CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021210
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-acetyltransferase 10 
Protein Synonyms/Alias
  
Gene Name
 NAT10 
Gene Synonyms/Alias
 ALP; KIAA1709 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
239DLELRELKESLQDTQubiquitination[1]
256GVLVDCCKTLDQAKAubiquitination[1]
262CKTLDQAKAVLKFIEubiquitination[1]
266DQAKAVLKFIEGISEubiquitination[1]
274FIEGISEKTLRSTVAubiquitination[1, 2]
426TGRSLSLKLIQQLRQacetylation[3]
426TGRSLSLKLIQQLRQubiquitination[1]
447VSTTAENKTTTTARLubiquitination[1, 2, 4]
520DTLFCYHKASEVFLQubiquitination[1]
599NSLSRGKKASGDLIPubiquitination[1, 2]
823LFLPYDLKRLEMYSRubiquitination[1, 2]
904RIIRKVVKLFNEVQEubiquitination[5]
942DDLDEAAKEFQEKHKubiquitination[1]
989NASIISLKSDKKRKLubiquitination[1]
1003LEAKQEPKQSKKLKNubiquitination[4]
1006KQEPKQSKKLKNRETubiquitination[4]
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] 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] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Has protein acetyltransferase activity in vitro. Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division. 
Sequence Annotation
 DOMAIN 558 753 N-acetyltransferase.
 NP_BIND 284 291 ATP (Potential).
 REGION 702 1025 Required for localization to the
 MOD_RES 426 426 N6-acetyllysine.
 MOD_RES 934 934 Phosphoserine.
 MOD_RES 984 984 Phosphoserine.
 MOD_RES 987 987 Phosphoserine.  
Keyword
 Acetylation; Acyltransferase; ATP-binding; Complete proteome; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1025 AA 
Protein Sequence
MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK 60
KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT NIRYCYYNET HKILGNTFGM 120
CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV 180
GRFNERFILS LASCKKCLVI DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE 240
SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG 300
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE FNKAVIRVNV 360
FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG 420
RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL YEVSLQESIR YAPGDAVEKW 480
LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN 540
SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA 600
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGRFPCLE 660
EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL 720
KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLTDEDEADQ GGWLAAFWKD FRRRFLALLS 780
YQFSTFSPSL ALNIIQNRNM GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD 840
MIPAISRIYF LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR 900
KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKSMDL 960
SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ EPKQSKKLKN RETKNKKDMK 1020
LKRKK 1025 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR013562; DUF1726.
 IPR000182; GNAT_dom.
 IPR007807; Helicase_dom. 
Pfam
 PF08351; DUF1726
 PF05127; Helicase_RecD 
SMART
  
PROSITE
 PS51186; GNAT 
PRINTS