Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
ARTS1 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ARTS1 Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. Belongs to the peptidase M1 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.11.-; Membrane protein, integral; Protease
Chromosomal Location of Human Ortholog: 5q15
Cellular Component: cytosol; endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; extracellular region; extracellular space; integral to membrane; membrane; plasma membrane
Molecular Function: aminopeptidase activity; interleukin-1, Type II receptor binding; interleukin-6 receptor binding; metalloexopeptidase activity; peptide binding; protein binding; tumor necrosis factor receptor binding; zinc ion binding
Biological Process: adaptive immune response; angiogenesis; antigen processing and presentation of endogenous peptide antigen via MHC class I; antigen processing and presentation of peptide antigen via MHC class I; fat cell differentiation; membrane protein ectodomain proteolysis; peptide catabolic process; positive regulation of angiogenesis; regulation of blood pressure; regulation of innate immune response; response to bacterium
Reference #:  Q9NZ08 (UniProtKB)
Alt. Names/Synonyms: A-LAP; Adipocyte-derived leucine aminopeptidase; ALAP; Aminopeptidase PILS; aminopeptidase regulator of TNFR1 shedding; APPILS; ARTS-1; ARTS1; Endoplasmic reticulum aminopeptidase 1; ERAAP; ERAAP1; ERAP1; KIAA0525; PILS-AP; PILSAP; Puromycin-insensitive leucyl-specific aminopeptidase; Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
Gene Symbols: ERAP1
Molecular weight: 107,235 Da
Basal Isoelectric point: 6.02  Predict pI for various phosphorylation states
Select Structure to View Below

ARTS1

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S179‑p GELRILAsTQFEPtA
0 2 T185‑p AsTQFEPtAARMAFP
0 1 S217 EPRHLAISNMPLVKS
0 1 S268‑p TKSGVKVsVyAVPDK
0 2 Y270‑p SGVKVsVyAVPDKIN
0 1 Y399‑p PELKVGDyFFGKCFD
0 1 S437 REMFDDVSYDKGACI
0 1 Y451 ILNMLREYLSADAFK
0 1 Y464‑p FKSGIVQyLQKHSYK
0 1 H468 IVQyLQKHSYKNtKN
0 1 Y470 QyLQKHSYKNtKNED
0 1 T473‑p QKHSYKNtKNEDLWD
0 1 Y608‑p NVGMNGYyIVHYEDD
0 1 K811‑ac ALCRTQNkEKLQWLL
0 1 K899 KGFFSSLKENGSQLR
  ARTS1 iso2  
S179 GELRILASTQFEPTA
T185 ASTQFEPTAARMAFP
S217 EPRHLAISNMPLVKS
S268 TKSGVKVSVYAVPDK
Y270 SGVKVSVYAVPDKIN
Y399 PELKVGDYFFGKCFD
S437 REMFDDVSYDKGACI
Y451 ILNMLREYLSADAFK
Y464 FKSGIVQYLQKHSYK
H468 IVQYLQKHSYKNTKN
Y470 QYLQKHSYKNTKNED
T473 QKHSYKNTKNEDLWD
Y608 NVGMNGYYIVHYEDD
K811 ALCRTQNKEKLQWLL
K899 KGFFSSLKENGSQLR
  mouse

 
A168 GEMRILAATQFEPTA
T174 AATQFEPTAARMAFP
S206‑p DPRHLAIsNMPLVKS
S257 TKSGVKVSVYAVPDK
Y259 SGVKVSVYAVPDKIN
Y388 PELKVEDYFFGKCFN
S426 REMFDDVSYEKGACI
Y440 ILNMLRDYLSADTFK
Y453 FKRGIVQYLQKYSYK
Y457 IVQYLQKYSYKNTKN
Y459 QYLQKYSYKNTKNED
T462 QKYSYKNTKNEDLWN
Y597 NVGMNGYYIVHYADD
P800 SLCTSKDPEKLQWLL
K888‑ub KGFFSSLkENGSQLR
  rat

 
A168 GERRILAATQFEPTA
T174 AATQFEPTAARMAFP
S206 DPRHLAISNMPLVKS
S257 TKSGVKVSVYAVPDK
Y259 SGVKVSVYAVPDKIN
Y388 PELKVEEYFFGKCFN
S426‑p REMFDEVsYEKGACI
Y440‑p ILNMLRDyLSADTFK
Y453 FKRGIVQYLQKySyK
Y457‑p IVQYLQKySyKNTKN
Y459‑p QYLQKySyKNTKNED
T462 QKySyKNTKNEDLWN
Y597 NVGMNGYYIVHYGDD
P800 SLCISQDPEKLQWLL
K888 KGFFSSLKKNGSQLR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.