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{{Infobox_gene}}
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'''Dipeptidyl peptidase 8''' is an [[enzyme]] that in humans is encoded by the ''DPP8'' [[gene]].<ref name="pmid11012666">{{cite journal | vauthors = Abbott CA, Yu DM, Woollatt E, Sutherland GR, McCaughan GW, Gorrell MD | title = Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8 | journal = Eur J Biochem | volume = 267 | issue = 20 | pages = 6140–50 |date=Nov 2000 | pmid = 11012666 | pmc =  | doi =10.1046/j.1432-1327.2000.01617.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DPP8 dipeptidyl-peptidase 8| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54878| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Dipeptidyl-peptidase 8
| HGNCid = 16490
| Symbol = DPP8
| AltSymbols =; DP8; DPRP1; FLJ14920; FLJ20283; MGC26191; MSTP141
| OMIM = 606819
| ECnumber = 
| Homologene = 57098
| MGIid = 1921638
| GeneAtlas_image1 = PBB_GE_DPP8_220939_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0004274 |text = dipeptidyl-peptidase IV activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006955 |text = immune response}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 54878
    | Hs_Ensembl = ENSG00000074603
    | Hs_RefseqProtein = NP_060213
    | Hs_RefseqmRNA = NM_017743
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 63526028
    | Hs_GenLoc_end = 63597095
    | Hs_Uniprot = Q6V1X1
    | Mm_EntrezGene = 74388
    | Mm_Ensembl = ENSMUSG00000032393
    | Mm_RefseqmRNA = NM_028906
    | Mm_RefseqProtein = NP_083182
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 64830464
    | Mm_GenLoc_end = 64880661
    | Mm_Uniprot = Q3TAE3
  }}
}}
'''Dipeptidyl-peptidase 8''', also known as '''DPP8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPP8 dipeptidyl-peptidase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54878| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: DPP8 dipeptidyl-peptidase 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54878| accessdate = }}</ref>
| summary_text = This gene encodes a member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
;Notes
==Further reading==
{{reflist}}
 
