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Q9UHL4 (DPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidyl peptidase 2

EC=3.4.14.2
Alternative name(s):
Dipeptidyl aminopeptidase II
Dipeptidyl peptidase 7
Dipeptidyl peptidase II
Short name=DPP II
Quiescent cell proline dipeptidase
Gene names
Name:DPP7
Synonyms:DPP2, QPP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the degradation of some oligopeptides. Ref.8

Catalytic activity

Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides. Ref.8

Subunit structure

Homodimer. Ref.8

Subcellular location

Lysosome. Cytoplasmic vesicle. Secreted Ref.8.

Tissue specificity

Detected in seminal plasma (at protein level). Ref.8

Post-translational modification

N-glycosylated. Ref.8

Sequence similarities

Belongs to the peptidase S28 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 254 Potential
PRO_0000027314
Chain26 – 492467Dipeptidyl peptidase 2
PRO_0000027315

Sites

Active site1621Charge relay system Potential
Active site4181Charge relay system Potential
Active site4431Charge relay system Potential

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Ref.6
Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Ref.6
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential

Natural variations

Natural variant891A → G. Ref.1 Ref.4
Corresponds to variant rs10747049 [ dbSNP | Ensembl ].
VAR_047087

Experimental info

Sequence conflict711I → T in AAF12747. Ref.1

Secondary structure

........................................................................ 492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UHL4 [UniParc].

Last modified November 4, 2008. Version 3.
Checksum: 6C3EDECA90FA7583

FASTA49254,341
        10         20         30         40         50         60 
MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN KTFPQRFLVS 

        70         80         90        100        110        120 
DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA LLVFAEHRYY GKSLPFGAQS 

       130        140        150        160        170        180 
TQRGHTELLT VEQALADFAE LLRALRRDLG AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA 

       190        200        210        220        230        240 
GALAASAPVL AVAGLGDSNQ FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR 

       250        260        270        280        290        300 
WEFGTCQPLS DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA 

       310        320        330        340        350        360 
QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ ACTEINLTFA 

       370        380        390        400        410        420 
SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW GGDLRAASNI IFSNGNLDPW 

       430        440        450        460        470        480 
AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS HPEDPASVVE ARKLEATIIG EWVKAARREQ 

       490 
QPALRGGPRL SL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase."
Underwood R., Chiravuri M., Lee H., Schmitz T., Kabcenell A.K., Yardley Y., Huber B.T.
J. Biol. Chem. 274:34053-34058(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-89.
[2]"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].
Tissue: Synovial cell.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT GLY-89.
Tissue: Brain.
[5]"Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase."
Chiravuri M., Agarraberes F., Mathieu S.L., Lee H., Huber B.T.
J. Immunol. 165:5695-5702(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-315.
Tissue: Liver.
[7]"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].
[8]"Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)."
Maes M.B., Lambeir A.M., Gilany K., Senten K., Van der Veken P., Leiting B., Augustyns K., Scharpe S., De Meester I.
Biochem. J. 386:315-324(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 28-492, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF154502 mRNA. Translation: AAF12747.1.
AK292112 mRNA. Translation: BAF84801.1.
AL929554 Genomic DNA. Translation: CAH72872.1.
BC011907 mRNA. Translation: AAH11907.1.
BC016961 mRNA. Translation: AAH16961.1.
PIRS77568.
RefSeqNP_037511.2. NM_013379.2.
UniGeneHs.37916.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYHX-ray2.19A/B/C/D28-492[»]
3N0TX-ray2.45A/B/C/D28-492[»]
4EBBX-ray2.00A/B27-492[»]
ProteinModelPortalQ9UHL4.
SMRQ9UHL4. Positions 28-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118989. 10 interactions.
IntActQ9UHL4. 8 interactions.
STRING9606.ENSP00000360635.

Chemistry

BindingDBQ9UHL4.
ChEMBLCHEMBL2111469.
GuidetoPHARMACOLOGY1605.

Protein family/group databases

MEROPSS28.002.

PTM databases

PhosphoSiteQ9UHL4.

Polymorphism databases

DMDM212276510.

Proteomic databases

PaxDbQ9UHL4.
PRIDEQ9UHL4.

Protocols and materials databases

DNASU29952.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371579; ENSP00000360635; ENSG00000176978.
GeneID29952.
KEGGhsa:29952.
UCSCuc004clh.3. human.

Organism-specific databases

CTD29952.
GeneCardsGC09M140004.
H-InvDBHIX0017204.
HIX0025819.
HGNCHGNC:14892. DPP7.
HPACAB025541.
HPA021282.
MIM610537. gene.
neXtProtNX_Q9UHL4.
PharmGKBPA27469.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290141.
HOGENOMHOG000238311.
HOVERGENHBG005526.
InParanoidQ9UHL4.
KOK01276.
OMAVWPRPDW.
OrthoDBEOG78WKRN.
PhylomeDBQ9UHL4.
TreeFamTF314414.

Gene expression databases

BgeeQ9UHL4.
CleanExHS_DPP7.
GenevestigatorQ9UHL4.

Family and domain databases

InterProIPR008758. Peptidase_S28.
[Graphical view]
PANTHERPTHR11010. PTHR11010. 1 hit.
PfamPF05577. Peptidase_S28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UHL4.
GeneWikiDPP7.
GenomeRNAi29952.
NextBio52649.
PROQ9UHL4.
SOURCESearch...

Entry information

Entry nameDPP2_HUMAN
AccessionPrimary (citable) accession number: Q9UHL4
Secondary accession number(s): A8K7U7, Q5VSF1, Q969X4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 123 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM