UniProt Accession

 DPP9_HUMAN; Q86TI2; O75273; O75868; Q1ZZB8; Q6AI37; Q6UAL0; Q6ZMT2; Q6ZNJ5; Q8N2J7; Q8N3F5; Q8WXD8; Q96NT8; Q9BVR3 

Genbank Protein ID

 AF452102; AY172660; AF542510; AY374518; DQ417928; AK054656; AK075030; AK122654; AK131100; AK131499; AC005594; AC005783; CH471139; CH471139; BC000970; BC037948; AL834376; CR627380 

Genbank Nucleotide ID

 AAL47179.1; AAO17262.1; AAO73880.2; AAQ83119.1; ABD83624.1; BAB70784.1; BAC11362.1; BAG53644.1; BAC85150.1; BAD18643.1; AAC33801.1; AAC62840.1; EAW69199.1; EAW69201.1; AAH00970.1; AAH37948.1; CAD39039.3; CAH10477.1 

Protein Name

 Dipeptidyl peptidase 9 

Protein Synonyms/Alias

 DP9; Dipeptidyl peptidase IV-related protein 2; DPRP-2; Dipeptidyl peptidase IX; DPP IX; Dipeptidyl peptidase-like protein 9; DPLP9 

Gene Name

 DPP9 

Gene Synonyms/Alias

 DPRP2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
51	YSGLIVNKAPHDFQF	acetylation	[1]
314	RTGSKNPKIALKLAE	acetylation	[2]
462	YKVTAVLKSQGYDWS	ubiquitination	[3]
828	SQLIRAGKPYQLQIY	ubiquitination	[3, 4, 5, 6, 7, 8]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. 

Sequence Annotation

 ACT_SITE 730 730 Charge relay system (By similarity).
 ACT_SITE 808 808 Charge relay system (By similarity).
 ACT_SITE 840 840 Charge relay system (By similarity).
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 Acetylation; Alternative splicing; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 863 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:InterPro.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 

Interpro

 IPR001375; Peptidase_S9.
 IPR002469; Peptidase_S9B. 

Pfam

 PF00930; DPPIV_N
 PF00326; Peptidase_S9 

SMART

  

PROSITE

  

PRINTS