WAPL_HUMAN
ID WAPL_HUMAN Reviewed; 1190 AA.
AC Q7Z5K2; A7E2B5; Q5VSK5; Q8IX10; Q92549;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Wings apart-like protein homolog;
DE AltName: Full=Friend of EBNA2 protein;
DE AltName: Full=WAPL cohesin release factor {ECO:0000312|HGNC:HGNC:23293};
GN Name=WAPL {ECO:0000312|HGNC:HGNC:23293}; Synonyms=FOE, KIAA0261, WAPAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15150110; DOI=10.1158/0008-5472.can-03-3822;
RA Oikawa K., Ohbayashi T., Kiyono T., Nishi H., Isaka K., Umezawa A.,
RA Kuroda M., Mukai K.;
RT "Expression of a novel human gene, human wings apart-like (hWAPL), is
RT associated with cervical carcinogenesis and tumor progression.";
RL Cancer Res. 64:3545-3549(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH EPSTEIN-BARR VIRUS
RP EBNA2 (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15383329; DOI=10.1016/j.yexcr.2004.06.028;
RA Kwiatkowski B.A., Ragoczy T., Ehly J., Schubach W.H.;
RT "Identification and cloning of a novel chromatin-associated protein partner
RT of Epstein-Barr nuclear protein 2.";
RL Exp. Cell Res. 300:223-233(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH THE COHESIN
RP COMPLEX AND PDS5A, AND SUBCELLULAR LOCATION.
RX PubMed=17113138; DOI=10.1016/j.cell.2006.09.040;
RA Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A., Mechtler K.,
RA Peters J.M.;
RT "Wapl controls the dynamic association of cohesin with chromatin.";
RL Cell 127:955-967(2006).
RN [9]
RP FUNCTION, INTERACTION WITH THE COHESIN COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17112726; DOI=10.1016/j.cub.2006.10.061;
RA Gandhi R., Gillespie P.J., Hirano T.;
RT "Human Wapl is a cohesin-binding protein that promotes sister-chromatid
RT resolution in mitotic prophase.";
RL Curr. Biol. 16:2406-2417(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221; SER-223;
RP SER-226; SER-380; SER-459; SER-461 AND SER-904, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP FUNCTION, INTERACTION WITH PDS5B AND RAD21, MUTAGENESIS OF 73-PHE--PHE-75;
RP 429-PHE--PHE-431 AND 453-PHE--PHE-455, AND FGF MOTIFS.
RX PubMed=19696148; DOI=10.1101/gad.1844309;
RA Shintomi K., Hirano T.;
RT "Releasing cohesin from chromosome arms in early mitosis: opposing actions
RT of Wapl-Pds5 and Sgo1.";
RL Genes Dev. 23:2224-2236(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP FUNCTION, AND INTERACTION WITH SMC3.
RX PubMed=19907496; DOI=10.1038/nature08550;
RA Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.;
RT "Cohesin acetylation speeds the replication fork.";
RL Nature 462:231-234(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP FUNCTION, AND INTERACTION WITH PDS5A.
RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031;
RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A.,
RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.;
RT "Sororin mediates sister chromatid cohesion by antagonizing wapl.";
RL Cell 143:737-749(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221; SER-226;
RP SER-347; SER-380 AND SER-443, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 631-1190, FUNCTION, INTERACTION
RP WITH PDS5A; SMC1; SMC3; STAG2 AND CDCA5, SUBUNIT, AND MUTAGENESIS OF
RP 639-VAL-LYS-640; 656-ASP-ASP-657; GLU-770; GLU-777; GLU-787; THR-790;
RP MET-1116 AND ILE-1120.
RX PubMed=23776203; DOI=10.1073/pnas.1304594110;
RA Ouyang Z., Zheng G., Song J., Borek D.M., Otwinowski Z., Brautigam C.A.,
RA Tomchick D.R., Rankin S., Yu H.;
RT "Structure of the human cohesin inhibitor Wapl.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11355-11360(2013).
RN [25]
RP VARIANT HIS-731.
RX PubMed=30158690; DOI=10.1038/s41436-018-0085-6;
RG DDD Study;
RA Yuan B., Neira J., Pehlivan D., Santiago-Sim T., Song X., Rosenfeld J.,
RA Posey J.E., Patel V., Jin W., Adam M.P., Baple E.L., Dean J., Fong C.T.,
RA Hickey S.E., Hudgins L., Leon E., Madan-Khetarpal S., Rawlins L.,
RA Rustad C.F., Stray-Pedersen A., Tveten K., Wenger O., Diaz J., Jenkins L.,
RA Martin L., McGuire M., Pietryga M., Ramsdell L., Slattery L., Abid F.,
RA Bertuch A.A., Grange D., Immken L., Schaaf C.P., Van Esch H., Bi W.,
RA Cheung S.W., Breman A.M., Smith J.L., Shaw C., Crosby A.H., Eng C.,
RA Yang Y., Lupski J.R., Xiao R., Liu P.;
RT "Clinical exome sequencing reveals locus heterogeneity and phenotypic
RT variability of cohesinopathies.";
RL Genet. Med. 21:663-675(2019).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which
CC negatively regulates cohesin association with chromatin. Involved in
CC both sister chromatid cohesion during interphase and sister-chromatid
CC resolution during early stages of mitosis. Couples DNA replication to
CC sister chromatid cohesion. Cohesion ensures that chromosome
CC partitioning is accurate in both meiotic and mitotic cells and plays an
CC important role in DNA repair. {ECO:0000269|PubMed:15150110,
CC ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138,
CC ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496,
CC ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203}.
CC -!- SUBUNIT: Interacts with the cohesin complex throughout the cell cycle;
CC interacts with both chromatin-bound and soluble pools of the complex.
CC Interacts with RAD21; the interaction is direct. Interacts with PDS5A;
CC the interaction is direct, cohesin-dependent and competitive with
CC CDCA5/SORORIN. Interacts (via FGF motifs) with PDS5B; the interaction
CC is direct. Interacts with a SMC1 protein (SMC1A or SMC1B) and SMC3.
CC {ECO:0000269|PubMed:17112726, ECO:0000269|PubMed:17113138,
CC ECO:0000269|PubMed:19696148, ECO:0000269|PubMed:19907496,
CC ECO:0000269|PubMed:21111234, ECO:0000269|PubMed:23776203}.
CC -!- SUBUNIT: (Microbial infection) Isoform 2 interacts with Epstein-Barr
CC virus EBNA2. {ECO:0000269|PubMed:15383329}.
CC -!- INTERACTION:
CC Q7Z5K2; Q9NTI5: PDS5B; NbExp=9; IntAct=EBI-1022242, EBI-1175604;
CC Q7Z5K2; O60216: RAD21; NbExp=15; IntAct=EBI-1022242, EBI-80739;
CC Q7Z5K2; Q8N3U4: STAG2; NbExp=13; IntAct=EBI-1022242, EBI-1057252;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasm. Note=Associates
CC with chromatin through the cohesin complex during interphase. Released
CC in the cytoplasm from nuclear envelope breakdown until anaphase, it
CC reaccumulates in nucleus at telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z5K2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5K2-2; Sequence=VSP_019649, VSP_019651;
CC Name=3;
CC IsoId=Q7Z5K2-3; Sequence=VSP_019650;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in uterine cervix
CC tumor. Isoform 2 is widely expressed with a high level in skeletal
CC muscle and heart. {ECO:0000269|PubMed:15150110,
CC ECO:0000269|PubMed:15383329}.
CC -!- SIMILARITY: Belongs to the WAPL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13391.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB065003; BAC78631.1; -; mRNA.
DR EMBL; AF479418; AAO14651.1; -; mRNA.
DR EMBL; D87450; BAA13391.1; ALT_INIT; mRNA.
DR EMBL; AL731569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471142; EAW80336.1; -; Genomic_DNA.
DR EMBL; BC150269; AAI50270.1; -; mRNA.
DR CCDS; CCDS7375.1; -. [Q7Z5K2-1]
DR RefSeq; NP_001305257.1; NM_001318328.1.
DR RefSeq; NP_055860.1; NM_015045.3. [Q7Z5K2-1]
DR PDB; 4K6J; X-ray; 2.62 A; A/B=631-1190.
DR PDB; 5HDT; X-ray; 2.71 A; E=1-33.
DR PDBsum; 4K6J; -.
DR PDBsum; 5HDT; -.
DR AlphaFoldDB; Q7Z5K2; -.
DR SMR; Q7Z5K2; -.
DR BioGRID; 116698; 156.
DR DIP; DIP-31176N; -.
DR IntAct; Q7Z5K2; 49.
DR MINT; Q7Z5K2; -.
DR STRING; 9606.ENSP00000298767; -.
DR GlyGen; Q7Z5K2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z5K2; -.
DR MetOSite; Q7Z5K2; -.
DR PhosphoSitePlus; Q7Z5K2; -.
DR BioMuta; WAPL; -.
DR DMDM; 74713658; -.
DR EPD; Q7Z5K2; -.
DR jPOST; Q7Z5K2; -.
DR MassIVE; Q7Z5K2; -.
DR MaxQB; Q7Z5K2; -.
DR PaxDb; Q7Z5K2; -.
