PDS5A_HUMAN
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 03-AUG-2022, entry version 149.
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},
GN PDS5 {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
RC Testis {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};
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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. [Q29RF7-1]
DR AlphaFoldDB; Q29RF7; -.
DR SMR; Q29RF7; -.
DR BioGRID; 116848; 252.
DR CORUM; Q29RF7; -.
DR DIP; DIP-35419N; -.
DR IntAct; Q29RF7; 75.
DR MINT; Q29RF7; -.
DR STRING; 9606.ENSP00000303427; -.
DR GlyGen; Q29RF7; 1 site, 1 O-linked glycan (1 site).
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; Q29RF7; -.
DR PeptideAtlas; Q29RF7; -.
DR PRIDE; Q29RF7; -.
DR ProteomicsDB; 61286; -. [Q29RF7-1]
DR ProteomicsDB; 61287; -. [Q29RF7-3]
DR Antibodypedia; 23497; 238 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 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; VVACDIM; -.
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; 186 hits in 1085 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 216 other tissues.
DR ExpressionAtlas; Q29RF7; baseline and differential.
DR Genevisible; Q29RF7; 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: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:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IPI:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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 unknown pathological 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
