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Q9Z2W0

- DNPEP_MOUSE

UniProt

Q9Z2W0 - DNPEP_MOUSE

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Protein
Aspartyl aminopeptidase
Gene
Dnpep
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism By similarity.

Catalytic activityi

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.

Cofactori

Binds 2 zinc ions per subunit By similarity.

Enzyme regulationi

One of the zinc ions is readily exchangeable with other divalent cations such as manganese, which strongly stimulates the enzymatic activity By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 1 By similarity
Binding sitei168 – 1681Substrate By similarity
Metal bindingi262 – 2621Zinc 1 By similarity
Metal bindingi262 – 2621Zinc 2 By similarity
Binding sitei299 – 2991Substrate By similarity
Metal bindingi300 – 3001Zinc 2 By similarity
Metal bindingi344 – 3441Zinc 1 By similarity
Binding sitei344 – 3441Substrate By similarity
Binding sitei347 – 3471Substrate By similarity
Binding sitei372 – 3721Substrate By similarity
Binding sitei379 – 3791Substrate By similarity
Metal bindingi438 – 4381Zinc 2 By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM18.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl aminopeptidase (EC:3.4.11.21)
Gene namesi
Name:Dnpep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1278328. Dnpep.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Aspartyl aminopeptidase
PRO_0000173452Add
BLAST

Proteomic databases

MaxQBiQ9Z2W0.
PaxDbiQ9Z2W0.
PRIDEiQ9Z2W0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2W0.

PTM databases

PhosphoSiteiQ9Z2W0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ9Z2W0.
BgeeiQ9Z2W0.
CleanExiMM_DNPEP.
GenevestigatoriQ9Z2W0.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers By similarity.

Protein-protein interaction databases

IntActiQ9Z2W0. 2 interactions.
MINTiMINT-4093364.
STRINGi10090.ENSMUSP00000070821.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2W0.
SMRiQ9Z2W0. Positions 5-473.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.

Phylogenomic databases

eggNOGiCOG1362.
GeneTreeiENSGT00390000003164.
HOGENOMiHOG000253244.
HOVERGENiHBG051386.
InParanoidiQ56A00.
KOiK01267.
OMAiIVKCPTS.
OrthoDBiEOG789CB1.
TreeFamiTF300487.

Family and domain databases

Gene3Di2.30.250.10. 1 hit.
InterProiIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamiPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSiPR00932. AMINO1PTASE.

Sequencei

Sequence statusi: Complete.

Q9Z2W0-1 [UniParc]FASTAAdd to Basket

« Hide

MAMNGRARKE AIQATARELL KFVNRSPSPF HVVAECRSRL LQAGFRELKE    50
TEGWDIVPEN KYFLTRNSSS IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV 100
KRKSRRSQVG YHQVGVETYG GGIWSTWFDR DLTLAGRVII KCPTSGRLEQ 150
RLVHIERPIL RIPHLAIHLQ RNINENFGPN TEIHLVPILA TAVQEELEKG 200
TPEPGPLGAT DERHHSVLMS LLCTHLGLSP DSIMEMELCL ADTQPAVLGG 250
AYEEFIFAPR LDNLHSCFCA LQALIDSCAS PASLARDPHV RMVTLYDNEE 300
VGSESAQGAQ SLLTELILRR ISASPQRLTA FEEAIPKSFM ISADMAHAVH 350
PNYSDKHEEN HRPLFHKGPV IKVNSKQRYA SNAVSESMIR EVAGQVGVPL 400
QDLMVRNDSP CGTTIGPILA SRLGLRVLDL GSPQLAMHSI RETACTTGVL 450
QTLTLFKGFF ELFPSVSRNL LVD 473
Length:473
Mass (Da):52,207
Last modified:July 27, 2011 - v2
Checksum:i0350CC27C4A5AC8E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611K → N in AAD01212. 1 Publication
Sequence conflicti364 – 3641L → S in AAD01212. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF005051 mRNA. Translation: AAD01212.1.
AK166276 mRNA. Translation: BAE38675.1.
CH466548 Genomic DNA. Translation: EDL00396.1.
CH466548 Genomic DNA. Translation: EDL00398.1.
CH466548 Genomic DNA. Translation: EDL00400.1.
CH466548 Genomic DNA. Translation: EDL00401.1.
BC092232 mRNA. Translation: AAH92232.1.
CCDSiCCDS15070.1.
RefSeqiNP_001104301.1. NM_001110831.1.
NP_058574.3. NM_016878.4.
XP_006496468.1. XM_006496405.1.
XP_006496469.1. XM_006496406.1.
UniGeneiMm.24680.

Genome annotation databases

EnsembliENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
GeneIDi13437.
KEGGimmu:13437.
UCSCiuc007bot.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF005051 mRNA. Translation: AAD01212.1 .
AK166276 mRNA. Translation: BAE38675.1 .
CH466548 Genomic DNA. Translation: EDL00396.1 .
CH466548 Genomic DNA. Translation: EDL00398.1 .
CH466548 Genomic DNA. Translation: EDL00400.1 .
CH466548 Genomic DNA. Translation: EDL00401.1 .
BC092232 mRNA. Translation: AAH92232.1 .
CCDSi CCDS15070.1.
RefSeqi NP_001104301.1. NM_001110831.1.
NP_058574.3. NM_016878.4.
XP_006496468.1. XM_006496405.1.
XP_006496469.1. XM_006496406.1.
UniGenei Mm.24680.

3D structure databases

ProteinModelPortali Q9Z2W0.
SMRi Q9Z2W0. Positions 5-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Z2W0. 2 interactions.
MINTi MINT-4093364.
STRINGi 10090.ENSMUSP00000070821.

Protein family/group databases

MEROPSi M18.002.

PTM databases

PhosphoSitei Q9Z2W0.

2D gel databases

REPRODUCTION-2DPAGE Q9Z2W0.

Proteomic databases

MaxQBi Q9Z2W0.
PaxDbi Q9Z2W0.
PRIDEi Q9Z2W0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000066668 ; ENSMUSP00000070821 ; ENSMUSG00000026209 .
ENSMUST00000113605 ; ENSMUSP00000109235 ; ENSMUSG00000026209 .
GeneIDi 13437.
KEGGi mmu:13437.
UCSCi uc007bot.2. mouse.

Organism-specific databases

CTDi 23549.
MGIi MGI:1278328. Dnpep.

Phylogenomic databases

eggNOGi COG1362.
GeneTreei ENSGT00390000003164.
HOGENOMi HOG000253244.
HOVERGENi HBG051386.
InParanoidi Q56A00.
KOi K01267.
OMAi IVKCPTS.
OrthoDBi EOG789CB1.
TreeFami TF300487.

Miscellaneous databases

ChiTaRSi DNPEP. mouse.
NextBioi 283883.
PROi Q9Z2W0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z2W0.
Bgeei Q9Z2W0.
CleanExi MM_DNPEP.
Genevestigatori Q9Z2W0.

Family and domain databases

Gene3Di 2.30.250.10. 1 hit.
InterProi IPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view ]
Pfami PF02127. Peptidase_M18. 1 hit.
[Graphical view ]
PRINTSi PR00932. AMINO1PTASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase."
    Wilk S., Wilk E., Magnusson R.P.
    J. Biol. Chem. 273:15961-15970(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: C57BL/6.
    Tissue: Eye.

Entry informationi

Entry nameiDNPEP_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2W0
Secondary accession number(s): Q56A00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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