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Q86TI2 (DPP9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytosol 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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7475352,EBI-7475352

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 863862Dipeptidyl peptidase 9
PRO_0000122415

Sites

Active site7301Charge relay system By similarity
Active site8081Charge relay system By similarity
Active site8401Charge relay system By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Alternative sequence11M → MRKVKKLRLDKENTGSWRSF SLNSEGAERM in isoform 2.
VSP_013865
Alternative sequence832 – 85827Missing in isoform 3.
VSP_013869

Experimental info

Sequence conflict2041I → N in AAO73880. Ref.3
Sequence conflict2041I → N in AAQ83119. Ref.3
Sequence conflict4611L → F in CAD39039. Ref.9
Sequence conflict5711C → W in BAC85150. Ref.5
Sequence conflict7091L → P in BAD18643. Ref.5
Sequence conflict7531G → C in BAB70784. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Short) [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: 40FE0B78E26CDED5

FASTA86398,263
        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 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: 2CDB8E40E428AE73
Show »

FASTA892101,669
Isoform 3 [UniParc].

Checksum: EF3B224CF112B857
Show »

FASTA83695,013

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"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.
CCDSCCDS45928.1. [Q86TI2-2]
RefSeqNP_631898.3. NM_139159.4. [Q86TI2-2]
XP_005259730.1. XM_005259673.2. [Q86TI2-2]
UniGeneHs.515081.

3D structure databases

ProteinModelPortalQ86TI2.
SMRQ86TI2. Positions 489-861.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124789. 15 interactions.
MINTMINT-4535936.

Chemistry

BindingDBQ86TI2.
ChEMBLCHEMBL4793.

Protein family/group databases

MEROPSS09.019.

PTM databases

PhosphoSiteQ86TI2.

Polymorphism databases

DMDM67460390.

Proteomic databases

MaxQBQ86TI2.
PaxDbQ86TI2.
PRIDEQ86TI2.

Protocols and materials databases

DNASU91039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
ENST00000598800; ENSP00000469603; ENSG00000142002. [Q86TI2-1]
GeneID91039.
KEGGhsa:91039.
UCSCuc002mba.3. human. [Q86TI2-2]

Organism-specific databases

CTD91039.
GeneCardsGC19M004675.
H-InvDBHIX0027578.
HGNCHGNC:18648. DPP9.
HPAHPA036059.
MIM608258. gene.
neXtProtNX_Q86TI2.
Orphanet2032. Idiopathic pulmonary fibrosis.
PharmGKBPA38620.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1506.
HOVERGENHBG061620.
InParanoidQ86TI2.
KOK08656.
OMAFPRVEYI.
OrthoDBEOG7XWPN8.
PhylomeDBQ86TI2.
TreeFamTF313309.

Enzyme and pathway databases

SABIO-RKQ86TI2.

Gene expression databases

ArrayExpressQ86TI2.
BgeeQ86TI2.
GenevestigatorQ86TI2.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDPP9. human.
GeneWikiDPP9.
GenomeRNAi91039.
NextBio77078.
PROQ86TI2.
SOURCESearch...

Entry information

Entry nameDPP9_HUMAN
AccessionPrimary (citable) accession number: Q86TI2
Secondary accession number(s): O75273 expand/collapse secondary AC list , 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: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM