Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BX68

- HINT2_HUMAN

UniProt

Q9BX68 - HINT2_HUMAN

Protein

Histidine triad nucleotide-binding protein 2, mitochondrial

Gene

HINT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. hydrolase activity Source: UniProtKB-KW
    2. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. steroid biosynthetic process Source: UniProtKB-KW

    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:18344. HINT2.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    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.

    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.
    GenevestigatoriQ9BX68.

    Organism-specific databases

    HPAiHPA020961.

    Interactioni

    Protein-protein interaction databases

    BioGridi124200. 2 interactions.
    STRINGi9606.ENSP00000259667.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000061064.
    HOVERGENiHBG051906.
    InParanoidiQ9BX68.
    OMAiDRELVGH.
    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

    MAAAVVLAAG LRAARRAVAA TGVRGGQVRG AAGVTDGNEV AKAQQATPGG    50
    AAPTIFSRIL DKSLPADILY EDQQCLVFRD VAPQAPVHFL VIPKKPIPRI 100
    SQAEEEDQQL LGHLLLVAKQ TAKAEGLGDG YRLVINDGKL GAQSVYHLHI 150
    HVLGGRQLQW PPG 163
    Length:163
    Mass (Da):17,162
    Last modified:June 1, 2001 - v1
    Checksum:i63A0C15D13749F99
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi51701612.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6594.1.
    RefSeqi NP_115982.1. NM_032593.2.
    UniGenei Hs.70573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4INC X-ray 1.19 A/B 37-163 [» ]
    4INI X-ray 1.65 A/B 37-163 [» ]
    4NJX X-ray 2.83 A/B/C/D 1-163 [» ]
    4NJY X-ray 1.32 A 1-163 [» ]
    4NJZ X-ray 2.40 A/B/C/D 1-163 [» ]
    4NK0 X-ray 2.02 A/B 1-163 [» ]
    ProteinModelPortali Q9BX68.
    SMRi Q9BX68. Positions 52-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124200. 2 interactions.
    STRINGi 9606.ENSP00000259667.

    PTM databases

    PhosphoSitei Q9BX68.

    Polymorphism databases

    DMDMi 51701612.

    2D gel databases

    OGPi Q9BX68.

    Proteomic databases

    MaxQBi Q9BX68.
    PaxDbi Q9BX68.
    PeptideAtlasi Q9BX68.
    PRIDEi Q9BX68.

    Protocols and materials databases

    DNASUi 84681.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259667 ; ENSP00000259667 ; ENSG00000137133 .
    GeneIDi 84681.
    KEGGi hsa:84681.
    UCSCi uc003zyh.3. human.

    Organism-specific databases

    CTDi 84681.
    GeneCardsi GC09M035802.
    HGNCi HGNC:18344. HINT2.
    HPAi HPA020961.
    MIMi 609997. gene.
    neXtProti NX_Q9BX68.
    PharmGKBi PA29287.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0537.
    HOGENOMi HOG000061064.
    HOVERGENi HBG051906.
    InParanoidi Q9BX68.
    OMAi DRELVGH.
    OrthoDBi EOG75QR5T.
    PhylomeDBi Q9BX68.
    TreeFami TF314862.

    Miscellaneous databases

    GenomeRNAii 84681.
    NextBioi 74724.
    PROi Q9BX68.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BX68.
    CleanExi HS_HINT2.
    Genevestigatori Q9BX68.

    Family and domain databases

    Gene3Di 3.30.428.10. 1 hit.
    InterProi IPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    [Graphical view ]
    PANTHERi PTHR23089. PTHR23089. 1 hit.
    Pfami PF01230. HIT. 1 hit.
    [Graphical view ]
    PRINTSi PR00332. HISTRIAD.
    SUPFAMi SSF54197. SSF54197. 1 hit.
    PROSITEi PS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 92 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