ID PDS5A_HUMAN Reviewed; 1337 AA. AC Q29RF7; Q2TTR5; Q68DF7; Q8N7J4; Q8NG14; Q9Y4D4; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog A; DE AltName: Full=Cell proliferation-inducing gene 54 protein; DE AltName: Full=Sister chromatid cohesion protein 112; DE Short=SCC-112; GN Name=PDS5A {ECO:0000312|HGNC:HGNC:29088}; GN Synonyms=KIAA0648 {ECO:0000312|EMBL:BAA31623.1}, PDS5 GN {ECO:0000303|PubMed:11076961}; ORFNames=PIG54; 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] {ECO:0000305, ECO:0000312|EMBL:AAT52214.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kim J.W.; RT "Identification of a human cell proliferation inducing gene."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC05286.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus {ECO:0000312|EMBL:BAC05286.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI14219.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Eye {ECO:0000312|EMBL:AAI14219.1}, and Testis RC {ECO:0000312|EMBL:AAH41361.1}; 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 [4] {ECO:0000305, ECO:0000312|EMBL:AAM82347.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-1337 (ISOFORM 1), SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=15019998; DOI=10.1016/j.gene.2003.12.013; RA Kumar D., Sakabe I., Patel S., Zhang Y., Ahmad I., Gehan E.A., RA Whiteside T.L., Kasid U.; RT "SCC-112, a novel cell cycle-regulated molecule, exhibits reduced RT expression in human renal carcinomas."; RL Gene 328:187-196(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-1337 (ISOFORM 2). RC TISSUE=Salivary gland; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] {ECO:0000312|EMBL:BAA31623.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1337 (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:BAA31623.1}; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [7] {ECO:0000305} RP SUBCELLULAR LOCATION, AND INTERACTION WITH THE COHESIN COMPLEX. RX PubMed=11076961; DOI=10.1083/jcb.151.4.749; RA Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.; RT "Characterization of vertebrate cohesin complexes and their regulation in RT prophase."; RL J. Cell Biol. 151:749-762(2000). RN [8] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH CHROMATIN. RX PubMed=15855230; DOI=10.1242/jcs.02355; RA Losada A., Yokochi T., Hirano T.; RT "Functional contribution of Pds5 to cohesin-mediated cohesion in human RT cells and Xenopus egg extracts."; RL J. Cell Sci. 118:2133-2141(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, 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 [10] RP INTERACTION WITH WAPL. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [13] RP INTERACTION WITH TP63. RX PubMed=17846787; DOI=10.1007/s00432-007-0306-x; RA Zheng M.Z., Zheng L.M., Zeng Y.X.; RT "SCC-112 gene is involved in tumor progression and promotes the cell RT proliferation in G2/M phase."; RL J. Cancer Res. Clin. Oncol. 134:453-462(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION BY RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195 AND THR-1208, AND RP IDENTIFICATION BY MASS 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195, AND IDENTIFICATION BY RP 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1146; LYS-1211 AND LYS-1290, AND RP IDENTIFICATION BY MASS 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 [20] RP INTERACTION WITH WAPL AND CDCA5. 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195; THR-1208 AND SER-1305, RP AND 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 [22] 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION BY RP 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1097; SER-1195; THR-1208 AND RP SER-1305, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1208, AND IDENTIFICATION BY RP 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 [26] RP VARIANT 759-GLU--ARG-1337 DEL. 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: Probable regulator of sister chromatid cohesion in mitosis CC which may stabilize cohesin complex association with chromatin. May CC couple sister chromatid cohesion during mitosis to DNA replication. CC Cohesion ensures that chromosome partitioning is accurate in both CC meiotic and mitotic cells and plays an important role in DNA repair. CC {ECO:0000269|PubMed:15855230, ECO:0000269|PubMed:19907496}. CC -!