CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020462
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 B-cell lymphoma/leukemia 11B 
Protein Synonyms/Alias
 BCL-11B; B-cell CLL/lymphoma 11B; COUP-TF-interacting protein 2; Radiation-induced tumor suppressor gene 1 protein; hRit1 
Gene Name
 BCL11B 
Gene Synonyms/Alias
 CTIP2; RIT1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
79VFIEHKRKQCGGSLGubiquitination[1, 2]
95CYDKALDKDSPPPSSubiquitination[2]
215CQCQLSGKDEPSSYIubiquitination[2]
591AKALADEKALVLGKVubiquitination[3]
617YGELLADKQKRGAFLubiquitination[3]
619ELLADKQKRGAFLKRubiquitination[3]
672FPGLFPRKPAPLPSPubiquitination[3]
686PGLNSAAKRIKVEKDubiquitination[3]
723AASRHFMKDPFLGFTubiquitination[3]
803DTCEYCGKVFKNCSNubiquitination[3]
838YACAQSSKLTRHMKTubiquitination[3]
851KTHGQIGKEVYRCDIacetylation[4]
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] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Tumor-suppressor protein involved in T-cell lymphomas. May function on the P53-signaling pathway. May be a key regulator of both differentiation and survival during thymocyte development. Repress transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity). 
Sequence Annotation
 ZN_FING 221 251 C2H2-type 1.
 ZN_FING 427 454 C2H2-type 2.
 ZN_FING 455 482 C2H2-type 3.
 ZN_FING 796 823 C2H2-type 4.
 ZN_FING 824 853 C2H2-type 5.
 ZN_FING 854 884 C2H2-type 6.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 120 120 Phosphothreonine.
 MOD_RES 256 256 Phosphoserine.
 MOD_RES 260 260 Phosphothreonine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 376 376 Phosphothreonine.
 MOD_RES 381 381 Phosphoserine.
 MOD_RES 398 398 Phosphoserine.
 MOD_RES 417 417 Phosphothreonine.
 MOD_RES 483 483 Phosphoserine.
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 496 496 Phosphoserine.
 MOD_RES 497 497 Phosphoserine.
 MOD_RES 678 678 Phosphoserine.
 MOD_RES 765 765 Phosphoserine.
 MOD_RES 851 851 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 894 AA 
Protein Sequence
MSRRKQGNPQ HLSQRELITP EADHVEAAIL EEDEGLEIEE PSGLGLMVGG PDPDLLTCGQ 60
CQMNFPLGDI LVFIEHKRKQ CGGSLGACYD KALDKDSPPP SSRSELRKVS EPVEIGIQVT 120
PDEDDHLLSP TKGICPKQEN IAGPCRPAQL PAVAPIAASS HPHSSVITSP LRALGALPPC 180
LPLPCCSARP VSGDGTQGEG QTEAPFGCQC QLSGKDEPSS YICTTCKQPF NSAWFLLQHA 240
QNTHGFRIYL EPGPASSSLT PRLTIPPPLG PEAVAQSPLM NFLGDSNPFN LLRMTGPILR 300
DHPGFGEGRL PGTPPLFSPP PRHHLDPHRL SAEEMGLVAQ HPSAFDRVMR LNPMAIDSPA 360
MDFSRRLREL AGNSSTPPPV SPGRGNPMHR LLNPFQPSPK SPFLSTPPLP PMPPGGTPPP 420
QPPAKSKSCE FCGKTFKFQS NLIVHRRSHT GEKPYKCQLC DHACSQASKL KRHMKTHMHK 480
AGSLAGRSDD GLSAASSPEP GTSELAGEGL KAADGDFRHH ESDPSLGHEP EEEDEEEEEE 540
EEELLLENES RPESSFSMDS ELSRNRENGG GGVPGVPGAG GGAAKALADE KALVLGKVME 600
NVGLGALPQY GELLADKQKR GAFLKRAAGG GDAGDDDDAG GCGDAGAGGA VNGRGGGFAP 660
GTEPFPGLFP RKPAPLPSPG LNSAAKRIKV EKDLELPPAA LIPSENVYSQ WLVGYAASRH 720
FMKDPFLGFT DARQSPFATS SEHSSENGSL RFSTPPGDLL DGGLSGRSGT ASGGSTPHLG 780
GPGPGRPSSK EGRRSDTCEY CGKVFKNCSN LTVHRRSHTG ERPYKCELCN YACAQSSKLT 840
RHMKTHGQIG KEVYRCDICQ MPFSVYSTLE KHMKKWHGEH LLTNDVKIEQ AERS 894 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Compara.
 GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0046632; P:alpha-beta T cell differentiation; IEA:Compara.
 GO:0003382; P:epithelial cell morphogenesis; IEA:Compara.
 GO:0003334; P:keratinocyte development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0071678; P:olfactory bulb axon guidance; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
 GO:0043368; P:positive T cell selection; IEA:Compara.
 GO:0031077; P:post-embryonic camera-type eye development; IEA:Compara.
 GO:0010837; P:regulation of keratinocyte proliferation; IEA:Compara.
 GO:0019216; P:regulation of lipid metabolic process; IEA:Compara.
 GO:0045664; P:regulation of neuron differentiation; IEA:Compara.
 GO:0043588; P:skin development; IEA:Compara.
 GO:0021773; P:striatal medium spiny neuron differentiation; IEA:Compara.
 GO:0033077; P:T cell differentiation in thymus; IEA:Compara.
 GO:0033153; P:T cell receptor V(D)J recombination; IEA:Compara.
 GO:0048538; P:thymus development; IEA:Compara. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00096; zf-C2H2 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS