Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NY33

- DPP3_HUMAN

UniProt

Q9NY33 - DPP3_HUMAN

Protein

Dipeptidyl peptidase 3

Gene

DPP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cleaves and degrades of the opioid peptide enkephalin. Also cleaves Arg-Arg-beta-naphthylamide.1 Publication

    Catalytic activityi

    Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Enzyme regulationi

    Inhibited by spinorphin, an opioid peptide derived from hemoglobin.1 Publication

    pH dependencei

    Optimum pH is 8.8.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi450 – 4501Zinc; catalytic
    Active sitei451 – 4511By similarity
    Metal bindingi455 – 4551Zinc; catalytic
    Metal bindingi508 – 5081Zinc; catalytic

    GO - Molecular functioni

    1. dipeptidyl-peptidase activity Source: UniProtKB
    2. metallopeptidase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM49.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 3 (EC:3.4.14.4)
    Alternative name(s):
    Dipeptidyl aminopeptidase III
    Dipeptidyl arylamidase III
    Dipeptidyl peptidase III
    Short name:
    DPP III
    Enkephalinase B
    Gene namesi
    Name:DPP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3008. DPP3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: HPA
    4. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27466.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 737736Dipeptidyl peptidase 3PRO_0000078238Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NY33.
    PeptideAtlasiQ9NY33.
    PRIDEiQ9NY33.

    PTM databases

    PhosphoSiteiQ9NY33.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NY33.
    BgeeiQ9NY33.
    CleanExiHS_DPP3.
    GenevestigatoriQ9NY33.

    Organism-specific databases

    HPAiHPA035780.
    HPA035781.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KEAP1Q141452EBI-718333,EBI-751001

    Protein-protein interaction databases

    BioGridi115383. 20 interactions.
    DIPiDIP-53793N.
    IntActiQ9NY33. 4 interactions.

    Structurei

    Secondary structure

    1
    737
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi14 – 163
    Helixi20 – 245
    Helixi28 – 4518
    Helixi47 – 504
    Helixi56 – 6914
    Helixi72 – 8110
    Helixi86 – 10217
    Beta strandi104 – 1063
    Turni108 – 1103
    Helixi120 – 12910
    Helixi131 – 1355
    Helixi137 – 15216
    Helixi156 – 1583
    Beta strandi159 – 1613
    Helixi164 – 1663
    Beta strandi170 – 1723
    Helixi178 – 19013
    Beta strandi198 – 2047
    Beta strandi206 – 2083
    Beta strandi210 – 2178
    Beta strandi222 – 2243
    Helixi231 – 2333
    Beta strandi235 – 2395
    Beta strandi242 – 2509
    Helixi252 – 26615
    Helixi272 – 28716
    Helixi290 – 30213
    Beta strandi307 – 31610
    Beta strandi318 – 3203
    Beta strandi321 – 3233
    Beta strandi327 – 3348
    Helixi337 – 34812
    Helixi350 – 3556
    Beta strandi357 – 3593
    Helixi361 – 3633
    Beta strandi375 – 38410
    Beta strandi388 – 3925
    Helixi396 – 4016
    Beta strandi405 – 4095
    Helixi410 – 4134
    Helixi421 – 4233
    Helixi429 – 45224
    Turni453 – 4564
    Beta strandi465 – 4673
    Beta strandi469 – 4713
    Turni473 – 4753
    Turni479 – 4813
    Beta strandi482 – 4843
    Helixi495 – 4984
    Turni500 – 5023
    Helixi503 – 51816
    Helixi522 – 5287
    Helixi532 – 55221
    Helixi553 – 5564
    Helixi559 – 5613
    Beta strandi563 – 5653
    Helixi567 – 58115
    Beta strandi586 – 5938
    Beta strandi597 – 6059
    Helixi607 – 6093
    Turni610 – 6134
    Helixi614 – 63017
    Helixi634 – 64411
    Turni651 – 6533
    Helixi655 – 66410
    Beta strandi671 – 6733
    Beta strandi676 – 6805
    Beta strandi683 – 6875
    Helixi693 – 7019
    Turni705 – 7073
    Helixi708 – 72215
    Helixi723 – 7253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FVYX-ray1.90A1-726[»]
    3T6BX-ray2.40A/B1-726[»]
    3T6JX-ray2.98A1-726[»]
    ProteinModelPortaliQ9NY33.
    SMRiQ9NY33. Positions 3-726.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NY33.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M49 family.Curated

    Phylogenomic databases

    HOGENOMiHOG000187784.
    HOVERGENiHBG025680.
    InParanoidiQ9NY33.
    KOiK01277.
    PhylomeDBiQ9NY33.
    TreeFamiTF300598.

    Family and domain databases

    InterProiIPR005317. Dipeptidyl-peptase3.
    [Graphical view]
    PIRSFiPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NY33-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL    50
    QTSPEAPYIY ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY 100
    SNMGNYKSFG DTKFVPNLPK EKLERVILGS EAAQQHPEEV RGLWQTCGEL 150
    MFSLEPRLRH LGLGKEGITT YFSGNCTMED AKLAQDFLDS QNLSAYNTRL 200
    FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR GSPFQVTRGD 250
    YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW 300
    IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA 350
    EQLLKELPWP PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ 400
    TEGFKNVSLG NVLAVAYATQ REKLTFLEED DKDLYILWKG PSFDVQVGLH 450
    ELLGHGSGKL FVQDEKGAFN FDQETVINPE TGEQIQSWYR SGETWDSKFS 500
    TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY VNWLNMVRAG 550
    LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD 600
    ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA 650
    PPECFLTLRD TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF 700
    SERFPEDGPE LEEILTQLAT ADARFWKGPS EAPSGQA 737
    Length:737
    Mass (Da):82,589
    Last modified:May 10, 2002 - v2
    Checksum:iE2BB1923C9CAFDEC
    GO
    Isoform 2 (identifier: Q9NY33-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         182-601: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:317
    Mass (Da):35,489
    Checksum:iA172153E757C72E5
    GO
    Isoform 3 (identifier: Q8NFJ9-2) [UniParc]FASTAAdd to Basket

    Also known as: DPP3-BBS1

    The sequence of this isoform can be found in the external entry Q8NFJ9.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Based on a readthrough transcript which may produce a DPP3-BBS1 fusion protein. No experimental confirmation available.

    Length:630
    Mass (Da):69,658
    GO
    Isoform 4 (identifier: Q9NY33-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         91-120: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:707
    Mass (Da):79,307
    Checksum:i52EAAAFC59AB9AFA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti224 – 2241P → S in BAG59686. (PubMed:14702039)Curated
    Sequence conflicti417 – 4193YAT → TA in BAA75785. (PubMed:9425109)Curated
    Sequence conflicti697 – 6971I → Y in BAA75785. (PubMed:9425109)Curated

    Mass spectrometryi

    Isoform 1 : Molecular mass is 82500±60 Da from positions 1 - 737. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761R → H.1 Publication
    Corresponds to variant rs11826683 [ dbSNP | Ensembl ].
    VAR_033494
    Natural varianti145 – 1451Q → H.1 Publication
    Corresponds to variant rs11550299 [ dbSNP | Ensembl ].
    VAR_033495
    Natural varianti678 – 6781R → H.2 Publications
    Corresponds to variant rs2305535 [ dbSNP | Ensembl ].
    VAR_021850
    Natural varianti690 – 6901E → K.
    Corresponds to variant rs12421620 [ dbSNP | Ensembl ].
    VAR_051597

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei91 – 12030Missing in isoform 4. 1 PublicationVSP_044696Add
    BLAST
    Alternative sequencei182 – 601420Missing in isoform 2. 1 PublicationVSP_005510Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271216 mRNA. Translation: CAB72433.1.
    AK021449 mRNA. Translation: BAB13828.1.
    AK297199 mRNA. Translation: BAG59686.1.
    AK315478 mRNA. Translation: BAG37862.1.
    AP002748 Genomic DNA. No translation available.
    BC001446 mRNA. Translation: AAH01446.1.
    BC007221 mRNA. Translation: AAH07221.1.
    BC014038 mRNA. Translation: AAH14038.1.
    BC024271 mRNA. Translation: AAH24271.1.
    AB017970 mRNA. Translation: BAA75785.1.
    CCDSiCCDS58147.1. [Q9NY33-4]
    CCDS8141.1. [Q9NY33-1]
    RefSeqiNP_001243599.1. NM_001256670.1. [Q9NY33-4]
    NP_005691.2. NM_005700.4. [Q9NY33-1]
    NP_569710.2. NM_130443.3. [Q9NY33-1]
    UniGeneiHs.502914.
    Hs.740670.

