Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei136 – 1361Purine nucleotide phosphoramidateBy similarity
    Active sitei149 – 1491Tele-AMP-histidine intermediate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi80 – 812Purine nucleotide phosphoramidateBy similarity
    Nucleotide bindingi142 – 1443Purine nucleotide phosphoramidateBy similarity
    Nucleotide bindingi149 – 1513Purine nucleotide phosphoramidateBy similarity

    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

    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
    ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491H → A: Loss of adenosine phosphoramidase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29287.

    Polymorphism and mutation databases

    BioMutaiHINT2.
    DMDMi51701612.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1717MitochondrionSequence AnalysisAdd
    BLAST
    Chaini18 – 163146Histidine triad nucleotide-binding protein 2, mitochondrialPRO_0000109786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191N6-acetyllysineBy similarity
    Modified residuei139 – 1391N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BX68.
    PaxDbiQ9BX68.
    PeptideAtlasiQ9BX68.
    PRIDEiQ9BX68.

    2D gel databases

    OGPiQ9BX68.

    PTM databases

    PhosphoSiteiQ9BX68.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ9BX68.
    CleanExiHS_HINT2.
    GenevisibleiQ9BX68. HS.

    Organism-specific databases

    HPAiHPA020961.
    HPA059109.

    Interactioni

    Protein-protein interaction databases

    BioGridi124200. 3 interactions.
    STRINGi9606.ENSP00000259667.

    Structurei

    Secondary structure

    1
    163
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 605Combined sources
    Helixi65 – 673Combined sources
    Beta strandi68 – 714Combined sources
    Beta strandi73 – 797Combined sources
    Beta strandi84 – 9512Combined sources
    Helixi100 – 1023Combined sources
    Helixi105 – 1073Combined sources
    Helixi108 – 12417Combined sources
    Beta strandi131 – 1377Combined sources
    Turni138 – 1425Combined sources
    Beta strandi145 – 1473Combined sources
    Beta strandi150 – 1567Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 52-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 163109HITPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi147 – 1515Histidine triad motif

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0537.
    GeneTreeiENSGT00510000046448.
    HOGENOMiHOG000061064.
    HOVERGENiHBG051906.
    InParanoidiQ9BX68.
    OMAiNNGVEAC.
    OrthoDBiEOG75QR5T.
    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.3. 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
    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. Positions 52-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124200. 3 interactions.
    STRINGi9606.ENSP00000259667.

    PTM databases

    PhosphoSiteiQ9BX68.

    Polymorphism and mutation databases

    BioMutaiHINT2.
    DMDMi51701612.

    2D gel databases

    OGPiQ9BX68.

    Proteomic databases

    MaxQBiQ9BX68.
    PaxDbiQ9BX68.
    PeptideAtlasiQ9BX68.
    PRIDEiQ9BX68.

    Protocols and materials databases

    DNASUi84681.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000259667; ENSP00000259667; ENSG00000137133.
    GeneIDi84681.
    KEGGihsa:84681.
    UCSCiuc003zyh.3. human.

    Organism-specific databases

    CTDi84681.
    GeneCardsiGC09M035812.
    HGNCiHGNC:18344. HINT2.
    HPAiHPA020961.
    HPA059109.
    MIMi609997. gene.
    neXtProtiNX_Q9BX68.
    PharmGKBiPA29287.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0537.
    GeneTreeiENSGT00510000046448.
    HOGENOMiHOG000061064.
    HOVERGENiHBG051906.
    InParanoidiQ9BX68.
    OMAiNNGVEAC.
    OrthoDBiEOG75QR5T.
    PhylomeDBiQ9BX68.
    TreeFamiTF314862.

    Miscellaneous databases

    GenomeRNAii84681.
    NextBioi74724.
    PROiQ9BX68.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9BX68.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "HIT-17kDa is a new protein from the HIT family with high homology to PKCI-1."
      Magnino F., Dufour J.-F.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "PKCI-1-related HIT protein."
      Takada F., Lugus J.J., Beggs A.H.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Hint-2 genomic sequence."
      Takada F., Lugus J.J., Beggs A.H.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "HINT-3 is a novel member of the histidine triad protein family."
      Chen H., Peng J., Huang C.-H.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Pancreas.
    8. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACTIVE SITE, MUTAGENESIS OF HIS-149.
    9. "Hint2 is expressed in the mitochondria of H295R cells and is involved in steroidogenesis."
      Lenglet S., Antigny F., Vetterli L., Dufour J.-F., Rossier M.F.
      Endocrinology 149:5461-5469(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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.

    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: July 22, 2015
    This is version 100 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

    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.