CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022442
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sacsin 
Protein Synonyms/Alias
 DnaJ homolog subfamily C member 29; DNAJC29 
Gene Name
 SACS 
Gene Synonyms/Alias
 KIAA0730 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
289LSSNLYNKQKVLELFubiquitination[1]
291SNLYNKQKVLELFESubiquitination[1]
361TAISNYCKKTPSNNIubiquitination[1]
406GGRGISSKLDSLADEubiquitination[1, 2]
434SSRDDEAKGATSDFSubiquitination[1]
514TLILDSIKRLEMEKSubiquitination[1]
533LSVDVIYKLWPEASKubiquitination[2]
625SGTTPVRKVTPAWVRubiquitination[1]
714RFILDNLKPHLVAALubiquitination[1]
722PHLVAALKEAAQTRGubiquitination[1]
853KLGGFVLKKLDASIQubiquitination[1]
854LGGFVLKKLDASIQHubiquitination[1]
905THKDALRKFLASLTDubiquitination[1]
928IQELAIFKRINHSSDubiquitination[1]
943QGISSYTKLKGCKVLacetylation[3, 4, 5, 6]
943QGISSYTKLKGCKVLubiquitination[1]
955KVLHHTAKLPADLRLubiquitination[1]
982IRLANMLKIEQLKTTubiquitination[1]
987MLKIEQLKTTSCLKLubiquitination[1]
1274KDSFRALKFPWVWTGubiquitination[1]
1342VIQKIYLKSDQDLSEubiquitination[2]
1435MKTAEWLKVPCLSTRubiquitination[1, 6]
1465EPLTVRIKNILEEYPubiquitination[1]
1715AQDTVIIKKKSCSSKubiquitination[2]
1733TPVLSVLKEAAKLMKubiquitination[1]
1797AALFEMAKSGQSKKPubiquitination[2]
1802MAKSGQSKKPSDELSubiquitination[1]
1989GSTWVSMKNVRFLDDubiquitination[1]
2000FLDDSILKRRDVGSAubiquitination[1]
2043GFEEAGCKQILLENTubiquitination[1]
2195LLSLIDEKLKIRDPRubiquitination[1]
2197SLIDEKLKIRDPRAKubiquitination[1]
2334LMQNEITKMSIIDKLacetylation[7]
2358NAYVDSEKVSFHLNFacetylation[7]
2414IDQERGTKQITEENFubiquitination[8]
2709LRNAEMAKVSEISSVubiquitination[1]
3894SLQNDSVKVRSDLENubiquitination[1]
3918SQDGRLVKSSILVFDubiquitination[1]
4135DIYRIGEKLDSLGVKacetylation[5]
4419RQQQNKEKCPPSAGQubiquitination[1]
4439FFVPPTFKSVGNPVEubiquitination[1]
4578LENFMQQKV******ubiquitination[1]
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] 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]
 [5] 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]
 [6] 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]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [8] 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
 Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. 
Sequence Annotation
 DOMAIN 9 84 Ubiquitin-like.
 DOMAIN 4306 4393 J.
 DOMAIN 4451 4567 HEPN.
 MOD_RES 943 943 N6-acetyllysine.
 MOD_RES 1779 1779 Phosphoserine.
 MOD_RES 3435 3435 Phosphoserine.
 MOD_RES 4263 4263 Phosphothreonine (By similarity).
