CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002472
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription elongation factor S-II 
Protein Synonyms/Alias
 DNA strand transfer protein alpha; STP-alpha; DNA strand transferase 1; Pyrimidine pathway regulatory protein 2 
Gene Name
 DST1 
Gene Synonyms/Alias
 PPR2; YGL043W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
39KEFVPTEKLLRETKVacetylation[1]
184AIESEMNKVNNCDTNubiquitination[2]
278CGKCKEKKVSYYQLQubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. 
Sequence Annotation
 DOMAIN 5 79 TFIIS N-terminal.
 DOMAIN 148 264 TFIIS central.
 ZN_FING 267 307 TFIIS-type.
 MOD_RES 116 116 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 309 AA 
Protein Sequence
MDSKEVLVHV KNLEKNKSND AAVLEILHVL DKEFVPTEKL LRETKVGVEV NKFKKSTNVE 60
ISKLVKKMIS SWKDAINKNK RSRQAQQHHQ DHAPGNAEDK TTVGESVNGV QQPASSQSDA 120
MKQDKYVSTK PRNSKNDGVD TAIYHHKLRD QVLKALYDVL AKESEHPPQS ILHTAKAIES 180
EMNKVNNCDT NEAAYKARYR IIYSNVISKN NPDLKHKIAN GDITPEFLAT CDAKDLAPAP 240
LKQKIEEIAK QNLYNAQGAT IERSVTDRFT CGKCKEKKVS YYQLQTRSAD EPLTTFCTCE 300
ACGNRWKFS 309 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0001139; F:core RNA polymerase II recruiting transcription factor activity; IMP:SGD.
 GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0001193; P:maintenance of transcriptional fidelity during DNA-dependent transcription elongation from RNA polymerase II promoter; IMP:SGD.
 GO:0006379; P:mRNA cleavage; IDA:SGD.
 GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:SGD.
 GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
 GO:0031440; P:regulation of mRNA 3'-end processing; IMP:SGD.
 GO:0031564; P:transcription antitermination; IDA:SGD.
 GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:SGD.
 GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IMP:SGD. 
Interpro
 IPR016492; TF_IIS-rel.
 IPR003617; TFIIS/CRSP70_N_sub.
 IPR003618; TFIIS_cen_dom.
 IPR017923; TFIIS_N.
 IPR017890; TFS2M.
 IPR006289; TFSII.
 IPR001222; Znf_TFIIS. 
Pfam
 PF08711; Med26
 PF01096; TFIIS_C
 PF07500; TFIIS_M 
SMART
 SM00510; TFS2M
 SM00509; TFS2N
 SM00440; ZnF_C2C2 
PROSITE
 PS51321; TFIIS_CENTRAL
 PS51319; TFIIS_N
 PS00466; ZF_TFIIS_1
 PS51133; ZF_TFIIS_2 
PRINTS