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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)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
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:18344. HINT2.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
  2. nucleolus Source: HPA
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.

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 – 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.

Polymorphism databases

DMDMi51701612.

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. 2 interactions.
STRINGi9606.ENSP00000259667.

PTM databases

PhosphoSiteiQ9BX68.

Polymorphism databases

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.
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.
GenevestigatoriQ9BX68.

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].

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: February 4, 2015
This is version 96 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.