 MOD_RES 4264 4264 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Disease mutation; Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4579 AA 
Protein Sequence
METKENRWVP VTVLPGCVGC RTVAALASWT VRDVKERIFA ETGFPVSEQR LWRGGRELSD 60
WIKIGDLTSK NCHLFVNLQS KGLKGGGRFG QTTPPLVDFL KDILRRYPEG GQILKELIQN 120
AEDAGATEVK FLYDETQYGT ETLWSKDMAP YQGPALYVYN NAVFTPEDWH GIQEIARSRK 180
KDDPLKVGRF GIGFNSVYHI TDVPCIFSGD QIGMLDPHQT LFGPHESGQC WNLKDDSKEI 240
SELSDQFAPF VGIFGSTKET FINGNFPGTF FRFPLRLQPS QLSSNLYNKQ KVLELFESFR 300
ADADTVLLFL KSVQDVSLYV READGTEKLV FRVTSSESKA LKHERPNSIK ILGTAISNYC 360
KKTPSNNITC VTYHVNIVLE EESTKDAQKT SWLVCNSVGG RGISSKLDSL ADELKFVPII 420
GIAMPLSSRD DEAKGATSDF SGKAFCFLPL PPGEESSTGL PVHISGFFGL TDNRRSIKWR 480
ELDQWRDPAA LWNEFLVMNV VPKAYATLIL DSIKRLEMEK SSDFPLSVDV IYKLWPEASK 540
VKVHWQPVLE PLFSELLQNA VIYSISCDWV RLEQVYFSEL DENLEYTKTV LNYLQSSGKQ 600
IAKVPGNVDA AVQLTAASGT TPVRKVTPAW VRQVLRKCAH LGCAEEKLHL LEFVLSDQAY 660
SELLGLELLP LQNGNFVPFS SSVSDQDVIY ITSAEYPRSL FPSLEGRFIL DNLKPHLVAA 720
LKEAAQTRGR PCTQLQLLNP ERFARLIKEV MNTFWPGREL IVQWYPFDEN RNHPSVSWLK 780
MVWKNLYIHF SEDLTLFDEM PLIPRTILEE GQTCVELIRL RIPSLVILDD ESEAQLPEFL 840
ADIVQKLGGF VLKKLDASIQ HPLIKKYIHS PLPSAVLQIM EKMPLQKLCN QITSLLPTHK 900
DALRKFLASL TDSSEKEKRI IQELAIFKRI NHSSDQGISS YTKLKGCKVL HHTAKLPADL 960
RLSISVIDSS DEATIRLANM LKIEQLKTTS CLKLVLKDIE NAFYSHEEVT QLMLWVLENL 1020
SSLKNENPNV LEWLTPLKFI QISQEQMVSA GELFDPDIEV LKDLFCNEEG TYFPPSVFTS 1080
PDILHSLRQI GLKNEASLKE KDVVQVAKKI EALQVGACPD QDVLLKKAKT LLLVLNKNHT 1140
LLQSSEGKMT LKKIKWVPAC KERPPNYPGS LVWKGDLCNL CAPPDMCDVG HAILIGSSLP 1200
LVESIHVNLE KALGIFTKPS LSAVLKHFKI VVDWYSSKTF SDEDYYQFQH ILLEIYGFMH 1260
DHLNEGKDSF RALKFPWVWT GKKFCPLAQA VIKPIHDLDL QPYLHNVPKT MAKFHQLFKV 1320
CGSIEELTSD HISMVIQKIY LKSDQDLSEQ ESKQNLHLML NIIRWLYSNQ IPASPNTPVP 1380
IHHSKNPSKL IMKPIHECCY CDIKVDDLND LLEDSVEPII LVHEDIPMKT AEWLKVPCLS 1440
TRLINPENMG FEQSGQREPL TVRIKNILEE YPSVSDIFKE LLQNADDANA TECSFLIDMR 1500
RNMDIRENLL DPGMAACHGP ALWSFNNSQF SDSDFVNITR LGESLKRGEV DKVGKFGLGF 1560
NSVYHITDIP IIMSREFMIM FDPNINHISK HIKDKSNPGI KINWSKQQKR LRKFPNQFKP 1620
FIDVFGCQLP LTVEAPYSYN GTLFRLSFRT QQEAKVSEVS STCYNTADIY SLVDEFSLCG 1680
