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Protein Page:
hnRNP A0 (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
hnRNP A0 a ubiquitously expressed heterogeneous nuclear ribonucleoprotein (hnRNP) of the A/B subfamily. hnRNPs are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. Has two repeats of RNA recognition motif domains (RRM), followed by a glycine-rich C-terminus. Note: This description may include information from UniProtKB.
Protein type: RNA binding protein; RNA splicing
Cellular Component: nucleoplasm; nucleus; ribonucleoprotein complex
Molecular Function: RNA binding; nucleotide binding; AU-rich element binding; protein kinase binding
Biological Process: nuclear mRNA splicing, via spliceosome; RNA splicing; gene expression; response to lipopolysaccharide; inflammatory response; mRNA processing
Reference #:  Q13151 (UniProtKB)
Alt. Names/Synonyms: Heterogeneous nuclear ribonucleoprotein A0; hnRNA binding protein; hnRNP A0; HNRNPA0; HNRPA0; ROA0
Gene Symbols: HNRNPA0
Molecular weight: 30,841 Da
Basal Isoelectric point: 9.34  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

hnRNP A0

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 2 S19-p GGLNVQTsESGLRGH
0 14 K45-u VVVNPQTkRSRCFGF
0 1 S68-p ADAAMAAsPHAVDGN
0 1 T76-p PHAVDGNtVELKRAV
1 3 S84-p VELKRAVsREDSARP
0 2 K99-u GAHAKVKkLFVGGLk
0 8 K106-u kLFVGGLkGDVAEGD
0 20 K133-u KAEIIADkQSGKKrG
0 2 R139-m1 DkQSGKKrGFGFVyF
0 16 Y145-p KrGFGFVyFQNHDAA
0 2 N148 FGFVyFQNHDAADKA
0 2 K159-u ADKAAVVkFHPIQGH
0 564 Y180-p AVPKEDIysGGGGGG
0 17 S181-p VPKEDIysGGGGGGs
0 1 S188-p sGGGGGGsrSSRGGR
0 2 - gap
0 4 R189-m1 GGGGGGsrSSRGGRG
0 2 Y217-p SKGGGGGyNSYGGYG
0 1 S279-p GGGGGGGsSWGGrSN
0 3 R284-m1 GGsSWGGrSNSGPYr
0 26 R291-m1 rSNSGPYrGGYGGGG
0 41 R291-m2 rSNSGPYrGGYGGGG
0 1 S304 GGGYGGSSF______
  mouse

 
S19 GGLNVQTSESGLRGH
K45 VVVNPQTKRSRCFGF
S68 ADAAMAASPHAVDGN
T76 PHAVDGNTVELKRAV
S84-p VELKRAVsREDSARP
K99-u GAHAKVKkLFVGGLK
K106 kLFVGGLKGDVAEGD
K133-u KAEIIADkQSGKKrG
R139-m1 DkQSGKKrGFGFVYF
Y145 KrGFGFVYFQsHDAA
S148-p FGFVYFQsHDAADKA
K159 ADKAAVVKFHPIQGH
H180 AVPKEDIHAGGGGAr
A181 VPKEDIHAGGGGArA
A186 IHAGGGGArAARGGR
R187-m1 HAGGGGArAARGGRG
R190 GGGArAARGGRGGGR
Y224-p GGGGGGGyNSYGGYG
S282 GGGGGGGSWGGrSNS
R286-m1 GGGSWGGrSNSGPYr
R293-m1 rSNSGPYrGGYGGGY
R293-m2 rSNSGPYrGGYGGGY
S304-p GGGYGGGsF______
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