CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018776
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Translational activator GCN1 
Protein Synonyms/Alias
 HsGCN1; GCN1-like protein 1 
Gene Name
 GCN1L1 
Gene Synonyms/Alias
 KIAA0219 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12TQVSETLKRFAGKVTubiquitination[1, 2]
17TLKRFAGKVTTASVKubiquitination[2]
35EILSELGKCVAGKDLacetylation[3]
35EILSELGKCVAGKDLubiquitination[2]
101QSSGIGSKAGVPSKSubiquitination[2, 4]
268LILPTIQKSLLRSPEacetylation[5]
268LILPTIQKSLLRSPEubiquitination[2, 4, 6, 7, 8]
308KGLAGHLKSNSPRLMubiquitination[6]
521WQLIVDEKKQVFTSEubiquitination[6]
590QAQQTVRKLLSSLGGubiquitination[6]
609HGLLEELKTVLSSHKubiquitination[2, 7, 8]
616KTVLSSHKVLPLEALubiquitination[2, 4, 6, 7, 8]
635GEVTEAGKAYVPPRVubiquitination[8]
695PALLARMKIDPEAFIubiquitination[1, 2, 6, 7, 8]
776PAGELYDKSIIQSAQubiquitination[6]
788SAQQDSIKKANMKREubiquitination[2, 8]
802ENKAYSFKEQIIELEubiquitination[4]
821IKKKKGIKEEVQLTSubiquitination[2]
831VQLTSKQKEMLQAQLubiquitination[2]
898PLAAPRIKNPFLSLAubiquitination[2, 7]
914CVMPSRLKALGTLVSubiquitination[2]
948EELSVAVKRAVMLLHubiquitination[2, 6, 7, 9]
965TITSRVGKGEPGAAPubiquitination[2, 4, 6, 8, 9, 10]
1134LRRLWVVKFDKEEEIubiquitination[4]
1208LMEIYQEKLYRPPPVubiquitination[1, 2, 6, 8]
1304PVFEEFLKNAPNDASubiquitination[8]
1390QQLLESDKYAERKGAubiquitination[2, 4]
1395SDKYAERKGAAYGLAubiquitination[2]
1406YGLAGLVKGLGILSLubiquitination[6]
1414GLGILSLKQQEMMAAubiquitination[2, 8]
1484EAADDCAKAVMSNLSubiquitination[2]
1514EEESWRTKAGSVELLubiquitination[2]
1556DSHVKVQKAGQQALRubiquitination[2, 6, 11]
1594DPSRKTQKCLQTLLDubiquitination[6]
1663PSVTPGLKASLLDPVubiquitination[2, 4, 6, 8]
1679EVRTVSAKALGAMVKubiquitination[2]
1731MAGLGVEKLEKLMPEubiquitination[2, 6]
1745EIVATASKVDIAPHVubiquitination[2]
1871FGTAQSNKAIITALGubiquitination[6]
1959LVRKLGEKILPEIIPubiquitination[2, 8]
1992IGLSEIMKSTSRDAVubiquitination[2]
2066EFALDGLKQVMAIKSubiquitination[6]
2072LKQVMAIKSRVVLPYubiquitination[2]
2083VLPYLVPKLTTPPVNubiquitination[2, 4]
2183NIYCSRSKADYTSHLubiquitination[2, 6]
2221DALNAITKKLDAGNQubiquitination[2, 6, 7, 8]
2222ALNAITKKLDAGNQLubiquitination[2]
2237ALIEELHKEIRLIGNubiquitination[2, 4]
2247RLIGNESKGEHVPGFubiquitination[2]
2259PGFCLPKKGVTSILPubiquitination[2]
2280LTGSPEQKEEAAKALubiquitination[2, 6, 8]
2285EQKEEAAKALGLVIRubiquitination[2, 4, 6]
2366SNRGVRLKAADALGKubiquitination[2, 6, 8]
2380KLISIHIKVDPLFTEubiquitination[6]
2418VIQGAGAKVDAVIRKubiquitination[6]
2550GGGQLPAKLSSLFVKubiquitination[2, 4, 7]
2557KLSSLFVKCLQNPSSubiquitination[2, 6]
2572DIRLVAEKMIWWANKubiquitination[4]
2591PLDPQAIKPILKALLubiquitination[4]
2602KALLDNTKDKNTVVRubiquitination[2]
2621QAIVNLLKMRQGEEVubiquitination[1, 2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048
Functional Description
 Acts as a translation activator that mediates translational control and perform an EF3-related function on the ribosome by regulating GCN2 protein kinase (EIF2AK1-4) activity (By similarity). 
Sequence Annotation
 REPEAT 257 294 HEAT 1.
 REPEAT 295 331 HEAT 2.
 REPEAT 460 503 HEAT 3.
 REPEAT 1078 1115 HEAT 4.
 REPEAT 1290 1332 HEAT 5.
 REPEAT 1335 1372 HEAT 6.
 REPEAT 1455 1492 HEAT 7.
 REPEAT 1493 1530 HEAT 8.
 REPEAT 1534 1571 HEAT 9.
 REPEAT 1573 1609 HEAT 10.
 REPEAT 1611 1648 HEAT 11.
 REPEAT 1653 1690 HEAT 12.
 REPEAT 1773 1810 HEAT 13.
 REPEAT 1812 1848 HEAT 14.
 REPEAT 1921 1958 HEAT 15.
 REPEAT 1959 1996 HEAT 16.
 REPEAT 2001 2038 HEAT 17.
 REPEAT 2039 2076 HEAT 18.
 REPEAT 2188 2225 HEAT 19.
 REPEAT 2259 2296 HEAT 20.
 REPEAT 2339 2380 HEAT 21.
 REPEAT 2422 2459 HEAT 22.
 REPEAT 2560 2583 HEAT 23.
 REPEAT 2588 2625 HEAT 24.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 786 786 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2671 AA 
Protein Sequence
MAADTQVSET LKRFAGKVTT ASVKERREIL SELGKCVAGK DLPEGAVKGL CKLFCLTLHR 60
YRDAASRRAL QAAIQQLAEA QPEATAKNLL HSLQSSGIGS KAGVPSKSSG SAALLALTWT 120
CLLVRIVFPS RAKRQGDIWN KLVEVQCLLL LEVLGGSHKH AVDGAVKKLT KLWKENPGLV 180
EQYLSAILSL EPNQNYAGML GLLVQFCTSH KEMDVVSQHK SALLDFYMKN ILMSKVKPPK 240
YLLDSCAPLL RYLSHSEFKD LILPTIQKSL LRSPENVIET ISSLLASVTL DLSQYAMDIV 300
KGLAGHLKSN SPRLMDEAVL ALRNLARQCS DSSAMESLTK HLFAILGGSE GKLTVVAQKM 360
SVLSGIGSVS HHVVSGPSSQ VLNGIVAELF IPFLQQEVHE GTLVHAVSVL ALWCNRFTME 420
VPKKLTEWFK KAFSLKTSTS AVRHAYLQCM LASYRGDTLL QALDLLPLLI QTVEKAASQS 480
TQVPTITEGV AAALLLLKLS VADSQAEAKL SSFWQLIVDE KKQVFTSEKF LVMASEDALC 540
TVLHLTERLF LDHPHRLTGN KVQQYHRALV AVLLSRTWHV RRQAQQTVRK LLSSLGGFKL 600
AHGLLEELKT VLSSHKVLPL EALVTDAGEV TEAGKAYVPP RVLQEALCVI SGVPGLKGDV 660
TDTEQLAQEM LIISHHPSLV AVQSGLWPAL LARMKIDPEA FITRHLDQII PRMTTQSPLN 720
QSSMNAMGSL SVLSPDRVLP QLISTITASV QNPALRLVTR EEFAIMQTPA GELYDKSIIQ 780
SAQQDSIKKA NMKRENKAYS FKEQIIELEL KEEIKKKKGI KEEVQLTSKQ KEMLQAQLDR 840
EAQVRRRLQE LDGELEAALG LLDIILAKNP SGLTQYIPVL VDSFLPLLKS PLAAPRIKNP 900
FLSLAACVMP SRLKALGTLV SHVTLRLLKP ECVLDKSWCQ EELSVAVKRA VMLLHTHTIT 960
SRVGKGEPGA APLSAPAFSL VFPFLKMVLT EMPHHSEEEE EWMAQILQIL TVQAQLRASP 1020
NTPPGRVDEN GPELLPRVAM LRLLTWVIGT GSPRLQVLAS DTLTTLCASS SGDDGCAFAE 1080
QEEVDVLLCA LQSPCASVRE TVLRGLMELH MVLPAPDTDE KNGLNLLRRL WVVKFDKEEE 1140
IRKLAERLWS MMGLDLQPDL CSLLIDDVIY HEAAVRQAGA EALSQAVARY QRQAAEVMGR 1200
LMEIYQEKLY RPPPVLDALG RVISESPPDQ WEARCGLALA LNKLSQYLDS SQVKPLFQFF 1260
VPDALNDRHP DVRKCMLDAA LATLNTHGKE NVNSLLPVFE EFLKNAPNDA SYDAVRQSVV 1320
VLMGSLAKHL DKSDPKVKPI VAKLIAALST PSQQVQESVA SCLPPLVPAI KEDAGGMIQR 1380
LMQQLLESDK YAERKGAAYG LAGLVKGLGI LSLKQQEMMA ALTDAIQDKK NFRRREGALF 1440
AFEMLCTMLG KLFEPYVVHV LPHLLLCFGD GNQYVREAAD DCAKAVMSNL SAHGVKLVLP 1500
SLLAALEEES WRTKAGSVEL LGAMAYCAPK QLSSCLPNIV PKLTEVLTDS HVKVQKAGQQ 1560
ALRQIGSVIR NPEILAIAPV LLDALTDPSR KTQKCLQTLL DTKFVHFIDA PSLALIMPIV 1620
QRAFQDRSTD TRKMAAQIIG NMYSLTDQKD LAPYLPSVTP GLKASLLDPV PEVRTVSAKA 1680
LGAMVKGMGE SCFEDLLPWL METLTYEQSS VDRSGAAQGL AEVMAGLGVE KLEKLMPEIV 1740
ATASKVDIAP HVRDGYIMMF NYLPITFGDK FTPYVGPIIP CILKALADEN EFVRDTALRA 1800
GQRVISMYAE TAIALLLPQL EQGLFDDLWR IRFSSVQLLG DLLFHISGVT GKMTTETASE 1860
DDNFGTAQSN KAIITALGVE RRNRVLAGLY MGRSDTQLVV RQASLHVWKI VVSNTPRTLR 1920
EILPTLFGLL LGFLASTCAD KRTIAARTLG DLVRKLGEKI LPEIIPILEE GLRSQKSDER 1980
QGVCIGLSEI MKSTSRDAVL YFSESLVPTA RKALCDPLEE VREAAAKTFE QLHSTIGHQA 2040
LEDILPFLLK QLDDEEVSEF ALDGLKQVMA IKSRVVLPYL VPKLTTPPVN TRVLAFLSSV 2100
AGDALTRHLG VILPAVMLAL KEKLGTPDEQ LEMANCQAVI LSVEDDTGHR IIIEYLLEAT 2160
RSPEVGMRQA AAIILNIYCS RSKADYTSHL RSLVSGLIRL FNDSSPVVLE ESWDALNAIT 2220
KKLDAGNQLA LIEELHKEIR LIGNESKGEH VPGFCLPKKG VTSILPVLRE GVLTGSPEQK 2280
EEAAKALGLV IRLTSADALR PSVVSITGPL IRILGDRFSW NVKAALLETL SLLLAKVGIA 2340
LKPFLPQLQT TFTKALQDSN RGVRLKAADA LGKLISIHIK VDPLFTELLN GIRAMEDPGV 2400
RDTMLQALRF VIQGAGAKVD AVIRKNIVSL LLSMLGHDED NTRISSAGCL GELCAFLTEE 2460
ELSAVLQQCL LADVSGIDWM VRHGRSLALS VAVNVAPGRL CAGRYSSDVQ EMILSSATAD 2520
RIPIAVSGVR GMGFLMRHHI ETGGGQLPAK LSSLFVKCLQ NPSSDIRLVA EKMIWWANKD 2580
PLPPLDPQAI KPILKALLDN TKDKNTVVRA YSDQAIVNLL KMRQGEEVFQ SLSKILDVAS 2640
LEVLNEVNRR SLKKLASQAD STEQVDDTIL T 2671 
Gene Ontology
 GO:0005840; C:ribosome; NAS:UniProtKB.
 GO:0008135; F:translation factor activity, nucleic acid binding; NAS:UniProtKB.
 GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR000225; Armadillo.
 IPR022716; DUF3554.
 IPR026827; ECM29/GCN1.
 IPR021133; HEAT_type_2. 
Pfam
 PF12074; DUF3554 
SMART
 SM00185; ARM 
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS