HUMAN:DPP4

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	DPP4 (synonyms: ADCP2, CD26)
Protein Name(s)	Dipeptidyl peptidase 4 ADABP Adenosine deaminase complexing protein 2 ADCP-2 Dipeptidyl peptidase IV DPP IV T-cell activation antigen CD26 TP103 Dipeptidyl peptidase 4 membrane form Dipeptidyl peptidase IV membrane form Dipeptidyl peptidase 4 soluble form Dipeptidyl peptidase IV soluble form
External Links
UniProt	P27487
EMBL	X60708 M80536 M74777 U13735 U13710 U13711 U13712 U13713 U13714 U13715 U13716 U13717 U13718 U13719 U13720 U13721 U13722 U13723 U13724 U13725 U13726 U13727 U13728 U13729 U13730 U13731 U13732 U13733 U13734 AB451339 AB451488 AC008063 CH471058 BC013329 BC065265 S79876
CCDS	CCDS2216.1
PIR	S24313
RefSeq	NP_001926.2
UniGene	Hs.368912
PDB	1J2E 1N1M 1NU6 1NU8 1PFQ 1R9M 1R9N 1RWQ 1TK3 1TKR 1U8E 1W1I 1WCY 1X70 2AJL 2BGN 2BGR 2BUB 2FJP 2G5P 2G5T 2G63 2HHA 2I03 2I78 2IIT 2IIV 2JID 2OAG 2OGZ 2OLE 2ONC 2OPH 2OQI 2OQV 2P8S 2QJR 2QKY 2QOE 2QT9 2QTB 2RGU 2RIP 3BJM 3C43 3C45 3CCB 3CCC 3D4L 3EIO 3F8S 3G0B 3G0C 3G0D 3G0G 3H0C 3HAB 3HAC 3KWF 3KWJ 3NOX 3O95 3O9V 3OC0 3OPM 3Q0T 3Q8W 3QBJ 3SWW 3SX4 3VJK 3VJL 3VJM 3W2T 4A5S 4DSA 4DSZ 4DTC 4G1F 4J3J 4JH0 4KR0 4L72 4LKO 4N8D 4N8E 4PNZ 4QZV
PDBsum	1J2E 1N1M 1NU6 1NU8 1PFQ 1R9M 1R9N 1RWQ 1TK3 1TKR 1U8E 1W1I 1WCY 1X70 2AJL 2BGN 2BGR 2BUB 2FJP 2G5P 2G5T 2G63 2HHA 2I03 2I78 2IIT 2IIV 2JID 2OAG 2OGZ 2OLE 2ONC 2OPH 2OQI 2OQV 2P8S 2QJR 2QKY 2QOE 2QT9 2QTB 2RGU 2RIP 3BJM 3C43 3C45 3CCB 3CCC 3D4L 3EIO 3F8S 3G0B 3G0C 3G0D 3G0G 3H0C 3HAB 3HAC 3KWF 3KWJ 3NOX 3O95 3O9V 3OC0 3OPM 3Q0T 3Q8W 3QBJ 3SWW 3SX4 3VJK 3VJL 3VJM 3W2T 4A5S 4DSA 4DSZ 4DTC 4G1F 4J3J 4JH0 4KR0 4L72 4LKO 4N8D 4N8E 4PNZ 4QZV
ProteinModelPortal	P27487
SMR	P27487
BioGrid	108137
DIP	DIP-351N
IntAct	P27487
MINT	MINT-4998658
STRING	9606.ENSP00000353731
BindingDB	P27487
ChEMBL	CHEMBL2111469
DrugBank	DB06203 DB01076 DB08882 DB06655 DB06335 DB01261 DB04876
GuidetoPHARMACOLOGY	1612
MEROPS	S09.003
PhosphoSite	P27487
DMDM	1352311
MaxQB	P27487
PaxDb	P27487
PeptideAtlas	P27487
PRIDE	P27487
DNASU	1803
Ensembl	ENST00000360534
GeneID	1803
KEGG	hsa:1803
UCSC	uc002ubz.3
CTD	1803
GeneCards	GC02M162848
HGNC	HGNC:3009
HPA	CAB045970
MIM	102720
neXtProt	NX_P27487
PharmGKB	PA27467
eggNOG	COG1506
GeneTree	ENSGT00760000119233
HOGENOM	HOG000231875
HOVERGEN	HBG005527
InParanoid	P27487
KO	K01278
OMA	ETKFWYQ
OrthoDB	EOG761BT2
PhylomeDB	P27487
TreeFam	TF313309
BRENDA	3.4.14.5
Reactome	REACT_23824 REACT_24019
SABIO-RK	P27487
ChiTaRS	DPP4
EvolutionaryTrace	P27487
GeneWiki	Dipeptidyl_peptidase-4
GenomeRNAi	1803
NextBio	7345
PRO	PR:P27487
Proteomes	UP000005640
Bgee	P27487
CleanEx	HS_DPP4
ExpressionAtlas	P27487
Genevestigator	P27487
GO	GO:0016324 GO:0009986 GO:0030139 GO:0070062 GO:0005925 GO:0016021 GO:0046581 GO:0071438 GO:0030027 GO:0031258 GO:0005765 GO:0016020 GO:0045121 GO:0005886 GO:0008239 GO:0042802 GO:0002020 GO:0042803 GO:0005102 GO:0004252 GO:0008236 GO:0007155 GO:0043542 GO:0010716 GO:0008284 GO:0033632 GO:0001666 GO:0042110 GO:0031295
Gene3D	2.140.10.30 3.40.50.1820
InterPro	IPR029058 IPR002471 IPR001375 IPR002469
Pfam	PF00930 PF00326
SUPFAM	SSF53474
PROSITE	PS00708

