CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020051
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myb-binding protein 1A 
Protein Synonyms/Alias
  
Gene Name
 MYBBP1A 
Gene Synonyms/Alias
 P160 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30ADRYGLLKHSREFLDubiquitination[1]
56TRLAATEKLLEYLRGubiquitination[1, 2, 3]
71RPKGSEMKYALKRLIubiquitination[1]
151FQSGRLVKDQEALMKubiquitination[1]
161EALMKSVKLLQALAQubiquitination[3]
179HLQEQPRKALVDILSubiquitination[1, 3]
231KVPSKLKKLVGSVNLubiquitination[1, 3]
341GEHVCTAKLPKQFKFubiquitination[1]
432FSTNNQKKAQDSSLHubiquitination[1]
581DRMLQTLKELEAHSAubiquitination[1]
866SLRSSSSKQEQDLLHubiquitination[1]
874QEQDLLHKTARIFTHubiquitination[1]
935LYLLRVLKGNTAEGCubiquitination[1]
988ALSSFLTKRNSPLTVubiquitination[1, 3]
1036QACLLLQKTLSMREVubiquitination[1, 3]
1062LMGQVLAKVTENLRVubiquitination[1]
1140DLYWQAMKTLGVQRPubiquitination[1, 3]
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] 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]
 [3] 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] 
Functional Description
 May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) (By similarity). 
Sequence Annotation
 REGION 1 582 Interaction with MYB (By similarity).
 REGION 1151 1328 Required for nuclear and nucleolar
 MOTIF 240 258 Nuclear export signal 1 (By similarity).
 MOTIF 263 281 Nuclear export signal 2 (By similarity).
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 71 71 N6-acetyllysine.
 MOD_RES 158 158 N6-acetyllysine.
 MOD_RES 775 775 Phosphoserine.
 MOD_RES 1159 1159 Phosphoserine.
 MOD_RES 1163 1163 Phosphoserine.
 MOD_RES 1186 1186 Phosphoserine.
 MOD_RES 1190 1190 Phosphothreonine.
 MOD_RES 1196 1196 Phosphothreonine.
 MOD_RES 1207 1207 Phosphoserine.
 MOD_RES 1232 1232 Phosphoserine.
 MOD_RES 1241 1241 Phosphoserine (By similarity).
 MOD_RES 1248 1248 Phosphoserine.
 MOD_RES 1267 1267 Phosphoserine.
 MOD_RES 1269 1269 Phosphothreonine.
 MOD_RES 1290 1290 Phosphoserine.
 MOD_RES 1303 1303 Phosphoserine.
 MOD_RES 1308 1308 Phosphoserine.
 MOD_RES 1310 1310 Phosphoserine.
 MOD_RES 1314 1314 Phosphoserine.  
Keyword
 Acetylation; Activator; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1328 AA 
Protein Sequence
MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY 60
LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD 120
LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA 180
LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS 240
DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 300
ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL 360
EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD 420
SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL 480
FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP 540
WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 600
LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA 660
QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE 720
DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE 780
LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP 840
ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 900
HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP 960
TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI 1020
TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ 1080
QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK 1140
TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 1200
GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ 1260
VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA 1320
QTLRFTISSS KK 1332 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0042564; C:NLS-dependent protein nuclear import complex; ISS:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
 GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
 GO:0008134; F:transcription factor binding; TAS:ProtInc.
 GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
 GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
 GO:0071158; P:positive regulation of cell cycle arrest; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:ProtInc.
 GO:0022904; P:respiratory electron transport chain; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016024; ARM-type_fold.
 IPR007015; DNA_pol_V. 
Pfam
 PF04931; DNA_pol_phi 
SMART
  
PROSITE
  
PRINTS