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Protein Page:
ARIH2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ARIH2 E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys- 63'-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis. Belongs to the RBR family. Ariadne subfamily. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Ligase; EC 6.3.2.-; Ubiquitin conjugating system
Cellular Component: cytoplasm; nucleus
Molecular Function: protein binding; nucleic acid binding; zinc ion binding; ubiquitin-protein ligase activity; ligase activity
Biological Process: developmental cell growth; protein polyubiquitination; multicellular organismal development; protein ubiquitination during ubiquitin-dependent protein catabolic process
Reference #:  O95376 (UniProtKB)
Alt. Names/Synonyms: all-trans retinoic acid inducible RING finger; ARI-2; ARI2; ariadne homolog 2 (Drosophila); ARIH2; FLJ10938; FLJ33921; Protein ariadne-2 homolog; TRIAD1; Triad1 protein
Gene Symbols: ARIH2
Molecular weight: 57,819 Da
Basal Isoelectric point: 5.4  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ARIH2

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 5 Y337-p WKTHGSEyyECSRYk
0 7 Y338-p KTHGSEyyECSRYkE
0 1 K344-ub yyECSRYkENPDIVN
0 32 S353-p NPDIVNQsQQAQARE
0 2 K364-ub QAREALKkYLFYFER
0 15 K377-ub ERWENHNkSLQLEAQ
0 2 K419-ub NAAKLLAkCRYTLQY
0 1 Y428-p RYTLQYTyPYAyyME
0 1 Y432-p QYTyPYAyyMESGPR
0 1 Y433-p YTyPYAyyMESGPRK
0 6 K460-ub EIENLSWkVERADsY
0 1 S466-p WkVERADsYDRGDLE
  mouse

 
Y336 WKTHGSEYYECSRYK
Y337 KTHGSEYYECSRYKE
K343 YYECSRYKENPDIVN
S352-p NPDIVNQsQQAQARE
K363 QAREALKKYLFYFER
K376-ub ERWENHNkSLQLEAQ
K418-ub NAAKLLAkCRYTLQY
Y427 RYTLQYTYPYAYYME
Y431 QYTYPYAYYMESGPR
Y432 YTYPYAYYMESGPRK
K459-ub EIENLSWkVERADSY
S465 WkVERADSYDRGDLE
  rat

 
Y336 WKTHGSEYYECSRYK
Y337 KTHGSEYYECSRYKE
K343 YYECSRYKENPDIVN
S352 NPDIVNQSQQAQARE
K363 QAREALKKYLFYFER
K376 ERWENHNKSLQLEAQ
K418 NAAKLLAKCRYTLQY
Y427 RYTLQYTYPYAYYME
Y431 QYTYPYAYYMESGPR
Y432 YTYPYAYYMESGPRK
K459 EIENLSWKVERADSY
S465 WKVERADSYDRGDLE
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