- SUBUNIT: Interacts with the cohesin complex. Interacts with WAPL (via CC FGF motifs) or CDCA5 (via the FGF motif); the interaction is direct, CC cohesin-dependent and competitive. Interacts with SMC3. Interacts with CC TP63. {ECO:0000269|PubMed:11076961, ECO:0000269|PubMed:15855230, CC ECO:0000269|PubMed:17113138, ECO:0000269|PubMed:17846787, CC ECO:0000269|PubMed:19907496, ECO:0000269|PubMed:21111234}. CC -!- INTERACTION: CC Q29RF7; Q96FF9: CDCA5; NbExp=3; IntAct=EBI-1175454, EBI-718805; CC Q29RF7; O60216: RAD21; NbExp=5; IntAct=EBI-1175454, EBI-80739; CC Q29RF7; Q9UQE7: SMC3; NbExp=4; IntAct=EBI-1175454, EBI-80718; CC Q29RF7; Q8WVM7: STAG1; NbExp=3; IntAct=EBI-1175454, EBI-1175097; CC Q29RF7; Q8N3U4: STAG2; NbExp=6; IntAct=EBI-1175454, EBI-1057252; CC Q29RF7-3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-12067280, EBI-1955541; CC Q29RF7-3; Q99750: MDFI; NbExp=3; IntAct=EBI-12067280, EBI-724076; CC Q29RF7-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12067280, EBI-16439278; CC Q29RF7-3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12067280, EBI-79165; CC Q29RF7-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12067280, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076961, CC ECO:0000269|PubMed:15019998}. Note=Associated with chromatin through CC most of the cell cycle. Dissociates from chromatin in late prophase, CC reassociates during late telophase. {ECO:0000269|PubMed:11076961, CC ECO:0000269|PubMed:15019998}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:15489334}; CC IsoId=Q29RF7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q29RF7-3; Sequence=VSP_052491, VSP_052492; CC -!- TISSUE SPECIFICITY: Highest level in colon. Low levels in lung, ovary, CC breast and kidney. Reduced level in renal tumor tissue. Isoform 2 is CC expressed in kidney. {ECO:0000269|PubMed:15019998}. CC -!- DEVELOPMENTAL STAGE: Cell cycle-regulated with highest level in G2 CC phase. {ECO:0000269|PubMed:15019998}. CC -!- MISCELLANEOUS: HeLa cells with a reduced level of PDS5A show a mild CC defect in sister chromatid cohesion. HeLa cells with a reduced level of CC RAD21 show reduced association of PDS5A with chromatin. CC {ECO:0000269|PubMed:15855230}. CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI26226.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAM82347.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=CAH18263.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY550968; AAT52214.1; -; mRNA. DR EMBL; AK098331; BAC05286.1; -; mRNA. DR EMBL; BC041361; AAH41361.1; -; mRNA. DR EMBL; BC114218; AAI14219.1; -; mRNA. DR EMBL; BC126225; AAI26226.1; ALT_INIT; mRNA. DR EMBL; AF294791; AAM82347.1; ALT_SEQ; mRNA. DR EMBL; CR749425; CAH18263.1; ALT_INIT; mRNA. DR EMBL; AB014548; BAA31623.1; -; mRNA. DR CCDS; CCDS47045.1; -. [Q29RF7-1] DR CCDS; CCDS54759.1; -. [Q29RF7-3] DR RefSeq; NP_001093869.1; NM_001100399.1. [Q29RF7-1] DR RefSeq; NP_001093870.1; NM_001100400.1. [Q29RF7-3] DR RefSeq; XP_011511974.1; XM_011513672.2. [Q29RF7-1] DR RefSeq; XP_016863417.1; XM_017007928.1. DR AlphaFoldDB; Q29RF7; -. DR SMR; Q29RF7; -. DR BioGRID; 116848; 280. DR CORUM; Q29RF7; -. DR DIP; DIP-35419N; -. DR IntAct; Q29RF7; 78. DR MINT; Q29RF7; -. DR STRING; 9606.ENSP00000303427; -. DR GlyGen; Q29RF7; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q29RF7; -. DR MetOSite; Q29RF7; -. DR PhosphoSitePlus; Q29RF7; -. DR SwissPalm; Q29RF7; -. DR BioMuta; PDS5A; -. DR DMDM; 121947590; -. DR EPD; Q29RF7; -. DR jPOST; Q29RF7; -. DR MassIVE; Q29RF7; -. DR MaxQB; Q29RF7; -. DR PaxDb; 9606-ENSP00000303427; -. DR PeptideAtlas; Q29RF7; -. DR ProteomicsDB; 61286; -. [Q29RF7-1] DR ProteomicsDB; 61287; -. [Q29RF7-3] DR Pumba; Q29RF7; -. DR Antibodypedia; 23497; 264 antibodies from 27 providers. DR DNASU; 23244; -. DR Ensembl; ENST00000303538.13; ENSP00000303427.8; ENSG00000121892.15. [Q29RF7-1] DR Ensembl; ENST00000503396.5; ENSP00000426749.1; ENSG00000121892.15. [Q29RF7-3] DR GeneID; 23244; -. DR KEGG; hsa:23244; -. DR MANE-Select; ENST00000303538.13; ENSP00000303427.8; NM_001100399.2; NP_001093869.1. DR UCSC; uc003guv.4; human. [Q29RF7-1] DR AGR; HGNC:29088; -. DR CTD; 23244; -. DR DisGeNET; 23244; -. DR GeneCards; PDS5A; -. DR HGNC; HGNC:29088; PDS5A. DR HPA; ENSG00000121892; Low tissue specificity. DR MIM; 613200; gene. DR neXtProt; NX_Q29RF7; -. DR OpenTargets; ENSG00000121892; -. DR PharmGKB; PA162399027; -. DR VEuPathDB; HostDB:ENSG00000121892; -. DR eggNOG; KOG1525; Eukaryota. DR GeneTree; ENSGT00940000155155; -. DR HOGENOM; CLU_004041_0_0_1; -. DR InParanoid; Q29RF7; -. DR OMA; YPEYMIS; -. DR OrthoDB; 3148168at2759; -. DR PhylomeDB; Q29RF7; -. DR TreeFam; TF106415; -. DR PathwayCommons; Q29RF7; -. 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; Q29RF7; -. DR BioGRID-ORCS; 23244; 194 hits in 1161 CRISPR screens. DR ChiTaRS; PDS5A; human. DR GeneWiki; PDS5A; -. DR GenomeRNAi; 23244; -. DR Pharos; Q29RF7; Tbio. DR PRO; PR:Q29RF7; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q29RF7; Protein. DR Bgee; ENSG00000121892; Expressed in germinal epithelium of ovary and 218 other cell types or tissues. DR ExpressionAtlas; Q29RF7; baseline and differential. 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:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IPI:UniProtKB. DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB. DR CDD; cd19953; PDS5; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR039776; Pds5. DR PANTHER; PTHR12663; ANDROGEN INDUCED INHIBITOR OF PROLIFERATION AS3 / PDS5-RELATED; 1. DR PANTHER; PTHR12663:SF2; SISTER CHROMATID COHESION PROTEIN PDS5 HOMOLOG A; 1. DR Pfam; PF20168; PDS5; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q29RF7; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis; KW Nucleus; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..1337 FT /note="Sister chromatid cohesion protein PDS5 homolog A" FT /id="PRO_0000296341" FT REPEAT 393..429 FT /note="HEAT" FT /evidence="ECO:0000255" FT REGION 1150..1337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1155..1202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1219..1237 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1251..1280 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 1097 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1146 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1195 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1208 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1211 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1290 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1305 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 591..600 FT /note="REIARKLANP -> VSKSYFTLFL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.1" FT /id="VSP_052491" FT VAR_SEQ 601..1337 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.1" FT /id="VSP_052492" FT VARIANT 759..1337 FT /note="Missing (found in a patient with cohesinopathy; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:30158690" FT /id="VAR_082313" FT CONFLICT 207 FT /note="D -> G (in Ref. 4; AAM82347)" FT /evidence="ECO:0000305" FT CONFLICT 471 FT /note="Q -> R (in Ref. 1; AAT52214)" FT /evidence="ECO:0000305" SQ SEQUENCE 1337 AA; 150830 MW; FA28EA9EF77499D9 CRC64; MDFTAQPKPA TALCGVVSAD GKIAYPPGVK EITDKITTDE MIKRLKMVVK TFMDMDQDSE DEKQQYLPLA LHLASEFFLR NPNKDVRLLV ACCLADIFRI YAPEAPYTSH DKLKDIFLFI TRQLKGLEDT KSPQFNRYFY LLENLAWVKS YNICFELEDC NEIFIQLFRT LFSVINNSHN KKVQMHMLDL MSSIIMEGDG VTQELLDSIL INLIPAHKNL NKQSFDLAKV LLKRTVQTIE ACIANFFNQV LVLGRSSVSD LSEHVFDLIQ ELFAIDPHLL LSVMPQLEFK LKSNDGEERL AVVRLLAKLF GSKDSDLATQ NRPLWQCFLG RFNDIHVPVR LESVKFASHC LMNHPDLAKD LTEYLKVRSH DPEEAIRHDV IVTIITAAKR DLALVNDQLL GFVRERTLDK RWRVRKEAMM GLAQLYKKYC LHGEAGKEAA EKVSWIKDKL LHIYYQNSID DKLLVEKIFA QYLVPHNLET EERMKCLYYL YASLDPNAVK ALNEMWKCQN MLRSHVRELL DLHKQPTSEA NCSAMFGKLM TIAKNLPDPG KAQDFVKKFN QVLGDDEKLR SQLELLISPT CSCKQADICV REIARKLANP KQPTNPFLEM VKFLLERIAP VHIDSEAISA LVKLMNKSIE GTADDEEEGV SPDTAIRSGL ELLKVLSFTH PTSFHSAETY ESLLQCLRME DDKVAEAAIQ IFRNTGHKIE TDLPQIRSTL IPILHQKAKR GTPHQAKQAV HCIHAIFTNK EVQLAQIFEP LSRSLNADVP EQLITPLVSL GHISMLAPDQ FASPMKSVVA NFIVKDLLMN DRSTGEKNGK LWSPDEEVSP EVLAKVQAIK LLVRWLLGMK NNQSKSANST LRLLSAMLVS EGDLTEQKRI SKSDMSRLRL AAGSAIMKLA QEPCYHEIIT PEQFQLCALV INDECYQVRQ IFAQKLHKAL VKLLLPLEYM AIFALCAKDP VKERRAHARQ CLLKNISIRR EYIKQNPMAT EKLLSLLPEY VVPYMIHLLA HDPDFTRSQD VDQLRDIKEC LWFMLEVLMT KNENNSHAFM KKMAENIKLT RDAQSPDESK TNEKLYTVCD VALCVINSKS ALCNADSPKD PVLPMKFFTQ PEKDFCNDKS YISEETRVLL LTGKPKPAGV LGAVNKPLSA TGRKPYVRST GTETGSNINV NSELNPSTGN RSREQSSEAA ETGVSENEEN PVRIISVTPV KNIDPVKNKE INSDQATQGN ISSDRGKKRT VTAAGAENIQ QKTDEKVDES GPPAPSKPRR GRRPKSESQG NATKNDDLNK PINKGRKRAA VGQESPGGLE AGNAKAPKLQ DLAKKAAPAE RQIDLQR //