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P15144 (AMPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | 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:
Aminopeptidase N

Short name=AP-N
Short name=hAPN
EC=3.4.11.2
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name=AP-M
Microsomal aminopeptidase
Myeloid plasma membrane glycoprotein CD13
gp150
CD_antigen=CD13
Gene names
Name:ANPEP
Synonyms:APN, CD13, PEPN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection. Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. Ref.28

Cofactor

Binds 1 zinc ion per subunit. Ref.28

Subunit structure

Homodimer. Interacts with the S1 domain of HCoV-229E spike protein. Ref.9 Ref.11 Ref.23 Ref.28

Subcellular location

Cell membrane; Single-pass type II membrane protein. Cytoplasmcytosol Potential. Note: A soluble form has also been detected.

Tissue specificity

Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood-brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.

Induction

Estradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively. Ref.20

Domain

Amino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E (in porcine/human chimeric studies) and more specifically amino acids 288-295 (mutagenesis studies). Ref.14 Ref.17

Post-translational modification

Sulfated By similarity.

N- and O-glycosylated. Ref.10 Ref.15 Ref.28

May undergo proteolysis and give rise to a soluble form.

Miscellaneous

Found to serve as a receptor for tumor-homing peptides, more specifically NGR peptides. It could serve thus as a target for delivering drugs into tumors. Concentration in human hepatic bile, varies from 17.3 to 57.6 micrograms/ml.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Host-virus interaction
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Developmental protein
Host cell receptor for virus entry
Hydrolase
Metalloprotease
Protease
Receptor
   PTMDisulfide bond
Glycoprotein
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

angiotensin maturation

Traceable author statement. Source: Reactome

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 15308636. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

   Molecular_functionaminopeptidase activity

Traceable author statement PubMed 10734069. Source: ProtInc

metallopeptidase activity

Traceable author statement Ref.2. Source: ProtInc

receptor activity

Traceable author statement Ref.11. Source: ProtInc

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.7 Ref.8
Chain2 – 967966Aminopeptidase N
PRO_0000095081

Regions

Topological domain2 – 87Cytoplasmic
Transmembrane9 – 3224Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 967935Extracellular
Region33 – 6836Cytosolic Ser/Thr-rich junction
Region69 – 967899Metalloprotease
Region260 – 35394Interaction with HCoV-229E
Region352 – 3565Substrate binding

Sites

Active site3891Proton acceptor Ref.28
Metal binding3881Zinc; catalytic
Metal binding3921Zinc; catalytic
Metal binding4111Zinc; catalytic
Site4771Transition state stabilizer

Amino acid modifications

Modified residue1761Sulfotyrosine Potential
Modified residue4191Sulfotyrosine Potential
Modified residue4241Sulfotyrosine Potential
Modified residue9131Sulfotyrosine Potential
Glycosylation1281N-linked (GlcNAc...) Ref.25 Ref.26 Ref.28
Glycosylation2341N-linked (GlcNAc...) Ref.25 Ref.26 Ref.28
Glycosylation2651N-linked (GlcNAc...) Ref.24 Ref.25 Ref.26 Ref.28
Glycosylation3191N-linked (GlcNAc...) Ref.28
Glycosylation5271N-linked (GlcNAc...) Ref.28
Glycosylation5731N-linked (GlcNAc...) Ref.26
Glycosylation6251N-linked (GlcNAc...) Ref.28
Glycosylation6811N-linked (GlcNAc...) Ref.25 Ref.26 Ref.28
Glycosylation7351N-linked (GlcNAc...)
Glycosylation8181N-linked (GlcNAc...) Ref.25 Ref.26 Ref.28
Disulfide bond761 ↔ 768 Ref.28
Disulfide bond798 ↔ 834 Ref.28

Natural variations

Natural variant201V → M.
Corresponds to variant rs10152474 [ dbSNP | Ensembl ].
VAR_031262
Natural variant861R → Q. Ref.1 Ref.2 Ref.6
Corresponds to variant rs25653 [ dbSNP | Ensembl ].
VAR_014736
Natural variant2421D → Y. Ref.29
VAR_006727
Natural variant2431L → P. Ref.29
VAR_006728
Natural variant3111A → V.
Corresponds to variant rs17240268 [ dbSNP | Ensembl ].
VAR_031263
Natural variant3211T → M.
Corresponds to variant rs8179199 [ dbSNP | Ensembl ].
VAR_031264
Natural variant6031I → K.
Corresponds to variant rs17240212 [ dbSNP | Ensembl ].
VAR_031265
Natural variant6031I → M. Ref.1
Corresponds to variant rs8192297 [ dbSNP | Ensembl ].
VAR_031266
Natural variant7521S → N.
Corresponds to variant rs25651 [ dbSNP | Ensembl ].
VAR_014737

Experimental info

Mutagenesis288 – 2958DYVEKQAS → QSVEETAQ: No change in receptor activity and HCoV-229E infection. Ref.21
Mutagenesis288 – 2958DYVEKQAS → QSVNEQAQ: No change in receptor activity and HCoV-229E infection. Ref.21
Mutagenesis288 – 2958DYVEKQAS → QSVNETAQ: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity. Ref.21
Mutagenesis291 – 2933EKQ → NKT: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.
Mutagenesis2911E → N: No change of receptor activity and HCoV-229E infection.
Mutagenesis2931Q → T: No change of receptor activity and HCoV-229E infection.
Mutagenesis8181N → E: Very low receptor activity and HCoV-229E infection. Ref.21
Sequence conflict5361V → E in CAA31640. Ref.1
Sequence conflict8871L → P in CAA31640. Ref.1

Secondary structure

..................................................................................................................................................... 967
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15144 [UniParc].

Last modified April 3, 2007. Version 4.
Checksum: 37B6BC1BF0D6B1F2

FASTA967109,540
        10         20         30         40         50         60 
MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT PSASATTNPA 

        70         80         90        100        110        120 
SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL YVFKGSSTVR FTCKEATDVI 

       130        140        150        160        170        180 
IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI DKTELVEPTE YLVVHLKGSL VKDSQYEMDS 

       190        200        210        220        230        240 
EFEGELADDL AGFYRSEYME GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP 

       250        260        270        280        290        300 
KDLTALSNML PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI 

       310        320        330        340        350        360 
RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN AGAMENWGLV 

       370        380        390        400        410        420 
TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT IEWWNDLWLN EGFASYVEYL 

       430        440        450        460        470        480 
GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSTPAS EINTPAQISE LFDAISYSKG 

       490        500        510        520        530        540 
ASVLRMLSSF LSEDVFKQGL ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM 

       550        560        570        580        590        600 
NRWTLQMGFP VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY 

       610        620        630        640        650        660 
WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH SAIPVINRAQ 

       670        680        690        700        710        720 
IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS SLSYFKLMFD RSEVYGPMKN 

       730        740        750        760        770        780 
YLKKQVTPLF IHFRNNTNNW REIPENLMDQ YSEVNAISTA CSNGVPECEE MVSGLFKQWM 

       790        800        810        820        830        840 
ENPNNNPIHP NLRSTVYCNA IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI 

       850        860        870        880        890        900 
LNRYLSYTLN PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN 

       910        920        930        940        950        960 
LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW VKENKEVVLQ 


WFTENSK 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA."
Olsen J., Cowell G.M., Koenigshoefer E., Danielsen E.M., Moeller J., Laustsen L., Hansen O.C., Welinder K.G., Engberg J., Hunziker W., Spiess M., Sjoestroem H., Noren O.
FEBS Lett. 238:307-314(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-86 AND MET-603.
Tissue: Intestine.
[2]"Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N."
Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.
J. Clin. Invest. 83:1299-1307(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, VARIANT GLN-86.
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [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: Pancreas.
[5]"Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells."
Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.
J. Biol. Chem. 266:11999-12007(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
Tissue: Intestinal epithelium.
[6]"Genomic organisation of aminopeptidase N."
Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S., Blasczyk R.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, VARIANT GLN-86.
Tissue: Peripheral blood.
[7]"Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N."
Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.
Biol. Chem. Hoppe-Seyler 376:397-400(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20 AND 70-81.
[8]"Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids."
Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V., Nervi F.
FEBS Lett. 329:84-88(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18.
[9]"Purification and characterization of aminopeptidase N from human plasma."
Tokioka-Terao M., Hiwada K., Kokubu T.
Enzyme 32:65-75(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBUNIT.
[10]"Variable O-glycosylation of CD13 (aminopeptidase N)."
O'Connell P.J., Gerkis V., d'Apice A.J.F.
J. Biol. Chem. 266:4593-4597(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[11]"Human aminopeptidase N is a receptor for human coronavirus 229E."
Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B., Shapiro L.H., Look A.T., Holmes K.V.
Nature 357:420-422(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN, CHARACTERIZATION OF HCOV-229E RECEPTOR FUNCTION.
[12]"CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated."
Favaloro E.J., Browning T., Facey D.
Exp. Hematol. 21:1695-1701(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF SOLUBLE FORM.
[13]"CD13 (human aminopeptidase N) mediates human cytomegalovirus infection."
Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E.
J. Virol. 67:6576-6585(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF CMV RECEPTOR FUNCTION.
[14]"Characterization of functional domains in the human coronavirus HCV 229E receptor."
Kolb A.F., Maile J., Heister A., Siddell S.G.
J. Gen. Virol. 77:2515-2521(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR HCOV-229E INFECTION.
[15]"Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity."
Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.
Exp. Cell Res. 231:112-118(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GLYCOSYLATION.
[16]"Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N."
Kolb A.F., Hegyi A., Siddell S.G.
J. Gen. Virol. 78:2795-2802(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RESIDUES CRITICAL FOR HCOV-229E INFECTION.
[17]"Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N."
Hegyi A., Kolb A.F.
J. Gen. Virol. 79:1387-1391(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
[18]"Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells."
Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A., Salter R.D.
J. Immunol. 164:129-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
[19]"Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis."
Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M., Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.
Cancer Res. 60:722-727(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN ANGIOGENESIS, CHARACTERIZATION OF RECEPTOR FOR TUMOR-HOMING PEPTIDES FUNCTION.
[20]"Expression of aminopeptidase N in human endometrium and regulation of its activity by estrogen."
Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.
Fertil. Steril. 75:1172-1176(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY ESTRADIOL AND IL8.
[21]"Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation."
Wentworth D.E., Holmes K.V.
J. Virol. 75:9741-9752(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818.
[22]"Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and intratumoral fluid."
van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S., van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.
Clin. Cancer Res. 8:3747-3754(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SOLUBLE FORM.
[23]"Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E."
Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.
J. Virol. 77:2530-2538(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN.
[24]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
Tissue: Bile.
[25]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-681 AND ASN-818.
Tissue: Plasma.
[26]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-573; ASN-681 AND ASN-818.
Tissue: Liver.
[27]"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].
[28]"The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing."
Wong A.H., Zhou D., Rini J.M.
J. Biol. Chem. 287:36804-36813(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 66-967 IN COMPLEX WITH ANGIOTENSIN-4 AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE-BINDING REGION, ZINC-BINDING SITES, ACTIVE SITE, GLYCOSYLATION AT ASN-128; ASN-234; ASN-265; ASN-319; ASN-527; ASN-625; ASN-681 AND ASN-818, SUBUNIT, DISULFIDE BONDS.
[29]"Identification of point mutations in the aminopeptidase N gene by SSCP analysis and sequencing."
Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.
Hum. Mutat. Suppl. 1:S158-S160(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TYR-242 AND PRO-243.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13276 mRNA. Translation: CAA31640.1.
M22324 mRNA. Translation: AAA51719.1.
AC018988 Genomic DNA. No translation available.
AC079075 Genomic DNA. No translation available.
BC058928 mRNA. Translation: AAH58928.1.
M55522 Genomic DNA. Translation: AAA83399.1.
AJ421875, AJ421876 Genomic DNA. Translation: CAD19098.2.
AJ426050 Genomic DNA. Translation: CAD19802.1.
AJ427985 expand/collapse EMBL AC list , AJ427986, AJ427987, AJ427988 Genomic DNA. Translation: CAD20931.1.
CCDSCCDS10356.1.
PIRA30325.
RefSeqNP_001141.2. NM_001150.2.
XP_005254949.1. XM_005254892.2.
UniGeneHs.1239.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FYQX-ray1.90A66-967[»]
4FYRX-ray1.91A66-967[»]
4FYSX-ray2.01A66-967[»]
4FYTX-ray1.85A66-967[»]
ProteinModelPortalP15144.
SMRP15144. Positions 66-967.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106787. 2 interactions.
IntActP15144. 5 interactions.
STRING9606.ENSP00000300060.

Chemistry

BindingDBP15144.
ChEMBLCHEMBL1907.
DrugBankDB00973. Ezetimibe.

Protein family/group databases

MEROPSM01.001.

PTM databases

PhosphoSiteP15144.

Polymorphism databases

DMDM143811362.

Proteomic databases

MaxQBP15144.
PaxDbP15144.
PRIDEP15144.

Protocols and materials databases

DNASU290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300060; ENSP00000300060; ENSG00000166825.
GeneID290.
KEGGhsa:290.
UCSCuc002bop.4. human.

Organism-specific databases

CTD290.
GeneCardsGC15M090328.
H-InvDBHIX0038141.
HGNCHGNC:500. ANPEP.
HPACAB002417.
HPA004625.
MIM151530. gene.
neXtProtNX_P15144.
PharmGKBPA24815.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0308.
HOVERGENHBG006616.
InParanoidP15144.
KOK11140.
OMAWVLLNLN.
OrthoDBEOG754HNR.
PhylomeDBP15144.
TreeFamTF300395.

Enzyme and pathway databases

BRENDA3.4.11.2. 2681.
ReactomeREACT_17015. Metabolism of proteins.
SABIO-RKP15144.

Gene expression databases

ArrayExpressP15144.
BgeeP15144.
CleanExHS_ANPEP.
GenevestigatorP15144.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAlanine_aminopeptidase.
GenomeRNAi290.
NextBio1183.
PROP15144.
SOURCESearch...

Entry information

Entry nameAMPN_HUMAN
AccessionPrimary (citable) accession number: P15144
Secondary accession number(s): Q16728 expand/collapse secondary AC list , Q6GT90, Q8IUK3, Q8IVH3, Q9UCE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 173 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries