CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022160
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Double-stranded RNA-binding protein Staufen homolog 2 
Protein Synonyms/Alias
  
Gene Name
 STAU2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
60SEGSSIKKAQQAVANubiquitination[1]
106ELNGLAMKRGEPAIYubiquitination[1, 2]
257AEGEGNSKKLSKKRAubiquitination[1]
283PPLPVVEKPKLFFKKubiquitination[3]
297KRPKTIVKAGPEYGQubiquitination[1, 3, 4]
358ATGTGPNKKIAKKNAubiquitination[1]
359TGTGPNKKIAKKNAAubiquitination[3]
387NLQDQLEKTGENKGWubiquitination[3]
392LEKTGENKGWSGPKPubiquitination[3]
429EMEASRHKVISGTTLubiquitination[2, 4]
498CSPVQPSKQLEYLARubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 RNA-binding protein required for the microtubule- dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity). 
Sequence Annotation
 DOMAIN 8 75 DRBM 1.
 DOMAIN 95 181 DRBM 2.
 DOMAIN 207 274 DRBM 3.
 DOMAIN 307 375 DRBM 4.
 REGION 381 570 Required for dendritic transport (By
 MOTIF 273 291 Nuclear localization signal 1 (By
 MOTIF 373 412 Nuclear localization signal 2 (By
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 405 405 Phosphothreonine.
 MOD_RES 416 416 Phosphoserine.
 MOD_RES 426 426 Phosphoserine.
 MOD_RES 440 440 Phosphoserine.
 MOD_RES 455 455 Phosphoserine.
 MOD_RES 492 492 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Endoplasmic reticulum; Microtubule; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 570 AA 
Protein Sequence
MANPKEKTAM CLVNELARFN RVQPQYKLLN ERGPAHSKMF SVQLSLGEQT WESEGSSIKK 60
AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP 120
FPNYRANYNF RGMYNQRYHC PVPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ 180
NEPIPERSPQ NGESGKDMDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV 240
TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP 300
EYGQGMNPIS RLAQIQQAKK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI 360
AKKNAAEAML LQLGYKASTN LQDQLEKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY 420
QEMEASRHKV ISGTTLGYLS PKDMNQPSSS FFSISPTSNS SATIARELLM NGTSSTAEAI 480
GLKGSSPTPP CSPVQPSKQL EYLARIQGFQ AALSALKQFS EQGLDPIDGA MNIEKGSLEK 540
QAKHLREKAD NNQAPPGSIA QDCKKSNSAV 570 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0003725; F:double-stranded RNA binding; TAS:ProtInc.
 GO:0006810; P:transport; IEA:UniProtKB-KW. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom. 
Pfam
 PF00035; dsrm 
SMART
 SM00358; DSRM 
PROSITE
 PS50137; DS_RBD 
PRINTS