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P15144

- AMPN_HUMAN

UniProt

P15144 - AMPN_HUMAN

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Protein
Aminopeptidase N
Gene
ANPEP, APN, CD13, PEPN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.9 Publications

Catalytic activityi

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.1 Publication

Cofactori

Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi388 – 3881Zinc; catalytic
Active sitei389 – 3891Proton acceptor1 Publication
Metal bindingi392 – 3921Zinc; catalytic
Metal bindingi411 – 4111Zinc; catalytic
Sitei477 – 4771Transition state stabilizer

GO - Molecular functioni

  1. aminopeptidase activity Source: ProtInc
  2. metallopeptidase activity Source: ProtInc
  3. receptor activity Source: ProtInc
  4. virus receptor activity Source: UniProtKB-KW
  5. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. angiotensin maturation Source: Reactome
  3. cell differentiation Source: UniProtKB-KW
  4. cellular protein metabolic process Source: Reactome
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Host-virus interaction

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.2. 2681.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RKP15144.

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
hAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
Myeloid plasma membrane glycoprotein CD13
gp150
CD_antigen: CD13
Gene namesi
Name:ANPEP
Synonyms:APN, CD13, PEPN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:500. ANPEP.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – 967935Extracellular
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. external side of plasma membrane Source: Ensembl
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. integral component of plasma membrane Source: ProtInc
  7. lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi288 – 2958DYVEKQAS → QSVEETAQ: No change in receptor activity and HCoV-229E infection. 1 Publication
Mutagenesisi288 – 2958DYVEKQAS → QSVNEQAQ: No change in receptor activity and HCoV-229E infection. 1 Publication
Mutagenesisi288 – 2958DYVEKQAS → QSVNETAQ: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity. 1 Publication
Mutagenesisi291 – 2933EKQ → NKT: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.
Mutagenesisi291 – 2911E → N: No change of receptor activity and HCoV-229E infection.
Mutagenesisi293 – 2931Q → T: No change of receptor activity and HCoV-229E infection.
Mutagenesisi818 – 8181N → E: Very low receptor activity and HCoV-229E infection. 1 Publication

Organism-specific databases

PharmGKBiPA24815.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 967966Aminopeptidase N
PRO_0000095081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)3 Publications
Modified residuei176 – 1761Sulfotyrosine Reviewed prediction
Glycosylationi234 – 2341N-linked (GlcNAc...)3 Publications
Glycosylationi265 – 2651N-linked (GlcNAc...)4 Publications
Glycosylationi319 – 3191N-linked (GlcNAc...)1 Publication
Modified residuei419 – 4191Sulfotyrosine Reviewed prediction
Modified residuei424 – 4241Sulfotyrosine Reviewed prediction
Glycosylationi527 – 5271N-linked (GlcNAc...)1 Publication
Glycosylationi573 – 5731N-linked (GlcNAc...)1 Publication
Glycosylationi625 – 6251N-linked (GlcNAc...)1 Publication
Glycosylationi681 – 6811N-linked (GlcNAc...)3 Publications
Glycosylationi735 – 7351N-linked (GlcNAc...)
Disulfide bondi761 ↔ 7681 Publication
Disulfide bondi798 ↔ 8341 Publication
Glycosylationi818 – 8181N-linked (GlcNAc...)3 Publications
Modified residuei913 – 9131Sulfotyrosine Reviewed prediction

Post-translational modificationi

Sulfated By similarity.
N- and O-glycosylated.3 Publications
May undergo proteolysis and give rise to a soluble form.

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

MaxQBiP15144.
PaxDbiP15144.
PRIDEiP15144.

PTM databases

PhosphoSiteiP15144.

Expressioni

Tissue specificityi

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.

Inductioni

Estradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively.1 Publication

Gene expression databases

ArrayExpressiP15144.
BgeeiP15144.
CleanExiHS_ANPEP.
GenevestigatoriP15144.

Organism-specific databases

HPAiCAB002417.
HPA004625.

Interactioni

Subunit structurei

Homodimer. Interacts with the S1 domain of HCoV-229E spike protein.4 Publications

Protein-protein interaction databases

BioGridi106787. 2 interactions.
IntActiP15144. 5 interactions.
STRINGi9606.ENSP00000300060.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi70 – 723
Beta strandi73 – 753
Beta strandi78 – 9114
Beta strandi102 – 11514
Beta strandi118 – 1236
Beta strandi135 – 1428
Beta strandi150 – 1567
Turni157 – 1604
Beta strandi161 – 1688
Beta strandi175 – 18511
Beta strandi188 – 20013
Beta strandi203 – 2119
Turni213 – 2164
Helixi217 – 2193
Beta strandi231 – 24010
Beta strandi243 – 2497
Beta strandi251 – 2533
Beta strandi256 – 2583
Beta strandi261 – 2699
Helixi277 – 2793
Beta strandi282 – 2854
Beta strandi288 – 2936
Beta strandi299 – 3046
Helixi306 – 3105
Turni311 – 3144
Helixi315 – 33117
Beta strandi338 – 34811
Beta strandi350 – 3545
Beta strandi359 – 3635
Helixi364 – 3674
Turni371 – 3733
Helixi376 – 39419
Turni396 – 3983
Beta strandi399 – 4035
Helixi404 – 4074
Helixi408 – 42518
Helixi427 – 4293
Helixi431 – 4344
Helixi435 – 4384
Helixi440 – 4478
Helixi459 – 4613
Helixi465 – 4706
Helixi474 – 49118
Helixi493 – 50715
Beta strandi510 – 5123
Helixi514 – 52714
Helixi536 – 5449
Beta strandi550 – 5556
Turni556 – 5594
Beta strandi560 – 5656
Turni579 – 5824
Beta strandi586 – 5883
Beta strandi590 – 5923
Beta strandi600 – 6023
Beta strandi604 – 6085
Helixi610 – 6123
Beta strandi620 – 6234
Helixi624 – 6263
Beta strandi631 – 6344
Helixi636 – 64914
Helixi650 – 6523
Helixi655 – 67016
Helixi676 – 6816
Helixi682 – 6887
Helixi692 – 70918
Helixi715 – 73622
Turni737 – 7415
Helixi747 – 76216
Helixi766 – 78116
Helixi790 – 7923
Helixi793 – 80311
Helixi806 – 81712
Helixi822 – 83211
Helixi838 – 84811
Turni851 – 8533
Helixi856 – 8583
Helixi859 – 86810
Helixi872 – 88211
Helixi884 – 8907
Turni891 – 8944
Helixi898 – 9069
Helixi912 – 92413
Turni925 – 9284
Helixi931 – 9333
Helixi934 – 96532

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FYQX-ray1.90A66-967[»]
4FYRX-ray1.91A66-967[»]
4FYSX-ray2.01A66-967[»]
4FYTX-ray1.85A66-967[»]
ProteinModelPortaliP15144.
SMRiP15144. Positions 66-967.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6836Cytosolic Ser/Thr-rich junction
Add
BLAST
Regioni69 – 967899Metalloprotease
Add
BLAST
Regioni260 – 35394Interaction with HCoV-229E
Add
BLAST
Regioni352 – 3565Substrate binding

Domaini

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).2 Publications

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOVERGENiHBG006616.
InParanoidiP15144.
KOiK11140.
OMAiWVLLNLN.
OrthoDBiEOG754HNR.
PhylomeDBiP15144.
TreeFamiTF300395.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15144-1 [UniParc]FASTAAdd to Basket

« Hide

MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT    50
PSASATTNPA SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL 100
YVFKGSSTVR FTCKEATDVI IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI 150
DKTELVEPTE YLVVHLKGSL VKDSQYEMDS EFEGELADDL AGFYRSEYME 200
GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP KDLTALSNML 250
PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI 300
RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN 350
AGAMENWGLV TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT 400
IEWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA 450
SSHPLSTPAS EINTPAQISE LFDAISYSKG ASVLRMLSSF LSEDVFKQGL 500
ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM NRWTLQMGFP 550
VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY 600
WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH 650
SAIPVINRAQ IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS 700
SLSYFKLMFD RSEVYGPMKN YLKKQVTPLF IHFRNNTNNW REIPENLMDQ 750
YSEVNAISTA CSNGVPECEE MVSGLFKQWM ENPNNNPIHP NLRSTVYCNA 800
IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI LNRYLSYTLN 850
PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN 900
LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW 950
VKENKEVVLQ WFTENSK 967
Length:967
Mass (Da):109,540
Last modified:April 3, 2007 - v4
Checksum:i37B6BC1BF0D6B1F2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201V → M.
Corresponds to variant rs10152474 [ dbSNP | Ensembl ].
VAR_031262
Natural varianti86 – 861R → Q.3 Publications
Corresponds to variant rs25653 [ dbSNP | Ensembl ].
VAR_014736
Natural varianti242 – 2421D → Y.1 Publication
VAR_006727
Natural varianti243 – 2431L → P.1 Publication
VAR_006728
Natural varianti311 – 3111A → V.
Corresponds to variant rs17240268 [ dbSNP | Ensembl ].
VAR_031263
Natural varianti321 – 3211T → M.
Corresponds to variant rs8179199 [ dbSNP | Ensembl ].
VAR_031264
Natural varianti603 – 6031I → K.
Corresponds to variant rs17240212 [ dbSNP | Ensembl ].
VAR_031265
Natural varianti603 – 6031I → M.1 Publication
Corresponds to variant rs8192297 [ dbSNP | Ensembl ].
VAR_031266
Natural varianti752 – 7521S → N.
Corresponds to variant rs25651 [ dbSNP | Ensembl ].
VAR_014737

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti536 – 5361V → E in CAA31640. 1 Publication
Sequence conflicti887 – 8871L → P in CAA31640. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, AJ427986, AJ427987, AJ427988 Genomic DNA. Translation: CAD20931.1.
CCDSiCCDS10356.1.
PIRiA30325.
RefSeqiNP_001141.2. NM_001150.2.
XP_005254949.1. XM_005254892.2.
UniGeneiHs.1239.

Genome annotation databases

EnsembliENST00000300060; ENSP00000300060; ENSG00000166825.
GeneIDi290.
KEGGihsa:290.
UCSCiuc002bop.4. human.

Polymorphism databases

DMDMi143811362.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, AJ427986 , AJ427987 , AJ427988 Genomic DNA. Translation: CAD20931.1 .
CCDSi CCDS10356.1.
PIRi A30325.
RefSeqi NP_001141.2. NM_001150.2.
XP_005254949.1. XM_005254892.2.
UniGenei Hs.1239.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FYQ X-ray 1.90 A 66-967 [» ]
4FYR X-ray 1.91 A 66-967 [» ]
4FYS X-ray 2.01 A 66-967 [» ]
4FYT X-ray 1.85 A 66-967 [» ]
ProteinModelPortali P15144.
SMRi P15144. Positions 66-967.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106787. 2 interactions.
IntActi P15144. 5 interactions.
STRINGi 9606.ENSP00000300060.

Chemistry

BindingDBi P15144.
ChEMBLi CHEMBL1907.
DrugBanki DB00973. Ezetimibe.

Protein family/group databases

MEROPSi M01.001.

PTM databases

PhosphoSitei P15144.

Polymorphism databases

DMDMi 143811362.

Proteomic databases

MaxQBi P15144.
PaxDbi P15144.
PRIDEi P15144.

Protocols and materials databases

DNASUi 290.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300060 ; ENSP00000300060 ; ENSG00000166825 .
GeneIDi 290.
KEGGi hsa:290.
UCSCi uc002bop.4. human.

Organism-specific databases

CTDi 290.
GeneCardsi GC15M090328.
H-InvDB HIX0038141.
HGNCi HGNC:500. ANPEP.
HPAi CAB002417.
HPA004625.
MIMi 151530. gene.
neXtProti NX_P15144.
PharmGKBi PA24815.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0308.
HOVERGENi HBG006616.
InParanoidi P15144.
KOi K11140.
OMAi WVLLNLN.
OrthoDBi EOG754HNR.
PhylomeDBi P15144.
TreeFami TF300395.

Enzyme and pathway databases

BRENDAi 3.4.11.2. 2681.
Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RK P15144.

Miscellaneous databases

GeneWikii Alanine_aminopeptidase.
GenomeRNAii 290.
NextBioi 1183.
PROi P15144.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15144.
Bgeei P15144.
CleanExi HS_ANPEP.
Genevestigatori P15144.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiAMPN_HUMAN
AccessioniPrimary (citable) accession number: P15144
Secondary accession number(s): Q16728
, Q6GT90, Q8IUK3, Q8IVH3, Q9UCE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 174 of the entry and version 4 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

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Peptidase families
    Classification of peptidase families and list of entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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