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0001618	viral receptor activity	PMID:23486063^[1]	ECO:0000314			F		Figure 2 shows human coronavirus-Erasmus Medical Center (hCoV-EMC) tail spike binding to DPP4 which is the event needed for viral infection, Figure 3 shows DPP4 is present on hCoV-EMC succeptible cells and figure 4 confirms DDP4 is essential for the virus infection.	complete CACAO 6940
involved_in	GO:0006508	proteolysis	PMID:27198182^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:27198182^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001618	virus receptor activity	PMID:23486063^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:10593948^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:11487543^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0002563)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0071438	invadopodium membrane	PMID:16651416^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
	GO:0090024	negative regulation of neutrophil chemotaxis	PMID:23677473^[13]	ECO:0000315			P		Figure(3) shows that human neutrophils in a DPPIV gradient with a DPPIV inhibitor demonstrated significantly less chemorepellent activity than neutrophils in just a DPPIV gradient.	complete CACAO 13058
involved_in	GO:0043542	endothelial cell migration	PMID:16651416^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0045499	chemorepellent activity	PMID:23677473^[13]	ECO:0000314			F		Figures (2) show that human neutrophils in a DPPIV gradient with a DPPIV inhibitor demonstrated significantly less chemorepellent activity than neutrophils in just a DPPIV gradient.	complete CACAO 13059
enables	GO:0042803	protein homodimerization activity	PMID:14684150^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27487	F		Seeded From UniProt	complete
	GO:0045499	chemorepellent activity	PMID:23677473^[13]	ECO:0000315			F		Figure (3) shows that human neutrophils in a DPPIV gradient with a DPPIV inhibitor demonstrated significantly less chemorepellent activity than neutrophils in just a DPPIV gradient.	complete CACAO 13085
enables	GO:0042803	protein homodimerization activity	PMID:15448155^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27487	F		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	PMID:7594462^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033632	regulation of cell-cell adhesion mediated by integrin	PMID:11772392^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031295	T cell costimulation	PMID:10900005^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031295	T cell costimulation	PMID:17287217^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030139	endocytic vesicle	PMID:10900005^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	PMID:16651416^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	PMID:15052268^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010716	negative regulation of extracellular matrix disassembly	PMID:16651416^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:11772392^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:7594462^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:8101391^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:10900005^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:17549790^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:14684150^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:16651416^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:17549790^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	PMID:14684150^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16670267^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:17897319^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:10900005^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P11717	F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:16651416^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12884	F		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	PMID:16670267^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:8798518^[25]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:8100523^[26]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:15584901^[27]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22001206^[28]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27487	F		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0001618	P		Seeded From UniProt	complete
part_of	GO:0046581	intercellular canaliculus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28843 ensembl:ENSMUSP00000044050	C		Seeded From UniProt	complete
involved_in	GO:0036343	psychomotor behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28843 ensembl:ENSMUSP00000044050	P		Seeded From UniProt	complete
involved_in	GO:0035641	locomotory exploration behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28843 ensembl:ENSMUSP00000044050	P		Seeded From UniProt	complete
involved_in	GO:0001662	behavioral fear response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P28843 ensembl:ENSMUSP00000044050	P		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002471	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001375 InterPro:IPR002469 InterPro:IPR002471	P		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001375	F		Seeded From UniProt	complete
involved_in	GO:0050796	regulation of insulin secretion	Reactome:R-HSA-400508	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-9023633 Reactome:R-HSA-9023627	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-9023632 Reactome:R-HSA-9023626	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965 UniProtKB-SubCell:SL-0038	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0004177	aminopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0031	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	P		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0015	C		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0370	C		Seeded From UniProt	complete
part_of	GO:0071438	invadopodium membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0290	C		Seeded From UniProt	complete
part_of	GO:0031258	lamellipodium membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0292	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Raj, VS et al. (2013) Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495 251-4 PubMed GONUTS page
↑ ^2.0 ^2.1 Shiina, Y et al. (2016) Fly DPP10 acts as a channel ancillary subunit and possesses peptidase activity. Sci Rep 6 26290 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Park, JE et al. (1999) Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts. J. Biol. Chem. 274 36505-12 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 Ghersi, G et al. (2006) The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices. Cancer Res. 66 4652-61 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Herlihy, SE et al. (2013) Dipeptidyl peptidase IV is a human and murine neutrophil chemorepellent. J. Immunol. 190 6468-77 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Ludwig, K et al. (2004) 3D structure of the CD26-ADA complex obtained by cryo-EM and single particle analysis. Biochem. Biophys. Res. Commun. 313 223-9 PubMed GONUTS page
↑ Chien, CH et al. (2004) One site mutation disrupts dimer formation in human DPP-IV proteins. J. Biol. Chem. 279 52338-45 PubMed GONUTS page
↑ ^16.0 ^16.1 Martín, M et al. (1995) Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule. J. Immunol. 155 4630-43 PubMed GONUTS page
↑ ^17.0 ^17.1 Ginés, S et al. (2002) Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction. Biochem. J. 361 203-9 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Ikushima, H et al. (2000) Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation. Proc. Natl. Acad. Sci. U.S.A. 97 8439-44 PubMed GONUTS page
↑ Ohnuma, K et al. (2007) Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1. J. Biol. Chem. 282 10117-31 PubMed GONUTS page
↑ Gissen, P et al. (2004) Mutations in VPS33B, encoding a regulator of SNARE-dependent membrane fusion, cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome. Nat. Genet. 36 400-4 PubMed GONUTS page
↑ Kameoka, J et al. (1993) Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261 466-9 PubMed GONUTS page
↑ ^22.0 ^22.1 Davoodi, J et al. (2007) The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26. Proteomics 7 2300-10 PubMed GONUTS page
↑ ^23.0 ^23.1 Eltzschig, HK et al. (2006) Endothelial catabolism of extracellular adenosine during hypoxia: the role of surface adenosine deaminase and CD26. Blood 108 1602-10 PubMed GONUTS page
↑ Schröder, B et al. (2007) Integral and associated lysosomal membrane proteins. Traffic 8 1676-86 PubMed GONUTS page
↑ Pauly, RP et al. (1996) Investigation of glucose-dependent insulinotropic polypeptide-(1-42) and glucagon-like peptide-1-(7-36) degradation in vitro by dipeptidyl peptidase IV using matrix-assisted laser desorption/ionization-time of flight mass spectrometry. A novel kinetic approach. J. Biol. Chem. 271 23222-9 PubMed GONUTS page
↑ Mentlein, R et al. (1993) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. 214 829-35 PubMed GONUTS page
↑ Gorrell, MD (2005) Dipeptidyl peptidase IV and related enzymes in cell biology and liver disorders. Clin. Sci. 108 277-92 PubMed GONUTS page
↑ Tang, HK et al. (2011) Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9. FEBS Lett. 585 3409-14 PubMed GONUTS page

[PMID:23486063-1] 1.0 ^1.1 Raj, VS et al. (2013) Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495 251-4 PubMed GONUTS page

[PMID:27198182-2] 2.0 ^2.1 Shiina, Y et al. (2016) Fly DPP10 acts as a channel ancillary subunit and possesses peptidase activity. Sci Rep 6 26290 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:21423176-4] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:10593948-5] Park, JE et al. (1999) Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts. J. Biol. Chem. 274 36505-12 PubMed GONUTS page

[PMID:19946888-6] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19199708-7] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

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[PMID:16651416-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 Ghersi, G et al. (2006) The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices. Cancer Res. 66 4652-61 PubMed GONUTS page

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