HRLIIFTQSV KSMYLKYLKI EETNPSLAQD TVIIKKKSCS SKALNTPVLS VLKEAAKLMK 1740
TCSSSNKKLP SDEPKSSCIL QITVEEFHHV FRRIADLQSP LFRGPDDDPA ALFEMAKSGQ 1800
SKKPSDELSQ KTVECTTWLL CTCMDTGEAL KFSLSESGRR LGLVPCGAVG VQLSEIQDQK 1860
WTVKPHIGEV FCYLPLRIKT GLPVHINGCF AVTSNRKEIW KTDTKGRWNT TFMRHVIVKA 1920
YLQVLSVLRD LATSGELMDY TYYAVWPDPD LVHDDFSVIC QGFYEDIAHG KGKELTKVFS 1980
DGSTWVSMKN VRFLDDSILK RRDVGSAAFK IFLKYLKKTG SKNLCAVELP SSVKLGFEEA 2040
GCKQILLENT FSEKQFFSEV FFPNIQEIEA ELRDPLMIFV LNEKVDEFSG VLRVTPCIPC 2100
SLEGHPLVLP SRLIHPEGRV AKLFDIKDGR FPYGSTQDYL NPIILIKLVQ LGMAKDDILW 2160
DDMLERAVSV AEINKSDHVA ACLRSSILLS LIDEKLKIRD PRAKDFAAKY QTIRFLPFLT 2220
KPAGFSLDWK GNSFKPETMF AATDLYTAEH QDIVCLLQPI LNENSHSFRG CGSVSLAVKE 2280
FLGLLKKPTV DLVINQLKEV AKSVDDGITL YQENITNACY KYLHEALMQN EITKMSIIDK 2340
LKPFSFILVE NAYVDSEKVS FHLNFEAAPY LYQLPNKYKN NFRELFETVG VRQSCTVEDF 2400
ALVLESIDQE RGTKQITEEN FQLCRRIISE GIWSLIREKK QEFCEKNYGK ILLPDTNLML 2460
LPAKSLCYND CPWIKVKDTT VKYCHADIPR EVAVKLGAVP KRHKALERYA SNVCFTTLGT 2520
EFGQKEKLTS RIKSILNAYP SEKEMLKELL QNADDAKATE ICFVFDPRQH PVDRIFDDKW 2580
APLQGPALCV YNNQPFTEDD VRGIQNLGKG TKEGNPYKTG QYGIGFNSVY HITDCPSFIS 2640
GNDILCIFDP HARYAPGATS ISPGRMFRDL DADFRTQFSD VLDLYLGTHF KLDNCTMFRF 2700
PLRNAEMAKV SEISSVPASD RMVQNLLDKL RSDGAELLMF LNHMEKISIC EIDKSTGALN 2760
VLYSVKGKIT DGDRLKRKQF HASVIDSVTK KRQLKDIPVQ QITYTMDTED SEGNLTTWLI 2820
CNRSGFSSME KVSKSVISAH KNQDITLFPR GGVAACITHN YKKPHRAFCF LPLSLETGLP 2880
FHVNGHFALD SARRNLWRDD NGVGVRSDWN NSLMTALIAP AYVELLIQLK KRYFPGSDPT 2940
LSVLQNTPIH VVKDTLKKFL SFFPVNRLDL QPDLYCLVKA LYNCIHEDMK RLLPVVRAPN 3000
IDGSDLHSAV IITWINMSTS NKTRPFFDNL LQDELQHLKN ADYNITTRKT VAENVYRLKH 3060
LLLEIGFNLV YNCDETANLY HCLIDADIPV SYVTPADIRS FLMTFSSPDT NCHIGKLPCR 3120
LQQTNLKLFH SLKLLVDYCF KDAEENEIEV EGLPLLITLD SVLQTFDAKR PKFLTTYHEL 3180
IPSRKDLFMN TLYLKYSNIL LNCKVAKVFD ISSFADLLSS VLPREYKTKS CTKWKDNFAS 3240
ESWLKNAWHF ISESVSVKED QEETKPTFDI VVDTLKDWAL LPGTKFTVSA NQLVVPEGDV 3300
LLPLSLMHIA VFPNAQSDKV FHALMKAGCI QLALNKICSK DSAFVPLLSC HTANIESPTS 3360
ILKALHYMVQ TSTFRAEKLV ENDFEALLMY FNCNLNHLMS QDDIKILKSL PCYKSISGRY 3420
VSIGKFGTCY VLTKSIPSAE VEKWTQSSSS AFLEEKIHLK ELYEVIGCVP VDDLEVYLKH 3480
LLPKIENLSY DAKLEHLIYL KNRLSSAEEL SEIKEQLFEK LESLLIIHDA NSRLKQAKHF 3540
YDRTVRVFEV MLPEKLFIPN DFFKKLEQLI KPKNHVTFMT SWVEFLRNIG LKYILSQQQL 3600
LQFAKEISVR ANTENWSKET LQNTVDILLH HIFQERMDLL SGNFLKELSL IPFLCPERAP 3660
AEFIRFHPQY QEVNGTLPLI KFNGAQVNPK FKQCDVLQLL WTSCPILPEK ATPLSIKEQE 3720
GSDLGPQEQL EQVLNMLNVN LDPPLDKVIN NCRNICNITT LDEEMVKTRA KVLRSIYEFL 3780
SAEKREFRFQ LRGVAFVMVE DGWKLLKPEE VVINLEYESD FKPYLYKLPL ELGTFHQLFK 3840
HLGTEDIIST KQYVEVLSRI FKNSEGKQLD PNEMRTVKRV VSGLFRSLQN DSVKVRSDLE 3900
NVRDLALYLP SQDGRLVKSS ILVFDDAPHY KSRIQGNIGV QMLVDLSQCY LGKDHGFHTK 3960
LIMLFPQKLR PRLLSSILEE QLDEETPKVC QFGALCSLQG RLQLLLSSEQ FITGLIRIMK 4020
HENDNAFLAN EEKAIRLCKA LREGLKVSCF EKLQTTLRVK GFNPIPHSRS ETFAFLKRFG 4080
NAVILLYIQH SDSKDINFLL ALAMTLKSAT DNLISDTSYL IAMLGCNDIY RIGEKLDSLG 4140
VKYDSSEPSK LELPMPGTPI PAEIHYTLLM DPMNVFYPGE YVGYLVDAEG GDIYGSYQPT 4200
YTYAIIVQEV EREDADNSSF LGKIYQIDIG YSEYKIVSSL DLYKFSRPEE SSQSRDSAPS 4260
TPTSPTEFLT PGLRSIPPLF SGRESHKTSS KHQSPKKLKV NSLPEILKEV TSVVEQAWKL 4320
PESERKKIIR RLYLKWHPDK NPENHDIANE VFKHLQNEIN RLEKQAFLDQ NADRASRRTF 4380
STSASRFQSD KYSFQRFYTS WNQEATSHKS ERQQQNKEKC PPSAGQTYSQ RFFVPPTFKS 4440
VGNPVEARRW LRQARANFSA ARNDLHKNAN EWVCFKCYLS TKLALIAADY AVRGKSDKDV 4500
KPTALAQKIE EYSQQLEGLT NDVHTLEAYG VDSLKTRYPD LLPFPQIPND RFTSEVAMRV 4560
MECTACIIIK LENFMQQKV 4579 
Gene Ontology
 GO:0030424; C:axon; TAS:BHF-UCL.
 GO:0070852; C:cell body fiber; TAS:BHF-UCL.
 GO:0030425; C:dendrite; TAS:BHF-UCL.
 GO:0005739; C:mitochondrion; IDA:BHF-UCL.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0051087; F:chaperone binding; IDA:UniProtKB.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0090084; P:negative regulation of inclusion body assembly; IMP:BHF-UCL.
 GO:0006457; P:protein folding; NAS:UniProtKB. 
Interpro
 IPR001623; DnaJ_domain.
 IPR003594; HATPase_ATP-bd.
 IPR007842; HEPN.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF05168; HEPN
 PF00240; ubiquitin 
SMART
 SM00271; DnaJ
 SM00748; HEPN 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS50910; HEPN
 PS00299; UBIQUITIN_1
 PS50053; UBIQUITIN_2 
PRINTS