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Q9ULA0

- DNPEP_HUMAN

UniProt

Q9ULA0 - DNPEP_HUMAN

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Protein

Aspartyl aminopeptidase

Gene
DNPEP, ASPEP, DAP
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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.

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 bindingi94 – 941Zinc 1
Binding sitei170 – 1701Substrate
Metal bindingi264 – 2641Zinc 1
Metal bindingi264 – 2641Zinc 2
Binding sitei301 – 3011Substrate
Metal bindingi302 – 3021Zinc 2
Metal bindingi346 – 3461Zinc 1
Binding sitei346 – 3461Substrate
Binding sitei349 – 3491Substrate
Binding sitei374 – 3741Substrate
Binding sitei381 – 3811Substrate
Metal bindingi440 – 4401Zinc 2

GO - Molecular functioni

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

GO - Biological processi

  1. peptide metabolic process Source: ProtInc
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
Synonyms:ASPEP, DAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2981. DNPEP.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cytoplasm Source: ProtInc
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27448.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Aspartyl aminopeptidasePRO_0000173451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9ULA0.
PaxDbiQ9ULA0.
PRIDEiQ9ULA0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ9ULA0.
BgeeiQ9ULA0.
CleanExiHS_DAP.
HS_DNPEP.
GenevestigatoriQ9ULA0.

Organism-specific databases

HPAiHPA036398.
HPA044860.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

Protein-protein interaction databases

BioGridi117093. 22 interactions.
IntActiQ9ULA0. 3 interactions.
STRINGi9606.ENSP00000273075.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2619
Helixi31 – 4414
Beta strandi63 – 686
Turni69 – 713
Beta strandi72 – 787
Beta strandi88 – 947
Beta strandi99 – 11012
Beta strandi113 – 12311
Helixi126 – 1294
Beta strandi134 – 14310
Turni145 – 1473
Beta strandi150 – 1567
Helixi169 – 1713
Turni173 – 1775
Turni183 – 1864
Beta strandi190 – 1934
Helixi194 – 2007
Helixi218 – 22811
Helixi232 – 2343
Beta strandi235 – 24410
Beta strandi249 – 2513
Turni252 – 2554
Beta strandi257 – 2604
Helixi263 – 27917
Turni283 – 2886
Beta strandi291 – 2999
Helixi301 – 3033
Helixi315 – 32410
Helixi332 – 3365
Helixi337 – 3393
Beta strandi341 – 3455
Helixi356 – 3583
Beta strandi372 – 3743
Turni377 – 3804
Helixi385 – 39814
Beta strandi403 – 4053
Helixi417 – 4259
Beta strandi428 – 4336
Beta strandi435 – 4384
Beta strandi441 – 4488
Helixi449 – 46820

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DYOX-ray2.20A1-468[»]
ProteinModelPortaliQ9ULA0.
SMRiQ9ULA0. Positions 7-472.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.

Phylogenomic databases

eggNOGiCOG1362.
HOVERGENiHBG051386.
InParanoidiQ9ULA0.
KOiK01267.
OrthoDBiEOG789CB1.
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

MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL    50
KETEKWNIKP ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL 100
RVKRRSRRSQ VGFQQVGVET YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL 150
EQQLVHVERP ILRIPHLAIH LQRNINENFG PNTEMHLVPI LATAIQEELE 200
KGTPEPGPLN AVDERHHSVL MSLLCAHLGL SPKDIVEMEL CLADTQPAVL 250
GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP HVRMVTLYDN 300
EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA 350
VHPNYLDKHE ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV 400
PLQDLMVRND TPCGTTIGPI LASRLGLRVL DLGSPQLAMH SIREMACTTG 450
VLQTLTLFKG FFELFPSLSH NLLVD 475
Length:475
Mass (Da):52,428
Last modified:May 1, 2000 - v1
Checksum:iA02BDCFB516BD081
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191E → V in BAA92014. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqiNP_036232.2. NM_012100.2.
UniGeneiHs.258551.

Genome annotation databases

EnsembliENST00000273075; ENSP00000273075; ENSG00000123992.
GeneIDi23549.
KEGGihsa:23549.
UCSCiuc002vle.2. human.

Polymorphism databases

DMDMi17367145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_036232.2. NM_012100.2.
UniGenei Hs.258551.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DYO X-ray 2.20 A 1-468 [» ]
ProteinModelPortali Q9ULA0.
SMRi Q9ULA0. Positions 7-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117093. 22 interactions.
IntActi Q9ULA0. 3 interactions.
STRINGi 9606.ENSP00000273075.

Chemistry

BindingDBi Q9ULA0.
ChEMBLi CHEMBL2761.
DrugBanki DB00142. L-Glutamic Acid.

Protein family/group databases

MEROPSi M18.002.

Polymorphism databases

DMDMi 17367145.

Proteomic databases

MaxQBi Q9ULA0.
PaxDbi Q9ULA0.
PRIDEi Q9ULA0.

Protocols and materials databases

DNASUi 23549.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000273075 ; ENSP00000273075 ; ENSG00000123992 .
GeneIDi 23549.
KEGGi hsa:23549.
UCSCi uc002vle.2. human.

Organism-specific databases

CTDi 23549.
GeneCardsi GC02M220238.
HGNCi HGNC:2981. DNPEP.
HPAi HPA036398.
HPA044860.
MIMi 611367. gene.
neXtProti NX_Q9ULA0.
PharmGKBi PA27448.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1362.
HOVERGENi HBG051386.
InParanoidi Q9ULA0.
KOi K01267.
OrthoDBi EOG789CB1.
PhylomeDBi Q9ULA0.
TreeFami TF300487.

Miscellaneous databases

GeneWikii DNPEP.
GenomeRNAii 23549.
NextBioi 46092.
PROi Q9ULA0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULA0.
Bgeei Q9ULA0.
CleanExi HS_DAP.
HS_DNPEP.
Genevestigatori Q9ULA0.

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], 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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. 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.

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: September 3, 2014
This is version 125 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.

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

External Data

Dasty 3

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