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Q9ULA0

- DNPEP_HUMAN

UniProt

Q9ULA0 - DNPEP_HUMAN

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Protein

Aspartyl aminopeptidase

Gene

DNPEP

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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 zinc 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Zinc 11 Publication
Binding sitei170 – 1701Substrate1 Publication
Metal bindingi264 – 2641Zinc 11 Publication
Metal bindingi264 – 2641Zinc 21 Publication
Binding sitei301 – 3011Substrate1 Publication
Metal bindingi302 – 3021Zinc 21 Publication
Metal bindingi346 – 3461Zinc 11 Publication
Binding sitei346 – 3461Substrate1 Publication
Binding sitei349 – 3491Substrate1 Publication
Binding sitei374 – 3741Substrate1 Publication
Binding sitei381 – 3811Substrate1 Publication
Metal bindingi440 – 4401Zinc 21 Publication

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

Cytoplasm 1 Publication

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.1 Publication

Gene expression databases

BgeeiQ9ULA0.
CleanExiHS_DAP.
HS_DNPEP.
ExpressionAtlasiQ9ULA0. baseline and differential.
GenevestigatoriQ9ULA0.

Organism-specific databases

HPAiHPA036398.
HPA044860.

Interactioni

Subunit structurei

Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

Protein-protein interaction databases

BioGridi117093. 25 interactions.
IntActiQ9ULA0. 3 interactions.
STRINGi9606.ENSP00000273075.

Structurei

Secondary structure

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

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M18 family.Curated

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191E → V in BAA92014. (PubMed:14702039)Curated

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. 25 interactions.
IntActi Q9ULA0. 3 interactions.
STRINGi 9606.ENSP00000273075.

Chemistry

BindingDBi Q9ULA0.
ChEMBLi CHEMBL2761.

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

Bgeei Q9ULA0.
CleanExi HS_DAP.
HS_DNPEP.
ExpressionAtlasi Q9ULA0. baseline and differential.
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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: October 29, 2014
This is version 127 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

External Data

Dasty 3