CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018829
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TATA-binding protein-associated factor 2N 
Protein Synonyms/Alias
 68 kDa TATA-binding protein-associated factor; TAF(II)68; TAFII68; RNA-binding protein 56 
Gene Name
 TAF15 
Gene Synonyms/Alias
 RBP56; TAF2N 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
268KTNKKTGKPMINLYTacetylation[1]
297FDDPPSAKAAIDWFDubiquitination[2]
306AIDWFDGKEFHGNIIubiquitination[3]
354QGRGGDPKSGDWVCPubiquitination[4]
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] 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]
 [3] 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]
 [4] 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] 
Functional Description
 RNA and ssDNA-binding protein that may play specific roles during transcription initiation at distinct promoters. Can enter the preinitiation complex together with the RNA polymerase II (Pol II). 
Sequence Annotation
 DOMAIN 234 320 RRM.
 REPEAT 407 413 1.
 REPEAT 414 420 2.
 REPEAT 421 429 3.
 REPEAT 430 439 4.
 REPEAT 440 448 5.
 REPEAT 449 457 6.
 REPEAT 458 465 7.
 REPEAT 466 473 8.
 REPEAT 474 481 9.
 REPEAT 482 488 10.
 REPEAT 489 496 11.
 REPEAT 497 503 12.
 REPEAT 504 510 13.
 REPEAT 511 517 14.
 REPEAT 518 524 15.
 REPEAT 525 533 16.
 REPEAT 534 543 17.
 REPEAT 544 551 18.
 REPEAT 552 560 19.
 REPEAT 561 568 20.
 REPEAT 569 575 21.
 ZN_FING 354 385 RanBP2-type.
 REGION 407 575 21 X approximate tandem repeats of D-R-
 MOD_RES 206 206 Asymmetric dimethylarginine; by PRMT1.
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 268 268 N6-acetyllysine.
 MOD_RES 423 423 Phosphoserine.
 MOD_RES 438 438 Phosphoserine.
 MOD_RES 442 442 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 483 483 Dimethylated arginine.
 MOD_RES 528 528 Asymmetric dimethylarginine.
 MOD_RES 535 535 Asymmetric dimethylarginine.
 MOD_RES 554 554 Phosphoserine.
 MOD_RES 570 570 Asymmetric dimethylarginine.  
Keyword
 Acetylation; Alternative splicing; Chromosomal rearrangement; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Metal-binding; Methylation; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 592 AA 
Protein Sequence
MSDSGSYGQS GGEQQSYSTY GNPGSQGYGQ ASQSYSGYGQ TTDSSYGQNY SGYSSYGQSQ 60
SGYSQSYGGY ENQKQSSYSQ QPYNNQGQQQ NMESSGSQGG RAPSYDQPDY GQQDSYDQQS 120
GYDQHQGSYD EQSNYDQQHD SYSQNQQSYH SQRENYSHHT QDDRRDVSRY GEDNRGYGGS 180
QGGGRGRGGY DKDGRGPMTG SSGGDRGGFK NFGGHRDYGP RTDADSESDN SDNNTIFVQG 240
LGEGVSTDQV GEFFKQIGII KTNKKTGKPM INLYTDKDTG KPKGEATVSF DDPPSAKAAI 300
DWFDGKEFHG NIIKVSFATR RPEFMRGGGS GGGRRGRGGY RGRGGFQGRG GDPKSGDWVC 360
PNPSCGNMNF ARRNSCNQCN EPRPEDSRPS GGDFRGRGYG GERGYRGRGG RGGDRGGYGG 420
DRSGGGYGGD RSSGGGYSGD RSGGGYGGDR SGGGYGGDRG GGYGGDRGGG YGGDRGGGYG 480
GDRGGYGGDR GGGYGGDRGG YGGDRGGYGG DRGGYGGDRG GYGGDRSRGG YGGDRGGGSG 540
YGGDRSGGYG GDRSGGGYGG DRGGGYGGDR GGYGGKMGGR NDYRNDQRNR PY 592 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR001876; Znf_RanBP2. 
Pfam
 PF00076; RRM_1
 PF00641; zf-RanBP 
SMART
 SM00360; RRM
 SM00547; ZnF_RBZ 
PROSITE
 PS50102; RRM
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS