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Q86TI2

- DPP9_HUMAN

UniProt

Q86TI2 - DPP9_HUMAN

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Protein

Dipeptidyl peptidase 9

Gene
DPP9, DPRP2
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.

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-AFC

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei730 – 7301Charge relay system By similarity
Active sitei808 – 8081Charge relay system By similarity
Active sitei840 – 8401Charge relay system By 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: Chromosome 19

Organism-specific databases

HGNCiHGNC:18648. DPP9.

Subcellular locationi

Cytoplasmcytosol 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

Orphaneti2032. Idiopathic pulmonary fibrosis.
PharmGKBiPA38620.

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

ArrayExpressiQ86TI2.
BgeeiQ86TI2.
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. 17 interactions.
MINTiMINT-4535936.

Structurei

3D structure databases

ProteinModelPortaliQ86TI2.
SMRiQ86TI2. Positions 489-861.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1506.
HOVERGENiHBG061620.
InParanoidiQ86TI2.
KOiK08656.
OMAiFPRVEYI.
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. Align

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

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.

« Hide

MATTGTPTAD RGDAAATDDP AARFQVQKHS WDGLRSIIHG SRKYSGLIVN    50
KAPHDFQFVQ KTDESGPHSH RLYYLGMPYG SRENSLLYSE IPKKVRKEAL 100
LLLSWKQMLD HFQATPHHGV YSREEELLRE RKRLGVFGIT SYDFHSESGL 150
FLFQASNSLF HCRDGGKNGF MVSPMKPLEI KTQCSGPRMD PKICPADPAF 200
FSFINNSDLW VANIETGEER RLTFCHQGLS NVLDDPKSAG VATFVIQEEF 250
DRFTGYWWCP TASWEGSEGL KTLRILYEEV DESEVEVIHV PSPALEERKT 300
DSYRYPRTGS KNPKIALKLA EFQTDSQGKI VSTQEKELVQ PFSSLFPKVE 350
YIARAGWTRD GKYAWAMFLD RPQQWLQLVL LPPALFIPST ENEEQRLASA 400
RAVPRNVQPY VVYEEVTNVW INVHDIFYPF PQSEGEDELC FLRANECKTG 450
FCHLYKVTAV LKSQGYDWSE PFSPGEDEFK CPIKEEIALT SGEWEVLARH 500
GSKIWVNEET KLVYFQGTKD TPLEHHLYVV SYEAAGEIVR LTTPGFSHSC 550
SMSQNFDMFV SHYSSVSTPP CVHVYKLSGP DDDPLHKQPR FWASMMEAAS 600
CPPDYVPPEI FHFHTRSDVR LYGMIYKPHA LQPGKKHPTV LFVYGGPQVQ 650
LVNNSFKGIK YLRLNTLASL GYAVVVIDGR GSCQRGLRFE GALKNQMGQV 700
EIEDQVEGLQ FVAEKYGFID LSRVAIHGWS YGGFLSLMGL IHKPQVFKVA 750
IAGAPVTVWM AYDTGYTERY MDVPENNQHG YEAGSVALHV EKLPNEPNRL 800
LILHGFLDEN VHFFHTNFLV SQLIRAGKPY QLQIYPNERH SIRCPESGEH 850
YEVTLLHFLQ EYL 863
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: Long

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

Note: Incomplete sequence.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRKVKKLRLDKENTGSWRSF SLNSEGAERM in isoform 2. VSP_013865
Alternative sequencei832 – 85827Missing in isoform 3. VSP_013869Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041I → N in AAO73880. 1 Publication
Sequence conflicti204 – 2041I → N in AAQ83119. 1 Publication
Sequence conflicti461 – 4611L → F in CAD39039. 1 Publication
Sequence conflicti571 – 5711C → W in BAC85150. 1 Publication
Sequence conflicti709 – 7091L → P in BAD18643. 1 Publication
Sequence conflicti753 – 7531G → C in BAB70784. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi67460390.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS45928.1. [Q86TI2-2 ]
RefSeqi NP_631898.3. NM_139159.4. [Q86TI2-2 ]
XP_005259730.1. XM_005259673.2. [Q86TI2-2 ]
UniGenei Hs.515081.

3D structure databases

ProteinModelPortali Q86TI2.
SMRi Q86TI2. Positions 489-861.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124789. 17 interactions.
MINTi MINT-4535936.

Chemistry

BindingDBi Q86TI2.
ChEMBLi CHEMBL4793.

Protein family/group databases

MEROPSi S09.019.

PTM databases

PhosphoSitei Q86TI2.

Polymorphism databases

DMDMi 67460390.

Proteomic databases

MaxQBi Q86TI2.
PaxDbi Q86TI2.
PRIDEi Q86TI2.

Protocols and materials databases

DNASUi 91039.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262960 ; ENSP00000262960 ; ENSG00000142002 . [Q86TI2-2 ]
ENST00000594671 ; ENSP00000472224 ; ENSG00000142002 . [Q86TI2-4 ]
ENST00000598800 ; ENSP00000469603 ; ENSG00000142002 . [Q86TI2-1 ]
GeneIDi 91039.
KEGGi hsa:91039.
UCSCi uc002mba.3. human. [Q86TI2-2 ]

Organism-specific databases

CTDi 91039.
GeneCardsi GC19M004675.
H-InvDB HIX0027578.
HGNCi HGNC:18648. DPP9.
HPAi HPA036059.
MIMi 608258. gene.
neXtProti NX_Q86TI2.
Orphaneti 2032. Idiopathic pulmonary fibrosis.
PharmGKBi PA38620.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1506.
HOVERGENi HBG061620.
InParanoidi Q86TI2.
KOi K08656.
OMAi FPRVEYI.
OrthoDBi EOG7XWPN8.
PhylomeDBi Q86TI2.
TreeFami TF313309.

Enzyme and pathway databases

SABIO-RK Q86TI2.

Miscellaneous databases

ChiTaRSi DPP9. human.
GeneWikii DPP9.
GenomeRNAii 91039.
NextBioi 77078.
PROi Q86TI2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86TI2.
Bgeei Q86TI2.
Genevestigatori Q86TI2.

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. "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].

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: September 3, 2014
This is version 111 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

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