CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein NPAT 
Protein Synonyms/Alias
 Nuclear protein of the ataxia telangiectasia mutated locus; Nuclear protein of the ATM locus; p220 
Gene Name
 NPAT 
Gene Synonyms/Alias
 CAND3; E14 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
121RTGIAEIKRQRKLASubiquitination[1, 2, 3]
242PNAFAVEKQMVIENAacetylation[3, 4]
242PNAFAVEKQMVIENAubiquitination[2, 5]
262SNKSLQEKLAENINKubiquitination[2, 5]
269KLAENINKFLTSDNNacetylation[3, 6]
547LTGKPSKKSQFCENSubiquitination[2]
1228LSVGTAVKDLKQEQTacetylation[7]
1353TTSATPLKDNTQQFRubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] 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]
 [3] 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]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] 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]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] 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
 Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters. 
Sequence Annotation
 DOMAIN 3 35 LisH.
 REGION 1 318 Interaction with MIZF.
 REGION 5 25 Required for activation of histone gene
 REGION 121 145 Required for activation of histone gene
 REGION 262 338 Mediates transcriptional activation.
 REGION 629 653 Required for acceleration of G1 phase.
 REGION 828 853 Required for acceleration of G1 phase.
 REGION 1039 1054 Required for acceleration of G1 phase.
 REGION 1228 1252 Required for acceleration of G1 phase.
 REGION 1325 1349 Required for acceleration of G1 phase.
 MOD_RES 775 775 Phosphoserine; by CDK2.
 MOD_RES 779 779 Phosphoserine; by CDK2.
 MOD_RES 1100 1100 Phosphoserine; by CDK2.
 MOD_RES 1228 1228 N6-acetyllysine.
 MOD_RES 1270 1270 Phosphothreonine; by CDK2.
 MOD_RES 1350 1350 Phosphothreonine; by CDK2.  
Keyword
 Acetylation; Activator; Cell cycle; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1427 AA 
Protein Sequence
MLLPSDVARL VLGYLQQENL ISTCQTFILE SSDLKEYAEH CTDEGFIPAC LLSLFGKNLT 60
TILNEYVAMK TKETSNNVPA IMSSLWKKLD HTLSQIRSMQ SSPRFAGSQR ARTRTGIAEI 120
KRQRKLASQT APASAELLTL PYLSGQFTTP PSTGTQVTRP SGQISDPSRS YFVVVNHSQS 180
QDTVTTGEAL NVIPGAQEKK AHASLMSPGR RKSESQRKST TLSGPHSTIR NFQDPNAFAV 240
EKQMVIENAR EKILSNKSLQ EKLAENINKF LTSDNNIAQV PKQTDNNPTE PETSIDEFLG 300
LPSEIHMSEE AIQDILEQTE SDPAFQALFD LFDYGKTKNN KNISQSISSQ PMESNPSIVL 360
ADETNLAVKG SFETEESDGQ SGQPAFCTSY QNDDPLNALK NSNNHDVLRQ EDQENFSQIS 420
TSIQKKAFKT AVPTEQKCDI DITFESVPNL NDFNQRGNSN AECNPHCAEL YTNQMSTETE 480
MAIGIEKNSL SSNVPSESQL QPDQPDIPIT SFVSLGCEAN NENLILSGKS SQLLSQDTSL 540
TGKPSKKSQF CENSNDTVKL KINFHGSKSS DSSEVHKSKI EINVLEPVMS QLSNCQDNSC 600
LQSEILPVSV ESSHLNVSGQ VEIHLGDSLS STKQPSNDSA SVELNHTENE AQASKSENSQ 660
EPSSSVKEEN TIFLSLGGNA NCEKVALTPP EGTPVENSHS LPPESVCSSV GDSHPESQNT 720
DDKPSSNNSA EIDASNIVSL KVIISDDPFV SSDTELTSAV SSINGENLPT IILSSPTKSP 780
TKNAELVKCL SSEETVGAVV YAEVGDSASM EQSLLTFKSE DSAVNNTQNE DGIAFSANVT 840
PCVSKDGGYI QLMPATSTAF GNSNNILIAT CVTDPTALGT SVSQSNVVVL PGNSAPMTAQ 900
PLPPQLQTPP RSNSVFAVNQ AVSPNFSQGS AIIIASPVQP VLQGMVGMIP VSVVGQNGNN 960
FSTPPRQVLH MPLTAPVCNR SIPQFPVPPK SQKAQGLRNK PCIGKQVNNL VDSSGHSVGC 1020
HAQKTEVSDK SIATDLGKKS EETTVPFPEE SIVPAAKPCH RRVLCFDSTT APVANTQGPN 1080
HKMVSQNKER NAVSFPNLDS PNVSSTLKPP SNNAIKREKE KPPLPKILSK SESAISRHTT 1140
IRETQSEKKV SPTEIVLESF HKATANKENE LCSDVERQKN PENSKLSIGQ QNGGLRSEKS 1200
IASLQEMTKK QGTSSNNKNV LSVGTAVKDL KQEQTKSASS LITTEMLQDI QRHSSVSRLA 1260
DSSDLPVPRT PGSGAGEKHK EEPIDIIKAP SSRRFSEDSS TSKVMVPPVT PDLPACSPAS 1320
ETGSENSVNM AAHTLMILSR AAISRTTSAT PLKDNTQQFR ASSRSTTKKR KIEELDERER 1380
NSRPSSKNLT NSSIPMKKKK IKKKKLPSSF PAGMDVDKFL LSLHYDE 1427 
Gene Ontology
 GO:0015030; C:Cajal body; IDA:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0000083; P:regulation of transcription involved in G1/S phase of mitotic cell cycle; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR006594; LisH_dimerisation. 
Pfam
  
SMART
 SM00667; LisH 
PROSITE
 PS50896; LISH 
PRINTS