Q9ULA0 (DNPEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartyl aminopeptidase
EC=3.4.11.21

Gene names

Name:	DNPEP
Synonyms:	ASPEP, DAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Protein existence	Evidence 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.6
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptide metabolic process Traceable author statement Ref.1. Source: ProtInc proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc
Molecular_function	aminopeptidase activity Traceable author statement Ref.1. Source: ProtInc metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 475

475

Aspartyl aminopeptidase

PRO_0000173451

Sites

Metal binding

94

1

Zinc 1

Metal binding

264

1

Zinc 1

Metal binding

264

1

Zinc 2

Metal binding

302

1

Zinc 2

Metal binding

346

1

Zinc 1

Metal binding

440

1

Zinc 2

Binding site

170

1

Substrate

Binding site

301

1

Substrate

Binding site

346

1

Substrate

Binding site

349

1

Substrate

Binding site

374

1

Substrate

Binding site

381

1

Substrate

Experimental info

Sequence conflict

119

1

E → V in BAA92014. Ref.2

Secondary structure

1

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475

Helix Strand Turn

Details...

Helix

8 – 26

19

Helix

31 – 44

14

Beta strand

63 – 68

6

Turn

69 – 71

3

Beta strand

72 – 78

7

Beta strand

88 – 94

7

Beta strand

99 – 110

12

Beta strand

113 – 123

11

Helix

126 – 129

4

Beta strand

134 – 143

10

Turn

145 – 147

3

Beta strand

150 – 156

7

Helix

169 – 171

3

Turn

173 – 177

5

Turn

183 – 186

4

Beta strand

190 – 193

4

Helix

194 – 200

7

Helix

218 – 228

11

Helix

232 – 234

3

Beta strand

235 – 244

10

Beta strand

249 – 251

3

Turn

252 – 255

4

Beta strand

257 – 260

4

Helix

263 – 279

17

Turn

283 – 288

6

Beta strand

291 – 299

9

Helix

301 – 303

3

Helix

315 – 324

10

Helix

332 – 336

5

Helix

337 – 339

3

Beta strand

341 – 345

5

Helix

356 – 358

3

Beta strand

372 – 374

3

Turn

377 – 380

4

Helix

385 – 398

14

Beta strand

403 – 405

3

Helix

417 – 425

9

Beta strand

428 – 433

6

Beta strand

435 – 438

4

Beta strand

441 – 448

8

Helix

449 – 468

20

Sequences

	Sequence		Length	Mass (Da)
	Q9ULA0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: A02BDCFB516BD081	FASTA	475	52,428
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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]	"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.

IPI

IPI00015856.

RefSeq

NP_036232.2. NM_012100.2.

UniGene

Hs.258551.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DYO	X-ray	2.20	A	1-468	[»]

ProteinModelPortal

Q9ULA0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9ULA0. 3 interactions.

STRING

9606.ENSP00000273075.

Protein family/group databases

MEROPS

M18.002.

Polymorphism databases

DMDM

17367145.

Proteomic databases

PaxDb

Q9ULA0.

PRIDE

Q9ULA0.

Protocols and materials databases

DNASU

23549.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273075; ENSP00000273075; ENSG00000123992.

GeneID

23549.

KEGG

hsa:23549.

UCSC

uc002vle.2. human.

Organism-specific databases

CTD

23549.

GeneCards

GC02M220238.

HGNC

HGNC:2981. DNPEP.

HPA

HPA036398.
HPA044860.

MIM

611367. gene.

neXtProt

NX_Q9ULA0.

PharmGKB

PA27448.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1362.

HOVERGEN

HBG051386.

InParanoid

Q9ULA0.

KO

K01267.

OrthoDB

EOG4N8R4J.

Gene expression databases

ArrayExpress

Q9ULA0.

Bgee

Q9ULA0.

CleanEx

HS_DAP.
HS_DNPEP.

Genevestigator

Q9ULA0.

GermOnline

ENSG00000123992. Homo sapiens.

Family and domain databases

Gene3D

2.30.250.10. 1 hit.

InterPro

IPR001948. Peptidase_M18.
IPR023358. Peptidase_M18_dom2.
[Graphical view]

Pfam

PF02127. Peptidase_M18. 1 hit.
[Graphical view]

PRINTS

PR00932. AMINO1PTASE.

ProtoNet

Search...

Other

BindingDB

Q9ULA0.

ChEMBL

CHEMBL2761.

DrugBank

DB00142. L-Glutamic Acid.

GenomeRNAi

23549.

NextBio

46092.

SOURCE

Search...

Entry information

Entry name

DNPEP_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.