CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021234
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cleavage stimulation factor subunit 2 tau variant 
Protein Synonyms/Alias
 CF-1 64 kDa subunit tau variant; Cleavage stimulation factor 64 kDa subunit tau variant; CSTF 64 kDa subunit tau variant; TauCstF-64 
Gene Name
 CSTF2T 
Gene Synonyms/Alias
 KIAA0689 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55VYDRETGKPKGYGFCubiquitination[1]
145EQMFELMKQMKLCVQubiquitination[1, 2]
148FELMKQMKLCVQNSHubiquitination[1, 2, 3, 4, 5, 6]
189MDPEIALKILHRKIHubiquitination[1, 2, 3, 5, 6, 7]
194ALKILHRKIHVTPLIubiquitination[1, 3, 5, 6, 8]
611ILKEQIQKSTGAS**ubiquitination[1]
Reference
 [1] 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]
 [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] 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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
Functional Description
 May play a significant role in AAUAAA-independent mRNA polyadenylation in germ cells. Directly involved in the binding to pre-mRNAs (By similarity). 
Sequence Annotation
 DOMAIN 16 94 RRM.
 REPEAT 418 422 1-1.
 REPEAT 423 427 1-2; approximate.
 REPEAT 428 432 1-3; approximate.
 REPEAT 433 437 1-4; approximate.
 REPEAT 438 442 1-5; approximate.
 REPEAT 443 447 1-6.
 REPEAT 448 452 1-7; approximate.
 REPEAT 453 457 1-8; approximate.
 REPEAT 458 462 1-9; approximate.
 REPEAT 505 509 2-1.
 REPEAT 510 514 2-2.
 REPEAT 515 519 2-3.
 REPEAT 520 524 2-4.
 REPEAT 525 529 2-5; approximate.
 REPEAT 530 534 2-6.
 REPEAT 535 539 2-7; approximate.
 REPEAT 540 544 2-8; approximate.
 REPEAT 545 549 2-9; approximate.
 REGION 418 462 9 X 5 AA tandem repeats of M-E-T-R-[AG].
 REGION 505 549 9 X 5 AA tandem repeats of G-[AT]-G-[MI]-  
Keyword
 Complete proteome; mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 616 AA 
Protein Sequence
MSSLAVRDPA MDRSLRSVFV GNIPYEATEE QLKDIFSEVG SVVSFRLVYD RETGKPKGYG 60
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGPAAPI IDSPYGDPID 120
PEDAPESITR AVASLPPEQM FELMKQMKLC VQNSHQEARN MLLQNPQLAY ALLQAQVVMR 180
IMDPEIALKI LHRKIHVTPL IPGKSQSVSV SGPGPGPGPG LCPGPNVLLN QQNPPAPQPQ 240
HLARRPVKDI PPLMQTPIQG GIPAPGPIPA AVPGAGPGSL TPGGAMQPQL GMPGVGPVPL 300
ERGQVQMSDP RAPIPRGPVT PGGLPPRGLL GDAPNDPRGG TLLSVTGEVE PRGYLGPPHQ 360
GPPMHHASGH DTRGPSSHEM RGGPLGDPRL LIGEPRGPMI DQRGLPMDGR GGRDSRAMET 420
RAMETEVLET RVMERRGMET CAMETRGMEA RGMDARGLEM RGPVPSSRGP MTGGIQGPGP 480
INIGAGGPPQ GPRQVPGISG VGNPGAGMQG TGIQGTGMQG AGIQGGGMQG AGIQGVSIQG 540
GGIQGGGIQG ASKQGGSQPS SFSPGQSQVT PQDQEKAALI MQVLQLTADQ IAMLPPEQRQ 600
SILILKEQIQ KSTGAS 616 
Gene Ontology
 GO:0005622; C:intracellular; IDA:LIFEdb.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR025742; CSTF2_hinge.
 IPR026896; CSTF_C.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF14327; CSTF2_hinge
 PF14304; CSTF_C
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS