CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015948
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Wings apart-like protein homolog 
Protein Synonyms/Alias
 Friend of EBNA2 protein 
Gene Name
 WAPAL 
Gene Synonyms/Alias
 FOE; KIAA0261; WAPL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52GQKRPNFKPDIQEIPacetylation[1, 2]
168NKLITSDKVENFHEEacetylation[2, 3, 4]
604KAPAPPSKVIKTVTIacetylation[3]
763SAKLLNEKDMNKIKEacetylation[4]
763SAKLLNEKDMNKIKEubiquitination[5]
1178AVGTTGQKSISRVIEubiquitination[5]
Reference
 [1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [2] 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]
 [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] 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] 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] 
Functional Description
 Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister- chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. 
Sequence Annotation
 DOMAIN 626 1169 WAPL.
 REGION 1 659 Mediates interaction with the cohesin
 MOTIF 73 75 FGF motif 1.
 MOTIF 429 431 FGF motif 2.
 MOTIF 453 455 FGF motif 3.
 MOD_RES 77 77 Phosphoserine.
 MOD_RES 168 168 N6-acetyllysine.
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 223 223 Phosphoserine.
 MOD_RES 226 226 Phosphoserine.
 MOD_RES 380 380 Phosphoserine.
 MOD_RES 459 459 Phosphoserine.
 MOD_RES 461 461 Phosphoserine.
 MOD_RES 904 904 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Host-virus interaction; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1190 AA 
Protein Sequence
MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN FKPDIQEIPK 60
KPKVEEESTG DPFGFDSDDE SLPVSSKNLA QVKCSSYSES SEAAQLEEVT SVLEANSKIS 120
HVVVEDTVVS DKCFPLEDTL LGKEKSTNRI VEDDASISSC NKLITSDKVE NFHEEHEKNS 180
HHIHKNADDS TKKPNAETTV ASEIKETNDT WNSQFGKRPE SPSEISPIKG SVRTGLFEWD 240
NDFEDIRSED CILSLDSDPL LEMKDDDFKN RLENLNEAIE EDIVQSVLRP TNCRTYCRAN 300
KTKSSQGASN FDKLMDGTSQ ALAKANSESS KDGLNQAKKG GVSCGTSFRG TVGRTRDYTV 360
LHPSCLSVCN VTIQDTMERS MDEFTASTPA DLGEAGRLRK KADIATSKTT TRFRPSNTKS 420
KKDVKLEFFG FEDHETGGDE GGSGSSNYKI KYFGFDDLSE SEDDEDDDCQ VERKTSKKRT 480
KTAPSPSLQP PPESNDNSQD SQSGTNNAEN LDFTEDLPGV PESVKKPINK QGDKSKENTR 540
KIFSGPKRSP TKAVYNARHW NHPDSEELPG PPVVKPQSVT VRLSSKEPNQ KDDGVFKAPA 600
PPSKVIKTVT IPTQPYQDIV TALKCRREDK ELYTVVQHVK HFNDVVEFGE NQEFTDDIEY 660
LLSGLKSTQP LNTRCLSVIS LATKCAMPSF RMHLRAHGMV AMVFKTLDDS QHHQNLSLCT 720
AALMYILSRD RLNMDLDRAS LDLMIRLLEL EQDASSAKLL NEKDMNKIKE KIRRLCETVH 780
NKHLDLENIT TGHLAMETLL SLTSKRAGDW FKEELRLLGG LDHIVDKVKE CVDHLSRDED 840
EEKLVASLWG AERCLRVLES VTVHNPENQS YLIAYKDSQL IVSSAKALQH CEELIQQYNR 900
AEDSICLADS KPLPHQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK TGEQDGLIGT 960
ALNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH CLVNMETSCS FDSSICSGEG 1020
DDSLRIGGQV HAVQALVQLF LERERAAQLA ESKTDELIKD APTTQHDKSG EWQETSGEIQ 1080
WVSTEKTDGT EEKHKKEEED EELDLNKALQ HAGKHMEDCI VASYTALLLG CLCQESPINV 1140
TTVREYLPEG DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC 1190 
Gene Ontology
 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
 GO:0008278; C:cohesin complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000795; C:synaptonemal complex; IEA:Compara.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0035562; P:negative regulation of chromatin binding; IMP:UniProtKB.
 GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
 GO:0045875; P:negative regulation of sister chromatid cohesion; IMP:UniProtKB.
 GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
 GO:0071922; P:regulation of cohesin localization to chromatin; IMP:UniProtKB.
 GO:0009636; P:response to toxic substance; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016024; ARM-type_fold.
 IPR012502; WAPL_metazoan_plants.
 IPR022771; WAPL_prot. 
Pfam
 PF07814; WAPL 
SMART
  
PROSITE
 PS51271; WAPL 
PRINTS