CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016306
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ankyrin repeat and LEM domain-containing protein 2 
Protein Synonyms/Alias
 LEM domain-containing protein 4 
Gene Name
 ANKLE2 
Gene Synonyms/Alias
 KIAA0692; LEM4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73DALLARLKLLNPDDLubiquitination[1]
90EIVKAGLKCGPITSTubiquitination[1]
194RAGATASKEPPLYYGubiquitination[1]
271SLPLSPVKTAPLFSNubiquitination[1]
312RTQDLTAKLRKAVEKubiquitination[1]
394DDEAMLQKRIRYVVDubiquitination[1, 2]
439SSHHLIVKNSRNKYDubiquitination[1]
447NSRNKYDKTPEDVICubiquitination[1]
531AGPLSPAKAEDFRKLubiquitination[1]
546WKTPPREKAGFLHHVubiquitination[1]
555GFLHHVKKSDPERGFacetylation[3]
610LTQQEIGKKAQQETGubiquitination[1]
626REASCRDKATTSGSNubiquitination[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] 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] 
Functional Description
 Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. 
Sequence Annotation
 DOMAIN 69 113 LEM.
 REPEAT 411 440 ANK.
 MOD_RES 259 259 Phosphoserine.
 MOD_RES 268 268 Phosphoserine.
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 496 496 Phosphoserine.
 MOD_RES 512 512 Phosphoserine.
 MOD_RES 662 662 Phosphoserine.
 MOD_RES 896 896 Phosphoserine.
 MOD_RES 914 914 Phosphoserine.  
Keyword
 Alternative splicing; ANK repeat; Cell cycle; Cell division; Complete proteome; Endoplasmic reticulum; Membrane; Mitosis; Phosphoprotein; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 938 AA 
Protein Sequence
MLWPRLAAAE WAALAWELLG ASVLLIAVRW LVRRLGPRPG GLGRSGTPVP PPSAAAAPAS 60
GEMTMDALLA RLKLLNPDDL REEIVKAGLK CGPITSTTRF IFEKKLAQAL LEQGGRLSSF 120
YHHEAGVTAL SQDPQRILKP AEGNPTDQAG FSEDRDFGYS VGLNPPEEEA VTSKTCSVPP 180
SDTDTYRAGA TASKEPPLYY GVCPVYEDVP ARNERIYVYE NKKEALQAVK MIKGSRFKAF 240
STREDAEKFA RGICDYFPSP SKTSLPLSPV KTAPLFSNDR LKDGLCLSES ETVNKERANS 300
YKNPRTQDLT AKLRKAVEKG EEDTFSDLIW SNPRYLIGSG DNPTIVQEGC RYNVMHVAAK 360
ENQASICQLT LDVLENPDFM RLMYPDDDEA MLQKRIRYVV DLYLNTPDKM GYDTPLHFAC 420
KFGNADVVNV LSSHHLIVKN SRNKYDKTPE DVICERSKNK SVELKERIRE YLKGHYYVPL 480
LRAEETSSPV IGELWSPDQT AEASHVSRYG GSPRDPVLTL RAFAGPLSPA KAEDFRKLWK 540
TPPREKAGFL HHVKKSDPER GFERVGRELA HELGYPWVEY WEFLGCFVDL SSQEGLQRLE 600
EYLTQQEIGK KAQQETGERE ASCRDKATTS GSNSISVRAF LDEDDMSLEE IKNRQNAARN 660
NSPPTVGAFG HTRCSAFPLE QEADLIEAAE PGGPHSSRNG LCHPLNHSRT LAGKRPKAPR 720
GEEAHLPPVS DLTVEFDKLN LQNIGRSVSK TPDESTKTKD QILTSRINAV ERDLLEPSPA 780
DQLGNGHRRT ESEMSARIAK MSLSPSSPRH EDQLEVTREP ARRLFLFGEE PSKLDQDVLA 840
ALECADVDPH QFPAVHRWKS AVLCYSPSDR QSWPSPAVKG RFKSQLPDLS GPHSYSPGRN 900
SVAGSNPAKP GLGSPGRYSP VHGSQLRRMA RLAELAAL 938 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
 GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007084; P:mitotic nuclear envelope reassembly; IMP:UniProtKB.
 GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
 GO:0035307; P:positive regulation of protein dephosphorylation; IDA:UniProtKB. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR011015; LEM/LEM-like_dom.
 IPR003887; LEM_dom.
 IPR011320; RNase_H1_N. 
Pfam
 PF13606; Ank_3
 PF03020; LEM 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50954; LEM 
PRINTS