CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019647
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Paired amphipathic helix protein Sin3a 
Protein Synonyms/Alias
 Histone deacetylase complex subunit Sin3a; Transcriptional corepressor Sin3a 
Gene Name
 SIN3A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
122QQQFQRLKVEDALSYubiquitination[1]
469TESLFFDKVRKALRSacetylation[2]
639VLEAIQKKLSRLSAEubiquitination[3]
650LSAEEQAKFRLDNTLubiquitination[3]
676LQRIYADKAADIIDGubiquitination[3]
715EAQRGFNKVWREQNEubiquitination[3, 4]
723VWREQNEKYYLKSLDacetylation[2, 5]
727QNEKYYLKSLDHQGIacetylation[2]
727QNEKYYLKSLDHQGIubiquitination[3, 6, 7]
747DTKVLRSKSLLNEIEubiquitination[1, 3, 4]
806KRQTGIQKEDKYKIKacetylation[8]
865GGSPPKSKLLFSNTAacetylation[9]
875FSNTAAQKLRGMDEVacetylation[4]
875FSNTAAQKLRGMDEVubiquitination[3, 10]
934EREVLGIKRDKSDSPacetylation[2]
934EREVLGIKRDKSDSPubiquitination[3]
937VLGIKRDKSDSPAIQubiquitination[3, 4]
1053LESTYQRKAEQLMSDubiquitination[3]
1122LREHLAQKPVFLPRNubiquitination[3, 4, 6, 7]
1154GKEGNSKKTMENVDSubiquitination[3]
1164ENVDSLDKLECRFKLubiquitination[3]
1170DKLECRFKLNSYKMVubiquitination[3]
1271VKYGTVFKAP*****ubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA (By similarity). Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. 
Sequence Annotation
 DOMAIN 119 189 PAH 1.
 DOMAIN 300 383 PAH 2.
 DOMAIN 456 525 PAH 3.
 REGION 119 196 Interaction with HCFC1.
 REGION 205 480 Interaction with REST (By similarity).
 REGION 458 525 Interaction with SAP30 (By similarity).
 REGION 523 850 Interaction with NCOR1 (By similarity).
 REGION 524 659 Interaction with SUDS3 and SAP130.
 REGION 687 829 Interaction with HDAC1 and ARID4B.
 REGION 888 967 Interaction with OGT.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 469 469 N6-acetyllysine.
 MOD_RES 832 832 Phosphoserine.
 MOD_RES 860 860 Phosphoserine.
 MOD_RES 940 940 Phosphoserine.
 MOD_RES 1112 1112 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1273 AA 
Protein Sequence
MKRRLDDQES PVYAAQQRRI PGSTEAFPHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVTP 60
SYQVSAMPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR 120
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM 180
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SAQSAPAPAQ 240
PAPQPPPAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ 300
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA 360
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP 420
SQNGCQIRRH PTGTTPPVKK KPKLLNLKDS SMADASKHGG GTESLFFDKV RKALRSAEAY 480
ENFLRCLVIF NQEVISRAEL VQLVSPFLGK FPELFNWFKN FLGYKESVHL ETYPKERATE 540
GIAMEIDYAS CKRLGSSYRA LPKSYQQPKC TGRTPLCKEV LNDTWVSFPS WSEDSTFVSS 600
KKTQYEEHIY RCEDERFELD VVLETNLATI RVLEAIQKKL SRLSAEEQAK FRLDNTLGGT 660
SEVIHRKALQ RIYADKAADI IDGLRKNPSI AVPIVLKRLK MKEEEWREAQ RGFNKVWREQ 720
NEKYYLKSLD HQGINFKQND TKVLRSKSLL NEIESIYDER QEQATEENAG VPVGPHLSLA 780
YEDKQILEDA AALIIHHVKR QTGIQKEDKY KIKQIMHHFI PDLLFAQRGD LSDVEEEEEE 840
EMDVDEATGA VKKHNGVGGS PPKSKLLFSN TAAQKLRGMD EVYNLFYVNN NWYIFMRLHQ 900
ILCLRLLRIC SQAERQIEEE NREREWEREV LGIKRDKSDS PAIQLRLKEP MDVDVEDYYP 960
AFLDMVRSLL DGNIDSSQYE DSLREMFTIH AYIAFTMDKL IQSIVRQLQH IVSDEICVQV 1020
TDLYLAENNN GATGGQLNTQ NSRSLLESTY QRKAEQLMSD ENCFKLMFIQ SQGQVQLTIE 1080
LLDTEEENSD DPVEAERWSD YVERYMNSDT TSPELREHLA QKPVFLPRNL RRIRKCQRGR 1140
EQQEKEGKEG NSKKTMENVD SLDKLECRFK LNSYKMVYVI KSEDYMYRRT ALLRAHQSHE 1200
RVSKRLHQRF QAWVDKWTKE HVPREMAAET SKWLMGEGLE GLVPCTTTCD TETLHFVSIN 1260
KYRVKYGTVF KAP 1273 
Gene Ontology
 GO:0000776; C:kinetochore; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0016580; C:Sin3 complex; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0017053; C:transcriptional repressor complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0033558; F:protein deacetylase activity; IMP:BHF-UCL.
 GO:0001106; F:RNA polymerase II transcription corepressor activity; IEA:Compara.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0002218; P:activation of innate immune response; IMP:BHF-UCL.
 GO:0007568; P:aging; IEA:Compara.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0034613; P:cellular protein localization; IEA:Compara.
 GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
 GO:0006260; P:DNA replication; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:1901675; P:negative regulation of histone H3-K27 acetylation; IMP:BHF-UCL.
 GO:1900181; P:negative regulation of protein localization to nucleus; IMP:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
 GO:0031937; P:positive regulation of chromatin silencing; IMP:BHF-UCL.
 GO:0002230; P:positive regulation of defense response to virus by host; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Compara.
 GO:0051595; P:response to methylglyoxal; IEA:Compara.
 GO:0010243; P:response to organic nitrogen; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR013194; HDAC_interact.
 IPR003822; PAH. 
Pfam
 PF02671; PAH
 PF08295; Sin3_corepress 
SMART
 SM00761; HDAC_interact 
PROSITE
 PS51477; PAH 
PRINTS