CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018376
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein ELYS 
Protein Synonyms/Alias
 Embryonic large molecule derived from yolk sac; Protein MEL-28; Putative AT-hook-containing transcription factor 1 
Gene Name
 AHCTF1 
Gene Synonyms/Alias
 ELYS; TMBS62; MSTP108 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
84PPVVLAVKEFSWQKRubiquitination[1, 2]
90VKEFSWQKRTGLLIGubiquitination[3]
118LGISKVVKAVVLPGRubiquitination[2, 3]
312QLAFGNRKCLASGQIubiquitination[3]
350RGQTSNTKLLGCQSIubiquitination[2, 3, 4]
359LGCQSIEKFRSHGDRubiquitination[3]
504KETLTFLKKSGPSLNubiquitination[1, 2, 3, 4]
505ETLTFLKKSGPSLNEubiquitination[2, 3, 4]
717FERLSRGKWNPDCLMubiquitination[2, 3, 5]
738QLGERIEKLWKRDEGubiquitination[3]
969ANYVPALKLNQTLKIubiquitination[1, 2, 3, 4, 6]
975LKLNQTLKINVMNDRubiquitination[3]
1002SILDQYGKILPRVHRubiquitination[1, 2, 3, 4, 5]
1017KLAIERAKPYHLSTSacetylation[7]
1017KLAIERAKPYHLSTSubiquitination[3]
1041KPLSAVPKQVVTGTVubiquitination[4]
1069IGEVWASKEPINSTTubiquitination[1, 2, 3, 4, 8]
1109FFGTPISKASQKISRubiquitination[1, 2, 8]
1141FIQQSSMKSPLYLVSubiquitination[3, 4]
1158LPSSSQLKGSPQAISubiquitination[2, 3, 4]
1181ETPLVVKKAKSLAMSubiquitination[3]
1677ENLLDVIKDTRSKEIubiquitination[1, 8]
2024SENVDVGKPALGKSIacetylation[9, 10]
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] 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]
 [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] 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]
 [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] 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]
 [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] 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]
 [10] 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
 Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. 
Sequence Annotation
 DNA_BIND 1971 1983 A.T hook.
 REGION 1 981 Necessary for cytoplasmic localization
 REGION 1149 2266 Necessary for nuclear localization (By
 REGION 1446 1698 Mediates transcriptional activity (By
 MOD_RES 528 528 Phosphoserine.
 MOD_RES 1142 1142 Phosphoserine.
 MOD_RES 1150 1150 Phosphoserine.
 MOD_RES 1155 1155 Phosphoserine.
 MOD_RES 1160 1160 Phosphoserine.
 MOD_RES 1175 1175 Phosphothreonine.
 MOD_RES 1214 1214 Phosphoserine.
 MOD_RES 1222 1222 Phosphoserine.
 MOD_RES 1232 1232 Phosphoserine.
 MOD_RES 1250 1250 Phosphoserine.
 MOD_RES 1283 1283 Phosphoserine.
 MOD_RES 1297 1297 Phosphoserine.
 MOD_RES 1369 1369 Phosphothreonine.
 MOD_RES 1371 1371 Phosphoserine (By similarity).
 MOD_RES 1513 1513 Phosphoserine.
 MOD_RES 1517 1517 Phosphothreonine.
 MOD_RES 1533 1533 Phosphoserine.
 MOD_RES 1541 1541 Phosphoserine.
 MOD_RES 1729 1729 Phosphoserine.
 MOD_RES 1806 1806 Phosphoserine.
 MOD_RES 1808 1808 Phosphothreonine.
 MOD_RES 1878 1878 Phosphoserine.
 MOD_RES 1884 1884 Phosphoserine.
 MOD_RES 1898 1898 Phosphoserine.
 MOD_RES 1944 1944 Phosphoserine.
 MOD_RES 1946 1946 Phosphoserine.
 MOD_RES 1996 1996 Phosphoserine.
 MOD_RES 2043 2043 Phosphoserine.
 MOD_RES 2044 2044 Phosphoserine.
 MOD_RES 2060 2060 Phosphoserine.
 MOD_RES 2089 2089 Phosphoserine.
 MOD_RES 2120 2120 Phosphoserine.
 MOD_RES 2123 2123 Phosphoserine.
 MOD_RES 2154 2154 Phosphoserine.
 MOD_RES 2212 2212 Phosphoserine.
 MOD_RES 2222 2222 Phosphoserine.
 MOD_RES 2226 2226 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; DNA-binding; Kinetochore; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2266 AA 
Protein Sequence
MRDLRAQVTS GLLPFPEVTL QALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSI 60
TGERLSAYRF SGVNEQPPVV LAVKEFSWQK RTGLLIGLEE TEGSVLCLYD LGISKVVKAV 120
VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLVDL CLDDLSCNQN 180
EVEASDLEVL TGIPAEVPHI RESVMRQGRH LCFQLVSPTG TAVSTLSYIS RTNQLAVGFS 240
DGYLALWNMK SMKREYYIQL ESGQVPVYAV TFQEPENDPR NCCYLWAVQS TQDSEGDVLS 300
LHLLQLAFGN RKCLASGQIL YEGLEYCEER YTLDLTGGMF PLRGQTSNTK LLGCQSIEKF 360
RSHGDREEGV NEALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE 420
YLHNCSYFAL WSLESVVSRT SPHGILDILV HERSLNRGVP PSYPPPEQFF NPSTYNFDAT 480
CLLNSGVVHL TCTGFQKETL TFLKKSGPSL NELIPDGYNR CLVAGLLSPR FVDVQPSSLS 540
QEEQLEAILS AAIQTSSLGL LTGYIRRWIT EEQPNSATNL RFVLEWTWNK VVLTKEEFDR 600
LCVPLFDGSC HFMDPQTIQS IQQCYLLLSN LNIVLSCFAS EAREITERGL IDLSNKFVVS 660
HLICQYAQVV LWFSHSGLLP EGIDDSVQLS RLCYNYPVIQ NYYTSRRQKF ERLSRGKWNP 720
DCLMIDGLVS QLGERIEKLW KRDEGGTGKY PPASLHAVLD MYLLDGVTEA AKHSITIYLL 780
LDIMYSFPNK TDTPIESFPT VFAISWGQVK LIQGFWLIDH NDYESGLDLL FHPATAKPLS 840
WQHSKIIQAF MSQGEHRQAL RYIQTMKPTV SSGNDVILHL TVLLFNRCMV EAWNFLRQHC 900
NRLNIEELLK HMYEVCQEMG LMEDLLKLPF TDTEQECLVK FLQSSASVQN HEFLLVHHLQ 960
RANYVPALKL NQTLKINVMN DRDPRLRERS LARNSILDQY GKILPRVHRK LAIERAKPYH 1020
LSTSSVFRLV SRPKPLSAVP KQVVTGTVLT RSVFINNVLS KIGEVWASKE PINSTTPFNS 1080
SKIEEPSPIV YSLPAPELPE AFFGTPISKA SQKISRLLDL VVQPVPRPSQ CSEFIQQSSM 1140
KSPLYLVSRS LPSSSQLKGS PQAISRASEL HLLETPLVVK KAKSLAMSVT TSGFSEFTPQ 1200
SILRSTLRST PLASPSPSPG RSPQRLKETR ISFVEEDVHP KWIPGAADDS KLEVFTTPKK 1260
CAVPVETEWL KSKDRTTSFF LNSPEKEHQE MDEGSQSLEK LDVSKGNSSV SITSDETTLE 1320
YQDAPSPEDL EETVFTASKP KSSSTALTTN VTEQTEKDGD KDVFASEVTP SDLQKQMGNL 1380
EDAETKDLLV AAEAFSELNH LSPVQGTEAS LCAPSVYEGK IFTQKSKVPV LDEGLTSVET 1440
YTPAIRANDN KSMADVLGDG GNSSLTISEG PIVSERRLNQ EVALNLKEDH EVEVGVLKES 1500
VDLPEEKLPI SDSPPDTQEI HVIEQEKLEA QDSGEEARNL SFNELYPSGT LKLQYNFDTI 1560
DQQFCDLADN KDTAECDIAE VDGELFVAQS NFTLILEGEE GEVEPGDFAS SDVLPKAANT 1620
ATEEKLVCSG ENDNHGQIAN LPSAVTSDQK SQKVDTLPYV PEPIKVAIAE NLLDVIKDTR 1680
SKEITSDTME QSIHETIPLV SQNIMCPTKL VKSAFKTAQE TSTMTMNVSQ VDDVVSSKTR 1740
TRGQRIQNVN VKSAQQEASA DVATPKMPGQ SVRKKTRKAK EISEASENIY SDVRGLSQNQ 1800
QIPQNSVTPR RGRRKKEVNQ DILENTSSVE QELQITTGRE SKRLKSSQLL EPAVEETTKK 1860
EVKVSSVTKR TPRRIKRSVE NQESVEIIND LKVSTVTSPS RMIRKLRSTN LDASENTGNK 1920
QDDKSSDKQL RIKHVRRVRG REVSPSDVRE DSNLESSQLT VQAEFDMSAI PRKRGRPRKI 1980
NPSEDVGSKA VKEERSPKKK EAPSIRRRST RNTPAKSENV DVGKPALGKS ILVPNEELSM 2040
VMSSKKKLTK KTESQSQKRS LHSVSEERTD EMTHKETNEQ EERLLATASF TKSSRSSRTR 2100
SSKAILLPDL SEPNNEPLFS PASEVPRKAK AKKIEVPAQL KELVSDLSSQ FVISPPALRS 2160
RQKNTSNKNK LEDELKDDAQ SVETLGKPKA KRIRTSKTKQ ASKNTEKESA WSPPPIEIRL 2220
ISPLASPADG VKSKPRKTTE VTGTGLGRNR KKLSSYPKQI LRRKML 2266 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW. 
Interpro
 IPR017956; AT_hook_DNA-bd_motif.
 IPR025151; ELYS_dom. 
Pfam
 PF13934; ELYS 
SMART
 SM00384; AT_hook 
PROSITE
  
PRINTS