CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009987
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nascent polypeptide-associated complex subunit alpha, muscle-specific form 
Protein Synonyms/Alias
 Alpha-NAC, muscle-specific form 
Gene Name
 Naca 
Gene Synonyms/Alias
 Gm1878 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
2070VTRVTIRKSKNILFVubiquitination[1]
2072RVTIRKSKNILFVITubiquitination[1, 2]
2080NILFVITKPDVYKSPacetylation[3, 4, 5]
2080NILFVITKPDVYKSPubiquitination[2]
2114AQLAAAEKFKVQGEAacetylation[3, 4, 5]
2114AQLAAAEKFKVQGEAsuccinylation[5]
2114AQLAAAEKFKVQGEAubiquitination[1, 2]
Reference
 [1] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [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] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites) (By similarity). Isoform 1 and isoform 2 appear to bind DNA and play roles in transcription. May act to regulate the expression of genes involved in the development of myotubes. 
Sequence Annotation
 DOMAIN 2042 2107 NAC-A/B.
 DOMAIN 2148 2185 UBA.
 REGION 2041 2052 Required for DNA-binding.
 MOD_RES 1024 1024 Phosphoserine.
 MOD_RES 2015 2015 Phosphoserine; by ILK1 (Probable).
 MOD_RES 2131 2131 Phosphothreonine; by GSK3-beta
 MOD_RES 2133 2133 Phosphothreonine.
 MOD_RES 2138 2138 Phosphoserine.  
Keyword
 Activator; Alternative splicing; Complete proteome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transcription; Transcription regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2187 AA 
Protein Sequence
MPGEATETVP ATEQELPQPQ AETAVLPMSS ALKVAAVGQP GPTPPSSLGP QQSPIVTAHQ 60
PSPLPSSVSS TPFEVPFAQP ITAETALPSG TAPPTPTFLP HLIGPPISPA ALALASPMIG 120
LAQKGARSSS APLSLVALAP HSVQKSSVCP PHPLTSPPSA AGAELGALTA SIPPLEPKTS 180
TSQVPSQGTL NLKGTAPCPP DVVRAFPSHL ENPLASVQPG LMSCPQTLSN TSPVKGVPIS 240
SALTQSRLSL NLKGPVSPPA RNTAAPSIPL APSTSLGCHL PLLHHSSVDS PIQPPGQSGL 300
AVSNPTSVGH SGIAASCPPE RCVVPALPSR LLAVDSGAAP SDDKGSSAVT NELCSPPGSS 360
NVAGTSLSPK ASLVPKGSNV ALQPLVTQVP ASQKTGLKEI PVSCIGATHH ALDNPSAISV 420
APATHVPPPT SSGLVSSKDP ASPVTSLVVP AAHKQFPAPP ASATLGVPVS PLPATEGLKN 480
LPISALVNVG APVSPAQAGL PTRKDTTLQP LAPIALKESP SSQSASSLEV LSEDTVTKKT 540
TGGPAPVVRP AIAGVATTTS LRADSPPAVI RADSCVSPNT VSQPLKRSVT DPAMAPRTAK 600
NTAPSTTSPL VPLASEGCPV ASSMALSPQN ASVSETALAL SPEIPKSVPF PDPPLAEISF 660
SNARKVDAVS HMESSGSSRQ GHPDASVTAK GTVVCLADSS LDTSVSASKG SALSGASSPL 720
YPLEVSFLPE AGLAVQGPKG SLNKLSPTPP SSKGAPVPST GAPPSPKGAP IVPTESSISS 780
KQVPAEILPS PQKTPEVTAS RLISAVQSPK VDPIMSDVTP TSPKKTSATA VPKDTSATLS 840
LKSVPAVTSL SPPKAPVAPS NEATIVPTEI PTSLKNALAA ATPKETLATS IPKVTSPSPQ 900
KTPKSVSLKG APAMTSKKAT EIAASKDVSP SQFPKEVPLL PHVPPTSPPK SPVSDTLSGA 960
LTSPPPKGPP ATLAETPTYP KKSPKPAASK KTPATPSPEG VTAVPLEIPP CSKKAPKTAA 1020
PKESSATSSS KRAPKTAVSK EIPSKGVTAV PLEISLPLKE TSKSATPGEK SASSPKRSPK 1080
TAGPKETPPG GVTAVPPEIS LPPKETPQNA TPNESLAASS QKRSPKTSVP KETPPGGVTA 1140
MPLEIPSAPQ KAPKTAVPKQ IPTPEDAVTI LAGSPLSPKK ASKTAAPKEA PATPSVGVIA 1200
VSGEISPSPK KTSKTAAPKE NSATLPPKRS PKTAAPKETP ATSSEGVTAV PSEISPSPPT 1260
PASKGVPVTL TPKGAPNALA ESPASPKKVP KTAAPEETST TPSPQKIPKV AGPKEASATP 1320
PSKKTPKTAV PKETSAPSEG VTAVPLEIPP SPRKAPKTAA PKETPAPSPE GATTAPVQIP 1380
PSPRKGSKKA GSKETPTTPS PEGVTAAPLE IPISSKKTSK MASPKETLVT PSSKKLSQTV 1440
GPKETSLEGA TAVPLEIPPS HKKAPKTVDP KQVPLTPSPK DAPTTLAESP SSPKKAPKTA 1500
APPSERVTTV PPEKPATPQK ASATTASKVP VPAETQEVAV SSRETPVTPA VPPVKNPSSH 1560
KKTSKTIELK EAPATLPPSP TKSPKIPSSK KAPRTSAPKE FPASPSIKPV TTSLAQTAPP 1620
SLQKAPSTTI PKENLAAPAV LPVSSKSPAA PAAASASLSP ATAAPQTAPK EATTIPSCKK 1680
AAATETPIET STAPSLEGAP KETSETSVSK VLMSSPPKKA SSSKRASTLP ATTLPSLKEA 1740
SVLSPTATSS GKDSHISPVS DACSTGTTTP QASEKLPSKK GPTAFTEMLA APAPESALAI 1800
TAPIQKSPGA NSNSASSPKC PDPSSKKDTK GLPSAVALAP QTVPVEKDTS KAIETLLVSP 1860
AKGSDCLHSP KGPVGSQVAT PLAAFTSDKV PPEAVSASVA PKPAPAASLT LAPSPVAPLP 1920
PKQPLLESAP GSVLESPSKL PVPAEEDELP PLIPPEAVSG GEPFQPILVN MPAPKPAGTP 1980
APAPSAKQPV LKNNKGSGTE SDSDESVPEL EEQDSTQTAT QQAQLAAAAE IDEEPVSKAK 2040
QSRSEKKARK AMSKLGLRQV TGVTRVTIRK SKNILFVITK PDVYKSPASD TYIVFGEAKI 2100
EDLSQQAQLA AAEKFKVQGE AVSNIQENTQ TPTVQEESEE EEVDETGVEV KDIELVMSQA 2160
NVSRAKAVRA LKNNSNDIVN AIMELTM 2187 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0017025; F:TBP-class protein binding; IDA:MGI.
 GO:0003713; F:transcription coactivator activity; IDA:MGI.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016641; EGD2/NACA.
 IPR002715; Nas_poly-pep-assoc_cplx_dom. 
Pfam
 PF01849; NAC 
SMART
  
PROSITE
 PS51151; NAC_AB
 PS50030; UBA 
PRINTS