Q86TI2 (DPP9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidyl peptidase 9
Short name=DP9
EC=3.4.14.5

Alternative name(s):
Dipeptidyl peptidase IV-related protein 2
Short name=DPRP-2
Dipeptidyl peptidase IX
Short name=DPP IX
Dipeptidyl peptidase-like protein 9
Short name=DPLP9

Gene names

Name:	DPP9
Synonyms:	DPRP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	863 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.
Catalytic activity	Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Ref.2 Ref.3 Ref.4
Enzyme regulation	Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate. Ref.2
Subunit structure	Homodimer. Ref.4
Subcellular location	Cytoplasm › cytosol Ref.2 Ref.3.
Tissue specificity	Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain. Ref.1 Ref.2 Ref.3
Sequence similarities	Belongs to the peptidase S9B family. DPPIV subfamily.
Biophysicochemical properties	Kinetic parameters: KM=161 µM for Ala-Pro-AMC Ref.2 Ref.3 KM=180 µM for Ala-Pro-AFC pH dependence: Optimum pH is 7.5-8.5. Little activity below pH 6.5.
Sequence caution	The sequence AAC33801.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAC62840.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAH37948.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAL47179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAO73880.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB70784.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC11362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC85150.1 differs from that shown. Reason: Probable cloning artifact. The sequence BAD18643.1 differs from that shown. Reason: Aberrant splicing. The sequence CAD39039.3 differs from that shown. Reason: Frameshift at positions 432 and 460.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86TI2-1)

Also known as: Short;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q86TI2-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKVKKLRLDKENTGSWRSFSLNSEGAERM

Note: Incomplete sequence.

Isoform 3 (identifier: Q86TI2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     832-858: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 863	863	Dipeptidyl peptidase 9		PRO_0000122415
Sites
	Active site	730	1	Charge relay system By similarity
	Active site	808	1	Charge relay system By similarity
	Active site	840	1	Charge relay system By similarity
Natural variations
	Alternative sequence	1	1	M → MRKVKKLRLDKENTGSWRSF SLNSEGAERM in isoform 2.		VSP_013865
	Alternative sequence	832 – 858	27	Missing in isoform 3.		VSP_013869
Experimental info
	Sequence conflict	204	1	I → N in AAO73880. Ref.3
	Sequence conflict	204	1	I → N in AAQ83119. Ref.3
	Sequence conflict	461	1	L → F in CAD39039. Ref.9
	Sequence conflict	571	1	C → W in BAC85150. Ref.5
	Sequence conflict	709	1	L → P in BAD18643. Ref.5
	Sequence conflict	753	1	G → C in BAB70784. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Short) [UniParc]. Last modified June 7, 2005. Version 3. Checksum: 40FE0B78E26CDED5	FASTA	863	98,263
	10 20 30 40 50 60 MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN KAPHDFQFVQ 70 80 90 100 110 120 KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL LLLSWKQMLD HFQATPHHGV 130 140 150 160 170 180 YSREEELLRE RKRLGVFGIT SYDFHSESGL FLFQASNSLF HCRDGGKNGF MVSPMKPLEI 190 200 210 220 230 240 KTQCSGPRMD PKICPADPAF FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG 250 260 270 280 290 300 VATFVIQEEF DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT 310 320 330 340 350 360 DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE YIARAGWTRD 370 380 390 400 410 420 GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA RAVPRNVQPY VVYEEVTNVW 430 440 450 460 470 480 INVHDIFYPF PQSEGEDELC FLRANECKTG FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK 490 500 510 520 530 540 CPIKEEIALT SGEWEVLARH GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR 550 560 570 580 590 600 LTTPGFSHSC SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS 610 620 630 640 650 660 CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ LVNNSFKGIK 670 680 690 700 710 720 YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV EIEDQVEGLQ FVAEKYGFID 730 740 750 760 770 780 LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA IAGAPVTVWM AYDTGYTERY MDVPENNQHG 790 800 810 820 830 840 YEAGSVALHV EKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH 850 860 SIRCPESGEH YEVTLLHFLQ EYL
	Isoform 2 (Long) [UniParc]. Checksum: 2CDB8E40E428AE73	FASTA	892	101,669
	10 20 30 40 50 60 MRKVKKLRLD KENTGSWRSF SLNSEGAERM ATTGTPTADR GDAAATDDPA ARFQVQKHSW 70 80 90 100 110 120 DGLRSIIHGS RKYSGLIVNK APHDFQFVQK TDESGPHSHR LYYLGMPYGS RENSLLYSEI 130 140 150 160 170 180 PKKVRKEALL LLSWKQMLDH FQATPHHGVY SREEELLRER KRLGVFGITS YDFHSESGLF 190 200 210 220 230 240 LFQASNSLFH CRDGGKNGFM VSPMKPLEIK TQCSGPRMDP KICPADPAFF SFINNSDLWV 250 260 270 280 290 300 ANIETGEERR LTFCHQGLSN VLDDPKSAGV ATFVIQEEFD RFTGYWWCPT ASWEGSEGLK 310 320 330 340 350 360 TLRILYEEVD ESEVEVIHVP SPALEERKTD SYRYPRTGSK NPKIALKLAE FQTDSQGKIV 370 380 390 400 410 420 STQEKELVQP FSSLFPKVEY IARAGWTRDG KYAWAMFLDR PQQWLQLVLL PPALFIPSTE 430 440 450 460 470 480 NEEQRLASAR AVPRNVQPYV VYEEVTNVWI NVHDIFYPFP QSEGEDELCF LRANECKTGF 490 500 510 520 530 540 CHLYKVTAVL KSQGYDWSEP FSPGEDEFKC PIKEEIALTS GEWEVLARHG SKIWVNEETK 550 560 570 580 590 600 LVYFQGTKDT PLEHHLYVVS YEAAGEIVRL TTPGFSHSCS MSQNFDMFVS HYSSVSTPPC 610 620 630 640 650 660 VHVYKLSGPD DDPLHKQPRF WASMMEAASC PPDYVPPEIF HFHTRSDVRL YGMIYKPHAL 670 680 690 700 710 720 QPGKKHPTVL FVYGGPQVQL VNNSFKGIKY LRLNTLASLG YAVVVIDGRG SCQRGLRFEG 730 740 750 760 770 780 ALKNQMGQVE IEDQVEGLQF VAEKYGFIDL SRVAIHGWSY GGFLSLMGLI HKPQVFKVAI 790 800 810 820 830 840 AGAPVTVWMA YDTGYTERYM DVPENNQHGY EAGSVALHVE KLPNEPNRLL ILHGFLDENV 850 860 870 880 890 HFFHTNFLVS QLIRAGKPYQ LQIYPNERHS IRCPESGEHY EVTLLHFLQE YL
	Isoform 3 [UniParc]. Checksum: EF3B224CF112B857	FASTA	836	95,013
	10 20 30 40 50 60 MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN KAPHDFQFVQ 70 80 90 100 110 120 KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL LLLSWKQMLD HFQATPHHGV 130 140 150 160 170 180 YSREEELLRE RKRLGVFGIT SYDFHSESGL FLFQASNSLF HCRDGGKNGF MVSPMKPLEI 190 200 210 220 230 240 KTQCSGPRMD PKICPADPAF FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG 250 260 270 280 290 300 VATFVIQEEF DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT 310 320 330 340 350 360 DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE YIARAGWTRD 370 380 390 400 410 420 GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA RAVPRNVQPY VVYEEVTNVW 430 440 450 460 470 480 INVHDIFYPF PQSEGEDELC FLRANECKTG FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK 490 500 510 520 530 540 CPIKEEIALT SGEWEVLARH GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR 550 560 570 580 590 600 LTTPGFSHSC SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS 610 620 630 640 650 660 CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ LVNNSFKGIK 670 680 690 700 710 720 YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV EIEDQVEGLQ FVAEKYGFID 730 740 750 760 770 780 LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA IAGAPVTVWM AYDTGYTERY MDVPENNQHG 790 800 810 820 830 YEAGSVALHV EKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQEYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV." Olsen C., Wagtmann N. Gene 299:185-193(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases." Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O. Biochem. J. 373:179-189(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Colon.
[3]	"Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity." Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D. Biochim. Biophys. Acta 1679:18-28(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[4]	"Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV." Bjelke J.R., Christensen J., Nielsen P.F., Branner S., Kanstrup A.B., Wagtmann N., Rasmussen H.B. Biochem. J. 396:391-399(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-649 (ISOFORMS 1/3). Tissue: Glial tumor, Ovary, Spleen and Trachea.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORM 2). Tissue: Placenta and Skin.
[9]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORMS 1/2). Tissue: Melanoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF452102 mRNA. Translation: AAL47179.1. Different initiation. AY172660 mRNA. Translation: AAO17262.1. AF542510 mRNA. Translation: AAO73880.2. Different initiation. AY374518 mRNA. Translation: AAQ83119.1. DQ417928 mRNA. Translation: ABD83624.1. AK054656 mRNA. Translation: BAB70784.1. Different initiation. AK075030 mRNA. Translation: BAC11362.1. Different initiation. AK122654 mRNA. Translation: BAG53644.1. AK131100 mRNA. Translation: BAC85150.1. Sequence problems. AK131499 mRNA. Translation: BAD18643.1. Sequence problems. AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems. AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems. CH471139 Genomic DNA. Translation: EAW69199.1. CH471139 Genomic DNA. Translation: EAW69201.1. BC000970 mRNA. Translation: AAH00970.1. BC037948 mRNA. Translation: AAH37948.1. Different initiation. AL834376 mRNA. Translation: CAD39039.3. Frameshift. CR627380 mRNA. Translation: CAH10477.1.
IPI	IPI00604483. IPI00604645. IPI00604694. IPI00604777. IPI01008830.
RefSeq	NP_631898.3. NM_139159.4.
UniGene	Hs.515081.
3D structure databases
ProteinModelPortal	Q86TI2.
ModBase	Search...
Protein family/group databases
MEROPS	S09.019.
PTM databases
PhosphoSite	Q86TI2.
Polymorphism databases
DMDM	67460390.
Proteomic databases
PaxDb	Q86TI2.
PRIDE	Q86TI2.
Protocols and materials databases
DNASU	91039.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262960; ENSP00000262960; ENSG00000142002. ENST00000594671; ENSP00000472224; ENSG00000142002. ENST00000598800; ENSP00000469603; ENSG00000142002.
GeneID	91039.
KEGG	hsa:91039.
Organism-specific databases
CTD	91039.
GeneCards	GC19M004626.
H-InvDB	HIX0027578.
HGNC	HGNC:18648. DPP9.
HPA	HPA036059.
MIM	608258. gene.
neXtProt	NX_Q86TI2.
PharmGKB	PA38620.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1506.
HOVERGEN	HBG061620.
InParanoid	Q86TI2.
KO	K08656.
OrthoDB	EOG4BVRSX.
Gene expression databases
ArrayExpress	Q86TI2.
Bgee	Q86TI2.
Genevestigator	Q86TI2.
GermOnline	ENSG00000142002. Homo sapiens.
Family and domain databases
InterPro	IPR001375. Peptidase_S9. IPR002469. Peptidase_S9B. [Graphical view]
Pfam	PF00930. DPPIV_N. 1 hit. PF00326. Peptidase_S9. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q86TI2.
ChEMBL	CHEMBL4793.
ChiTaRS	DPP9. human.
GenomeRNAi	91039.
NextBio	77078.
SOURCE	Search...

Entry information

Entry name

DPP9_HUMAN

Accession

Primary (citable) accession number: Q86TI2
Secondary accession number(s): O75273 , O75868, Q1ZZB8, Q6AI37, Q6UAL0, Q6ZMT2, Q6ZNJ5, Q8N2J7, Q8N3F5, Q8WXD8, Q96NT8, Q9BVR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.