CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017331
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DBIRD complex subunit KIAA1967 
Protein Synonyms/Alias
 Deleted in breast cancer gene 1 protein; DBC-1; DBC.1; p30 DBC 
Gene Name
 KIAA1967 
Gene Synonyms/Alias
 DBC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93RLPQLGEKVLVKAAYubiquitination[1, 2, 3, 4, 5]
97LGEKVLVKAAYNPGQubiquitination[3, 4]
112AVPWNAVKVQTLSNQubiquitination[2, 3, 4]
123LSNQPLLKSPAPPLLubiquitination[2, 3, 4]
138HVAALGQKQGILGAQubiquitination[4]
215GGEPWGAKKPRHDLPacetylation[6]
215GGEPWGAKKPRHDLPubiquitination[4]
287RIQVSSEKEAAPDAGubiquitination[2, 4]
309SDPAYSSKVLLLSSPubiquitination[1, 2, 3, 4, 5]
344ETPEHPLKQIKFLLGubiquitination[4]
347EHPLKQIKFLLGRKEubiquitination[1, 4, 5]
401IDLSGCTKWWRFAEFubiquitination[4]
667EEEFAGAKLEDSEVRubiquitination[2]
742RLSAEQAKQLVSRVVubiquitination[1, 2, 4, 5]
800GAAPTEHKALVSHNGubiquitination[4]
832GRLYLENKIHTLELKubiquitination[1, 4, 5]
839KIHTLELKLEESHNRubiquitination[1, 5]
855SATEVTNKTLAAEMQubiquitination[2, 4]
909EIQRVVEKADSWVEKubiquitination[4]
916KADSWVEKEEPAPSNubiquitination[2, 4]
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] 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] 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] 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]
 [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] 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
 Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits SUV39H1 methyltransferase activity. As part of a histone H3- specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. 
Sequence Annotation
 MOD_RES 35 35 Phosphothreonine.
 MOD_RES 124 124 Phosphoserine.
 MOD_RES 215 215 N6-acetyllysine.
 MOD_RES 675 675 Phosphoserine.
 MOD_RES 678 678 Phosphoserine.
 MOD_RES 681 681 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Coiled coil; Complete proteome; Metalloenzyme inhibitor; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 923 AA 
Protein Sequence
MSQFKRQRIN PLPGGRNFSG TASTSLLGPP PGLLTPPVAT ELSQNARHLQ GGEKQRVFTG 60
IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP 120
LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR 180
FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LPPYRVHLTP YTVDSPICDF 240
LELQRRYRSL LVPSDFLSVH LSWLSAFPLS QPFSLHHPSR IQVSSEKEAA PDAGAEPITA 300
DSDPAYSSKV LLLSSPGLEE LYRCCMLFVD DMAEPRETPE HPLKQIKFLL GRKEEEAVLV 360
GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSGCT KWWRFAEFQY LQPGPPRRLQ 420
TVVVYLPDVW TIMPTLEEWE ALCQQKAAEA APPTQEAQGE TEPTEQAPDA LEQAADTSRR 480
NAETPEATTQ QETDTDLPEA PPPPLEPAVI ARPGCVNLSL HGIVEDRRPK ERISFEVMVL 540
AELFLEMLQR DFGYRVYKML LSLPEKVVSP PEPEKEEAAK EEATKEEEAI KEEVVKEPKD 600
EAQNEGPATE SEAPLKEDGL LPKPLSSGGE EEEKPRGEAS EDLCEMALDP ELLLLRDDGE 660
EEFAGAKLED SEVRSVASNQ SEMEFSSLQD MPKELDPSAV LPLDCLLAFV FFDANWCGYL 720
HRRDLERILL TLGIRLSAEQ AKQLVSRVVT QNICQYRSLQ YSRQEGLDGG LPEEVLFGNL 780
DLLPPPGKST KPGAAPTEHK ALVSHNGSLI NVGSLLQRAE QQDSGRLYLE NKIHTLELKL 840
EESHNRFSAT EVTNKTLAAE MQELRVRLAE AEETARTAER QKSQLQRLLQ ELRRRLTPLQ 900
LEIQRVVEKA DSWVEKEEPA PSN 923 
Gene Ontology
 GO:0044609; C:DBIRD complex; IDA:UniProtKB.
 GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
 GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
 GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IMP:UniProtKB. 
Interpro
 IPR025224; DBC1/CARP1.
 IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
 IPR025223; S1-like_RNA-bd_dom. 
Pfam
 PF14443; DBC1
 PF14444; S1-like 
SMART
  
PROSITE
  
PRINTS