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Q6V1X1

- DPP8_HUMAN

UniProt

Q6V1X1 - DPP8_HUMAN

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Protein
Dipeptidyl peptidase 8
Gene
DPP8, DPRP1, MSTP097, MSTP135, MSTP141
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. May play a role in T-cell activation and immune function.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.3 Publications

Enzyme regulationi

Inhibited by zinc. Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate. Specifically inhibited by isoindoline derivatives.3 Publications

Kineticsi

  1. KM=208 µM for Ala-Pro-AMC3 Publications
  2. KM=130 µM for Ala-Pro-AFC
  3. KM=120 µM for H-Ala-Pro-pNa
  4. KM=1420 µM for H-Ala-Ala-pNa
  5. KM=310 µM for H-Arg-Pro-pNa
  6. KM=2050 µM for H-Asp-Pro-pNa
  7. KM=480 µM for H-Gly-Pro-pNa

pH dependencei

Optimum pH is 7.4-8.5. Little activity below pH 6.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei755 – 7551Charge relay system Inferred
Active sitei833 – 8331Charge relay system Inferred
Active sitei865 – 8651Charge relay system Inferred

GO - Molecular functioni

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

GO - Biological processi

  1. immune response Source: UniProtKB
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

SABIO-RKQ6V1X1.

Protein family/group databases

MEROPSiS09.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 8 (EC:3.4.14.5)
Short name:
DP8
Alternative name(s):
Dipeptidyl peptidase IV-related protein 1
Short name:
DPRP-1
Dipeptidyl peptidase VIII
Short name:
DPP VIII
Prolyl dipeptidase DPP8
Gene namesi
Name:DPP8
Synonyms:DPRP1
ORF Names:MSTP097, MSTP135, MSTP141
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:16490. DPP8.

Subcellular locationi

Cytoplasm 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: InterPro
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi275 – 2751E → K: 13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location. 1 Publication
Mutagenesisi755 – 7551S → A: Abolishes activity; no effect on subcellular location. 1 Publication
Mutagenesisi833 – 8331D → A: Abolishes activity; no effect on subcellular location. 1 Publication
Mutagenesisi865 – 8651H → A: Abolishes activity; no effect on subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA27470.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Dipeptidyl peptidase 8
PRO_0000122413Add
BLAST

Proteomic databases

MaxQBiQ6V1X1.
PaxDbiQ6V1X1.
PRIDEiQ6V1X1.

PTM databases

PhosphoSiteiQ6V1X1.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testis, placenta, prostate, muscle and brain.2 Publications

Inductioni

In activated T-cells.3 Publications

Gene expression databases

ArrayExpressiQ6V1X1.
BgeeiQ6V1X1.
GenevestigatoriQ6V1X1.

Organism-specific databases

HPAiHPA008706.

Interactioni

Protein-protein interaction databases

BioGridi120226. 14 interactions.
IntActiQ6V1X1. 3 interactions.
MINTiMINT-4539721.

Structurei

3D structure databases

ProteinModelPortaliQ6V1X1.
SMRiQ6V1X1. Positions 136-886.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1506.
HOVERGENiHBG061620.
InParanoidiQ6V1X1.
KOiK08655.
OMAiSRHCDFF.
OrthoDBiEOG7XWPN8.
PhylomeDBiQ6V1X1.
TreeFamiTF313309.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6V1X1-1) [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

MWKRSEQMKI KSGKCNMAAA METEQLGVEI FETADCEENI ESQDRPKLEP    50
FYVERYSWSQ LKKLLADTRK YHGYMMAKAP HDFMFVKRND PDGPHSDRIY 100
YLAMSGENRE NTLFYSEIPK TINRAAVLML SWKPLLDLFQ ATLDYGMYSR 150
EEELLRERKR IGTVGIASYD YHQGSGTFLF QAGSGIYHVK DGGPQGFTQQ 200
PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSNDIWISN IVTREERRLT 250
YVHNELANME EDARSAGVAT FVLQEEFDRY SGYWWCPKAE TTPSGGKILR 300
ILYEENDESE VEIIHVTSPM LETRRADSFR YPKTGTANPK VTFKMSEIMI 350
DAEGRIIDVI DKELIQPFEI LFEGVEYIAR AGWTPEGKYA WSILLDRSQT 400
RLQIVLISPE LFIPVEDDVM ERQRLIESVP DSVTPLIIYE ETTDIWINIH 450
DIFHVFPQSH EEEIEFIFAS ECKTGFRHLY KITSILKESK YKRSSGGLPA 500
PSDFKCPIKE EIAITSGEWE VLGRHGSNIQ VDEVRRLVYF EGTKDSPLEH 550
HLYVVSYVNP GEVTRLTDRG YSHSCCISQH CDFFISKYSN QKNPHCVSLY 600
KLSSPEDDPT CKTKEFWATI LDSAGPLPDY TPPEIFSFES TTGFTLYGML 650
YKPHDLQPGK KYPTVLFIYG GPQVQLVNNR FKGVKYFRLN TLASLGYVVV 700
VIDNRGSCHR GLKFEGAFKY KMGQIEIDDQ VEGLQYLASR YDFIDLDRVG 750
IHGWSYGGYL SLMALMQRSD IFRVAIAGAP VTLWIFYDTG YTERYMGHPD 800
QNEQGYYLGS VAMQAEKFPS EPNRLLLLHG FLDENVHFAH TSILLSFLVR 850
AGKPYDLQIY PQERHSIRVP ESGEHYELHL LHYLQENLGS RIAALKVI 898
Length:898
Mass (Da):103,358
Last modified:July 5, 2004 - v1
Checksum:i60B0D036F026DE2A
GO
Isoform 2 (identifier: Q6V1X1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     723-773: Missing.

Show »
Length:847
Mass (Da):97,464
Checksum:iAB07EF0087231B56
GO
Isoform 3 (identifier: Q6V1X1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Show »
Length:882
Mass (Da):101,422
Checksum:iAD801C302DB4652B
GO
Isoform 4 (identifier: Q6V1X1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     674-773: Missing.

Show »
Length:782
Mass (Da):89,908
Checksum:i784922477DB8F5B5
GO
Isoform 5 (identifier: Q6V1X1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     674-722: Missing.

Show »
Length:849
Mass (Da):97,739
Checksum:i4B6C88F29CA55475
GO
Isoform 6 (identifier: Q6V1X1-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     358-530: Missing.

