CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001663
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Double-stranded RNA-binding protein Staufen homolog 1 
Protein Synonyms/Alias
  
Gene Name
 STAU1 
Gene Synonyms/Alias
 STAU 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
270PRIKKKTKPIVKPQTacetylation[1]
299AQIQQAKKEKEPEYTubiquitination[2]
507QGFQVEYKDFPKNNKubiquitination[3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site. 
Sequence Annotation
 DOMAIN 72 162 DRBM 1.
 DOMAIN 184 251 DRBM 2.
 DOMAIN 286 354 DRBM 3.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 390 390 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Endoplasmic reticulum; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 577 AA 
Protein Sequence
MSQVQVQVQN PSAALSGSQI LNKNQSLLSQ PLMSIPSTTS SLPSENAGRP IQNSALPSAS 60
ITSTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ STYNYNMRGG AYPPRYFYPF 120
PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH DAAAKALRIL QNEPLPERLE VNGRESEEEN 180
LNKSEISQVF EIALKRNLPV NFEVARESGP PHMKNFVTKV SVGEFVGEGE GKSKKISKKN 240
AAIAVLEELK KLPPLPAVER VKPRIKKKTK PIVKPQTSPE YGQGINPISR LAQIQQAKKE 300
KEPEYTLLTE RGLPRRREFV MQVKVGNHTA EGTGTNKKVA KRNAAENMLE ILGFKVPQAQ 360
PTKPALKSEE KTPIKKPGDG RKVTFFEPGS GDENGTSNKE DEFRMPYLSH QQLPAGILPM 420
VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT VTAMIARELL YGGTSPTAET ILKNNISSGH 480
VPHGPLTRPS EQLDYLSRVQ GFQVEYKDFP KNNKNEFVSL INCSSQPPLI SHGIGKDVES 540
CHDMAALNIL KLLSELDQQS TEMPRTGNGP MSVCGRC 577 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; ISS:BHF-UCL.
 GO:0005875; C:microtubule associated complex; TAS:ProtInc.
 GO:0005791; C:rough endoplasmic reticulum; TAS:ProtInc.
 GO:0003725; F:double-stranded RNA binding; TAS:ProtInc.
 GO:0008298; P:intracellular mRNA localization; IEA:Compara. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom. 
Pfam
 PF00035; dsrm 
SMART
 SM00358; DSRM 
PROSITE
 PS50137; DS_RBD 
PRINTS