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Protein

Aspartyl aminopeptidase

Gene

DNPEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

Catalytic activityi

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi94Zinc 11 Publication1
Binding sitei170Substrate1 Publication1
Metal bindingi264Zinc 11 Publication1
Metal bindingi264Zinc 21 Publication1
Binding sitei301Substrate1 Publication1
Metal bindingi302Zinc 21 Publication1
Metal bindingi346Zinc 11 Publication1
Binding sitei346Substrate1 Publication1
Binding sitei349Substrate1 Publication1
Binding sitei374Substrate1 Publication1
Binding sitei381Substrate1 Publication1
Metal bindingi440Zinc 21 Publication1

GO - Molecular functioni

  • aminopeptidase activity Source: ProtInc
  • metalloaminopeptidase activity Source: GO_Central
  • zinc ion binding Source: InterPro

GO - Biological processi

  • peptide metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS04704-MONOMER.

Protein family/group databases

MEROPSiM18.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl aminopeptidase (EC:3.4.11.21)
Gene namesi
Name:DNPEP
Synonyms:ASPEP, DAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2981. DNPEP.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi23549.
PharmGKBiPA27448.

Chemistry databases

ChEMBLiCHEMBL2761.
GuidetoPHARMACOLOGYi1559.

Polymorphism and mutation databases

BioMutaiDNPEP.
DMDMi17367145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001734511 – 475Aspartyl aminopeptidaseAdd BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei203PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9ULA0.
MaxQBiQ9ULA0.
PaxDbiQ9ULA0.
PeptideAtlasiQ9ULA0.
PRIDEiQ9ULA0.

PTM databases

iPTMnetiQ9ULA0.
PhosphoSitePlusiQ9ULA0.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000123992.
CleanExiHS_DAP.
HS_DNPEP.
ExpressionAtlasiQ9ULA0. baseline and differential.
GenevisibleiQ9ULA0. HS.

Organism-specific databases

HPAiHPA036398.
HPA044860.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-748356,EBI-748356
LNX1Q8TBB15EBI-748356,EBI-739832
MPP1Q000135EBI-748356,EBI-711788

Protein-protein interaction databases

BioGridi117093. 32 interactors.
IntActiQ9ULA0. 7 interactors.
STRINGi9606.ENSP00000273075.

Chemistry databases

BindingDBiQ9ULA0.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 26Combined sources19
Helixi31 – 44Combined sources14
Beta strandi63 – 68Combined sources6
Turni69 – 71Combined sources3
Beta strandi72 – 78Combined sources7
Beta strandi88 – 94Combined sources7
Beta strandi99 – 110Combined sources12
Beta strandi113 – 123Combined sources11
Helixi126 – 129Combined sources4
Beta strandi134 – 143Combined sources10
Turni145 – 147Combined sources3
Beta strandi150 – 156Combined sources7
Helixi169 – 171Combined sources3
Turni173 – 177Combined sources5
Turni183 – 186Combined sources4
Beta strandi190 – 193Combined sources4
Helixi194 – 200Combined sources7
Helixi218 – 228Combined sources11
Helixi232 – 234Combined sources3
Beta strandi235 – 244Combined sources10
Beta strandi249 – 251Combined sources3
Turni252 – 255Combined sources4
Beta strandi257 – 260Combined sources4
Helixi263 – 279Combined sources17
Turni283 – 288Combined sources6
Beta strandi291 – 299Combined sources9
Helixi301 – 303Combined sources3
Helixi315 – 324Combined sources10
Helixi332 – 336Combined sources5
Helixi337 – 339Combined sources3
Beta strandi341 – 345Combined sources5
Helixi356 – 358Combined sources3
Beta strandi372 – 374Combined sources3
Turni377 – 380Combined sources4
Helixi385 – 398Combined sources14
Beta strandi403 – 405Combined sources3
Helixi417 – 425Combined sources9
Beta strandi428 – 433Combined sources6
Beta strandi435 – 438Combined sources4
Beta strandi441 – 448Combined sources8
Helixi449 – 468Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DYOX-ray2.20A1-468[»]
ProteinModelPortaliQ9ULA0.
SMRiQ9ULA0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

Phylogenomic databases

eggNOGiKOG2596. Eukaryota.
COG1362. LUCA.
HOVERGENiHBG051386.
InParanoidiQ9ULA0.
PhylomeDBiQ9ULA0.
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.

Q9ULA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL
60 70 80 90 100
KETEKWNIKP ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL
110 120 130 140 150
RVKRRSRRSQ VGFQQVGVET YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL
160 170 180 190 200
EQQLVHVERP ILRIPHLAIH LQRNINENFG PNTEMHLVPI LATAIQEELE
210 220 230 240 250
KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL CLADTQPAVL
260 270 280 290 300
GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN
310 320 330 340 350
EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA
360 370 380 390 400
VHPNYLDKHE ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV
410 420 430 440 450
PLQDLMVRND TPCGTTIGPI LASRLGLRVL DLGSPQLAMH SIREMACTTG
460 470
VLQTLTLFKG FFELFPSLSH NLLVD
Length:475
Mass (Da):52,428
Last modified:May 1, 2000 - v1
Checksum:iA02BDCFB516BD081
GO

Sequence cautioni

The sequence BAA92014 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119E → V in BAA92014 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005050 mRNA. Translation: AAD01211.2.
AK001977 mRNA. Translation: BAA92014.1. Different initiation.
AC053503 Genomic DNA. No translation available.
BC000653 mRNA. Translation: AAH00653.2.
UniGeneiHs.258551.
Hs.635110.

Genome annotation databases

EnsembliENST00000273075; ENSP00000273075; ENSG00000123992.
UCSCiuc002vle.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005050 mRNA. Translation: AAD01211.2.
AK001977 mRNA. Translation: BAA92014.1. Different initiation.
AC053503 Genomic DNA. No translation available.
BC000653 mRNA. Translation: AAH00653.2.
UniGeneiHs.258551.
Hs.635110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DYOX-ray2.20A1-468[»]
ProteinModelPortaliQ9ULA0.
SMRiQ9ULA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117093. 32 interactors.
IntActiQ9ULA0. 7 interactors.
STRINGi9606.ENSP00000273075.

Chemistry databases

BindingDBiQ9ULA0.
ChEMBLiCHEMBL2761.
GuidetoPHARMACOLOGYi1559.

Protein family/group databases

MEROPSiM18.002.

PTM databases

iPTMnetiQ9ULA0.
PhosphoSitePlusiQ9ULA0.

Polymorphism and mutation databases

BioMutaiDNPEP.
DMDMi17367145.

Proteomic databases

EPDiQ9ULA0.
MaxQBiQ9ULA0.
PaxDbiQ9ULA0.
PeptideAtlasiQ9ULA0.
PRIDEiQ9ULA0.

Protocols and materials databases

DNASUi23549.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273075; ENSP00000273075; ENSG00000123992.
UCSCiuc002vle.3. human.

Organism-specific databases

DisGeNETi23549.
GeneCardsiDNPEP.
HGNCiHGNC:2981. DNPEP.
HPAiHPA036398.
HPA044860.
MIMi611367. gene.
neXtProtiNX_Q9ULA0.
PharmGKBiPA27448.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2596. Eukaryota.
COG1362. LUCA.
HOVERGENiHBG051386.
InParanoidiQ9ULA0.
PhylomeDBiQ9ULA0.
TreeFamiTF300487.

Enzyme and pathway databases

BioCyciZFISH:HS04704-MONOMER.

Miscellaneous databases

GeneWikiiDNPEP.
GenomeRNAii23549.
PROiQ9ULA0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123992.
CleanExiHS_DAP.
HS_DNPEP.
ExpressionAtlasiQ9ULA0. baseline and differential.
GenevisibleiQ9ULA0. HS.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiDNPEP_HUMAN
AccessioniPrimary (citable) accession number: Q9ULA0
Secondary accession number(s): Q9BW44, Q9NUV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 148 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

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.