    Genome annotation databases

    EnsembliENST00000360510; ENSP00000353701; ENSG00000254986. [Q9NY33-1]
    ENST00000530165; ENSP00000436941; ENSG00000254986. [Q9NY33-4]
    ENST00000541961; ENSP00000440502; ENSG00000254986. [Q9NY33-1]
    GeneIDi10072.
    KEGGihsa:10072.
    UCSCiuc001oif.2. human. [Q9NY33-1]

    Polymorphism databases

    DMDMi20532389.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271216 mRNA. Translation: CAB72433.1 .
    AK021449 mRNA. Translation: BAB13828.1 .
    AK297199 mRNA. Translation: BAG59686.1 .
    AK315478 mRNA. Translation: BAG37862.1 .
    AP002748 Genomic DNA. No translation available.
    BC001446 mRNA. Translation: AAH01446.1 .
    BC007221 mRNA. Translation: AAH07221.1 .
    BC014038 mRNA. Translation: AAH14038.1 .
    BC024271 mRNA. Translation: AAH24271.1 .
    AB017970 mRNA. Translation: BAA75785.1 .
    CCDSi CCDS58147.1. [Q9NY33-4 ]
    CCDS8141.1. [Q9NY33-1 ]
    RefSeqi NP_001243599.1. NM_001256670.1. [Q9NY33-4 ]
    NP_005691.2. NM_005700.4. [Q9NY33-1 ]
    NP_569710.2. NM_130443.3. [Q9NY33-1 ]
    UniGenei Hs.502914.
    Hs.740670.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FVY X-ray 1.90 A 1-726 [» ]
    3T6B X-ray 2.40 A/B 1-726 [» ]
    3T6J X-ray 2.98 A 1-726 [» ]
    ProteinModelPortali Q9NY33.
    SMRi Q9NY33. Positions 3-726.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115383. 20 interactions.
    DIPi DIP-53793N.
    IntActi Q9NY33. 4 interactions.

    Chemistry

    BindingDBi Q9NY33.
    ChEMBLi CHEMBL4520.

    Protein family/group databases

    MEROPSi M49.001.

    PTM databases

    PhosphoSitei Q9NY33.

    Polymorphism databases

    DMDMi 20532389.

    Proteomic databases

    MaxQBi Q9NY33.
    PeptideAtlasi Q9NY33.
    PRIDEi Q9NY33.

    Protocols and materials databases

    DNASUi 10072.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360510 ; ENSP00000353701 ; ENSG00000254986 . [Q9NY33-1 ]
    ENST00000530165 ; ENSP00000436941 ; ENSG00000254986 . [Q9NY33-4 ]
    ENST00000541961 ; ENSP00000440502 ; ENSG00000254986 . [Q9NY33-1 ]
    GeneIDi 10072.
    KEGGi hsa:10072.
    UCSCi uc001oif.2. human. [Q9NY33-1 ]

    Organism-specific databases

    CTDi 10072.
    GeneCardsi GC11P066249.
    HGNCi HGNC:3008. DPP3.
    HPAi HPA035780.
    HPA035781.
    MIMi 606818. gene.
    neXtProti NX_Q9NY33.
    PharmGKBi PA27466.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000187784.
    HOVERGENi HBG025680.
    InParanoidi Q9NY33.
    KOi K01277.
    PhylomeDBi Q9NY33.
    TreeFami TF300598.

    Miscellaneous databases

    ChiTaRSi DPP3. human.
    EvolutionaryTracei Q9NY33.
    GeneWikii DPP3.
    GenomeRNAii 10072.
    NextBioi 38071.
    PROi Q9NY33.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NY33.
    Bgeei Q9NY33.
    CleanExi HS_DPP3.
    Genevestigatori Q9NY33.

    Family and domain databases

    InterProi IPR005317. Dipeptidyl-peptase3.
    [Graphical view ]
    PIRSFi PIRSF007828. Dipeptidyl-peptidase_III. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of human dipeptidyl-peptidase III."
      Chen J.M., Fortunato M., Barrett A.J.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS HIS-145 AND HIS-678.
    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] (ISOFORMS 1; 2 AND 4).
      Tissue: Brain and Embryo.
    3. 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] (ISOFORM 1), VARIANT HIS-76.
      Tissue: Colon, Kidney and Placenta.
    5. "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression."
      Fukasawa K., Fukusawa K.M., Kanai M., Fujii S., Hirose J., Harada M.
      Biochem. J. 329:275-282(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-723 (ISOFORM 1), CHARACTERIZATION, VARIANT HIS-678.
    6. "Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences."
      Abramic M., Schleuder D., Dolovcak L., Schroeder W., Strupat K., Sagi D., Peter-Katalini J., Vitale L.
      Biol. Chem. 381:1233-1243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
      Tissue: Erythrocyte.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III."
      Bezerra G.A., Dobrovetsky E., Viertlmayr R., Dong A., Binter A., Abramic M., Macheroux P., Dhe-Paganon S., Gruber K.
      Proc. Natl. Acad. Sci. U.S.A. 109:6525-6530(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-726 IN COMPLEX WITH OPIOID PEPTIDE, FUNCTION, ENZYME REGULATION, COFACTOR, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiDPP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NY33
    Secondary accession number(s): B2RDB5
    , B4DLX4, F5H8L6, O95748, Q969H2, Q9BV67, Q9HAL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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