Show »
Length:725
Mass (Da):83,398
Checksum:i0476E0AEBD94131B
GO

Sequence cautioni

The sequence AAQ13623.1 differs from that shown. Reason: Frameshift at several positions.
The sequence AAQ13650.1 differs from that shown. Reason: Frameshift at several positions.
The sequence BAA91059.1 differs from that shown. Reason: Frameshift at position 486.
The sequence AAQ13657.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB55395.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform 3 and isoform 4.
VSP_013860Add
BLAST
Alternative sequencei358 – 530173Missing in isoform 6.
VSP_013861Add
BLAST
Alternative sequencei674 – 773100Missing in isoform 4.
VSP_013862Add
BLAST
Alternative sequencei674 – 72249Missing in isoform 5.
VSP_013863Add
BLAST
Alternative sequencei723 – 77351Missing in isoform 2.
VSP_013864Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331S → G in BC040203. 1 Publication
Sequence conflicti570 – 5701G → S in BAB55395. 1 Publication
Sequence conflicti673 – 6731Q → K in AAQ13650. 1 Publication
Sequence conflicti686 – 6861Y → F in AAQ13650. 1 Publication
Sequence conflicti693 – 6942AS → PF in AAQ13650. 1 Publication
Sequence conflicti701 – 7011V → G in AAQ13650. 1 Publication
Sequence conflicti709 – 7091H → P in AAQ13650. 1 Publication
Sequence conflicti720 – 7201Y → F in AAQ13650. 1 Publication
Sequence conflicti799 – 8035PDQNE → LTRMN in AAQ13623. 1 Publication
Sequence conflicti820 – 8201S → F in AAQ13623. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF221634 mRNA. Translation: AAG29766.1.
AF221635 mRNA. Translation: AAG29767.1.
AF221636 mRNA. Translation: AAG29768.1.
AF221637 mRNA. Translation: AAG29769.1.
AY172659 mRNA. Translation: AAO17261.1.
AY354202 mRNA. Translation: AAQ63887.1.
AK000290 mRNA. Translation: BAA91059.1. Frameshift.
AK027826 mRNA. Translation: BAB55395.1. Different initiation.
BC030688 mRNA. Translation: AAH30688.3.
BC040203 mRNA. No translation available.
AF176779 mRNA. Translation: AAQ13657.1. Different initiation.
AF175225 mRNA. Translation: AAQ13650.1. Frameshift.
AF173382 mRNA. Translation: AAQ13623.1. Frameshift.
CCDSiCCDS10207.1. [Q6V1X1-1]
CCDS10208.1. [Q6V1X1-2]
CCDS10209.1. [Q6V1X1-4]
CCDS10210.1. [Q6V1X1-3]
RefSeqiNP_060213.2. NM_017743.4. [Q6V1X1-4]
NP_569118.1. NM_130434.3. [Q6V1X1-3]
NP_932064.1. NM_197960.2. [Q6V1X1-1]
NP_932065.1. NM_197961.2. [Q6V1X1-2]
XP_005254557.1. XM_005254500.1. [Q6V1X1-1]
UniGeneiHs.591106.

Genome annotation databases

EnsembliENST00000300141; ENSP00000300141; ENSG00000074603. [Q6V1X1-3]
ENST00000321118; ENSP00000316373; ENSG00000074603. [Q6V1X1-5]
ENST00000321147; ENSP00000318111; ENSG00000074603. [Q6V1X1-2]
ENST00000341861; ENSP00000339208; ENSG00000074603. [Q6V1X1-1]
ENST00000358939; ENSP00000351817; ENSG00000074603. [Q6V1X1-4]
ENST00000559233; ENSP00000453954; ENSG00000074603. [Q6V1X1-1]
GeneIDi54878.
KEGGihsa:54878.
UCSCiuc002aov.3. human. [Q6V1X1-1]
uc002aoy.3. human. [Q6V1X1-2]
uc002aoz.3. human. [Q6V1X1-4]

Polymorphism databases

DMDMi67460301.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF221634 mRNA. Translation: AAG29766.1 .
AF221635 mRNA. Translation: AAG29767.1 .
AF221636 mRNA. Translation: AAG29768.1 .
AF221637 mRNA. Translation: AAG29769.1 .
AY172659 mRNA. Translation: AAO17261.1 .
AY354202 mRNA. Translation: AAQ63887.1 .
AK000290 mRNA. Translation: BAA91059.1 . Frameshift.
AK027826 mRNA. Translation: BAB55395.1 . Different initiation.
BC030688 mRNA. Translation: AAH30688.3 .
BC040203 mRNA. No translation available.
AF176779 mRNA. Translation: AAQ13657.1 . Different initiation.
AF175225 mRNA. Translation: AAQ13650.1 . Frameshift.
AF173382 mRNA. Translation: AAQ13623.1 . Frameshift.
CCDSi CCDS10207.1. [Q6V1X1-1 ]
CCDS10208.1. [Q6V1X1-2 ]
CCDS10209.1. [Q6V1X1-4 ]
CCDS10210.1. [Q6V1X1-3 ]
RefSeqi NP_060213.2. NM_017743.4. [Q6V1X1-4 ]
NP_569118.1. NM_130434.3. [Q6V1X1-3 ]
NP_932064.1. NM_197960.2. [Q6V1X1-1 ]
NP_932065.1. NM_197961.2. [Q6V1X1-2 ]
XP_005254557.1. XM_005254500.1. [Q6V1X1-1 ]
UniGenei Hs.591106.

3D structure databases

ProteinModelPortali Q6V1X1.
SMRi Q6V1X1. Positions 136-886.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120226. 14 interactions.
IntActi Q6V1X1. 3 interactions.
MINTi MINT-4539721.

Chemistry

BindingDBi Q6V1X1.
ChEMBLi CHEMBL4657.
GuidetoPHARMACOLOGYi 2356.

Protein family/group databases

MEROPSi S09.018.

PTM databases

PhosphoSitei Q6V1X1.

Polymorphism databases

DMDMi 67460301.

Proteomic databases

MaxQBi Q6V1X1.
PaxDbi Q6V1X1.
PRIDEi Q6V1X1.

Protocols and materials databases

DNASUi 54878.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300141 ; ENSP00000300141 ; ENSG00000074603 . [Q6V1X1-3 ]
ENST00000321118 ; ENSP00000316373 ; ENSG00000074603 . [Q6V1X1-5 ]
ENST00000321147 ; ENSP00000318111 ; ENSG00000074603 . [Q6V1X1-2 ]
ENST00000341861 ; ENSP00000339208 ; ENSG00000074603 . [Q6V1X1-1 ]
ENST00000358939 ; ENSP00000351817 ; ENSG00000074603 . [Q6V1X1-4 ]
ENST00000559233 ; ENSP00000453954 ; ENSG00000074603 . [Q6V1X1-1 ]
GeneIDi 54878.
KEGGi hsa:54878.
UCSCi uc002aov.3. human. [Q6V1X1-1 ]
uc002aoy.3. human. [Q6V1X1-2 ]
uc002aoz.3. human. [Q6V1X1-4 ]

Organism-specific databases

CTDi 54878.
GeneCardsi GC15M065734.
HGNCi HGNC:16490. DPP8.
HPAi HPA008706.
MIMi 606819. gene.
neXtProti NX_Q6V1X1.
PharmGKBi PA27470.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1506.
HOVERGENi HBG061620.
InParanoidi Q6V1X1.
KOi K08655.
OMAi SRHCDFF.
OrthoDBi EOG7XWPN8.
PhylomeDBi Q6V1X1.
TreeFami TF313309.

Enzyme and pathway databases

SABIO-RK Q6V1X1.

Miscellaneous databases

GeneWikii DPP8.
GenomeRNAii 54878.
NextBioi 57817.
PROi Q6V1X1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6V1X1.
Bgeei Q6V1X1.
Genevestigatori Q6V1X1.

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8."
    Abbott C.A., Yu D.M.T., Woollatt E., Sutherland G.R., McCaughan G.W., Gorrell M.D.
    Eur. J. Biochem. 267:6140-6150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 334-898 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 540-898 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 260-792 (ISOFORM 6), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.
    Tissue: Placenta.
  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 3), CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  3. Sha J.H., Zhou Z.M., Li J.M.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-898 (ISOFORM 2).
    Tissue: Hepatoma and Placenta.
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-898.
    Tissue: Aorta.
  7. "Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family."
    Ajami K., Abbott C.A., Obradovic M., Gysbers V., Kaehne T., McCaughan G.W., Gorrell M.D.
    Biochemistry 42:694-701(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-275; SER-755; ASP-833 AND HIS-865, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  8. "Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells."
    Chen Y.-S., Chien C.-H., Goparaju C.M., Hsu J.T.-A., Liang P.-H., Chen X.
    Protein Expr. Purif. 35:142-146(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8."
    Jiaang W.-T., Chen Y.-S., Hsu T., Wu S.-H., Chien C.-H., Chang C.-N., Chang S.-P., Lee S.-J., Chen X.
    Bioorg. Med. Chem. Lett. 15:687-691(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiDPP8_HUMAN
AccessioniPrimary (citable) accession number: Q6V1X1
Secondary accession number(s): Q7Z4C8
, Q7Z4D3, Q7Z4E1, Q8IWG7, Q8NEM5, Q96JX1, Q9HBM2, Q9HBM3, Q9HBM4, Q9HBM5, Q9NXF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi