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Protein Page:
UBR1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
UBR1 E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Defects in UBR1 are a cause of Johanson-Blizzard syndrome (JBS). This disorder includes congenital exocrine pancreatic insufficiency, multiple malformations such as nasal wing aplasia, and frequent mental retardation. Pancreas of individuals with JBS do not express UBR1 and show intrauterine- onset destructive pancreatitis. Belongs to the UBR1 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.19; EC 6.3.2.-; Ubiquitin ligase; Ligase; Ubiquitin conjugating system
Cellular Component: proteasome complex; cytosol; ubiquitin ligase complex
Molecular Function: zinc ion binding; ubiquitin-protein ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; negative regulation of TOR signaling pathway
Reference #:  Q8IWV7 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase UBR1; E3a ligase; JBS; MGC142065; MGC142067; N-recognin-1; ubiquitin ligase E3 alpha-I; ubiquitin protein ligase E3 component n-recognin 1; ubiquitin-protein ligase E3-alpha; Ubiquitin-protein ligase E3-alpha-1; Ubiquitin-protein ligase E3-alpha-I; UBR1
Gene Symbols: UBR1
Molecular weight: 200,211 Da
Basal Isoelectric point: 5.67  Predict pI for various phosphorylation states
Select Structure to View Below

UBR1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: 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.


 MS 

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


       human

 
0 4 S15-p GTERMEIsAELPQtP
0 86 T21-p IsAELPQtPQRLASW
0 1 K458-u EYLDRNNkFNFQGYS
0 1 K468-u FQGYSQDkLGRVYAV
0 11 K806-u GLENVINkVATFKKP
0 2 K855-u HMQKKRRkQENKDEA
0 1 K944 VTFDFYHKASRLGSS
0 7 S1179-p FEAVQLSsQQRIHVD
0 2 Y1302-p ILFATTIyRIGLKVP
0 1 N1576 CADPALLNCLKQKNT
0 7 S1593-p RYPRKRNsLIELPDD
0 2 K1681-u RVVLVEGkARGCAYP
0 1 K1703 GETDPGLKRGNPLHL
  mouse

 
S15-p GAERMDVsPEPPLAP
A21 VsPEPPLAPQRPASW
K458 EYLDRNNKFNFQGYS
K468 FQGYSQDKLGRVYAV
K806-u GLENVINkVATFKKP
K855 HMQKKRRKQENKDEA
K944-u VAFDFYHkASRLGSS
S1182 FEAVQLSSQQRIHVD
Y1306 ILFATTIYRIGLKVP
K1584-u CGDPALLkSLKQKSA
S1601-p RYPRKRNsLIELPED
K1689 RVVLVEGKARGCAYP
K1711-u GETDPGLkRGNPLHL
  rat

 
S15 GAERMDVSPEPPLAP
A21 VSPEPPLAPQPPASW
K458 EYLDRNNKFNFQGYS
K468 FQGYSQDKLGRVYAV
K806 GLENVINKVATFKKP
K855 HMQKKRRKQENKDEA
K944 VAFDFYHKASRLGSS
S1182 FEAVQLSSQQRIHID
Y1296 ILFATTIYRIGLKVP
N1574 CGDPALLNSLKQKSA
S1591 RYPRKRNSLIELPDD
K1679 RVVLVEGKARGCAYP
K1701 GETDPGLKRGNPLHL
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