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P15144

- AMPN_HUMAN

UniProt

P15144 - AMPN_HUMAN

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Protein

Aminopeptidase N

Gene

ANPEP

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.5 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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi388 – 3881Zinc; catalytic
Active sitei389 – 3891Proton acceptor1 PublicationPROSITE-ProRule annotation
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

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 Curated
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 proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 967935ExtracellularAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  2. external side of plasma membrane Source: Ensembl
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. integral component of plasma membrane Source: ProtInc
  6. 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 NPRO_0000095081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)3 Publications
Modified residuei176 – 1761SulfotyrosineSequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)3 Publications
Glycosylationi265 – 2651N-linked (GlcNAc...)4 Publications
Glycosylationi319 – 3191N-linked (GlcNAc...)1 Publication
Modified residuei419 – 4191SulfotyrosineSequence Analysis
Modified residuei424 – 4241SulfotyrosineSequence Analysis
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 – 9131SulfotyrosineSequence Analysis

Post-translational modificationi

Sulfated.By similarity
N- and O-glycosylated.6 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

BgeeiP15144.
CleanExiHS_ANPEP.
ExpressionAtlasiP15144. baseline and differential.
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

1
967
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi70 – 723Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 9114Combined sources
Beta strandi102 – 11514Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi150 – 1567Combined sources
Turni157 – 1604Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi175 – 18511Combined sources
Beta strandi188 – 20013Combined sources
Beta strandi203 – 2119Combined sources
Turni213 – 2164Combined sources
Helixi217 – 2193Combined sources
Beta strandi231 – 24010Combined sources
Beta strandi243 – 2497Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi261 – 2699Combined sources
Helixi277 – 2793Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi299 – 3046Combined sources
Helixi306 – 3105Combined sources
Turni311 – 3144Combined sources
Helixi315 – 33117Combined sources
Beta strandi338 – 34811Combined sources
Beta strandi350 – 3545Combined sources
Beta strandi359 – 3635Combined sources
Helixi364 – 3674Combined sources
Turni371 – 3733Combined sources
Helixi376 – 39419Combined sources
Turni396 – 3983Combined sources
Beta strandi399 – 4035Combined sources
Helixi404 – 4074Combined sources
Helixi408 – 42518Combined sources
Helixi427 – 4293Combined sources
Helixi431 – 4344Combined sources
Helixi435 – 4384Combined sources
Helixi440 – 4478Combined sources
Helixi459 – 4613Combined sources
Helixi465 – 4706Combined sources
Helixi474 – 49118Combined sources
Helixi493 – 50715Combined sources
Beta strandi510 – 5123Combined sources
Helixi514 – 52714Combined sources
Helixi536 – 5449Combined sources
Beta strandi550 – 5556Combined sources
Turni556 – 5594Combined sources
Beta strandi560 – 5656Combined sources
Turni579 – 5824Combined sources
Beta strandi586 – 5883Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi604 – 6085Combined sources
Helixi610 – 6123Combined sources
Beta strandi620 – 6234Combined sources
Helixi624 – 6263Combined sources
Beta strandi631 – 6344Combined sources
Helixi636 – 64914Combined sources
Helixi650 – 6523Combined sources
Helixi655 – 67016Combined sources
Helixi676 – 6816Combined sources
Helixi682 – 6887Combined sources
Helixi692 – 70918Combined sources
Helixi715 – 73622Combined sources
Turni737 – 7415Combined sources
Helixi747 – 76216Combined sources
Helixi766 – 78116Combined sources
Helixi790 – 7923Combined sources
Helixi793 – 80311Combined sources
Helixi806 – 81712Combined sources
Helixi822 – 83211Combined sources
Helixi838 – 84811Combined sources
Turni851 – 8533Combined sources
Helixi856 – 8583Combined sources
Helixi859 – 86810Combined sources
Helixi872 – 88211Combined sources
Helixi884 – 8907Combined sources
Turni891 – 8944Combined sources
Helixi898 – 9069Combined sources
Helixi912 – 92413Combined sources
Turni925 – 9284Combined sources
Helixi931 – 9333Combined sources
Helixi934 – 96532Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6836Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni69 – 967899MetalloproteaseAdd
BLAST
Regioni260 – 35394Interaction with HCoV-229EAdd
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).

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
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

        10         20         30         40         50
MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT
60 70 80 90 100
PSASATTNPA SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL
110 120 130 140 150
YVFKGSSTVR FTCKEATDVI IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI
160 170 180 190 200
DKTELVEPTE YLVVHLKGSL VKDSQYEMDS EFEGELADDL AGFYRSEYME
210 220 230 240 250
GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP KDLTALSNML
260 270 280 290 300
PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI
310 320 330 340 350
RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN
360 370 380 390 400
AGAMENWGLV TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT
410 420 430 440 450
IEWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA
460 470 480 490 500
SSHPLSTPAS EINTPAQISE LFDAISYSKG ASVLRMLSSF LSEDVFKQGL
510 520 530 540 550
ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM NRWTLQMGFP
560 570 580 590 600
VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY
610 620 630 640 650
WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH
660 670 680 690 700
SAIPVINRAQ IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS
710 720 730 740 750
SLSYFKLMFD RSEVYGPMKN YLKKQVTPLF IHFRNNTNNW REIPENLMDQ
760 770 780 790 800
YSEVNAISTA CSNGVPECEE MVSGLFKQWM ENPNNNPIHP NLRSTVYCNA
810 820 830 840 850
IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI LNRYLSYTLN
860 870 880 890 900
PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN
910 920 930 940 950
LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW
960
VKENKEVVLQ WFTENSK
Length:967
Mass (Da):109,540
Last modified:April 3, 2007 - v4
Checksum:i37B6BC1BF0D6B1F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti536 – 5361V → E in CAA31640. (PubMed:2901990)Curated
Sequence conflicti887 – 8871L → P in CAA31640. (PubMed:2901990)Curated

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

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

Chemistry

BindingDBi P15144.
ChEMBLi CHEMBL1907.
DrugBanki DB00973. Ezetimibe.
DB06196. Icatibant.

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.
GeneTreei ENSGT00760000119082.
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

ChiTaRSi ANPEP. human.
GeneWikii Alanine_aminopeptidase.
GenomeRNAii 290.
NextBioi 1183.
PROi P15144.
SOURCEi Search...

Gene expression databases

Bgeei P15144.
CleanExi HS_ANPEP.
ExpressionAtlasi P15144. baseline and differential.
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: November 26, 2014
This is version 177 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