;Further reading
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Abbott CA, Yu DM, Woollatt E, ''et al.'' |title=Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8. |journal=Eur. J. Biochem. |volume=267 |issue= 20 |pages= 6140-50 |year= 2000 |pmid= 11012666 |doi=  }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Ajami K |title=Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family |journal=Biochemistry |volume=42 |issue= 3 |pages= 694–701 |year= 2003 |pmid= 12534281 |doi= 10.1021/bi026846s |name-list-format=vanc| author2=Abbott CA  | author3=Obradovic M  | display-authors=3  | last4=Gysbers  | first4=Vanessa  | last5=Kähne  | first5=Thilo  | last6=McCaughan  | first6=Geoffrey W.  | last7=Gorrell  | first7=Mark D. }}
*{{cite journal  | author=Ajami K, Abbott CA, Obradovic M, ''et al.'' |title=Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family. |journal=Biochemistry |volume=42 |issue= 3 |pages= 694-701 |year= 2003 |pmid= 12534281 |doi= 10.1021/bi026846s }}
*{{cite journal  | author=Qi SY |title=Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 179–89 |year= 2003 |pmid= 12662155 |doi= 10.1042/BJ20021914 | pmc=1223468  |name-list-format=vanc| author2=Riviere PJ  | author3=Trojnar J  | display-authors=3  | last4=Junien  | first4=Jean-Louis  | last5=Akinsanya  | first5=Karen O. }}
*{{cite journal  | author=Qi SY, Riviere PJ, Trojnar J, ''et al.'' |title=Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases. |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 179-89 |year= 2003 |pmid= 12662155 |doi= 10.1042/BJ20021914 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Shu H |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line |journal=Mol. Cell. Proteomics |volume=3 |issue= 3 |pages= 279–86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200 |name-list-format=vanc| author2=Chen S  | author3=Bi Q  | display-authors=3  | last4=Mumby  | first4=M  | last5=Brekken  | first5=DL }}
*{{cite journal  | author=Shu H, Chen S, Bi Q, ''et al.'' |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. |journal=Mol. Cell Proteomics |volume=3 |issue= 3 |pages= 279-86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200 }}
*{{cite journal  | author=Chen YS |title=Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells |journal=Protein Expr. Purif. |volume=35 |issue= 1 |pages= 142–6 |year= 2004 |pmid= 15039077 |doi= 10.1016/j.pep.2003.12.019 |name-list-format=vanc| author2=Chien CH  | author3=Goparaju CM  | display-authors=3  | last4=Hsu  | first4=JT  | last5=Liang  | first5=PH  | last6=Chen  | first6=X }}
*{{cite journal  | author=Chen YS, Chien CH, Goparaju CM, ''et al.'' |title=Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells. |journal=Protein Expr. Purif. |volume=35 |issue= 1 |pages= 142-6 |year= 2004 |pmid= 15039077 |doi= 10.1016/j.pep.2003.12.019 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Jiaang WT |title=Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8 |journal=Bioorg. Med. Chem. Lett. |volume=15 |issue= 3 |pages= 687–91 |year= 2005 |pmid= 15664838 |doi= 10.1016/j.bmcl.2004.11.023 |name-list-format=vanc| author2=Chen YS  | author3=Hsu T  | display-authors=3  | last4=Wu  | first4=Ssu-Hui  | last5=Chien  | first5=Chia-Hui  | last6=Chang  | first6=Chung-Nien  | last7=Chang  | first7=Sheng-Ping  | last8=Lee  | first8=Shiow-Ju  | last9=Chen  | first9=Xin }}
*{{cite journal  | author=Jiaang WT, Chen YS, Hsu T, ''et al.'' |title=Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8. |journal=Bioorg. Med. Chem. Lett. |volume=15 |issue= 3 |pages= 687-91 |year= 2005 |pmid= 15664838 |doi= 10.1016/j.bmcl.2004.11.023 }}
*{{cite journal  | author=Ogasawara W |title=Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role of the signal sequence and overexpression in Escherichia coli |journal=Protein Expr. Purif. |volume=41 |issue= 2 |pages= 241–51 |year= 2005 |pmid= 15866709 |doi= 10.1016/j.pep.2004.10.027 |name-list-format=vanc| author2=Tanaka C  | author3=Suzuki M  | display-authors=3  | last4=Kobayashi  | first4=G  | last5=Ogawa  | first5=Y  | last6=Okada  | first6=H  | last7=Morikawa  | first7=Y }}
*{{cite journal  | author=Ogasawara W, Tanaka C, Suzuki M, ''et al.'' |title=Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role of the signal sequence and overexpression in Escherichia coli. |journal=Protein Expr. Purif. |volume=41 |issue= 2 |pages= 241-51 |year= 2005 |pmid= 15866709 |doi= 10.1016/j.pep.2004.10.027 }}
*{{cite journal  | author=Kimura K |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129  |name-list-format=vanc| author2=Wakamatsu A  | author3=Suzuki Y  | display-authors=3  | last4=Ota  | first4=T  | last5=Nishikawa  | first5=T  | last6=Yamashita  | first6=R  | last7=Yamamoto  | first7=J  | last8=Sekine  | first8=M  | last9=Tsuritani  | first9=K }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Yu DM |title=DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis |journal=Adv. Exp. Med. Biol. |volume=575 |issue=  |pages= 63–72 |year= 2006 |pmid= 16700509 |doi=10.1007/0-387-32824-6_7  |name-list-format=vanc| author2=Wang XM  | author3=Ajami K  | display-authors=3  | series=Advances in Experimental Medicine and Biology  | last4=McCaughan  | first4=Geoffrey W.  | last5=Gorrell  | first5=Mark D.  | isbn=978-0-387-29058-4 }}
*{{cite journal  | author=Yu DM, Wang XM, Ajami K, ''et al.'' |title=DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis. |journal=Adv. Exp. Med. Biol. |volume=575 |issue=  |pages= 63-72 |year= 2006 |pmid= 16700509 |doi=  }}
*{{cite journal  | vauthors=Yu DM, Wang XM, McCaughan GW, Gorrell MD |title=Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis |journal=FEBS J. |volume=273 |issue= 11 |pages= 2447–60 |year= 2006 |pmid= 16704418 |doi= 10.1111/j.1742-4658.2006.05253.x }}
*{{cite journal  | author=Yu DM, Wang XM, McCaughan GW, Gorrell MD |title=Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis. |journal=FEBS J. |volume=273 |issue= 11 |pages= 2447-60 |year= 2006 |pmid= 16704418 |doi= 10.1111/j.1742-4658.2006.05253.x }}
*{{cite journal  | author=Lee HJ |title=Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8 |journal=J. Biol. Chem. |volume=281 |issue= 50 |pages= 38653–62 |year= 2007 |pmid= 17040910 |doi= 10.1074/jbc.M603895200 |name-list-format=vanc| author2=Chen YS  | author3=Chou CY  | display-authors=3  | last4=Chien  | first4=C.-H.  | last5=Lin  | first5=C.-H.  | last6=Chang  | first6=G.-G.  | last7=Chen  | first7=X. }}
*{{cite journal  | author=Lee HJ, Chen YS, Chou CY, ''et al.'' |title=Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8. |journal=J. Biol. Chem. |volume=281 |issue= 50 |pages= 38653-62 |year= 2007 |pmid= 17040910 |doi= 10.1074/jbc.M603895200 }}
}}
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Latest revision as of 18:42, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8 gene.[1][2]

This gene encodes a member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.[2]

References

Notes
  1. Abbott CA, Yu DM, Woollatt E, Sutherland GR, McCaughan GW, Gorrell MD (Nov 2000). "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8". Eur J Biochem. 267 (20): 6140–50. doi:10.1046/j.1432-1327.2000.01617.x. PMID 11012666.
  2. 2.0 2.1 "Entrez Gene: DPP8 dipeptidyl-peptidase 8".
Further reading