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Q9UHL4

- DPP2_HUMAN

UniProt

Q9UHL4 - DPP2_HUMAN

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Protein

Dipeptidyl peptidase 2

Gene
DPP7, DPP2, QPP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an important role in the degradation of some oligopeptides.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.1 Publication

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Charge relay system Reviewed prediction
Active sitei418 – 4181Charge relay system Reviewed prediction
Active sitei443 – 4431Charge relay system Reviewed prediction

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. dipeptidyl-peptidase activity Source: Ensembl
  3. serine-type peptidase activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS28.002.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DPP7
Synonyms:DPP2, QPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:14892. DPP7.

Subcellular locationi

Lysosome. Cytoplasmic vesicle. Secreted 1 Publication

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed predictionAdd
BLAST
Propeptidei22 – 254 Reviewed predictionPRO_0000027314
Chaini26 – 492467Dipeptidyl peptidase 2PRO_0000027315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)1 Publication
Glycosylationi86 – 861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi315 – 3151N-linked (GlcNAc...)1 Publication
Glycosylationi356 – 3561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi363 – 3631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi428 – 4281N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9UHL4.
PaxDbiQ9UHL4.
PRIDEiQ9UHL4.

PTM databases

PhosphoSiteiQ9UHL4.

Expressioni

Tissue specificityi

Detected in seminal plasma (at protein level).1 Publication

Gene expression databases

BgeeiQ9UHL4.
CleanExiHS_DPP7.
GenevestigatoriQ9UHL4.

Organism-specific databases

HPAiCAB025541.
HPA021282.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi118989. 10 interactions.
IntActiQ9UHL4. 8 interactions.
STRINGi9606.ENSP00000360635.

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 409
Turni47 – 504
Beta strandi52 – 609
Turni66 – 683
Beta strandi71 – 755
Helixi81 – 877
Helixi89 – 9810
Beta strandi101 – 1055
Helixi117 – 1215
Helixi131 – 14818
Beta strandi156 – 1616
Helixi163 – 17412
Turni176 – 1783
Beta strandi180 – 1856
Helixi191 – 1933
Helixi200 – 21011
Helixi214 – 23320
Helixi236 – 2438
Beta strandi245 – 2473
Helixi252 – 27120
Beta strandi278 – 2847
Helixi288 – 29710
Helixi302 – 31413
Beta strandi316 – 3183
Beta strandi321 – 3233
Helixi325 – 3284
Helixi342 – 35110
Turni352 – 3543
Beta strandi363 – 3686
Helixi375 – 38612
Helixi394 – 3996
Beta strandi409 – 4157
Helixi421 – 4233
Beta strandi430 – 4389
Helixi445 – 4473
Helixi456 – 47621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYHX-ray2.19A/B/C/D28-492[»]
3N0TX-ray2.45A/B/C/D28-492[»]
4EBBX-ray2.00A/B27-492[»]
ProteinModelPortaliQ9UHL4.
SMRiQ9UHL4. Positions 28-477.

Miscellaneous databases

EvolutionaryTraceiQ9UHL4.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S28 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290141.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
InParanoidiQ9UHL4.
KOiK01276.
OMAiVWPRPDW.
OrthoDBiEOG78WKRN.
PhylomeDBiQ9UHL4.
TreeFamiTF314414.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UHL4-1 [UniParc]FASTAAdd to Basket

« Hide

MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN    50
KTFPQRFLVS DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA 100
LLVFAEHRYY GKSLPFGAQS TQRGHTELLT VEQALADFAE LLRALRRDLG 150
AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA GALAASAPVL AVAGLGDSNQ 200
FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR WEFGTCQPLS 250
DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA 300
QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ 350
ACTEINLTFA SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW 400
GGDLRAASNI IFSNGNLDPW AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS 450
HPEDPASVVE ARKLEATIIG EWVKAARREQ QPALRGGPRL SL 492
Length:492
Mass (Da):54,341
Last modified:November 4, 2008 - v3
Checksum:i6C3EDECA90FA7583
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891A → G.2 Publications
Corresponds to variant rs10747049 [ dbSNP | Ensembl ].
VAR_047087

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711I → T in AAF12747. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7030.1.
PIRiS77568.
RefSeqiNP_037511.2. NM_013379.2.
UniGeneiHs.37916.

Genome annotation databases

EnsembliENST00000371579; ENSP00000360635; ENSG00000176978.
GeneIDi29952.
KEGGihsa:29952.
UCSCiuc004clh.3. human.

Polymorphism databases

DMDMi212276510.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS7030.1.
PIRi S77568.
RefSeqi NP_037511.2. NM_013379.2.
UniGenei Hs.37916.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JYH X-ray 2.19 A/B/C/D 28-492 [» ]
3N0T X-ray 2.45 A/B/C/D 28-492 [» ]
4EBB X-ray 2.00 A/B 27-492 [» ]
ProteinModelPortali Q9UHL4.
SMRi Q9UHL4. Positions 28-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118989. 10 interactions.
IntActi Q9UHL4. 8 interactions.
STRINGi 9606.ENSP00000360635.

Chemistry

BindingDBi Q9UHL4.
ChEMBLi CHEMBL3976.
GuidetoPHARMACOLOGYi 1605.

Protein family/group databases

MEROPSi S28.002.

PTM databases

PhosphoSitei Q9UHL4.

Polymorphism databases

DMDMi 212276510.

Proteomic databases

MaxQBi Q9UHL4.
PaxDbi Q9UHL4.
PRIDEi Q9UHL4.

Protocols and materials databases

DNASUi 29952.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371579 ; ENSP00000360635 ; ENSG00000176978 .
GeneIDi 29952.
KEGGi hsa:29952.
UCSCi uc004clh.3. human.

Organism-specific databases

CTDi 29952.
GeneCardsi GC09M140004.
H-InvDB HIX0017204.
HIX0025819.
HGNCi HGNC:14892. DPP7.
HPAi CAB025541.
HPA021282.
MIMi 610537. gene.
neXtProti NX_Q9UHL4.
PharmGKBi PA27469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290141.
HOGENOMi HOG000238311.
HOVERGENi HBG005526.
InParanoidi Q9UHL4.
KOi K01276.
OMAi VWPRPDW.
OrthoDBi EOG78WKRN.
PhylomeDBi Q9UHL4.
TreeFami TF314414.

Miscellaneous databases

EvolutionaryTracei Q9UHL4.
GeneWikii DPP7.
GenomeRNAii 29952.
NextBioi 52649.
PROi Q9UHL4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHL4.
CleanExi HS_DPP7.
Genevestigatori Q9UHL4.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view ]
PANTHERi PTHR11010. PTHR11010. 1 hit.
Pfami PF05577. Peptidase_S28. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiDPP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHL4
Secondary accession number(s): A8K7U7, Q5VSF1, Q969X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 4, 2008
Last modified: September 3, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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