CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012840
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA excision repair protein ERCC-6-like 
Protein Synonyms/Alias
 ATP-dependent helicase ERCC6-like; PLK1-interacting checkpoint helicase; Tumor antigen BJ-HCC-15 
Gene Name
 ERCC6L 
Gene Synonyms/Alias
 PICH 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33KEAKEATKNGDLEEAubiquitination[1]
42GDLEEAFKLFNLAKDubiquitination[1]
48FKLFNLAKDIFPNEKmethylation[2]
55KDIFPNEKVLSRIQKmethylation[2]
55KDIFPNEKVLSRIQKubiquitination[1, 3, 4, 5]
239KIKTSSTKSAICARAubiquitination[1]
287LGTLKTFKMEYENPIubiquitination[1]
307KDATPGEKALGFKISubiquitination[1]
322ENLMAIIKPYFLRRTubiquitination[1]
348PEARLNEKNPDVDAIubiquitination[1]
383LQEEIYRKFVSLDHIubiquitination[1, 6]
391FVSLDHIKELLMETRubiquitination[1]
409AELGVLKKLCDHPRLubiquitination[1]
470IFLMDLLKRLRDEGHubiquitination[1]
576RVYRIGQKENVVVYRubiquitination[1]
601IYRRQVFKDSLIRQTubiquitination[1]
621NPFRYFSKQELRELFubiquitination[1, 6]
885GPNLDQLKDDEILRHubiquitination[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] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
Functional Description
 DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. 
Sequence Annotation
 REPEAT 21 54 TPR 1.
 DOMAIN 109 277 Helicase ATP-binding.
 DOMAIN 464 620 Helicase C-terminal.
 REPEAT 1200 1233 TPR 2.
 NP_BIND 122 129 ATP (Probable).
 MOTIF 228 231 DEAH box.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 755 755 Phosphoserine.
 MOD_RES 774 774 Phosphoserine.
 MOD_RES 807 807 Phosphoserine.
 MOD_RES 810 810 Phosphoserine.
 MOD_RES 813 813 Phosphothreonine.
 MOD_RES 820 820 Phosphoserine.
 MOD_RES 995 995 Phosphoserine.
 MOD_RES 1021 1021 Phosphoserine (By similarity).
 MOD_RES 1028 1028 Phosphoserine.
 MOD_RES 1063 1063 Phosphothreonine; by PLK1.
 MOD_RES 1069 1069 Phosphoserine.
 MOD_RES 1098 1098 Phosphoserine.
 MOD_RES 1181 1181 Phosphoserine.
 MOD_RES 1188 1188 Phosphoserine.  
Keyword
 ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1250 AA 
Protein Sequence
MEASRRFPEA EALSPEQAAH YLRYVKEAKE ATKNGDLEEA FKLFNLAKDI FPNEKVLSRI 60
QKIQEALEEL AEQGDDEFTD VCNSGLLLYR ELHNQLFEHQ KEGIAFLYSL YRDGRKGGIL 120
ADDMGLGKTV QIIAFLSGMF DASLVNHVLL IMPTNLINTW VKEFIKWTPG MRVKTFHGPS 180
KDERTRNLNR IQQRNGVIIT TYQMLINNWQ QLSSFRGQEF VWDYVILDEA HKIKTSSTKS 240
AICARAIPAS NRLLLTGTPI QNNLQELWSL FDFACQGSLL GTLKTFKMEY ENPITRAREK 300
DATPGEKALG FKISENLMAI IKPYFLRRTK EDVQKKKSSN PEARLNEKNP DVDAICEMPS 360
LSRKNDLIIW IRLVPLQEEI YRKFVSLDHI KELLMETRSP LAELGVLKKL CDHPRLLSAR 420
ACCLLNLGTF SAQDGNEGED SPDVDHIDQV TDDTLMEESG KMIFLMDLLK RLRDEGHQTL 480
VFSQSRQILN IIERLLKNRH FKTLRIDGTV THLLEREKRI NLFQQNKDYS VFLLTTQVGG 540
VGLTLTAATR VVIFDPSWNP ATDAQAVDRV YRIGQKENVV VYRLITCGTV EEKIYRRQVF 600
KDSLIRQTTG EKKNPFRYFS KQELRELFTI EDLQNSVTQL QLQSLHAAQR KSDIKLDEHI 660
AYLQSLGIAG ISDHDLMYTC DLSVKEELDV VEESHYIQQR VQKAQFLVEF ESQNKEFLME 720
QQRTRNEGAW LREPVFPSST KKKCPKLNKP QPQPSPLLST HHTQEEDISS KMASVVIDDL 780
PKEGEKQDLS SIKVNVTTLQ DGKGTGSADS IATLPKGFGS VEELCTNSSL GMEKSFATKN 840
EAVQKETLQE GPKQEALQED PLESFNYVLS KSTKADIGPN LDQLKDDEIL RHCNPWPIIS 900
ITNESQNAES NVSIIEIADD LSASHSALQD AQASEAKLEE EPSASSPQYA CDFNLFLEDS 960
ADNRQNFSSQ SLEHVEKENS LCGSAPNSRA GFVHSKTCLS WEFSEKDDEP EEVVVKAKIR 1020
SKARRIVSDG EDEDDSFKDT SSINPFNTSL FQFSSVKQFD ASTPKNDISP PGRFFSSQIP 1080
SSVNKSMNSR RSLASRRSLI NMVLDHVEDM EERLDDSSEA KGPEDYPEEG VEESSGEASK 1140
YTEEDPSGET LSSENKSSWL MTSKPSALAQ ETSLGAPEPL SGEQLVGSPQ DKAAEATNDY 1200
ETLVKRGKEL KECGKIQEAL NCLVKALDIK SADPEVMLLT LSLYKQLNNN 1250 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical. 
Pfam
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS