CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020742
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histidine triad nucleotide-binding protein 2, mitochondrial 
Protein Synonyms/Alias
 HINT-2; HINT-3 
Gene Name
 Hint2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
45SEVAKAQKAAPGGASacetylation[1]
45SEVAKAQKAAPGGASsuccinylation[1]
45SEVAKAQKAAPGGASubiquitination[2]
119GHLLLVAKKIAQAQGacetylation[3, 4]
128IAQAQGLKDGYRLVVacetylation[1, 3, 4, 5, 6]
128IAQAQGLKDGYRLVVsuccinylation[1]
139RLVVNDGKMGAQSVYacetylation[3, 4, 6]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
 Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity (By similarity). 
Sequence Annotation
 DOMAIN 55 163 HIT.
 NP_BIND 80 81 Purine nucleotide phosphoramidate (By
 NP_BIND 142 144 Purine nucleotide phosphoramidate (By
 NP_BIND 149 151 Purine nucleotide phosphoramidate (By
 MOTIF 147 151 Histidine triad motif.
 ACT_SITE 149 149 Tele-AMP-histidine intermediate (By
 BINDING 136 136 Purine nucleotide phosphoramidate (By  
Keyword
 Apoptosis; Complete proteome; Hydrolase; Lipid biosynthesis; Lipid metabolism; Mitochondrion; Nucleotide-binding; Reference proteome; Steroid biosynthesis; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 163 AA 
Protein Sequence
MAAAVLLAVG LRAARRTLAA AGARGAQVRG NAGVSDGSEV AKAQKAAPGG ASPTIFSRIL 60
DRSLPADILY EDQQCLVFRD VAPQAPVHFL VIPRKPIPRI SQAEEDDQQL LGHLLLVAKK 120
IAQAQGLKDG YRLVVNDGKM GAQSVYHLHI HVLGGRQLQW PPG 163 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR019808; Histidine_triad_CS.
 IPR001310; Histidine_triad_HIT.
 IPR011146; HIT-like. 
Pfam
 PF01230; HIT 
SMART
  
PROSITE
 PS00892; HIT_1
 PS51084; HIT_2 
PRINTS
 PR00332; HISTRIAD.