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Q9NY33

- DPP3_HUMAN

UniProt

Q9NY33 - DPP3_HUMAN

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Protein

Dipeptidyl peptidase 3

Gene

DPP3

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

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

Zn2+1 PublicationNote: 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. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9NY33.
CleanExiHS_DPP3.
ExpressionAtlasiQ9NY33. baseline and differential.
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 – 63Combined sources
Beta strandi14 – 163Combined sources
Helixi20 – 245Combined sources
Helixi28 – 4518Combined sources
Helixi47 – 504Combined sources
Helixi56 – 6914Combined sources
Helixi72 – 8110Combined sources
Helixi86 – 10217Combined sources
Beta strandi104 – 1063Combined sources
Turni108 – 1103Combined sources
Helixi120 – 12910Combined sources
Helixi131 – 1355Combined sources
Helixi137 – 15216Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1613Combined sources
Helixi164 – 1663Combined sources
Beta strandi170 – 1723Combined sources
Helixi178 – 19013Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi222 – 2243Combined sources
Helixi231 – 2333Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi242 – 2509Combined sources
Helixi252 – 26615Combined sources
Helixi272 – 28716Combined sources
Helixi290 – 30213Combined sources
Beta strandi307 – 31610Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi327 – 3348Combined sources
Helixi337 – 34812Combined sources
Helixi350 – 3556Combined sources
Beta strandi357 – 3593Combined sources
Helixi361 – 3633Combined sources
Beta strandi375 – 38410Combined sources
Beta strandi388 – 3925Combined sources
Helixi396 – 4016Combined sources
Beta strandi405 – 4095Combined sources
Helixi410 – 4134Combined sources
Helixi421 – 4233Combined sources
Helixi429 – 45224Combined sources
Turni453 – 4564Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi469 – 4713Combined sources
Turni473 – 4753Combined sources
Turni479 – 4813Combined sources
Beta strandi482 – 4843Combined sources
Helixi495 – 4984Combined sources
Turni500 – 5023Combined sources
Helixi503 – 51816Combined sources
Helixi522 – 5287Combined sources
Helixi532 – 55221Combined sources
Helixi553 – 5564Combined sources
Helixi559 – 5613Combined sources
Beta strandi563 – 5653Combined sources
Helixi567 – 58115Combined sources
Beta strandi586 – 5938Combined sources
Beta strandi597 – 6059Combined sources
Helixi607 – 6093Combined sources
Turni610 – 6134Combined sources
Helixi614 – 63017Combined sources
Helixi634 – 64411Combined sources
Turni651 – 6533Combined sources
Helixi655 – 66410Combined sources
Beta strandi671 – 6733Combined sources
Beta strandi676 – 6805Combined sources
Beta strandi683 – 6875Combined sources
Helixi693 – 7019Combined sources
Turni705 – 7073Combined sources
Helixi708 – 72215Combined sources
Helixi723 – 7253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00390000007335.
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

        10         20         30         40         50
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL
60 70 80 90 100
QTSPEAPYIY ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY
110 120 130 140 150
SNMGNYKSFG DTKFVPNLPK EKLERVILGS EAAQQHPEEV RGLWQTCGEL
160 170 180 190 200
MFSLEPRLRH LGLGKEGITT YFSGNCTMED AKLAQDFLDS QNLSAYNTRL
210 220 230 240 250
FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR GSPFQVTRGD
260 270 280 290 300
YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW
310 320 330 340 350
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA
360 370 380 390 400
EQLLKELPWP PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ
410 420 430 440 450
TEGFKNVSLG NVLAVAYATQ REKLTFLEED DKDLYILWKG PSFDVQVGLH
460 470 480 490 500
ELLGHGSGKL FVQDEKGAFN FDQETVINPE TGEQIQSWYR SGETWDSKFS
510 520 530 540 550
TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY VNWLNMVRAG
560 570 580 590 600
LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD
610 620 630 640 650
ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA
660 670 680 690 700
PPECFLTLRD TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF
710 720 730
SERFPEDGPE LEEILTQLAT ADARFWKGPS EAPSGQA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

GeneTreei ENSGT00390000007335.
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

Bgeei Q9NY33.
CleanExi HS_DPP3.
ExpressionAtlasi Q9NY33. baseline and differential.
Genevestigatori Q9NY33.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 143 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