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Protein

Histidine triad nucleotide-binding protein 1

Gene

Hint1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, 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, as well as Met-AMP, His-AMP and Asp-AMP, 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. In addition, functions 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).By similarity

Sites

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

Regions

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

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
Protein kinase C inhibitor 1
Protein kinase C-interacting protein 1
Short name:
PKCI-1
Gene namesi
Name:Hint1
Synonyms:Hint, Pkci, Pkci1, Prkcnh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1321133. Hint1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • histone deacetylase complex Source: UniProtKB
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice display increased susceptibility to carcinogens.1 Publication

Chemistry

ChEMBLiCHEMBL1250364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 126125Histidine triad nucleotide-binding protein 1PRO_0000109782Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP70349.
MaxQBiP70349.
PaxDbiP70349.
PRIDEiP70349.

2D gel databases

REPRODUCTION-2DPAGEP70349.

PTM databases

iPTMnetiP70349.
PhosphoSiteiP70349.
SwissPalmiP70349.

Expressioni

Gene expression databases

BgeeiP70349.
CleanExiMM_HINT1.
ExpressionAtlasiP70349. baseline and differential.
GenevisibleiP70349. MM.

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

BioGridi200305. 1 interaction.
IntActiP70349. 4 interactions.
MINTiMINT-1868587.
STRINGi10090.ENSMUSP00000020504.

Chemistry

BindingDBiP70349.

Structurei

3D structure databases

ProteinModelPortaliP70349.
SMRiP70349. Positions 13-126.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiP70349.
KOiK02503.
OMAiCNPYPDG.
OrthoDBiEOG75QR5T.
PhylomeDBiP70349.
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.

P70349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEIAKAQV AQPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT
60 70 80 90 100
HFLVIPKKHI SQISVADDDD ESLLGHLMIV GKKCAADLGL KRGYRMVVNE
110 120
GADGGQSVYH IHLHVLGGRQ MNWPPG
Length:126
Mass (Da):13,777
Last modified:January 23, 2007 - v3
Checksum:i30DA241476389805
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60001 mRNA. Translation: AAC71076.1.
AK002965 mRNA. Translation: BAB22484.1.
AK012433 mRNA. Translation: BAB28235.1.
BC070415 mRNA. Translation: AAH70415.1.
BC080296 mRNA. Translation: AAH80296.1.
CCDSiCCDS24702.1.
PIRiPN0044.
RefSeqiNP_032274.1. NM_008248.2.
UniGeneiMm.425.

Genome annotation databases

EnsembliENSMUST00000020504; ENSMUSP00000020504; ENSMUSG00000020267.
GeneIDi15254.
KEGGimmu:15254.
UCSCiuc007iyj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60001 mRNA. Translation: AAC71076.1.
AK002965 mRNA. Translation: BAB22484.1.
AK012433 mRNA. Translation: BAB28235.1.
BC070415 mRNA. Translation: AAH70415.1.
BC080296 mRNA. Translation: AAH80296.1.
CCDSiCCDS24702.1.
PIRiPN0044.
RefSeqiNP_032274.1. NM_008248.2.
UniGeneiMm.425.

3D structure databases

ProteinModelPortaliP70349.
SMRiP70349. Positions 13-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200305. 1 interaction.
IntActiP70349. 4 interactions.
MINTiMINT-1868587.
STRINGi10090.ENSMUSP00000020504.

Chemistry

BindingDBiP70349.
ChEMBLiCHEMBL1250364.

PTM databases

iPTMnetiP70349.
PhosphoSiteiP70349.
SwissPalmiP70349.

2D gel databases

REPRODUCTION-2DPAGEP70349.

Proteomic databases

EPDiP70349.
MaxQBiP70349.
PaxDbiP70349.
PRIDEiP70349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020504; ENSMUSP00000020504; ENSMUSG00000020267.
GeneIDi15254.
KEGGimmu:15254.
UCSCiuc007iyj.1. mouse.

Organism-specific databases

CTDi3094.
MGIiMGI:1321133. Hint1.

Phylogenomic databases

eggNOGiKOG3275. Eukaryota.
COG0537. LUCA.
GeneTreeiENSGT00510000046448.
HOGENOMiHOG000061064.
HOVERGENiHBG051906.
InParanoidiP70349.
KOiK02503.
OMAiCNPYPDG.
OrthoDBiEOG75QR5T.
PhylomeDBiP70349.
TreeFamiTF314862.

Miscellaneous databases

NextBioi287869.
PROiP70349.
SOURCEiSearch...

Gene expression databases

BgeeiP70349.
CleanExiMM_HINT1.
ExpressionAtlasiP70349. baseline and differential.
GenevisibleiP70349. MM.

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. "Characterization of PKCI and comparative studies with FHIT, related members of the HIT protein family."
    Klein M.G., Yao Y., Slosberg E.D., Lima C.D., Doki Y., Weinstein I.B.
    Exp. Cell Res. 244:26-32(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 8-21; 38-57 AND 96-119, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. "Deletion of histidine triad nucleotide-binding protein 1/PKC-interacting protein in mice enhances cell growth and carcinogenesis."
    Su T., Suzui M., Wang L., Lin C.S., Xing W.Q., Weinstein I.B.
    Proc. Natl. Acad. Sci. U.S.A. 100:7824-7829(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHINT1_MOUSE
AccessioniPrimary (citable) accession number: P70349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 133 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.