Protein detail

AMPN

Aminopeptidase N (AP-N) (hAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (Myeloid plasma membrane glycoprotein CD13) (gp150) (CD antigen CD13)

Protein symbol
AMPN
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
1
Protein classification
CD markersEnzymesMetabolic proteinsPlasma proteinsPredicted membrane proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Aminopeptidase N (AP-N) (hAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (Myeloid plasma membrane glycoprotein CD13) (gp150) (CD antigen CD13)
Protein Class
CD markersEnzymesMetabolic proteinsPlasma proteinsPredicted membrane proteins
Protein Function
  • Peptidases:Metallopeptidases
  • Enzymes
  • CD markers
  • ENZYME proteins:Hydrolases
Transmembrane
9..32; Helical; Signal-anchor for type II membrane protein
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
AP-NCD13gp150hAPNLAP1p150PEPN
Gene Description
Alanyl aminopeptidase, membrane
Chromosome
15
Position
89784895-89815401
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificAdrenal cortex cellsSecretome LocationIntracellular and membraneSecretome FunctionReceptor
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

38 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
cell_adhesionligandICELLNETYesNoNoYesNo
ligandligandOmniPathYesNoNoYesNo
receptorreceptorscConnectNoYesNoYesNo
receptorreceptorCellCellInteractionsNoYesNoYesNo
transmembranetransmembrane_predictedPhobiusNoNoNoYesNo
transmembrane_phobiustransmembrane_predictedAlmen2009NoNoNoYesNo
transmembrane_sosuitransmembrane_predictedAlmen2009NoNoNoYesNo
transmembrane_tmhmmtransmembrane_predictedAlmen2009NoNoNoYesNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

3 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
AGTANPEPP01019P151441:1PDBPDB:4fys
ANPEPP151444PDBPDB:5lhdPDB:9caoPDB:9cam
ANPEPSFNP15144P319472:1PDBPDB:7aewPDB:6xwd

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationDensity Gradient CentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographySmall R sequencing (Illumi HiSeq 2000 (Solexa)Mass spectrometry1637786918398737263481790632795414387318682898658530608700337095103832153541201090307605383208974340311616398353864009145533709510
Sequence, Structure & Domains

Sequences

Length
967
Mass
109,540
Sequence
MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK

3D Structural Models

Turn
157..160; 213..216; 311..314; 371..373; 396..398; 556..559; 579..582; 737..741; 851..853; 891..894; 925..928
Helix
70..72; 217..219; 277..279; 306..310; 315..331; 364..367; 376..394; 404..407; 408..425; 427..429; 431..434; 435..438; 440..447; 459..461; 465..470; 474..491; 493..507; 514..527; 536..544; 610..612; 624..626; 636..649; 650..652; 655..670; 676..681; 682..688; 692..709; 715..736; 747..762; 766..781; 790..792; 793..803; 806..817; 822..832; 838..848; 856..858; 859..868; 872..882; 884..890; 898..906; 912..924; 931..933; 934..965
Beta Strand
73..75; 78..91; 102..115; 118..123; 126..129; 135..142; 150..156; 161..168; 175..185; 188..200; 203..211; 231..240; 243..249; 251..253; 256..258; 261..269; 282..285; 288..293; 299..304; 338..348; 350..354; 359..363; 399..403; 510..512; 550..555; 560..565; 586..588; 590..592; 600..602; 604..608; 620..623; 631..634; 742..746
3D Structure
Electron microscopy (3); X-ray crystallography (12)

Domain & Motif Annotations

Compositional Bias
41..62; Low complexity
Region
33..68; Cytosolic Ser/Thr-rich junction; 40..62; Disordered; 69..967; Metalloprotease; 288..295; Necessary and sufficient to mediate interaction with HCoV-229E
Protein Families
Peptidase M1 family
Sequence Similarities
Belongs to the peptidase M1 family.
Clinical Relevance