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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
(Microbial infection) Acts as a receptor for human coronavirus 229E/HCoV-229E.2 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)DescriptionActionsGraphical viewLength
Metal bindingi388Zinc; catalytic1
Active sitei389Proton acceptorPROSITE-ProRule annotation1 Publication1
Metal bindingi392Zinc; catalytic1
Metal bindingi411Zinc; catalytic1
Sitei477Transition state stabilizer1

GO - Molecular functioni

  • aminopeptidase activity Source: ProtInc
  • metalloaminopeptidase activity Source: GO_Central
  • metallopeptidase activity Source: ProtInc
  • peptide binding Source: GO_Central
  • receptor activity Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW
  • zinc ion binding Source: GO_Central

GO - Biological processi

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

BioCyciZFISH:HS09457-MONOMER.
BRENDAi3.4.11.2. 2681.
ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP15144.
SIGNORiP15144.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:500. ANPEP.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8Cytoplasmic7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 967ExtracellularAdd BLAST935

GO - Cellular componenti

  • cytosol Source: UniProtKB-SubCell
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi288 – 295DYVEKQAS → QSVEETAQ: No change in receptor activity and HCoV-229E infection. 1 Publication8
Mutagenesisi288 – 295DYVEKQAS → QSVNEQAQ: No change in receptor activity and HCoV-229E infection. 1 Publication8
Mutagenesisi288 – 295DYVEKQAS → QSVNETAQ: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity. 1 Publication8
Mutagenesisi291 – 293EKQ → NKT: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity. 3
Mutagenesisi291E → N: No change of receptor activity and HCoV-229E infection. 1
Mutagenesisi293Q → T: No change of receptor activity and HCoV-229E infection. 1
Mutagenesisi818N → E: Very low receptor activity and HCoV-229E infection. 1 Publication1

Organism-specific databases

DisGeNETi290.
OpenTargetsiENSG00000166825.
PharmGKBiPA24815.

Chemistry databases

ChEMBLiCHEMBL1907.
DrugBankiDB00973. Ezetimibe.
DB06196. Icatibant.
GuidetoPHARMACOLOGYi1560.

Polymorphism and mutation databases

BioMutaiANPEP.
DMDMi143811362.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000950812 – 967Aminopeptidase NAdd BLAST966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi128N-linked (GlcNAc...)3 Publications1
Modified residuei176SulfotyrosineSequence analysis1
Glycosylationi234N-linked (GlcNAc...)3 Publications1
Glycosylationi265N-linked (GlcNAc...)4 Publications1
Glycosylationi319N-linked (GlcNAc...)1 Publication1
Modified residuei419SulfotyrosineSequence analysis1
Modified residuei424SulfotyrosineSequence analysis1
Glycosylationi527N-linked (GlcNAc...)1 Publication1
Glycosylationi573N-linked (GlcNAc...)1 Publication1
Glycosylationi625N-linked (GlcNAc...)1 Publication1
Glycosylationi681N-linked (GlcNAc...)3 Publications1
Glycosylationi735N-linked (GlcNAc...)1
Disulfide bondi761 ↔ 7681 Publication
Disulfide bondi798 ↔ 8341 Publication
Glycosylationi818N-linked (GlcNAc...)3 Publications1
Modified residuei913SulfotyrosineSequence analysis1

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

EPDiP15144.
MaxQBiP15144.
PaxDbiP15144.
PeptideAtlasiP15144.
PRIDEiP15144.

PTM databases

iPTMnetiP15144.
PhosphoSitePlusiP15144.
SwissPalmiP15144.
UniCarbKBiP15144.

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

BgeeiENSG00000166825.
CleanExiHS_ANPEP.
ExpressionAtlasiP15144. baseline and differential.
GenevisibleiP15144. HS.

Organism-specific databases

HPAiCAB002417.
HPA004625.

Interactioni

Subunit structurei

Homodimer.2 Publications
(Microbial infection) Interacts with the S1 domain of human coronavirus 229E/HCoV-229E spike protein (PubMed:1350662, PubMed:12551991).2 Publications

Protein-protein interaction databases

BioGridi106787. 2 interactors.
IntActiP15144. 5 interactors.
STRINGi9606.ENSP00000300060.

Chemistry databases

BindingDBiP15144.

Structurei

Secondary structure

1967
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi70 – 72Combined sources3
Beta strandi73 – 75Combined sources3
Beta strandi78 – 91Combined sources14
Beta strandi102 – 115Combined sources14
Beta strandi118 – 123Combined sources6
Beta strandi135 – 142Combined sources8
Beta strandi150 – 156Combined sources7
Turni157 – 160Combined sources4
Beta strandi161 – 168Combined sources8
Beta strandi175 – 185Combined sources11
Beta strandi188 – 200Combined sources13
Beta strandi203 – 211Combined sources9
Turni213 – 216Combined sources4
Helixi217 – 219Combined sources3
Beta strandi231 – 240Combined sources10
Beta strandi243 – 249Combined sources7
Beta strandi251 – 253Combined sources3
Beta strandi256 – 258Combined sources3
Beta strandi261 – 269Combined sources9
Helixi277 – 279Combined sources3
Beta strandi282 – 285Combined sources4
Beta strandi288 – 293Combined sources6
Beta strandi299 – 304Combined sources6
Helixi306 – 310Combined sources5
Turni311 – 314Combined sources4
Helixi315 – 331Combined sources17
Beta strandi338 – 348Combined sources11
Beta strandi350 – 354Combined sources5
Beta strandi359 – 363Combined sources5
Helixi364 – 367Combined sources4
Turni371 – 373Combined sources3
Helixi376 – 394Combined sources19
Turni396 – 398Combined sources3
Beta strandi399 – 403Combined sources5
Helixi404 – 407Combined sources4
Helixi408 – 425Combined sources18
Helixi427 – 429Combined sources3
Helixi431 – 434Combined sources4
Helixi435 – 438Combined sources4
Helixi440 – 447Combined sources8
Helixi459 – 461Combined sources3
Helixi465 – 470Combined sources6
Helixi474 – 491Combined sources18
Helixi493 – 507Combined sources15
Beta strandi510 – 512Combined sources3
Helixi514 – 527Combined sources14
Helixi536 – 544Combined sources9
Beta strandi550 – 555Combined sources6
Turni556 – 559Combined sources4
Beta strandi560 – 565Combined sources6
Turni579 – 582Combined sources4
Beta strandi586 – 588Combined sources3
Beta strandi590 – 592Combined sources3
Beta strandi600 – 602Combined sources3
Beta strandi604 – 608Combined sources5
Helixi610 – 612Combined sources3
Beta strandi620 – 623Combined sources4
Helixi624 – 626Combined sources3
Beta strandi631 – 634Combined sources4
Helixi636 – 649Combined sources14
Helixi650 – 652Combined sources3
Helixi655 – 670Combined sources16
Helixi676 – 681Combined sources6
Helixi682 – 688Combined sources7
Helixi692 – 709Combined sources18
Helixi715 – 736Combined sources22
Turni737 – 741Combined sources5
Helixi747 – 762Combined sources16
Helixi766 – 781Combined sources16
Helixi790 – 792Combined sources3
Helixi793 – 803Combined sources11
Helixi806 – 817Combined sources12
Helixi822 – 832Combined sources11
Helixi838 – 848Combined sources11
Turni851 – 853Combined sources3
Helixi856 – 858Combined sources3
Helixi859 – 868Combined sources10
Helixi872 – 882Combined sources11
Helixi884 – 890Combined sources7
Turni891 – 894Combined sources4
Helixi898 – 906Combined sources9
Helixi912 – 924Combined sources13
Turni925 – 928Combined sources4
Helixi931 – 933Combined sources3
Helixi934 – 965Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FYQX-ray1.90A66-967[»]
4FYRX-ray1.91A66-967[»]
4FYSX-ray2.01A66-967[»]
4FYTX-ray1.85A66-967[»]
ProteinModelPortaliP15144.
SMRiP15144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 68Cytosolic Ser/Thr-rich junctionAdd BLAST36
Regioni69 – 967MetalloproteaseAdd BLAST899
Regioni260 – 353Interaction with HCoV-229EAdd BLAST94
Regioni352 – 356Substrate binding5

