CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003775
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcriptional activator Myb 
Protein Synonyms/Alias
 Proto-oncogene c-Myb 
Gene Name
 MYB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
92VLNPELIKGPWTKEEubiquitination[1]
109RVIELVQKYGPKRWSubiquitination[1]
471PRTPTPFKHALAAQEacetylation[2, 3, 4]
480ALAAQEIKYGPLKMLacetylation[2, 3]
485EIKYGPLKMLPQTPSacetylation[2]
503EDLQDVIKQESDESGsumoylation[5, 6, 7]
527PPLLKKIKQEVESPTsumoylation[5, 6, 7]
Reference
 [1] 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]
 [2] c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300.
 Tomita A, Towatari M, Tsuzuki S, Hayakawa F, Kosugi H, Tamai K, Miyazaki T, Kinoshita T, Saito H.
 Oncogene. 2000 Jan 20;19(3):444-51. [PMID: 10656693]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity.
 Bies J, Markus J, Wolff L.
 J Biol Chem. 2002 Mar 15;277(11):8999-9009. [PMID: 11779867]
 [6] Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner.
 Dahle Ø, Andersen TØ, Nordgård O, Matre V, Del Sal G, Gabrielsen OS.
 Eur J Biochem. 2003 Mar;270(6):1338-48. [PMID: 12631292]
 [7] TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation.
 Morita Y, Kanei-Ishii C, Nomura T, Ishii S.
 Mol Biol Cell. 2005 Nov;16(11):5433-44. [PMID: 16162816] 
Functional Description
 Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells. 
Sequence Annotation
 DOMAIN 35 86 HTH myb-type 1.
 DOMAIN 87 142 HTH myb-type 2.
 DOMAIN 143 193 HTH myb-type 3.
 DNA_BIND 63 86 H-T-H motif (By similarity).
 DNA_BIND 115 138 H-T-H motif (By similarity).
 DNA_BIND 166 189 H-T-H motif (By similarity).
 REGION 90 193 Interaction with HIPK2 and NLK (By
 REGION 275 327 Transcriptional activation domain.
 REGION 328 465 Negative regulatory domain (By
 REGION 376 397 Leucine-zipper.
 MOD_RES 471 471 N6-acetyllysine.
 MOD_RES 480 480 N6-acetyllysine.  
Keyword
 Acetylation; Activator; Alternative splicing; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 640 AA 
Protein Sequence
MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 60
DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 120
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 180
IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 240
NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 300
LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 360
PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE NSDLEMPSLT 420
STPLIGHKLT VTTPFHRDQT VKTQKENTVF RTPAIKRSIL ESSPRTPTPF KHALAAQEIK 480
YGPLKMLPQT PSHLVEDLQD VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF 540
FCSHHWEGDS LNTQLFTQTS PVADAPNILT SSVLMAPASE DEDNVLKAFT VPKNRSLASP 600
LQPCSSTWEP ASCGKMEEQM TSSSQARKYV NAFSARTLVM 640 
Gene Ontology
 GO:0016363; C:nuclear matrix; NAS:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0030183; P:B cell differentiation; IEA:Compara.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006816; P:calcium ion transport; IEA:Compara.
 GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
 GO:0048566; P:embryonic digestive tract development; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Compara.
 GO:0048872; P:homeostasis of number of cells; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
 GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:UniProtKB.
 GO:0045624; P:positive regulation of T-helper cell differentiation; IMP:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0048538; P:thymus development; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR015395; C-myb_C.
 IPR009057; Homeodomain-like.
 IPR017930; Myb_dom.
 IPR001005; SANT/Myb.
 IPR012642; Tscrpt_reg_Wos2-domain. 
Pfam
 PF09316; Cmyb_C
 PF07988; LMSTEN
 PF00249; Myb_DNA-binding 
SMART
 SM00717; SANT 
PROSITE
 PS51294; HTH_MYB 
PRINTS