PDS5B_HUMAN
ID PDS5B_HUMAN Reviewed; 1447 AA.
AC Q9NTI5; Q5R3S3; Q5W0K8; Q6NSC3; Q8IXT6; Q9H5N8; Q9Y2I5; Q9Y451;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog B;
DE AltName: Full=Androgen-induced proliferation inhibitor;
DE AltName: Full=Androgen-induced prostate proliferative shutoff-associated protein AS3;
GN Name=PDS5B;
GN Synonyms=APRIN, AS3 {ECO:0000312|EMBL:AAD22134.2},
GN KIAA0979 {ECO:0000312|EMBL:BAA76823.2};
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}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9459187; DOI=10.1016/s0960-0760(97)00122-2;
RA Geck P., Szelei J., Jimenez J., Lin T.-M., Sonnenschein C., Soto A.M.;
RT "Expression of novel genes linked to the androgen-induced, proliferative
RT shutoff in prostate cancer cells.";
RL J. Steroid Biochem. Mol. Biol. 63:211-218(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD22134.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Prostate {ECO:0000312|EMBL:AAD22134.2};
RX PubMed=10215036; DOI=10.1016/s0960-0760(98)00165-4;
RA Geck P., Szelei J., Jimenez J., Sonnenschein C., Soto A.M.;
RT "Early gene expression during androgen-induced inhibition of proliferation
RT of prostate cancer cells: a new suppressor candidate on chromosome 13, in
RT the BRCA2-Rb1 locus.";
RL J. Steroid Biochem. Mol. Biol. 68:41-50(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA76823.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA76823.2};
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAB15584.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Colon {ECO:0000312|EMBL:BAB15584.1};
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 [6] {ECO:0000312|EMBL:CAB69911.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S., Huckle E.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:CAB69911.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH39256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH70274.1}, and
RC Testis {ECO:0000312|EMBL:AAH39256.1};
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 [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=10963680; DOI=10.1073/pnas.97.18.10185;
RA Geck P., Maffini M.V., Szelei J., Sonnenschein C., Soto A.M.;
RT "Androgen-induced proliferative quiescence in prostate cancer cells: the
RT role of AS3 as its mediator.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10185-10190(2000).
RN [10] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH COHESIN COMPLEX.
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 [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358 AND THR-1370, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182; SER-1283 AND SER-1358,
RP AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1334, 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 [17]
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 [18]
RP FUNCTION, AND INTERACTION WITH WAPL AND RAD21.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1162; SER-1166; SER-1176;
RP SER-1182; SER-1191; SER-1257; SER-1283; SER-1358 AND THR-1370, 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1136, 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1182; SER-1283 AND
RP SER-1358, 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1182; SER-1283;
RP SER-1358; THR-1381 AND SER-1383, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140; SER-1166; SER-1176;
RP SER-1182; THR-1255; SER-1257; SER-1259; SER-1283; SER-1319; SER-1358 AND
RP THR-1370, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166, 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).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which may
CC stabilize cohesin complex association with chromatin. May couple sister
CC chromatid cohesion during mitosis to DNA replication. Cohesion ensures
CC that chromosome partitioning is accurate in both meiotic and mitotic
CC cells and plays an important role in DNA repair. Plays a role in
CC androgen-induced proliferative arrest in prostate cells.
CC {ECO:0000269|PubMed:10963680, ECO:0000269|PubMed:15855230,
CC ECO:0000269|PubMed:19696148}.
CC -!- SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21; the
CC interaction is direct. Interacts with WAPL (via FGF motifs) or CDCA5
CC (via the FGF motif); the interaction is direct, cohesin-dependent and
CC competitive (Probable). {ECO:0000305|PubMed:15855230,
CC ECO:0000305|PubMed:19696148, ECO:0000305|PubMed:21111234}.
CC -!- INTERACTION:
CC Q9NTI5; P51587: BRCA2; NbExp=26; IntAct=EBI-1175604, EBI-79792;
CC Q9NTI5; O60216: RAD21; NbExp=4; IntAct=EBI-1175604, EBI-80739;
CC Q9NTI5; Q9UQE7: SMC3; NbExp=7; IntAct=EBI-1175604, EBI-80718;
CC Q9NTI5; Q8WVM7: STAG1; NbExp=4; IntAct=EBI-1175604, EBI-1175097;
CC Q9NTI5; Q8N3U4: STAG2; NbExp=4; IntAct=EBI-1175604, EBI-1057252;
CC Q9NTI5; Q7Z5K2: WAPL; NbExp=9; IntAct=EBI-1175604, EBI-1022242;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:10231032};
CC IsoId=Q9NTI5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10215036};
CC IsoId=Q9NTI5-2; Sequence=VSP_052402;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9NTI5-3; Sequence=VSP_052399, VSP_052400;
CC Name=4 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9NTI5-4; Sequence=VSP_052397, VSP_052398;
CC Name=5 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9NTI5-5; Sequence=VSP_052396, VSP_052401;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9459187}.
