Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dipeptidyl peptidase 9

Gene

DPP9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

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 the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate.1 Publication

Kineticsi

  1. KM=161 µM for Ala-Pro-AMC2 Publications
  2. KM=180 µM for Ala-Pro-AFC2 Publications

pH dependencei

Optimum pH is 7.5-8.5. Little activity below pH 6.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei730 – 7301Charge relay systemBy similarity
Active sitei808 – 8081Charge relay systemBy similarity
Active sitei840 – 8401Charge relay systemBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. serine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

SABIO-RKQ86TI2.

Protein family/group databases

MEROPSiS09.019.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 9 (EC:3.4.14.5)
Short name:
DP9
Alternative name(s):
Dipeptidyl peptidase IV-related protein 2
Short name:
DPRP-2
Dipeptidyl peptidase IX
Short name:
DPP IX
Dipeptidyl peptidase-like protein 9
Short name:
DPLP9
Gene namesi
Name:DPP9
Synonyms:DPRP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:18648. DPP9.

Subcellular locationi

Isoform 1 :
  1. Cytoplasmcytosol 2 Publications
Isoform 2 :
  1. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB-SubCell
  3. membrane Source: InterPro
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti2032. Idiopathic pulmonary fibrosis.
PharmGKBiPA38620.

Polymorphism and mutation databases

DMDMi67460390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 863862Dipeptidyl peptidase 9PRO_0000122415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ86TI2.
PaxDbiQ86TI2.
PRIDEiQ86TI2.

PTM databases

PhosphoSiteiQ86TI2.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain.3 Publications

Gene expression databases

BgeeiQ86TI2.
ExpressionAtlasiQ86TI2. baseline and differential.
GenevestigatoriQ86TI2.

Organism-specific databases

HPAiHPA036059.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7475352,EBI-7475352

Protein-protein interaction databases

BioGridi124789. 35 interactions.
MINTiMINT-4535936.

Structurei

3D structure databases

ProteinModelPortaliQ86TI2.
SMRiQ86TI2. Positions 489-861.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000006870.
HOVERGENiHBG061620.
InParanoidiQ86TI2.
KOiK08656.
OMAiDGRARCY.
OrthoDBiEOG7XWPN8.
PhylomeDBiQ86TI2.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86TI2-1) [UniParc]FASTAAdd to basket

Also known as: DPP9-S, Short

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
MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN
60 70 80 90 100
KAPHDFQFVQ KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL
110 120 130 140 150
LLLSWKQMLD HFQATPHHGV YSREEELLRE RKRLGVFGIT SYDFHSESGL
160 170 180 190 200
FLFQASNSLF HCRDGGKNGF MVSPMKPLEI KTQCSGPRMD PKICPADPAF
210 220 230 240 250
FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG VATFVIQEEF
260 270 280 290 300
DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT
310 320 330 340 350
DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE
360 370 380 390 400
YIARAGWTRD GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA
410 420 430 440 450
RAVPRNVQPY VVYEEVTNVW INVHDIFYPF PQSEGEDELC FLRANECKTG
460 470 480 490 500
FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK CPIKEEIALT SGEWEVLARH
510 520 530 540 550
GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR LTTPGFSHSC
560 570 580 590 600
SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS
610 620 630 640 650
CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ
660 670 680 690 700
LVNNSFKGIK YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV
710 720 730 740 750
EIEDQVEGLQ FVAEKYGFID LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA
760 770 780 790 800
IAGAPVTVWM AYDTGYTERY MDVPENNQHG YEAGSVALHV EKLPNEPNRL
810 820 830 840 850
LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH SIRCPESGEH
860
YEVTLLHFLQ EYL
Length:863
Mass (Da):98,263
Last modified:June 7, 2005 - v3
Checksum:i40FE0B78E26CDED5
GO
Isoform 2 (identifier: Q86TI2-2) [UniParc]FASTAAdd to basket

Also known as: DPP9-L, Long

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKVKKLRLDKENTGSWRSFSLNSEGAERM

Note: Active peptidase. Contains a nuclear localization signal at positions 2-9.1 Publication

Show »
Length:892
Mass (Da):101,669
Checksum:i2CDB8E40E428AE73
GO
Isoform 3 (identifier: Q86TI2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     832-858: Missing.

Show »
Length:836
Mass (Da):95,013
Checksum:iEF3B224CF112B857
GO

Sequence cautioni

The sequence AAC33801.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAC62840.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAH37948.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL47179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO73880.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB70784.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC85150.1 differs from that shown.Probable cloning artifact.Curated
The sequence BAD18643.1 differs from that shown.Aberrant splicing.Curated
The sequence CAD39039.3 differs from that shown. Reason: Frameshift at positions 432 and 460. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041I → N in AAO73880 (PubMed:15245913).Curated
Sequence conflicti204 – 2041I → N in AAQ83119 (PubMed:15245913).Curated
Sequence conflicti461 – 4611L → F in CAD39039 (PubMed:17974005).Curated
Sequence conflicti571 – 5711C → W in BAC85150 (PubMed:14702039).Curated
Sequence conflicti709 – 7091L → P in BAD18643 (PubMed:14702039).Curated
Sequence conflicti753 – 7531G → C in BAB70784 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRKVKKLRLDKENTGSWRSF SLNSEGAERM in isoform 2. 4 PublicationsVSP_013865
Alternative sequencei832 – 85827Missing in isoform 3. 1 PublicationVSP_013869Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452102 mRNA. Translation: AAL47179.1. Different initiation.
AY172660 mRNA. Translation: AAO17262.1.
AF542510 mRNA. Translation: AAO73880.2. Different initiation.
AY374518 mRNA. Translation: AAQ83119.1.
DQ417928 mRNA. Translation: ABD83624.1.
AK054656 mRNA. Translation: BAB70784.1. Different initiation.
AK075030 mRNA. Translation: BAC11362.1. Different initiation.
AK122654 mRNA. Translation: BAG53644.1.
AK131100 mRNA. Translation: BAC85150.1. Sequence problems.
AK131499 mRNA. Translation: BAD18643.1. Sequence problems.
AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems.
AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems.
CH471139 Genomic DNA. Translation: EAW69199.1.
CH471139 Genomic DNA. Translation: EAW69201.1.
BC000970 mRNA. Translation: AAH00970.1.
BC037948 mRNA. Translation: AAH37948.1. Different initiation.
AL834376 mRNA. Translation: CAD39039.3. Frameshift.
CR627380 mRNA. Translation: CAH10477.1.
CCDSiCCDS45928.1. [Q86TI2-2]
RefSeqiNP_631898.3. NM_139159.4. [Q86TI2-2]
XP_005259730.1. XM_005259673.2. [Q86TI2-2]
UniGeneiHs.515081.

Genome annotation databases

EnsembliENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
ENST00000598800; ENSP00000469603; ENSG00000142002. [Q86TI2-1]
GeneIDi91039.
KEGGihsa:91039.
UCSCiuc002mba.3. human. [Q86TI2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452102 mRNA. Translation: AAL47179.1. Different initiation.
AY172660 mRNA. Translation: AAO17262.1.
AF542510 mRNA. Translation: AAO73880.2. Different initiation.
AY374518 mRNA. Translation: AAQ83119.1.
DQ417928 mRNA. Translation: ABD83624.1.
AK054656 mRNA. Translation: BAB70784.1. Different initiation.
AK075030 mRNA. Translation: BAC11362.1. Different initiation.
AK122654 mRNA. Translation: BAG53644.1.
AK131100 mRNA. Translation: BAC85150.1. Sequence problems.
AK131499 mRNA. Translation: BAD18643.1. Sequence problems.
AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems.
AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems.
CH471139 Genomic DNA. Translation: EAW69199.1.
CH471139 Genomic DNA. Translation: EAW69201.1.
BC000970 mRNA. Translation: AAH00970.1.
BC037948 mRNA. Translation: AAH37948.1. Different initiation.
AL834376 mRNA. Translation: CAD39039.3. Frameshift.
CR627380 mRNA. Translation: CAH10477.1.
CCDSiCCDS45928.1. [Q86TI2-2]
RefSeqiNP_631898.3. NM_139159.4. [Q86TI2-2]
XP_005259730.1. XM_005259673.2. [Q86TI2-2]
UniGeneiHs.515081.

3D structure databases

ProteinModelPortaliQ86TI2.
SMRiQ86TI2. Positions 489-861.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124789. 35 interactions.
MINTiMINT-4535936.

Chemistry

BindingDBiQ86TI2.
ChEMBLiCHEMBL4793.

Protein family/group databases

MEROPSiS09.019.

PTM databases

PhosphoSiteiQ86TI2.

Polymorphism and mutation databases

DMDMi67460390.

Proteomic databases

MaxQBiQ86TI2.
PaxDbiQ86TI2.
PRIDEiQ86TI2.

Protocols and materials databases

DNASUi91039.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262960; ENSP00000262960; ENSG00000142002. [Q86TI2-2]
ENST00000594671; ENSP00000472224; ENSG00000142002. [Q86TI2-4]
ENST00000598800; ENSP00000469603; ENSG00000142002. [Q86TI2-1]
GeneIDi91039.
KEGGihsa:91039.
UCSCiuc002mba.3. human. [Q86TI2-2]

Organism-specific databases

CTDi91039.
GeneCardsiGC19M004675.
H-InvDBHIX0027578.
HGNCiHGNC:18648. DPP9.
HPAiHPA036059.
MIMi608258. gene.
neXtProtiNX_Q86TI2.
Orphaneti2032. Idiopathic pulmonary fibrosis.
PharmGKBiPA38620.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000006870.
HOVERGENiHBG061620.
InParanoidiQ86TI2.
KOiK08656.
OMAiDGRARCY.
OrthoDBiEOG7XWPN8.
PhylomeDBiQ86TI2.
TreeFamiTF313309.

Enzyme and pathway databases

SABIO-RKQ86TI2.

Miscellaneous databases

ChiTaRSiDPP9. human.
GeneWikiiDPP9.
GenomeRNAii91039.
NextBioi77078.
PROiQ86TI2.
SOURCEiSearch...

Gene expression databases

BgeeiQ86TI2.
ExpressionAtlasiQ86TI2. baseline and differential.
GenevestigatoriQ86TI2.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV."
    Olsen C., Wagtmann N.
    Gene 299:185-193(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  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 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Colon.
  3. "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity."
    Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D.
    Biochim. Biophys. Acta 1679:18-28(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. "Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV."
    Bjelke J.R., Christensen J., Nielsen P.F., Branner S., Kanstrup A.B., Wagtmann N., Rasmussen H.B.
    Biochem. J. 396:391-399(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT.
  5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-649 (ISOFORMS 1/3).
    Tissue: Glial tumor, Ovary, Spleen and Trachea.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 2).
    Tissue: Placenta and Skin.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORMS 1/2).
    Tissue: Melanoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [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].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus."
    Justa-Schuch D., Moller U., Geiss-Friedlander R.
    Cell. Mol. Life Sci. 71:3611-3626(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM 2), NUCLEAR LOCALIZATION SIGNAL (ISOFORM 2).

Entry informationi

Entry nameiDPP9_HUMAN
AccessioniPrimary (citable) accession number: Q86TI2
Secondary accession number(s): O75273
, O75868, Q1ZZB8, Q6AI37, Q6UAL0, Q6ZMT2, Q6ZNJ5, Q8N2J7, Q8N3F5, Q8WXD8, Q96NT8, Q9BVR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 29, 2015
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.