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Protein

Histidine triad nucleotide-binding protein 3

Gene

HINT3

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

Functioni

Hydrolyzes phosphoramidate and acyl-adenylate substrates.1 Publication

Kineticsi

HINT3 prefers purine over pyrimidine-based substrates.

  1. KM=1.5 µM for indolepropinoic acyl-adenylate1 Publication
  2. KM=22 µM for adenine1 Publication
  3. KM=29 µM for guanine1 Publication
  4. KM=32 µM for hypoxanthine1 Publication
  5. KM=121 µM for uracil1 Publication
  6. KM=181 µM for cytosine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei145 – 1451Tele-AMP-histidine intermediate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi76 – 772Purine nucleotide phosphoramidateBy similarity
    Nucleotide bindingi145 – 1473Purine nucleotide phosphoramidateBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ9NQE9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine triad nucleotide-binding protein 3 (EC:3.-.-.-)
    Short name:
    HINT-3
    Gene namesi
    Name:HINT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:18468. HINT3.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Nucleus 1 Publication

    • Note: Localized as aggregates in the cytoplasm and the nucleus.

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB-SubCell
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi145 – 1451H → A: Abolishes hydrolase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29288.

    Polymorphism and mutation databases

    BioMutaiHINT3.
    DMDMi74752900.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 182181Histidine triad nucleotide-binding protein 3PRO_0000324327Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9NQE9.
    MaxQBiQ9NQE9.
    PaxDbiQ9NQE9.
    PeptideAtlasiQ8N0Y9.
    PRIDEiQ9NQE9.

    PTM databases

    iPTMnetiQ9NQE9.
    PhosphoSiteiQ9NQE9.

    Expressioni

    Gene expression databases

    BgeeiQ9NQE9.
    CleanExiHS_HINT3.
    GenevisibleiQ9NQE9. HS.

    Organism-specific databases

    HPAiHPA027914.

    Interactioni

    Subunit structurei

    Forms dimers to octamers and even larger oligomer.

    Protein-protein interaction databases

    BioGridi126420. 5 interactions.
    STRINGi9606.ENSP00000229633.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NQE9.
    SMRiQ9NQE9. Positions 57-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 160112HITPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi143 – 1475Histidine triad motif

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG4359. Eukaryota.
    ENOG4111MVJ. LUCA.
    GeneTreeiENSGT00510000047616.
    HOGENOMiHOG000061067.
    HOVERGENiHBG057291.
    InParanoidiQ9NQE9.
    OMAiELLHCEN.
    OrthoDBiEOG77M8Q7.
    PhylomeDBiQ9NQE9.
    TreeFamiTF353069.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR011146. HIT-like.
    [Graphical view]
    SUPFAMiSSF54197. SSF54197. 1 hit.
    PROSITEiPS51084. HIT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NQE9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAEEQVNRSA GLAPDCEASA TAETTVSSVG TCEAAGKSPE PKDYDSTCVF
    60 70 80 90 100
    CRIAGRQDPG TELLHCENED LICFKDIKPA ATHHYLVVPK KHIGNCRTLR
    110 120 130 140 150
    KDQVELVENM VTVGKTILER NNFTDFTNVR MGFHMPPFCS ISHLHLHVLA
    160 170 180
    PVDQLGFLSK LVYRVNSYWF ITADHLIEKL RT
    Length:182
    Mass (Da):20,361
    Last modified:October 1, 2000 - v1
    Checksum:iB5E7EA8A07068251
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361G → A 2.5-fold increase in affinity for indolepropinoic acyl-adenylate and cytosine; 2-fold decrease in hypoxanthine affinity; nearly no change in affinity for adenine, guanine and uracil. 3 Publications
    Corresponds to variant rs2295005 [ dbSNP | Ensembl ].
    VAR_039734

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY035387 mRNA. Translation: AAK71347.1.
    AY035388 mRNA. Translation: AAK71348.1.
    AY486460 mRNA. Translation: AAR89533.1.
    AY486461 mRNA. Translation: AAR89534.1.
    AK057688 mRNA. Translation: BAG51953.1.
    AL035689 Genomic DNA. Translation: CAB92728.1.
    CH471051 Genomic DNA. Translation: EAW48129.1.
    BC015732 mRNA. Translation: AAH15732.1.
    CCDSiCCDS5133.1.
    RefSeqiNP_612638.3. NM_138571.4.
    UniGeneiHs.72325.

    Genome annotation databases

    EnsembliENST00000229633; ENSP00000229633; ENSG00000111911.
    GeneIDi135114.
    KEGGihsa:135114.
    UCSCiuc003qal.5. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY035387 mRNA. Translation: AAK71347.1.
    AY035388 mRNA. Translation: AAK71348.1.
    AY486460 mRNA. Translation: AAR89533.1.
    AY486461 mRNA. Translation: AAR89534.1.
    AK057688 mRNA. Translation: BAG51953.1.
    AL035689 Genomic DNA. Translation: CAB92728.1.
    CH471051 Genomic DNA. Translation: EAW48129.1.
    BC015732 mRNA. Translation: AAH15732.1.
    CCDSiCCDS5133.1.
    RefSeqiNP_612638.3. NM_138571.4.
    UniGeneiHs.72325.

    3D structure databases

    ProteinModelPortaliQ9NQE9.
    SMRiQ9NQE9. Positions 57-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi126420. 5 interactions.
    STRINGi9606.ENSP00000229633.

    PTM databases

    iPTMnetiQ9NQE9.
    PhosphoSiteiQ9NQE9.

    Polymorphism and mutation databases

    BioMutaiHINT3.
    DMDMi74752900.

    Proteomic databases

    EPDiQ9NQE9.
    MaxQBiQ9NQE9.
    PaxDbiQ9NQE9.
    PeptideAtlasiQ8N0Y9.
    PRIDEiQ9NQE9.

    Protocols and materials databases

    DNASUi135114.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000229633; ENSP00000229633; ENSG00000111911.
    GeneIDi135114.
    KEGGihsa:135114.
    UCSCiuc003qal.5. human.

    Organism-specific databases

    CTDi135114.
    GeneCardsiHINT3.
    HGNCiHGNC:18468. HINT3.
    HPAiHPA027914.
    MIMi609998. gene.
    neXtProtiNX_Q9NQE9.
    PharmGKBiPA29288.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG4359. Eukaryota.
    ENOG4111MVJ. LUCA.
    GeneTreeiENSGT00510000047616.
    HOGENOMiHOG000061067.
    HOVERGENiHBG057291.
    InParanoidiQ9NQE9.
    OMAiELLHCEN.
    OrthoDBiEOG77M8Q7.
    PhylomeDBiQ9NQE9.
    TreeFamiTF353069.

    Enzyme and pathway databases

    SABIO-RKQ9NQE9.

    Miscellaneous databases

    ChiTaRSiHINT3. human.
    GenomeRNAii135114.
    PROiQ9NQE9.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NQE9.
    CleanExiHS_HINT3.
    GenevisibleiQ9NQE9. HS.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR011146. HIT-like.
    [Graphical view]
    SUPFAMiSSF54197. SSF54197. 1 hit.
    PROSITEiPS51084. HIT_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human HINT-4 is a novel member of the histidine triad protein family with differential polyadenylation."
      Huang C.-H.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-36.
    2. "HINT-3-2, a novel member of HIT family, and Hint3-1 with phosphoramidase activity."
      Cheng J.L., Liu B.L., Chou T.F., Drontle D., Wagner C.R.
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-36.
      Tissue: Trachea.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Eye.
    7. "Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases."
      Brenner C.
      Biochemistry 41:9003-9014(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    8. "Evidence that human histidine triad nucleotide binding protein 3 (Hint3) is a distinct branch of the histidine triad (HIT) superfamily."
      Chou T.-F., Cheng J., Tikh I.B., Wagner C.R.
      J. Mol. Biol. 373:978-989(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT ALA-36, ACTIVE SITE, MUTAGENESIS OF HIS-145.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHINT3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQE9
    Secondary accession number(s): B3KQ91, Q8N0Y9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: October 1, 2000
    Last modified: June 8, 2016
    This is version 117 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. 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.