DR PeptideAtlas; Q7Z5K2; -.
DR PRIDE; Q7Z5K2; -.
DR ProteomicsDB; 69311; -. [Q7Z5K2-1]
DR ProteomicsDB; 69312; -. [Q7Z5K2-2]
DR ProteomicsDB; 69313; -. [Q7Z5K2-3]
DR Antibodypedia; 30070; 173 antibodies from 30 providers.
DR DNASU; 23063; -.
DR Ensembl; ENST00000298767.10; ENSP00000298767.4; ENSG00000062650.20. [Q7Z5K2-1]
DR GeneID; 23063; -.
DR KEGG; hsa:23063; -.
DR MANE-Select; ENST00000298767.10; ENSP00000298767.4; NM_015045.5; NP_055860.1.
DR UCSC; uc001kdo.4; human. [Q7Z5K2-1]
DR CTD; 23063; -.
DR DisGeNET; 23063; -.
DR GeneCards; WAPL; -.
DR HGNC; HGNC:23293; WAPL.
DR HPA; ENSG00000062650; Low tissue specificity.
DR MIM; 610754; gene.
DR neXtProt; NX_Q7Z5K2; -.
DR OpenTargets; ENSG00000062650; -.
DR PharmGKB; PA134872402; -.
DR VEuPathDB; HostDB:ENSG00000062650; -.
DR eggNOG; KOG2152; Eukaryota.
DR GeneTree; ENSGT00390000015768; -.
DR HOGENOM; CLU_006912_0_0_1; -.
DR InParanoid; Q7Z5K2; -.
DR OMA; PPHRASY; -.
DR OrthoDB; 81845at2759; -.
DR PhylomeDB; Q7Z5K2; -.
DR TreeFam; TF323477; -.
DR PathwayCommons; Q7Z5K2; -.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR SignaLink; Q7Z5K2; -.
DR SIGNOR; Q7Z5K2; -.
DR BioGRID-ORCS; 23063; 185 hits in 1090 CRISPR screens.
DR ChiTaRS; WAPL; human.
DR GeneWiki; WAPAL; -.
DR GenomeRNAi; 23063; -.
DR Pharos; Q7Z5K2; Tbio.
DR PRO; PR:Q7Z5K2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q7Z5K2; protein.
DR Bgee; ENSG00000062650; Expressed in secondary oocyte and 206 other tissues.
DR ExpressionAtlas; Q7Z5K2; baseline and differential.
DR Genevisible; Q7Z5K2; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; TAS:Reactome.
DR GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IMP:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0045875; P:negative regulation of sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
DR GO; GO:0060623; P:regulation of chromosome condensation; IBA:GO_Central.
DR GO; GO:0051983; P:regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039874; WAPL.
DR InterPro; IPR022771; WAPL_C.
DR InterPro; IPR012502; WAPL_dom.
DR PANTHER; PTHR22100; PTHR22100; 1.
DR Pfam; PF07814; WAPL; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51271; WAPL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Chromosome; Coiled coil; Cytoplasm; Host-virus interaction; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1190
FT /note="Wings apart-like protein homolog"
FT /id="PRO_0000245232"
FT DOMAIN 626..1169
FT /note="WAPL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00603"
FT REGION 1..659
FT /note="Mediates interaction with the cohesin complex"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 260..286
FT /evidence="ECO:0000255"
FT COILED 749..782
FT /evidence="ECO:0000255"
FT MOTIF 73..75
FT /note="FGF motif 1"
FT MOTIF 429..431
FT /note="FGF motif 2"
FT MOTIF 453..455
FT /note="FGF motif 3"
FT COMPBIAS 53..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1
FT /note="M -> MVQGPVQTPALTIHRRKRRRRRRRRPVAKAPARLRGEYETGVKM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15383329"
FT /id="VSP_019649"
FT VAR_SEQ 1
FT /note="M -> MVQGPVQTPALTIHRRKRRRSCPPNRASYLPKAESLASLGSHLPALL
FT SRARVPRPPAGRRERERRRRPVAKAPARLRGEYETGVKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9039502"
FT /id="VSP_019650"
FT VAR_SEQ 510..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15383329"
FT /id="VSP_019651"
FT VARIANT 124
FT /note="V -> I (in dbSNP:rs10887621)"
FT /id="VAR_026967"
FT VARIANT 731
FT /note="R -> H (found in a patient with cohesinopathy;
FT unknown pathological significance; dbSNP:rs1564570621)"
FT /evidence="ECO:0000269|PubMed:30158690"
FT /id="VAR_082314"
FT MUTAGEN 73..75
FT /note="FGF->EGE: Loss of interaction with PDS5B; when
FT associated with 429-E--E-431 and 453-E--E-455."
FT /evidence="ECO:0000269|PubMed:19696148"
FT MUTAGEN 429..431
FT /note="FGF->EGE: Loss of interaction with PDS5B; when
FT associated with 73-E--E-75 and 453-E--E-455."
FT /evidence="ECO:0000269|PubMed:19696148"
FT MUTAGEN 453..455
FT /note="FGF->EGE: Loss of interaction with PDS5B; when
FT associated with 73-E--E-75 and 429-E--E-431."
FT /evidence="ECO:0000269|PubMed:19696148"
FT MUTAGEN 639..640
FT /note="VK->AE: Impaired sister chromatid cohesion and
FT resolution."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 656..657
FT /note="DD->KK: Impaired sister chromatid cohesion and
FT resolution."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 770
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 777
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 787
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 790
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 1116
FT /note="M->A: Impaired sister chromatid cohesion and
FT resolution; when associated with A-1120."
FT /evidence="ECO:0000269|PubMed:23776203"
FT MUTAGEN 1120
FT /note="I->A: Impaired sister chromatid cohesion and
FT resolution; when associated with A-1116."
FT /evidence="ECO:0000269|PubMed:23776203"
FT HELIX 631..640
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 652..664
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 671..684
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 688..696
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 700..706
FT /evidence="ECO:0007829|PDB:4K6J"
FT TURN 707..709
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 714..727
FT /evidence="ECO:0007829|PDB:4K6J"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 738..749
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 765..780
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 791..802
FT /evidence="ECO:0007829|PDB:4K6J"
FT TURN 805..807
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 810..817
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 820..836
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 841..862
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 866..897
FT /evidence="ECO:0007829|PDB:4K6J"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 917..941
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 945..952
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 957..966
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 968..971
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 974..976
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 977..992
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 996..1003
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1032..1058
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1107..1135
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1137..1146
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1148..1150
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1153..1169
FT /evidence="ECO:0007829|PDB:4K6J"
FT HELIX 1174..1188
FT /evidence="ECO:0007829|PDB:4K6J"
SQ SEQUENCE 1190 AA; 132946 MW; A01026E520BFAB2F CRC64;
MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN FKPDIQEIPK
KPKVEEESTG DPFGFDSDDE SLPVSSKNLA QVKCSSYSES SEAAQLEEVT SVLEANSKIS
HVVVEDTVVS DKCFPLEDTL LGKEKSTNRI VEDDASISSC NKLITSDKVE NFHEEHEKNS
HHIHKNADDS TKKPNAETTV ASEIKETNDT WNSQFGKRPE SPSEISPIKG SVRTGLFEWD
NDFEDIRSED CILSLDSDPL LEMKDDDFKN RLENLNEAIE EDIVQSVLRP TNCRTYCRAN
KTKSSQGASN FDKLMDGTSQ ALAKANSESS KDGLNQAKKG GVSCGTSFRG TVGRTRDYTV
LHPSCLSVCN VTIQDTMERS MDEFTASTPA DLGEAGRLRK KADIATSKTT TRFRPSNTKS
KKDVKLEFFG FEDHETGGDE GGSGSSNYKI KYFGFDDLSE SEDDEDDDCQ VERKTSKKRT
KTAPSPSLQP PPESNDNSQD SQSGTNNAEN LDFTEDLPGV PESVKKPINK QGDKSKENTR
KIFSGPKRSP TKAVYNARHW NHPDSEELPG PPVVKPQSVT VRLSSKEPNQ KDDGVFKAPA
PPSKVIKTVT IPTQPYQDIV TALKCRREDK ELYTVVQHVK HFNDVVEFGE NQEFTDDIEY
LLSGLKSTQP LNTRCLSVIS LATKCAMPSF RMHLRAHGMV AMVFKTLDDS QHHQNLSLCT
AALMYILSRD RLNMDLDRAS LDLMIRLLEL EQDASSAKLL NEKDMNKIKE KIRRLCETVH
NKHLDLENIT TGHLAMETLL SLTSKRAGDW FKEELRLLGG LDHIVDKVKE CVDHLSRDED
EEKLVASLWG AERCLRVLES VTVHNPENQS YLIAYKDSQL IVSSAKALQH CEELIQQYNR
AEDSICLADS KPLPHQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK TGEQDGLIGT
ALNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH CLVNMETSCS FDSSICSGEG
DDSLRIGGQV HAVQALVQLF LERERAAQLA ESKTDELIKD APTTQHDKSG EWQETSGEIQ
WVSTEKTDGT EEKHKKEEED EELDLNKALQ HAGKHMEDCI VASYTALLLG CLCQESPINV
TTVREYLPEG DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC
