1 hit.
    PfamiPF01230. HIT. 1 hit.
    [Graphical view]
    PRINTSiPR00332. HISTRIAD.
    SUPFAMiSSF54197. SSF54197. 1 hit.
    PROSITEiPS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BX68-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAAVVLAAG LRAARRAVAA TGVRGGQVRG AAGVTDGNEV AKAQQATPGG
    60 70 80 90 100
    AAPTIFSRIL DKSLPADILY EDQQCLVFRD VAPQAPVHFL VIPKKPIPRI
    110 120 130 140 150
    SQAEEEDQQL LGHLLLVAKQ TAKAEGLGDG YRLVINDGKL GAQSVYHLHI
    160
    HVLGGRQLQW PPG
    Length:163
    Mass (Da):17,162
    Last modified:June 1, 2001 - v1
    Checksum:i63A0C15D13749F99
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF356515 mRNA. Translation: AAK37562.1.
    AY033094 mRNA. Translation: AAK53455.1.
    AF490476 Genomic DNA. Translation: AAM09526.1.
    AF356875 mRNA. Translation: AAM00221.1.
    AL133410 Genomic DNA. Translation: CAI10991.1.
    CH471071 Genomic DNA. Translation: EAW58332.1.
    BC047737 mRNA. Translation: AAH47737.1.
    CCDSiCCDS6594.1.
    RefSeqiNP_115982.1. NM_032593.2.
    UniGeneiHs.70573.

    Genome annotation databases

    EnsembliENST00000259667; ENSP00000259667; ENSG00000137133.
    GeneIDi84681.
    KEGGihsa:84681.
    UCSCiuc003zyh.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF356515 mRNA. Translation: AAK37562.1.
    AY033094 mRNA. Translation: AAK53455.1.
    AF490476 Genomic DNA. Translation: AAM09526.1.
    AF356875 mRNA. Translation: AAM00221.1.
    AL133410 Genomic DNA. Translation: CAI10991.1.
    CH471071 Genomic DNA. Translation: EAW58332.1.
    BC047737 mRNA. Translation: AAH47737.1.
    CCDSiCCDS6594.1.
    RefSeqiNP_115982.1. NM_032593.2.
    UniGeneiHs.70573.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4INCX-ray1.19A/B37-163[»]
    4INIX-ray1.65A/B37-163[»]
    4NJXX-ray2.83A/B/C/D1-163[»]
    4NJYX-ray1.32A1-163[»]
    4NJZX-ray2.40A/B/C/D1-163[»]
    4NK0X-ray2.02A/B1-163[»]
    ProteinModelPortaliQ9BX68.
    SMRiQ9BX68.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124200. 3 interactors.
    STRINGi9606.ENSP00000259667.

    PTM databases

    iPTMnetiQ9BX68.
    PhosphoSitePlusiQ9BX68.

    Polymorphism and mutation databases

    BioMutaiHINT2.
    DMDMi51701612.

    2D gel databases

    OGPiQ9BX68.

    Proteomic databases

    EPDiQ9BX68.
    MaxQBiQ9BX68.
    PaxDbiQ9BX68.
    PeptideAtlasiQ9BX68.
    PRIDEiQ9BX68.
    TopDownProteomicsiQ9BX68.

    Protocols and materials databases

    DNASUi84681.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000259667; ENSP00000259667; ENSG00000137133.
    GeneIDi84681.
    KEGGihsa:84681.
    UCSCiuc003zyh.4. human.

    Organism-specific databases

    CTDi84681.
    DisGeNETi84681.
    GeneCardsiHINT2.
    HGNCiHGNC:18344. HINT2.
    HPAiHPA020961.
    HPA059109.
    MIMi609997. gene.
    neXtProtiNX_Q9BX68.
    OpenTargetsiENSG00000137133.
    PharmGKBiPA29287.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3275. Eukaryota.
    COG0537. LUCA.
    GeneTreeiENSGT00510000046448.
    HOGENOMiHOG000061064.
    HOVERGENiHBG051906.
    InParanoidiQ9BX68.
    OMAiNVAKQES.
    OrthoDBiEOG091G1001.
    PhylomeDBiQ9BX68.
    TreeFamiTF314862.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000137133-MONOMER.

    Miscellaneous databases

    GenomeRNAii84681.
    PROiQ9BX68.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000137133.
    CleanExiHS_HINT2.
    GenevisibleiQ9BX68. HS.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    [Graphical view]
    PANTHERiPTHR23089. PTHR23089. 1 hit.
    PfamiPF01230. HIT. 1 hit.
    [Graphical view]
    PRINTSiPR00332. HISTRIAD.
    SUPFAMiSSF54197. SSF54197. 1 hit.
    PROSITEiPS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHINT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BX68
    Secondary accession number(s): Q5TCW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: June 1, 2001
    Last modified: November 2, 2016
    This is version 107 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.