CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020327
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serrate RNA effector molecule homolog 
Protein Synonyms/Alias
 Arsenite-resistance protein 2 
Gene Name
 SRRT 
Gene Synonyms/Alias
 ARS2; ASR2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
153PPVMKTFKEFLLSLDubiquitination[1, 2, 3]
200DEEWFRSKYHPDEVGacetylation[4]
279EEEEQAGKPGEPSKKacetylation[5]
279EEEEQAGKPGEPSKKubiquitination[6]
442AEIISLCKRYPGFMRubiquitination[3]
476FDRSVNIKEICWNLQubiquitination[3]
514INGITQHKQIVRNDIubiquitination[3]
526NDIKLAAKLIHTLDDubiquitination[3, 7, 8]
611KLIKVLDKLLLYLRIubiquitination[3]
669WQKTFEEKLTPLLSVubiquitination[3]
687LSEEEAQKMGRKDPEubiquitination[3]
758NNFLTDAKRPALPEIubiquitination[7, 8]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity). 
Sequence Annotation
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 8 8 Phosphotyrosine.
 MOD_RES 74 74 Phosphoserine.
 MOD_RES 493 493 Phosphoserine.
 MOD_RES 540 540 Phosphoserine.
 MOD_RES 544 544 Phosphothreonine.  
Keyword
 Acetylation; Activator; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; RNA-mediated gene silencing; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 876 AA 
Protein Sequence
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR 60
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY AGGGGGPTYG PPQPWGHPDV 120
HIMQHHVLPI QARLGSIAEI DLGVPPPVMK TFKEFLLSLD DSVDETEAVK RYNDYKLDFR 180
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI 240
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPSKKEEGR AGAGLGDGER 300
KTNDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK KRNRKHSGDD 360
SFDEGSVSES ESESESGQAE EEKEEAEEAL KEKEKPKEEE WEKPKDAAGL ECKPRPLHKT 420
CSLFMRNIAP NISRAEIISL CKRYPGFMRV ALSEPQPERR FFRRGWVTFD RSVNIKEICW 480
NLQNIRLREC ELSPGVNRDL TRRVRNINGI TQHKQIVRND IKLAAKLIHT LDDRTQLWAS 540
EPGTPPLPTS LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE 600
RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP PNRISHGEVL 660
EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF VTSNTQELGK DKWLCPLSGK 720
KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF NNFLTDAKRP ALPEIKPAQP PGPAQILPPG 780
LTPGLPYPHQ TPQGLMPYGQ PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR 840
GQGGYPGKPR NRMVRGDPRA IVEYRDLDAP DDVDFF 876 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; ISS:UniProtKB.
 GO:0003677; F:DNA binding; ISS:UniProtKB.
 GO:0008283; P:cell proliferation; ISS:UniProtKB.
 GO:0097150; P:neuronal stem cell maintenance; ISS:UniProtKB.
 GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0046685; P:response to arsenic-containing substance; NAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007042; Arsenite-R_2.
 IPR021933; DUF3546. 
Pfam
 PF04959; ARS2
 PF12066; DUF3546 
SMART
  
PROSITE
  
PRINTS