CC -!- INDUCTION: By the synthetic androgen R1881 in prostate carcinoma cells
CC undergoing proliferative arrest. Maximum levels occur 18-20 hours after
CC androgen exposure. {ECO:0000269|PubMed:9459187}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76823.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U95825; AAD22134.2; -; mRNA.
DR EMBL; AB023196; BAA76823.2; ALT_INIT; mRNA.
DR EMBL; AK026889; BAB15584.1; -; mRNA.
DR EMBL; AL137201; CAB69911.1; -; mRNA.
DR EMBL; AL138820; CAH73160.2; -; Genomic_DNA.
DR EMBL; Z75889; CAH73160.2; JOINED; Genomic_DNA.
DR EMBL; Z75889; CAI10806.2; -; Genomic_DNA.
DR EMBL; AL138820; CAI10806.2; JOINED; Genomic_DNA.
DR EMBL; BC039256; AAH39256.1; -; mRNA.
DR EMBL; BC070274; AAH70274.1; -; mRNA.
DR CCDS; CCDS41878.1; -. [Q9NTI5-1]
DR RefSeq; NP_055847.1; NM_015032.3. [Q9NTI5-1]
DR RefSeq; XP_016875939.1; XM_017020450.1. [Q9NTI5-1]
DR PDB; 5HDT; X-ray; 2.71 A; A/B=21-1120.
DR PDBsum; 5HDT; -.
DR AlphaFoldDB; Q9NTI5; -.
DR SMR; Q9NTI5; -.
DR BioGRID; 116685; 147.
DR CORUM; Q9NTI5; -.
DR DIP; DIP-35420N; -.
DR IntAct; Q9NTI5; 50.
DR MINT; Q9NTI5; -.
DR STRING; 9606.ENSP00000313851; -.
DR GlyGen; Q9NTI5; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9NTI5; -.
DR MetOSite; Q9NTI5; -.
DR PhosphoSitePlus; Q9NTI5; -.
DR SwissPalm; Q9NTI5; -.
DR BioMuta; PDS5B; -.
DR DMDM; 74725312; -.
DR EPD; Q9NTI5; -.
DR jPOST; Q9NTI5; -.
DR MassIVE; Q9NTI5; -.
DR MaxQB; Q9NTI5; -.
DR PaxDb; Q9NTI5; -.
DR PeptideAtlas; Q9NTI5; -.
DR PRIDE; Q9NTI5; -.
DR ProteomicsDB; 82610; -. [Q9NTI5-1]
DR ProteomicsDB; 82611; -. [Q9NTI5-2]
DR ProteomicsDB; 82612; -. [Q9NTI5-3]
DR ProteomicsDB; 82613; -. [Q9NTI5-4]
DR ProteomicsDB; 82614; -. [Q9NTI5-5]
DR Antibodypedia; 22916; 179 antibodies from 29 providers.
DR DNASU; 23047; -.
DR Ensembl; ENST00000315596.15; ENSP00000313851.10; ENSG00000083642.19. [Q9NTI5-1]
DR Ensembl; ENST00000450460.5; ENSP00000401619.1; ENSG00000083642.19. [Q9NTI5-2]
DR GeneID; 23047; -.
DR KEGG; hsa:23047; -.
DR MANE-Select; ENST00000315596.15; ENSP00000313851.10; NM_015032.4; NP_055847.1.
DR UCSC; uc010abf.4; human. [Q9NTI5-1]
DR CTD; 23047; -.
DR DisGeNET; 23047; -.
DR GeneCards; PDS5B; -.
DR HGNC; HGNC:20418; PDS5B.
DR HPA; ENSG00000083642; Low tissue specificity.
DR MIM; 605333; gene.
DR neXtProt; NX_Q9NTI5; -.
DR OpenTargets; ENSG00000083642; -.
DR PharmGKB; PA162399098; -.
DR VEuPathDB; HostDB:ENSG00000083642; -.
DR eggNOG; KOG1525; Eukaryota.
DR GeneTree; ENSGT00940000157257; -.
DR HOGENOM; CLU_004041_0_0_1; -.
DR InParanoid; Q9NTI5; -.
DR OMA; CFDIVSG; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; Q9NTI5; -.
DR TreeFam; TF106415; -.
DR PathwayCommons; Q9NTI5; -.
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; Q9NTI5; -.
DR BioGRID-ORCS; 23047; 63 hits in 1093 CRISPR screens.
DR ChiTaRS; PDS5B; human.
DR GeneWiki; PDS5B; -.
DR GenomeRNAi; 23047; -.
DR Pharos; Q9NTI5; Tbio.
DR PRO; PR:Q9NTI5; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NTI5; protein.
DR Bgee; ENSG00000083642; Expressed in calcaneal tendon and 205 other tissues.
DR ExpressionAtlas; Q9NTI5; baseline and differential.
DR Genevisible; Q9NTI5; 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; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
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 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1447
FT /note="Sister chromatid cohesion protein PDS5 homolog B"
FT /id="PRO_0000287424"
FT REPEAT 383..419
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT DNA_BIND 1249..1261
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 1287..1299
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 1372..1384
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT REGION 1117..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1255
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT MOD_RES 1367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT MOD_RES 1370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT VAR_SEQ 1..1230
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052396"
FT VAR_SEQ 105..122
FT /note="DIFMFITRQLKGLEDTKS -> ASTDLNNSKIDRYFDLSF (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052397"
FT VAR_SEQ 123..1447
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052398"
FT VAR_SEQ 491..529
FT /note="ALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKV -> YVSNIKFCS
FT FHPLQYIGFYGKETTNTCILKCNLCSVNIV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052399"
FT VAR_SEQ 530..1447
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052400"
FT VAR_SEQ 1356..1447
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052401"
FT VAR_SEQ 1392..1447
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10215036"
FT /id="VSP_052402"
FT CONFLICT 256
FT /note="F -> S (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="H -> N (in Ref. 8; AAH39256)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="R -> G (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="N -> S (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="T -> A (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="E -> G (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="S -> G (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="K -> R (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1225
FT /note="Q -> R (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1242
FT /note="K -> R (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359
FT /note="P -> S (in Ref. 2; AAD22134)"
FT /evidence="ECO:0000305"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 74..91
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:5HDT"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5HDT"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 364..380
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:5HDT"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 470..481
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 486..514
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 519..533
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 539..555
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 557..567
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 573..585
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 596..608
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 615..629
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 634..638
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 642..659
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 667..677
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 682..695
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 704..720
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 723..736
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 740..754
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 764..776
FT /evidence="ECO:0007829|PDB:5HDT"
FT TURN 778..781
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 782..791
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 794..797
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 820..839
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 846..859
FT /evidence="ECO:0007829|PDB:5HDT"
FT TURN 860..862
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 872..890
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 893..896
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 901..908
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 909..912
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 916..931
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 937..939
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 941..948
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 952..975
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 980..984
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 991..1000
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 1011..1028
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 1036..1047
FT /evidence="ECO:0007829|PDB:5HDT"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:5HDT"
FT HELIX 1059..1079
FT /evidence="ECO:0007829|PDB:5HDT"
FT STRAND 1081..1085
FT /evidence="ECO:0007829|PDB:5HDT"
FT TURN 1095..1097
FT /evidence="ECO:0007829|PDB:5HDT"
SQ SEQUENCE 1447 AA; 164667 MW; 145C30308EA3EFD5 CRC64;
MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH
DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYA
LQSAAGKDAA KQIAWIKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG
KAQDFMKKFT QVLEDDEKIR KQLEVLVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK
GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ
FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK
NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
CLVKNINVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC
LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDAK MNEKLYTVCD VAMNIIMSKS
TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTTNV LGAVNKPLSS
AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK
RDDSDLVRSE LEKPRGRKKT PVTEQEEKLG MDDLTKLVQE QKPKGSQRSR KRGHTASESD
EQQWPEEKRL KEDILENEDE QNSPPKKGKR GRPPKPLGGG TPKEEPTMKT SKKGSKKKSG
PPAPEEEEEE ERQSGNTEQK SKSKQHRVSR RAQQRAESPE SSAIESTQST PQKGRGRPSK
TPSPSQPKKN VRVGRSKQAA TKENDSSEEV DVFQGSSPVD DIPQEETEEE EVSTVNVRRR
SAKRERR
