Atxn2l
entrez
233871
canonical
uniprot
Q7TQH0
canonical
ensembl
ENSMUSG00000032637
resolver
ensp
ENSMUSP00000035415
resolver
ensp
ENSMUSP00000125881
resolver
ensp
ENSMUSP00000132959
resolver
ensp
ENSMUSP00000146023
resolver
ensp
ENSMUSP00000246330
resolver
ensp
ENSMUSP00000246331
resolver
ensp
ENSMUSP00000246332
resolver
ensp
ENSMUSP00000246333
resolver
ensp
ENSMUSP00000340469
resolver
enst
ENSMUST00000167759
resolver
enst
ENSMUST00000206577
resolver
genesymbol
Atxn2l
resolver
genesymbol_syn
A2lp
resolver
uniprot
A0A0U1RPL0
resolver
uniprot
F6XQL2
resolver
uniprot
Q3TGG2
resolver
uniprot
Q80XN9
resolver
uniprot
Q8K059
resolver
uniprot_entry
A0A0U1RPL0_MOUSE
resolver
uniprot_entry
ATX2L_MOUSE
resolver
uniprot_entry
F6XQL2_MOUSE
resolver
uniprot_entry
Q3TGG2_MOUSE
resolver
uniprot_sec
Q80XN9
resolver
uniprot_sec
Q8K059
resolver
amino_acid_sequence
MLKPQPPQQTSQPQQPPPTQQAVARRSPGGTSPPNGGLPGPLTATAAPPGPPAAVSPCLGPAAAAGSGLRRGAESILAASAPPQHQERPGAVAIGSVRGQTTGKGPPQSPVFEGVYNNSRMLHFLTAVVGSTCDVKVKNGTTYEGIFKTLSSKFELAVDAVHRKASEPAGGPRREDIVDTMVFKPSDVLLVHFRNVDFNYATKDKFTDSAIAMNSKVNGEHKEKVLQRWEGGDSNSDDYDLESDMSNGWDPNEMFKFNEENYGVKTTYDSSLSSYTVPLEKDNSEEFRQRELRAAQLAREIESSPQYRLRIAMENDDGRTEEEKHSAVQRQGSGRESPSLVSREGKYIPLPQRVREGPRGGVRCSSSRGGRPGLSSLPPRGPHHLDNSSPGPGSEARGINGGPSRMSPKAQRPLRGAKTLSSPSNRPSGEASVPPTSAALPFLPVGRMYPPRSPKSAAPAPVSASCPEPPIGSAVASSASIPVTSSVVDPGAGSISPASPKLSLTPTDVKELPTKEPSRNLEAQELARIAGKVPGLQNEQKRFQLEELRKFGAQFKLQPSSSPETGLDPFPSRILKEEAKGKEKEVDGLLTSDPMGSPVSSKTESILDKEDKVPMAGVGGTEGPEQLPAPCPSQTGSPPVGLIKGDEKEEGPVTEQVKKSTLNPNAKEFNPTKPLLSVNKSTSTPTSPGPRTHSTPSIPVLTAGQSGLYSPQYISYIPQIHMGPAVQAPQMYPYPVSNSVPGQQGKYRGAKGSLPPQRSDQHQPASAPPMMQAAAAAAGPPLVAATPYSSYIPYNPQQFPGQPAMMQPMAHYPSQPVFAPMLQSNPRMLTSGSHPQAIVSSSTPQYPAAEQPTPQALYATVHQSYPHHATQLHGHQPQPATTPTGSQPQSQHAAPSPVQHQAGQAPHLGSGQPQQNLYHPGALTGTPPSLPPGPSAQSPQSSFPQPAAVYAIHPHQQLPHGFTNMAHVTQAHVQTGVTAAPPPHPGAPHPPQVMLLHPPQGHGGPPQGAVPPSGVPALSASTPSPYPYIGHPQVQSHPSQQLPFHPPGN
uniprot
proteins
function
FUNCTION: Involved in the regulation of stress granule and P-body formation. {ECO:0000250|UniProtKB:Q8WWM7}.
uniprot
proteins
mass_dalton
110649
uniprot
proteins
post_translational_modification
PTM: Thrombopoietin triggers the phosphorylation on tyrosine residues in a way that is dependent on MPL C-terminal domain. {ECO:0000250}.; PTM: Asymmetrically dimethylated. Probably methylated by PRMT1. {ECO:0000250|UniProtKB:Q8WWM7}.
uniprot
proteins
protein_family
Ataxin-2 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17322884
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
1049
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q8WWM7}. Nucleus speckle {ECO:0000250|UniProtKB:Q8WWM7}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q8WWM7}. Note=Predominantly cytoplasmic but is also detected in nuclear speckles. Component of cytoplasmic stress granules. Inhibition of methylation alters nuclear localization. Methylation does not seem to be required for localization to stress granules under stress conditions. {ECO:0000250|UniProtKB:Q8WWM7}.
uniprot
proteins