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 1

Gene

HINT1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as enzyme, and as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By similarity). Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Purine nucleotide phosphoramidate
Active sitei112 – 1121Tele-AMP-histidine intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 442Purine nucleotide phosphoramidate
Nucleotide bindingi105 – 1073Purine nucleotide phosphoramidate
Nucleotide bindingi112 – 1143Purine nucleotide phosphoramidate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine triad nucleotide-binding protein 1 (EC:3.-.-.-)
Alternative name(s):
Adenosine 5'-monophosphoramidase
P13.7
Gene namesi
Name:HINT1
Synonyms:HINT
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381C → A: No effect. 1 Publication
Mutagenesisi84 – 841C → A: No effect. 1 Publication
Mutagenesisi107 – 1071S → A: No effect. 1 Publication
Mutagenesisi114 – 1141H → D: Nearly abolishes enzyme activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3232701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 126125Histidine triad nucleotide-binding protein 1PRO_0000109783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei30 – 301N6-acetyllysineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei72 – 721PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Expressioni

Tissue specificityi

Widely expressed.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK7. Interacts with RUVBL1 and RUVBL2 and is associated with the LEF1/TCF1-CTNNB1 complex and with a KAT5 histone acetyltransferase complex. Identified in a complex with MITF and CTNNB1. Interacts with CDC34 and RBX1, and is part of a SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005709.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 236Combined sources
Beta strandi31 – 344Combined sources
Beta strandi36 – 427Combined sources
Beta strandi47 – 5812Combined sources
Helixi63 – 653Combined sources
Helixi68 – 703Combined sources
Helixi71 – 8717Combined sources
Beta strandi94 – 974Combined sources
Helixi101 – 1044Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi113 – 1197Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZYX-ray1.80A2-126[»]
3O1CX-ray1.08A1-126[»]
3O1XX-ray1.08A1-126[»]
3O1ZX-ray1.30A1-126[»]
3QGZX-ray1.10A1-126[»]
3RHNX-ray2.10A12-126[»]
4RHNX-ray1.90A12-126[»]
5RHNX-ray2.31A12-126[»]
6RHNX-ray2.15A12-126[»]
ProteinModelPortaliP80912.
SMRiP80912. Positions 12-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 126109HITPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1145Histidine triad motif

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3275. Eukaryota.
COG0537. LUCA.
GeneTreeiENSGT00510000046448.
HOGENOMiHOG000061064.
HOVERGENiHBG051906.
InParanoidiP80912.
KOiK02503.
OMAiYRLITNN.
OrthoDBiEOG091G1001.
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.

P80912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEIAKAQV ARPGGDTIFG KIIRKEIPAK IIFEDDQCLA FHDISPQAPT
60 70 80 90 100
HFLVIPKKHI SQISAAEDAD ESLLGHLMIV GKKCAADLGL KKGYRMVVNE
110 120
GSDGGQSVYH VHLHVLGGRQ MNWPPG
Length:126
Mass (Da):13,693
Last modified:January 23, 2007 - v2
Checksum:i7322271D00F2E099
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11175 mRNA. Translation: CAA72061.1.
RefSeqiNP_001076092.1. NM_001082623.1.
UniGeneiOcu.3078.

Genome annotation databases

EnsembliENSOCUT00000006605; ENSOCUP00000005709; ENSOCUG00000006607.
GeneIDi100009302.
KEGGiocu:100009302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11175 mRNA. Translation: CAA72061.1.
RefSeqiNP_001076092.1. NM_001082623.1.
UniGeneiOcu.3078.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZYX-ray1.80A2-126[»]
3O1CX-ray1.08A1-126[»]
3O1XX-ray1.08A1-126[»]
3O1ZX-ray1.30A1-126[»]
3QGZX-ray1.10A1-126[»]
3RHNX-ray2.10A12-126[»]
4RHNX-ray1.90A12-126[»]
5RHNX-ray2.31A12-126[»]
6RHNX-ray2.15A12-126[»]
ProteinModelPortaliP80912.
SMRiP80912. Positions 12-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005709.

Chemistry

ChEMBLiCHEMBL3232701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000006605; ENSOCUP00000005709; ENSOCUG00000006607.
GeneIDi100009302.
KEGGiocu:100009302.

Organism-specific databases

CTDi3094.

Phylogenomic databases

eggNOGiKOG3275. Eukaryota.
COG0537. LUCA.
GeneTreeiENSGT00510000046448.
HOGENOMiHOG000061064.
HOVERGENiHBG051906.
InParanoidiP80912.
KOiK02503.
OMAiYRLITNN.
OrthoDBiEOG091G1001.
TreeFamiTF314862.

Miscellaneous databases

EvolutionaryTraceiP80912.

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 nameiHINT1_RABIT
AccessioniPrimary (citable) accession number: P80912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a protein kinase C inhibitor and to bind zinc in solution. Both seem to be incorrect.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.