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

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOVERGENiHBG006616.
InParanoidiP15144.
KOiK11140.
OMAiQISEMFD.
OrthoDBiEOG091G01GH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti536V → E in CAA31640 (PubMed:2901990).Curated1
Sequence conflicti887L → P in CAA31640 (PubMed:2901990).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03126220V → M.Corresponds to variant rs10152474dbSNPEnsembl.1
Natural variantiVAR_01473686R → Q.3 PublicationsCorresponds to variant rs25653dbSNPEnsembl.1
Natural variantiVAR_006727242D → Y.1 Publication1
Natural variantiVAR_006728243L → P.1 Publication1
Natural variantiVAR_031263311A → V.Corresponds to variant rs17240268dbSNPEnsembl.1
Natural variantiVAR_031264321T → M.Corresponds to variant rs8179199dbSNPEnsembl.1
Natural variantiVAR_031265603I → K.Corresponds to variant rs17240212dbSNPEnsembl.1
Natural variantiVAR_031266603I → M.1 PublicationCorresponds to variant rs8192297dbSNPEnsembl.1
Natural variantiVAR_014737752S → N.Corresponds to variant rs25651dbSNPEnsembl.1

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_005254892.4.
XP_011519775.1. XM_011521473.1.
UniGeneiHs.1239.

Genome annotation databases

EnsembliENST00000300060; ENSP00000300060; ENSG00000166825.
GeneIDi290.
KEGGihsa:290.
UCSCiuc002bop.5. human.

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.
CCDSiCCDS10356.1.
PIRiA30325.
RefSeqiNP_001141.2. NM_001150.2.
XP_005254949.1. XM_005254892.4.
XP_011519775.1. XM_011521473.1.
UniGeneiHs.1239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FYQX-ray1.90A66-967[»]
4FYRX-ray1.91A66-967[»]
4FYSX-ray2.01A66-967[»]
4FYTX-ray1.85A66-967[»]
ProteinModelPortaliP15144.
SMRiP15144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106787. 2 interactors.
IntActiP15144. 5 interactors.
STRINGi9606.ENSP00000300060.

Chemistry databases

BindingDBiP15144.
ChEMBLiCHEMBL1907.
DrugBankiDB00973. Ezetimibe.
DB06196. Icatibant.
GuidetoPHARMACOLOGYi1560.

Protein family/group databases

MEROPSiM01.001.

PTM databases

iPTMnetiP15144.
PhosphoSitePlusiP15144.
SwissPalmiP15144.
UniCarbKBiP15144.

Polymorphism and mutation databases

BioMutaiANPEP.
DMDMi143811362.

Proteomic databases

EPDiP15144.
MaxQBiP15144.
PaxDbiP15144.
PeptideAtlasiP15144.
PRIDEiP15144.

Protocols and materials databases

DNASUi290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300060; ENSP00000300060; ENSG00000166825.
GeneIDi290.
KEGGihsa:290.
UCSCiuc002bop.5. human.

Organism-specific databases

CTDi290.
DisGeNETi290.
GeneCardsiANPEP.
H-InvDBHIX0038141.
HGNCiHGNC:500. ANPEP.
HPAiCAB002417.
HPA004625.
MIMi151530. gene.
neXtProtiNX_P15144.
OpenTargetsiENSG00000166825.
PharmGKBiPA24815.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOVERGENiHBG006616.
InParanoidiP15144.
KOiK11140.
OMAiQISEMFD.
OrthoDBiEOG091G01GH.
PhylomeDBiP15144.
TreeFamiTF300395.

Enzyme and pathway databases

BioCyciZFISH:HS09457-MONOMER.
BRENDAi3.4.11.2. 2681.
ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP15144.
SIGNORiP15144.

Miscellaneous databases

ChiTaRSiANPEP. human.
GeneWikiiAlanine_aminopeptidase.
GenomeRNAii290.
PROiP15144.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166825.
CleanExiHS_ANPEP.
ExpressionAtlasiP15144. baseline and differential.
GenevisibleiP15144. HS.

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]
ProtoNetiSearch...

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 30, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.