| Tag | Content |
|---|
| CPLM ID | CPLM-024779 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Activating signal cointegrator 1 complex subunit 3 |
Protein Synonyms/Alias | |
Gene Name | Ascc3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 573 | TGDMQLSKSEILRTQ | acetylation | [1] | | 1145 | ILTRLEEKNLTVDKL | acetylation | [1] | | 1400 | WKIRIEEKLGKKVIE | acetylation | [1] | | 1403 | RIEEKLGKKVIELTG | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3, enabling ALKHB3 to process alkylated N3- methylcytosine (3mC) within double-stranded regions. Enhances NF- kappa-B, SRF and AP1 transactivation (By similarity). |
Sequence Annotation | DOMAIN 487 670 Helicase ATP-binding 1.
DOMAIN 697 915 Helicase C-terminal 1.
DOMAIN 979 1288 SEC63 1.
DOMAIN 1337 1512 Helicase ATP-binding 2.
DOMAIN 1565 1739 Helicase C-terminal 2.
DOMAIN 1812 2175 SEC63 2.
NP_BIND 500 507 ATP (By similarity).
NP_BIND 1350 1357 ATP (By similarity).
MOTIF 612 615 DEVH box.
MOTIF 1454 1457 DEIH box.
MOD_RES 573 573 N6-acetyllysine (By similarity). |
Keyword | Acetylation; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2197 AA |
Protein Sequence | MALPRLTGAL RSFSNVTKQD NYNEEVADLK LKRSKLHEQA LDFGLSWKKI VKFLNEKLEK 60
NKMQTINEDL KDILQAAKQI VGTDNGNEAI ESGAAFLFMT FHMTDSVGYT ETKAIRQMFG 120
PFPSSSATSA CNATSRIISH FSQDDLTALV QATENQCNDR VVFGRNLAFS FDMHDLDHFD 180
ELPVNGEAQK TISLDYKKFL NEQFQEPYTP ELKPVEKSNG SLLWCEVEKY LNATLKEMTE 240
APRVEDLCCT LYDMLASAKS GDELQDELFE LLGPGGLDLI EKLLQNRITI VDRFLNSSSD 300
HKFQVLQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDGEV 360
SGEGLLPFDP KELRLQREHA LLNARSAPIL GRQRDTEVEK IRYPHVYDSQ AAARETSAFI 420
AGAKMILPEG IQRENTKLYE EVRIPYSEPM PVGFEEKPVY IQDLDEVGQL AFKGMKRLNR 480
IQSIVFDTAY NTNENMLICA PTGAGKTNIA MLTVLHEIRQ HFHQGVLKKN EFKIVYVAPM 540
KALAAEMTNY FSKRLEPLGI VVKELTGDMQ LSKSEILRTQ MLVTTPEKWD VVTRKSVGDV 600
ALSQIVKLLI LDEVHLLHED RGPVLESIVA RTLRQVESTQ SMIRILGLSA TLPNYLDVAT 660
FLHVNPYIGL FYFDGRFRPV PLGQTFLGIK SANKMQQLNN MDEVCYESVL KQVKAGHQVM 720
VFVHARNATV RTAMSLIERA KNSGQISCFL PTQGPEYGHA LKQVQKSRNK QVRELFSDGF 780
SIHHAGMLRQ DRNLVENLFS NGHIKVLVCT ATLAWGVNLP AHAVIIKGTQ IYAAKRGSFV 840
DLGILDVMQI FGRAGRPQFD KFGEGIIITT HDKLSHYLSL LTQQNPIESQ FLESLADNLN 900
AEIALGTVTN VEEAVKWMSY TYLYVRMRAN PLAYGISHKA YQMDPTLRKH REQLLIEVGQ 960
KLDKARMIRF EERTGYFSST DLGRTASHYY IKYNTIETFN ELFDAHKTEG DIFAIVSKAE 1020
EFDQIKVREE EIEELDALLN NFCELSAPGG VENSYGKINI LLQTYISRGE MDSFSLISDS 1080
AYVAQNAARI VRALFEIALR KRWPTMTYRL LNLSKVIDKR LWGWASPLRQ FSVLPPHILT 1140
RLEEKNLTVD KLKDMRKDEI GHILHHVNIG LKVKQCVHQI PSVTMEASIQ PITRTVLRVS 1200
LNIYPDFSWN DQVHGTVGEP WWIWVEDPTN DHIYHSEYFL ALKKQVINKE AQLLVFTIPI 1260
FEPLPSQYYI RAVSDRWLGA EAVCIINFQH LILPERHPPH TELLDLQPLP VTALGCKAYE 1320
ALYNFSHFNP VQTQIFHTLY HTDCNVLLGA PTGSGKTVAA ELAIFRVFNK YPTSKAVYIA 1380
PLKALVRERM DDWKIRIEEK LGKKVIELTG DVTPDMKSIA KADLIVTTPE KWDGVSRSWQ 1440
NRSYVQQVNI LIIDEIHLLG EERGPVLEVI VSRTNFISSH TEKPVRIVGL STALANARDL 1500
ADWLNIKQMG LFNFRPSVRP VPLEVHIQGF PGQHYCPRMA SMNKPAFQES HTHCPDRPCL 1560
LLPERMLSSM TKLELIAFLA TEEDPKQWLN MDEQEMENII ATVRDSNLKL TLAFGIGMHH 1620
AGLHERDRKT VEELFVNCKV QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI 1680
TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA 1740
GGTITSKQDA LDYITWTYFF RRLIMNPSYY NLGDVSQDAI NKFLSHLIGQ SLVELELSHC 1800
IEVGEDNRSI EPLTCGRIAS YYYLKHKTVK MFKDRLKPEC STEELLSILS DAEEYTDLPV 1860
RHNEDHTNNE LAKCLPIELN PHSFDSPHTK AHLLLQAHLS RAMLPCPDYD TDTKTVLDQA 1920
LRVCQAMLDV AASQGWLVTT LNITHLIQMV IQGRWLKDSS LLTIPNIEQH HLHLFRKWKP 1980
PVKGPHAKCR TSIECLPELI HACEGKEHVF SSMVEKELQP AKTKQAWNFL SHLPVINVGI 2040
SVKGSWDDSV EGHNELSIST LTADKRDENT WIKLHADQQY VLQVSLQRVH FEFHKVKHES 2100
HAVTPRFPKL KDEGWFLILG EVDKRELVAV KRVGFVRTHH EASISFFTPE APGRYIFTLY 2160
LMSDCYLGLD QQYDIFLNVT KADISTQINT EVPDVST 2197 |
Gene Ontology | GO:0005794; C:Golgi apparatus; IEA:Compara. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; ISS:UniProtKB. GO:0003676; F:nucleic acid binding; IEA:InterPro. GO:0008283; P:cell proliferation; ISS:UniProtKB. GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |