CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-alpha-acetyltransferase 15, NatA auxiliary subunit 
Protein Synonyms/Alias
 Gastric cancer antigen Ga19; N-terminal acetyltransferase; NMDA receptor-regulated protein 1; Protein tubedown-1; Tbdn100 
Gene Name
 NAA15 
Gene Synonyms/Alias
 GA19; NARG1; NATH; TBDN100 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34RNGLKFCKQILSNPKacetylation[1]
34RNGLKFCKQILSNPKubiquitination[2, 3]
41KQILSNPKFAEHGETubiquitination[4, 5]
52HGETLAMKGLTLNCLubiquitination[4, 5]
262PENWAYYKGLEKALKacetylation[1, 6]
262PENWAYYKGLEKALKubiquitination[2, 3, 4, 5, 7, 8, 9, 10]
266AYYKGLEKALKPANMubiquitination[2, 3]
269KGLEKALKPANMLERubiquitination[2, 3]
286IYEEAWTKYPRGLVPubiquitination[2, 3]
305LNFLSGEKFKECLDKubiquitination[4, 5]
307FLSGEKFKECLDKFLubiquitination[2]
312KFKECLDKFLRMNFSubiquitination[2, 4, 5]
425YKHAGNIKEAARWMDubiquitination[7]
447ADRFINSKCAKYMLKubiquitination[2]
454KCAKYMLKANLIKEAubiquitination[4, 5]
459MLKANLIKEAEEMCSubiquitination[2]
467EAEEMCSKFTREGTSubiquitination[2]
496TECAQAYKAMNKFGEubiquitination[8, 10]
543RSYVDLLKLEDVLRQubiquitination[2, 3, 5, 7, 11]
556RQHPFYFKAARIAIEubiquitination[7]
649LIPEKLAKVETPLEEubiquitination[3]
659TPLEEAIKFLTPLKNubiquitination[2, 3, 4, 5, 10]
665IKFLTPLKNLVKNKIubiquitination[2, 3, 4, 5, 7]
724NTAVCESKDLSDTVRacetylation[3]
724NTAVCESKDLSDTVRubiquitination[2, 3]
735DTVRTVLKQEMNRLFacetylation[1, 3]
735DTVRTVLKQEMNRLFubiquitination[2]
756NFNETFLKRNSDSLPacetylation[1, 3, 12]
756NFNETFLKRNSDSLPubiquitination[2, 3, 4, 5, 7, 9]
770PHRLSAAKMVYYLDPubiquitination[2, 4, 5, 7, 10]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] 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] 
Functional Description
 The NAA10-NAA15 complex displays alpha (N-terminal) acetyltransferase activity that may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. 
Sequence Annotation
 REPEAT 46 79 TPR 1.
 REPEAT 80 113 TPR 2.
 REPEAT 148 184 TPR 3.
 REPEAT 224 257 TPR 4.
 REPEAT 374 407 TPR 5.
 REPEAT 409 441 TPR 6.
 REPEAT 485 518 TPR 7.
 REPEAT 672 705 TPR 8.
 REGION 500 866 Interaction with HYPK.
 MOTIF 612 629 Bipartite nuclear localization signal
 MOD_RES 262 262 N6-acetyllysine.
 MOD_RES 399 399 Phosphothreonine.
 MOD_RES 403 403 Phosphoserine.
 MOD_RES 588 588 Phosphoserine.
 MOD_RES 735 735 N6-acetyllysine.
 MOD_RES 756 756 N6-acetyllysine.
 MOD_RES 855 855 Phosphoserine (By similarity).
 MOD_RES 856 856 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Angiogenesis; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 866 AA 
Protein Sequence
MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG 60
KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL 120
SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT 180
SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL 240
EDAADVYRGL QERNPENWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF 300
LSGEKFKECL DKFLRMNFSK GCPPVFNTLR SLYKDKEKVA IIEELVVGYE TSLKSCRLFN 360
PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH 420
AGNIKEAARW MDEAQALDTA DRFINSKCAK YMLKANLIKE AEEMCSKFTR EGTSAVENLN 480
EMQCMWFQTE CAQAYKAMNK FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD 540
LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR 600
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF 660
LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSSHPWLHE CMIRLFNTAV 720
CESKDLSDTV RTVLKQEMNR LFGATNPKNF NETFLKRNSD SLPHRLSAAK MVYYLDPSSQ 780
KRAIELATTL DESLTNRNLQ TCMEVLEALY DGSLGDCKEA AEIYRANCHK LFPYALAFMP 840
PGYEEDMKIT VNGDSSAEAE ELANEI 866 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IDA:UniProtKB.
 GO:0008080; F:N-acetyltransferase activity; IEA:Compara.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR021183; NatA_aux_su.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR013105; TPR_2.
 IPR019734; TPR_repeat. 
Pfam
 PF12569; NARP1
 PF07719; TPR_2 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS