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Reviewed, UniProtKB/Swiss-Prot Q86TI2 (DPP9_HUMAN)

Last modified October 13, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dipeptidyl peptidase 9
    EC=3.4.14.5
Alternative name(s):
    Dipeptidyl peptidase IX
    DP9
    Dipeptidyl peptidase-like protein 9
      Short name=DPLP9
    Dipeptidyl peptidase IV-related protein 2
      Short name=DPRP-2
Gene names
Name: DPP9
Synonyms: DPRP2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.

Catalytic activity

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Ref.2 Ref.3

Enzyme regulation

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

Subcellular location

Cytoplasmcytosol. Ref.2 Ref.3

Tissue specificity

Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain. Ref.2 Ref.3 Ref.1

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=161 µM for Ala-Pro-AMC

KM=180 µM for Ala-Pro-AFC

pH dependence:

Optimum pH is 7.5-8.5. Little activity below pH 6.5.

Sequence caution

The sequence AAC33801.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC62840.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAD39039.3 differs from that shown. Reason: Frameshift at positions 432 and 460.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionAminopeptidase
Hydrolase
Protease
Serine protease
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86TI2-1)

Also known as: 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.
Isoform 2 (identifier: Q86TI2-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → LSRRVPCVRR...FSLNSEGAER
Note: Incomplete sequence.
Isoform 3 (identifier: Q86TI2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     650-674: QLVNNSFKGIKYLRLNTLASLGYAV → SAHLLPRPPPHHPPEDSPSPLKCQL
     675-863: Missing.
Isoform 4 (identifier: Q86TI2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     832-858: Missing.
Isoform 5 (identifier: Q86TI2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → LSRRVPCVRR...FSLNSEGAER
     3-139: Missing.
Note: Incomplete sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863Dipeptidyl peptidase 9
PRO_0000122415

Sites

Active site7301Charge relay system By similarity
Active site8081Charge relay system By similarity
Active site8401Charge relay system By similarity

Amino acid modifications

Modified residue511N6-acetyllysine Ref.8

Natural variations

Alternative sequence11M → LSRRVPCVRRGCRPPLPPLP GSQSRAWSRDREAPLDPGRP AQSGRRPTSRSVSHACSWNG GSLDPLEGTPALLRSAERLM RKVKKLRLDKENTGSWRSFS LNSEGAER in isoform 2 and isoform 5.
VSP_013865
Alternative sequence3 – 139137Missing in isoform 5.
VSP_013866
Alternative sequence650 – 67425QLVNN…LGYAV → SAHLLPRPPPHHPPEDSPSP LKCQL in isoform 3.
VSP_013867
Alternative sequence675 – 863189Missing in isoform 3.
VSP_013868
Alternative sequence832 – 85827Missing in isoform 4.
VSP_013869

Experimental info

Sequence conflict2041I → N in AAO73880. Ref.3
Sequence conflict2041I → N in AAQ83119. Ref.3
Sequence conflict5711C → W in BAC85150. Ref.6
Sequence conflict7091L → P in BAD18643. Ref.6
Sequence conflict7531G → C in BAB70784. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Short) [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: 40FE0B78E26CDED5

FASTA86398,263
        10         20         30         40         50         60 
MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN KAPHDFQFVQ 

        70         80         90        100        110        120 
KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL LLLSWKQMLD HFQATPHHGV 

       130        140        150        160        170        180 
YSREEELLRE RKRLGVFGIT SYDFHSESGL FLFQASNSLF HCRDGGKNGF MVSPMKPLEI 

       190        200        210        220        230        240 
KTQCSGPRMD PKICPADPAF FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG 

       250        260        270        280        290        300 
VATFVIQEEF DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT 

       310        320        330        340        350        360 
DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE YIARAGWTRD 

       370        380        390        400        410        420 
GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA RAVPRNVQPY VVYEEVTNVW 

       430        440        450        460        470        480 
INVHDIFYPF PQSEGEDELC FLRANECKTG FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK 

       490        500        510        520        530        540 
CPIKEEIALT SGEWEVLARH GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR 

       550        560        570        580        590        600 
LTTPGFSHSC SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS 

       610        620        630        640        650        660 
CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ LVNNSFKGIK 

       670        680        690        700        710        720 
YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV EIEDQVEGLQ FVAEKYGFID 

       730        740        750        760        770        780 
LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA IAGAPVTVWM AYDTGYTERY MDVPENNQHG 

       790        800        810        820        830        840 
YEAGSVALHV EKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH 

       850        860 
SIRCPESGEH YEVTLLHFLQ EYL 

« Hide

Isoform 2 (Long).

Checksum: 397F78903F01A7F8
Show »

FASTA970110,114
Isoform 3.

Checksum: 8C5A7E386929CAA5
Show »

FASTA67476,702
Isoform 4.

Checksum: EF3B224CF112B857
Show »

FASTA83695,013
Isoform 5.

Checksum: E83D994DAEBC8C5B
Show »

FASTA83394,487

References

[1]"Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV."
Olsen C., Wagtmann N.
Gene 299:185-193(2002) [PubMed: 12459266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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: 12662155] [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: 15245913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[4]"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. expand/collapse author list , 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: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta and Skin.
[6]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-863 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 272-863 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Glial tumor, Ovary, Spleen and Trachea.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORM 2).
Tissue: Melanoma.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF452102 mRNA. Translation: AAL47179.1.
AY172660 mRNA. Translation: AAO17262.1.
AF542510 mRNA. Translation: AAO73880.2.
AY374518 mRNA. Translation: AAQ83119.1.
AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems.
AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems.
BC000970 mRNA. Translation: AAH00970.1.
BC037948 mRNA. Translation: AAH37948.1.
AK054656 mRNA. Translation: BAB70784.1. Different initiation.
AK075030 mRNA. Translation: BAC11362.1.
AK131100 mRNA. Translation: BAC85150.1.
AK131499 mRNA. Translation: BAD18643.1. Different initiation.
AL834376 mRNA. Translation: CAD39039.3. Frameshift.
CR627380 mRNA. Translation: CAH10477.1.
IPIIPI00604483.
IPI00604645.
IPI00604694.
IPI00604777.
IPI00940180.
RefSeqNP_631898.3.
UniGeneHs.515081

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ86TI2.

Proteomic databases

PRIDEQ86TI2.

Genome annotation databases

EnsemblENST00000262959; ENSP00000262959; ENSG00000142002; Homo sapiens. [Genome view]
ENST00000262960; ENSP00000262960; ENSG00000142002; Homo sapiens. [Genome view]
ENST00000357909; ENSP00000350583; ENSG00000142002; Homo sapiens. [Genome view]
ENST00000381797; ENSP00000371217; ENSG00000142002; Homo sapiens. [Genome view]
GeneID91039.
KEGGhsa:91039.
UCSCuc002mba.1. human.
uc002mbb.1. human.

Organism-specific databases

GeneCardsGC19M004626.
H-InvDBHIX0022644.
HGNCHGNC:18648. DPP9.
MIM608258. gene.
PharmGKBPA38620.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ86TI2.

Enzyme and pathway databases

BRENDA3.4.14.5. 247.

Gene expression databases

ArrayExpressQ86TI2.
BgeeQ86TI2.
GenevestigatorQ86TI2.
GermOnlineENSG00000142002. Homo sapiens.

Family and domain databases

InterProIPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio77078.
SOURCESearch...

Entry information

Entry nameDPP9_HUMAN
AccessionPrimary (citable) accession number: Q86TI2
Secondary accession number(s): O75273 expand/collapse secondary AC list , O75868, Q6AI37, Q6UAL0, Q6ZMT2, Q6ZNJ5, Q8N2J7, Q8N3F5, Q8WXD8, Q96NT8, Q9BVR3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: October 13, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents