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Q9ULA0 (DNPEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartyl aminopeptidase

EC=3.4.11.21
Gene names
Name:DNPEP
Synonyms:ASPEP, DAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit.

Enzyme regulation

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

Subunit structure

Tetrahedron-shaped homododecamer built from six homodimers. Ref.7

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase M18 family.

Caution

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

Sequence caution

The sequence BAA92014.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Aspartyl aminopeptidase
PRO_0000173451

Sites

Metal binding941Zinc 1
Metal binding2641Zinc 1
Metal binding2641Zinc 2
Metal binding3021Zinc 2
Metal binding3461Zinc 1
Metal binding4401Zinc 2
Binding site1701Substrate
Binding site3011Substrate
Binding site3461Substrate
Binding site3491Substrate
Binding site3741Substrate
Binding site3811Substrate

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Experimental info

Sequence conflict1191E → V in BAA92014. Ref.2

Secondary structure

............................................................................ 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ULA0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A02BDCFB516BD081

FASTA47552,428
        10         20         30         40         50         60 
MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL KETEKWNIKP 

        70         80         90        100        110        120 
ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL RVKRRSRRSQ VGFQQVGVET 

       130        140        150        160        170        180 
YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL EQQLVHVERP ILRIPHLAIH LQRNINENFG 

       190        200        210        220        230        240 
PNTEMHLVPI LATAIQEELE KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL 

       250        260        270        280        290        300 
CLADTQPAVL GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN 

       310        320        330        340        350        360 
EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA VHPNYLDKHE 

       370        380        390        400        410        420 
ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV PLQDLMVRND TPCGTTIGPI 

       430        440        450        460        470 
LASRLGLRVL DLGSPQLAMH SIREMACTTG VLQTLTLFKG FFELFPSLSH NLLVD 

« Hide

References

« Hide 'large scale' references
[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], CHARACTERIZATION.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Eye.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family."
Chaikuad A., Pilka E.S., Riso A.D., Delft F.V., Kavanagh K.L., Venien-Bryan C., Oppermann U., Yue W.W.
BMC Struct. Biol. 12:14-14(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-468 IN COMPLEX WITH SUBSTRATE ANALOG, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005050 mRNA. Translation: AAD01211.2.
AK001977 mRNA. Translation: BAA92014.1. Different initiation.
AC053503 Genomic DNA. No translation available.
BC000653 mRNA. Translation: AAH00653.2.
RefSeqNP_036232.2. NM_012100.2.
UniGeneHs.258551.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DYOX-ray2.20A1-468[»]
ProteinModelPortalQ9ULA0.
SMRQ9ULA0. Positions 7-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117093. 20 interactions.
IntActQ9ULA0. 3 interactions.
STRING9606.ENSP00000273075.

Chemistry

BindingDBQ9ULA0.
ChEMBLCHEMBL2761.
DrugBankDB00142. L-Glutamic Acid.

Protein family/group databases

MEROPSM18.002.

Polymorphism databases

DMDM17367145.

Proteomic databases

MaxQBQ9ULA0.
PaxDbQ9ULA0.
PRIDEQ9ULA0.

Protocols and materials databases

DNASU23549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273075; ENSP00000273075; ENSG00000123992.
GeneID23549.
KEGGhsa:23549.
UCSCuc002vle.2. human.

Organism-specific databases

CTD23549.
GeneCardsGC02M220238.
HGNCHGNC:2981. DNPEP.
HPAHPA036398.
HPA044860.
MIM611367. gene.
neXtProtNX_Q9ULA0.
PharmGKBPA27448.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1362.
HOVERGENHBG051386.
InParanoidQ9ULA0.
KOK01267.
OrthoDBEOG789CB1.
PhylomeDBQ9ULA0.
TreeFamTF300487.

Gene expression databases

ArrayExpressQ9ULA0.
BgeeQ9ULA0.
CleanExHS_DAP.
HS_DNPEP.
GenevestigatorQ9ULA0.

Family and domain databases

Gene3D2.30.250.10. 1 hit.
InterProIPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]
PfamPF02127. Peptidase_M18. 1 hit.
[Graphical view]
PRINTSPR00932. AMINO1PTASE.
ProtoNetSearch...

Other

GeneWikiDNPEP.
GenomeRNAi23549.
NextBio46092.
PROQ9ULA0.
SOURCESearch...

Entry information

Entry nameDNPEP_HUMAN
AccessionPrimary (citable) accession number: Q9ULA0
Secondary accession number(s): Q9BW44, Q9NUV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM