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Protein Page:
UPP1 (human)
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
UPP1 Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Belongs to the PNP/UDP phosphorylase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Xenobiotic Metabolism - drug metabolism - other enzymes; EC 2.4.2.3; Nucleotide Metabolism - pyrimidine; Transferase
Chromosomal Location of Human Ortholog: 7p12.3
Cellular Component: cytosol
Molecular Function: uridine phosphorylase activity
Biological Process: nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; pyrimidine nucleoside catabolic process; pyrimidine nucleoside salvage
Reference #:  Q16831 (UniProtKB)
Alt. Names/Synonyms: UDRPASE; UP; UPASE; UPase 1; UPP; UPP1; UrdPase 1; Uridine phosphorylase 1
Gene Symbols: UPP1
Molecular weight: 33,934 Da
Basal Isoelectric point: 8.17  Predict pI for various phosphorylation states
Select Structure to View Below

UPP1

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



 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

 
0 9 Y35‑p KMKEDILyHFNLTTS
0 4 S61‑p KFVCVGGsPsRMKAF
0 1 S63‑p VCVGGsPsRMKAFIR
0 1 K66 GGsPsRMKAFIRCVG
0 1 R83 LGLDCPGRDYPNICA
0 1 K232‑ub CSYTEKDkQAYLEAA
0 1 S283‑p LEGDQISsPRNVLSE
  mouse

 
Y36 AMKEDVLYHFNLSTS
S62 KFVCVGGSSSRMNTF
S64 VCVGGSSSRMNTFIK
N67 GGSSSRMNTFIKYVA
K84 LGLDHPGKEYPNICA
K233 CSYTEKDKQSYLRAA
T284 LQGDQINTPHDVLVE
  rat

 
Y37 TMKEDVLYHFNLSTS
S63 KFVCVGGSSSRMsAF
S65 VCVGGSSSRMsAFIK
S68‑p GGSSSRMsAFIKYVA
K85‑ac LGLDHPGkEYPNICA
K234 CSYTEKDKQAYLRAA
T285 LQGDQINTPHNVLVE
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