| Tag | Content |
|---|
| CPLM ID | CPLM-017225 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | N-acetyltransferase 10 |
Protein Synonyms/Alias | |
Gene Name | Nat10 |
Gene Synonyms/Alias | Kiaa1709 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 426 | TGRSLSLKLIQQLRQ | acetylation | [1] |
|
Reference | [1] 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] |
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 (By similarity). |
Sequence Annotation | DOMAIN 558 753 N-acetyltransferase.
NP_BIND 284 291 ATP (Potential).
REGION 702 1024 Required for localization to the
MOD_RES 426 426 N6-acetyllysine (By similarity).
MOD_RES 934 934 Phosphoserine (By similarity).
MOD_RES 984 984 Phosphoserine (By similarity).
MOD_RES 987 987 Phosphoserine (By similarity). |
Keyword | Acetylation; Acyltransferase; ATP-binding; Complete proteome; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1024 AA |
Protein Sequence | MNRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK 60
KELGFSSHRK KRMRQLQKKI KSGTLNLKQD DPFELFVAAT NIRYCYYNET HKILGNTFGM 120
CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTMTMDVHSR YRTEAHQDVV 180
GRFNERFILS LASCKKCLVI DDQLDILPIS SHVASIEALP PQAPDENLSP AALELLELKE 240
SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG 300
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIVQSLNPE FNKAVIRVNV 360
FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG 420
RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL HEVSLQESIR YAPGDAVEKW 480
LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN 540
SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVVQVC LEGEISRQSI LNSLSRGKKA 600
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGKFPCLE 660
EKVLETPQEI RTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL 720
KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLADEDEAEQ GAWLAAFWKD FRRRFLALLS 780
YQFSTFSPAL SLNIIQNRNV AKSALPALGR EHLEALFLPY DLKRLEMYSR NMVDYHLIMD 840
LIPAISRLYF LNQLGDLSLS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR 900
KVVKLFNDVQ EKAIEEQMVA VKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKDMDL 960
SQYVIRGDDE EWNEVLSKAG QNASIVSLKS DKKRKLETKQ EPKQSKKLKK RDNNRKDMKL 1020
KRKK 1024 |
Gene Ontology | GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |