PKCB1_HUMAN
ID PKCB1_HUMAN Reviewed; 1186 AA.
AC Q9ULU4; B3KVL2; B7Z2A8; B7Z3E0; B7Z680; B7ZM62; E1P5U5; F5H0X3; H7C0U2;
AC J3KPU3; Q13517; Q2HXV1; Q2HXV2; Q2HXV3; Q2HXV4; Q2HXV7; Q2HXV8; Q2HXV9;
AC Q2HXW0; Q2HXW1; Q2HXW2; Q4JJ94; Q4JJ95; Q5TH09; Q5TH11; Q6MZM1; Q8WXC5;
AC Q9H1F3; Q9H1F4; Q9H1F5; Q9H1L8; Q9H1L9; Q9H2G5; Q9NYN3; Q9UIX6;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Protein kinase C-binding protein 1;
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen se14-3;
DE Short=CTCL-associated antigen se14-3;
DE AltName: Full=Rack7;
DE AltName: Full=Zinc finger MYND domain-containing protein 8;
GN Name=ZMYND8; Synonyms=KIAA1125, PRKCBP1, RACK7;
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 2), AND INTERACTION WITH PRKCB1.
RC TISSUE=Hippocampus;
RX PubMed=11003709; DOI=10.1007/s003350010174;
RA Fossey S.C., Kuroda S., Price J.A., Pendleton J.K., Freedman B.I.,
RA Bowden D.W.;
RT "Identification and characterization of PRKCBP1, a candidate RACK-like
RT protein.";
RL Mamm. Genome 11:919-925(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7 AND 8), AND VARIANT ALA-752.
RC TISSUE=Mammary tumor;
RA Mikhailik A., Keller J., Yang J., Hearing P., Bar-Sagi D.;
RT "Characterization of a novel BS69-related transcriptional repressor, BSR.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 7; 10; 12; 13; 14; 15; 16 AND 18).
RA Grkovic S., Velasco G., Ansieau S.;
RT "Characterization of RACK7, a novel heterochromatin and mitotic chromosome
RT associated protein.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 11; 19; 20 AND 23).
RC TISSUE=Amygdala, Brain, Hippocampus, and Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 17).
RC TISSUE=Brain, Eye, and Testis;
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 [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 IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-462; SER-465;
RP SER-486; SER-490; SER-495; THR-541; SER-547 AND SER-756, AND IDENTIFICATION
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-486; SER-490 AND
RP SER-495, AND 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-413, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404; SER-406; SER-486;
RP SER-495 AND SER-668, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-432; SER-444;
RP SER-490; SER-547; SER-682; THR-746; SER-754 AND SER-756, AND IDENTIFICATION
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-406; SER-417;
RP SER-425; SER-444; SER-460; SER-465; SER-495; SER-514; SER-523; SER-547;
RP THR-563; SER-652; SER-655; SER-668; SER-737; SER-756; SER-1119 AND
RP SER-1141, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-490; SER-547;
RP SER-668; SER-707 AND SER-709, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611 AND LYS-645, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS 10; 12; 13; 14; 15; 16; 17; 18;
RP 22; 5; 7 AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611 AND LYS-645, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS 10; 12; 13; 14; 15; 16; 17; 18;
RP 22; 5; 7 AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-390; LYS-413;
RP LYS-453; LYS-505; LYS-530; LYS-549; LYS-611; LYS-645; LYS-657 AND LYS-1115,
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12 (ISOFORMS 10; 12; 13; 14; 15;
RP 16; 17; 18; 22; 5; 7 AND 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 93-426, FUNCTION, INTERACTION WITH
RP KDM5D; KDM1A AND HISTONE H3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-76; ASP-79; ASP-84; ASP-88; PHE-89; GLU-104 AND 227-TYR-ASN-228.
RX PubMed=27477906; DOI=10.1016/j.molcel.2016.06.035;
RA Li N., Li Y., Lv J., Zheng X., Wen H., Shen H., Zhu G., Chen T.Y.,
RA Dhar S.S., Kan P.Y., Wang Z., Shiekhattar R., Shi X., Lan F., Chen K.,
RA Li W., Li H., Lee M.G.;
RT "ZMYND8 reads the dual histone mark H3K4me1-H3K14ac to antagonize the
RT expression of metastasis-linked genes.";
RL Mol. Cell 63:470-484(2016).
RN [27] {ECO:0007744|PDB:5Y1Z}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 83-406 IN COMPLEX WITH ZINC AND
RP DBN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-240; HIS-311 AND
RP ASP-312.
RX PubMed=28966017; DOI=10.1016/j.str.2017.08.014;
RA Yao N., Li J., Liu H., Wan J., Liu W., Zhang M.;
RT "The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic
RT Sequestering Mechanism of ZMYND8 by Drebrin.";
RL Structure 25:1657-1666(2017).
CC -!- FUNCTION: May act as a transcriptional corepressor for KDM5D. Required
CC for KDM5D-mediated down-regulation of diverse metastasis-associated
CC genes; the function seems to involve the recognition of the dual
CC histone signature H3K4me1-H3K14ac. Suppresses prostate cancer cell
CC invasion. {ECO:0000269|PubMed:27477906}.
CC -!- SUBUNIT: Interacts in vitro with PRKCB1 (PubMed:11003709). Interacts
CC with KDM5D and KDM1A (PubMed:27477906). Interacts with histone H3 (via
CC N-terminus) that is both methylated at 'Lys-4' (H3K4me1) and acetylated
CC at 'Lys-14' (H3K14ac), and with histone H3 (via N-terminus) unmodified
CC at 'Lys-4' (H3K4me0) and acetylated at 'Lys-14' (H3K14ac)
CC (PubMed:27477906). Interacts (via PHD-type Zinc finger, Bromo and PWWP
CC domains) with DBN1 (via ADF-H domain); the interaction leads to
CC sequestering of ZMYND8 in the cytoplasm (PubMed:28966017).
CC {ECO:0000269|PubMed:11003709, ECO:0000269|PubMed:27477906,
CC ECO:0000269|PubMed:28966017}.
CC -!- INTERACTION:
CC Q9ULU4; P41182: BCL6; NbExp=3; IntAct=EBI-765834, EBI-765407;
CC Q9ULU4; Q16643: DBN1; NbExp=4; IntAct=EBI-765834, EBI-351394;
CC Q9ULU4; Q93009: USP7; NbExp=2; IntAct=EBI-765834, EBI-302474;
CC Q9ULU4-14; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12169985, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27477906,
CC ECO:0000269|PubMed:28966017}. Cytoplasm {ECO:0000269|PubMed:28966017}.
CC Note=Sequestered in the cytoplasm through the interaction with DBN1.
CC {ECO:0000269|PubMed:28966017}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=23;
CC Name=1;
CC IsoId=Q9ULU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULU4-2; Sequence=VSP_000566, VSP_000568;
CC Name=3;
CC IsoId=Q9ULU4-3; Sequence=VSP_000564, VSP_000568;
CC Name=4;
CC IsoId=Q9ULU4-4; Sequence=VSP_000565, VSP_000568;
CC Name=5;
CC IsoId=Q9ULU4-5; Sequence=VSP_000563, VSP_000567;
CC Name=6;
CC IsoId=Q9ULU4-6; Sequence=VSP_000564, VSP_000568, VSP_000570;
CC Name=7;
CC IsoId=Q9ULU4-7; Sequence=VSP_000563, VSP_000570;
CC Name=8;
CC IsoId=Q9ULU4-8; Sequence=VSP_000563, VSP_017096, VSP_000570;
CC Name=9;
CC IsoId=Q9ULU4-9; Sequence=VSP_000568, VSP_000570;
CC Name=10;
CC IsoId=Q9ULU4-10; Sequence=VSP_000563;
CC Name=11;
CC IsoId=Q9ULU4-11; Sequence=VSP_000570;
CC Name=12;
CC IsoId=Q9ULU4-12; Sequence=VSP_000563, VSP_000568;
CC Name=13;
CC IsoId=Q9ULU4-13; Sequence=VSP_000563, VSP_000568, VSP_000570;
CC Name=14;
CC IsoId=Q9ULU4-14; Sequence=VSP_000563, VSP_000567, VSP_000568;
CC Name=15;
CC IsoId=Q9ULU4-15; Sequence=VSP_000563, VSP_000567, VSP_053400,
CC VSP_000568;
CC Name=16;
CC IsoId=Q9ULU4-16; Sequence=VSP_000563, VSP_000567, VSP_000568,
CC VSP_000570;
CC Name=17;
CC IsoId=Q9ULU4-17; Sequence=VSP_000563, VSP_000567, VSP_017096;
CC Name=18;
CC IsoId=Q9ULU4-18; Sequence=VSP_000563, VSP_000567, VSP_053400;
CC Name=19;
CC IsoId=Q9ULU4-19; Sequence=VSP_054810, VSP_000570;
CC Name=20;
CC IsoId=Q9ULU4-20; Sequence=VSP_054811, VSP_000567;
CC Name=21;
CC IsoId=Q9ULU4-21; Sequence=VSP_000567, VSP_000568;
CC Name=22;
CC IsoId=Q9ULU4-22; Sequence=VSP_000563, VSP_000568, VSP_054814,
CC VSP_000570;
CC Name=23;
CC IsoId=Q9ULU4-23; Sequence=VSP_000567, VSP_054812, VSP_000568,
CC VSP_000570;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC expression in brain, lung, pancreas, and placenta. Expressed in
CC cutaneous T-cell lymphomas (CTCL).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72244.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA86439.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF233453; AAF71262.1; -; mRNA.
DR EMBL; U48251; AAC72244.1; ALT_FRAME; mRNA.
DR EMBL; AF454056; AAL50790.1; -; mRNA.
DR EMBL; AF273045; AAG34905.1; -; mRNA.
DR EMBL; DQ082998; AAY85630.1; -; mRNA.
DR EMBL; DQ082999; AAY85631.1; -; mRNA.
DR EMBL; DQ368669; ABC86680.1; -; mRNA.
DR EMBL; DQ368670; ABC86681.1; -; mRNA.
DR EMBL; DQ368671; ABC86682.1; -; mRNA.
DR EMBL; DQ368672; ABC86683.1; -; mRNA.
DR EMBL; DQ368673; ABC86684.1; -; mRNA.
DR EMBL; DQ368674; ABC86685.1; -; mRNA.
DR EMBL; DQ368677; ABC86688.1; -; mRNA.
DR EMBL; DQ368678; ABC86689.1; -; mRNA.
DR EMBL; DQ368679; ABC86690.1; -; mRNA.
DR EMBL; DQ368680; ABC86691.1; -; mRNA.
DR EMBL; AB032951; BAA86439.1; ALT_INIT; mRNA.
DR EMBL; AK122966; BAG53824.1; -; mRNA.
DR EMBL; AK294511; BAH11794.1; -; mRNA.
DR EMBL; AK295747; BAH12176.1; -; mRNA.
DR EMBL; AK299899; BAH13166.1; -; mRNA.
DR EMBL; BX641005; CAE46008.1; -; mRNA.
DR EMBL; AL031666; CAI21842.1; -; Genomic_DNA.
DR EMBL; AL049540; CAI21842.1; JOINED; Genomic_DNA.
DR EMBL; AL022342; CAI21842.1; JOINED; Genomic_DNA.
DR EMBL; AL049540; CAI23169.1; -; Genomic_DNA.
DR EMBL; AL031666; CAI23169.1; JOINED; Genomic_DNA.
DR EMBL; AL022342; CAI23169.1; JOINED; Genomic_DNA.
DR EMBL; AL049540; CAI23168.1; -; Genomic_DNA.
DR EMBL; AL031666; CAI23168.1; JOINED; Genomic_DNA.
DR EMBL; AL390212; CAI23168.1; JOINED; Genomic_DNA.
DR EMBL; CH471077; EAW75703.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75706.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75709.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75711.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75712.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75715.1; -; Genomic_DNA.
DR EMBL; BC030721; AAH30721.2; -; mRNA.
DR EMBL; BC136608; AAI36609.1; -; mRNA.
DR EMBL; BC144289; AAI44290.1; -; mRNA.
DR CCDS; CCDS13404.1; -. [Q9ULU4-12]
DR CCDS; CCDS13405.1; -. [Q9ULU4-13]
DR CCDS; CCDS46613.1; -. [Q9ULU4-14]
DR CCDS; CCDS63300.1; -. [Q9ULU4-11]
DR CCDS; CCDS63301.1; -. [Q9ULU4-9]
DR CCDS; CCDS63303.1; -. [Q9ULU4-18]
DR CCDS; CCDS63304.1; -. [Q9ULU4-17]
DR CCDS; CCDS63306.1; -. [Q9ULU4-7]
DR CCDS; CCDS74738.1; -. [Q9ULU4-20]
DR CCDS; CCDS86961.1; -. [Q9ULU4-1]
DR CCDS; CCDS86962.1; -. [Q9ULU4-19]
DR RefSeq; NP_001268700.1; NM_001281771.2. [Q9ULU4-17]
DR RefSeq; NP_001268701.1; NM_001281772.2. [Q9ULU4-20]
DR RefSeq; NP_001268702.1; NM_001281773.2. [Q9ULU4-11]
DR RefSeq; NP_001268703.1; NM_001281774.2. [Q9ULU4-9]
DR RefSeq; NP_001268704.1; NM_001281775.2. [Q9ULU4-7]
DR RefSeq; NP_001268705.1; NM_001281776.2. [Q9ULU4-8]
DR RefSeq; NP_001268706.1; NM_001281777.2. [Q9ULU4-16]
DR RefSeq; NP_001268707.1; NM_001281778.2. [Q9ULU4-5]
DR RefSeq; NP_001268710.1; NM_001281781.2. [Q9ULU4-15]
DR RefSeq; NP_001268711.1; NM_001281782.2.
DR RefSeq; NP_001268712.1; NM_001281783.2. [Q9ULU4-10]
DR RefSeq; NP_001268713.1; NM_001281784.2. [Q9ULU4-18]
DR RefSeq; NP_036540.3; NM_012408.5. [Q9ULU4-12]
DR RefSeq; NP_898868.1; NM_183047.3. [Q9ULU4-13]
DR RefSeq; NP_898869.1; NM_183048.3. [Q9ULU4-14]
DR RefSeq; XP_005260413.1; XM_005260356.4.
DR RefSeq; XP_005260417.1; XM_005260360.4.
DR RefSeq; XP_005260423.1; XM_005260366.2.
DR RefSeq; XP_006723825.1; XM_006723762.3.
DR RefSeq; XP_011527053.1; XM_011528751.1.
DR RefSeq; XP_016883250.1; XM_017027761.1.
DR RefSeq; XP_016883256.1; XM_017027767.1.
DR RefSeq; XP_016883257.1; XM_017027768.1.
DR PDB; 4COS; X-ray; 1.67 A; A=83-406.
DR PDB; 5B73; X-ray; 1.80 A; A=73-406.
DR PDB; 5MQ4; X-ray; 2.70 A; A/B/C/D/E/F=949-1073.
DR PDB; 5Y1Z; X-ray; 2.68 A; C/D=83-406.
DR PDB; 7CWH; NMR; -; B=83-143.
DR PDBsum; 4COS; -.
DR PDBsum; 5B73; -.
DR PDBsum; 5MQ4; -.
DR PDBsum; 5Y1Z; -.
DR PDBsum; 7CWH; -.
DR AlphaFoldDB; Q9ULU4; -.
DR SMR; Q9ULU4; -.
DR BioGRID; 117146; 154.
DR IntAct; Q9ULU4; 61.
DR MINT; Q9ULU4; -.
DR STRING; 9606.ENSP00000420095; -.
DR BindingDB; Q9ULU4; -.
DR ChEMBL; CHEMBL3627580; -.
DR GlyGen; Q9ULU4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULU4; -.
DR PhosphoSitePlus; Q9ULU4; -.
DR BioMuta; ZMYND8; -.
DR DMDM; 25453223; -.
DR EPD; Q9ULU4; -.
DR jPOST; Q9ULU4; -.
DR MassIVE; Q9ULU4; -.
DR MaxQB; Q9ULU4; -.
DR PeptideAtlas; Q9ULU4; -.
DR PRIDE; Q9ULU4; -.
DR ProteomicsDB; 25473; -.
DR ProteomicsDB; 44416; -.
DR ProteomicsDB; 61294; -.
DR ProteomicsDB; 61295; -.
DR ProteomicsDB; 7246; -.
DR ProteomicsDB; 85109; -. [Q9ULU4-1]
DR ProteomicsDB; 85110; -. [Q9ULU4-10]
DR ProteomicsDB; 85111; -. [Q9ULU4-11]
DR ProteomicsDB; 85112; -. [Q9ULU4-12]
DR ProteomicsDB; 85113; -. [Q9ULU4-13]
DR ProteomicsDB; 85114; -. [Q9ULU4-14]
DR ProteomicsDB; 85115; -. [Q9ULU4-2]
DR ProteomicsDB; 85116; -. [Q9ULU4-3]
DR ProteomicsDB; 85117; -. [Q9ULU4-4]
DR ProteomicsDB; 85118; -. [Q9ULU4-5]
DR ProteomicsDB; 85119; -. [Q9ULU4-6]
DR ProteomicsDB; 85120; -. [Q9ULU4-7]
DR ProteomicsDB; 85121; -. [Q9ULU4-8]
DR ProteomicsDB; 85122; -. [Q9ULU4-9]
DR Antibodypedia; 13294; 195 antibodies from 30 providers.
DR DNASU; 23613; -.
DR Ensembl; ENST00000262975.8; ENSP00000262975.4; ENSG00000101040.20. [Q9ULU4-9]
DR Ensembl; ENST00000311275.11; ENSP00000312237.7; ENSG00000101040.20. [Q9ULU4-1]
DR Ensembl; ENST00000352431.6; ENSP00000335537.3; ENSG00000101040.20. [Q9ULU4-12]
DR Ensembl; ENST00000355972.8; ENSP00000348246.4; ENSG00000101040.20. [Q9ULU4-11]
DR Ensembl; ENST00000360911.7; ENSP00000354166.3; ENSG00000101040.20. [Q9ULU4-14]
DR Ensembl; ENST00000372023.7; ENSP00000361093.5; ENSG00000101040.20. [Q9ULU4-23]
DR Ensembl; ENST00000396281.8; ENSP00000379577.4; ENSG00000101040.20. [Q9ULU4-20]
DR Ensembl; ENST00000446994.6; ENSP00000396725.3; ENSG00000101040.20. [Q9ULU4-11]
DR Ensembl; ENST00000458360.6; ENSP00000392964.2; ENSG00000101040.20. [Q9ULU4-17]
DR Ensembl; ENST00000461685.5; ENSP00000418210.1; ENSG00000101040.20. [Q9ULU4-13]
DR Ensembl; ENST00000471951.7; ENSP00000420095.2; ENSG00000101040.20. [Q9ULU4-7]
DR Ensembl; ENST00000536340.5; ENSP00000439800.1; ENSG00000101040.20. [Q9ULU4-19]
DR Ensembl; ENST00000540497.5; ENSP00000443086.3; ENSG00000101040.20. [Q9ULU4-18]
DR GeneID; 23613; -.
DR KEGG; hsa:23613; -.
DR MANE-Select; ENST00000471951.7; ENSP00000420095.2; NM_001281775.3; NP_001268704.1. [Q9ULU4-7]
DR UCSC; uc002xss.3; human. [Q9ULU4-1]
DR CTD; 23613; -.
DR DisGeNET; 23613; -.
DR GeneCards; ZMYND8; -.
DR HGNC; HGNC:9397; ZMYND8.
DR HPA; ENSG00000101040; Low tissue specificity.
DR neXtProt; NX_Q9ULU4; -.
DR OpenTargets; ENSG00000101040; -.
DR PharmGKB; PA162409890; -.
DR VEuPathDB; HostDB:ENSG00000101040; -.
DR eggNOG; KOG3612; Eukaryota.
DR GeneTree; ENSGT00940000154897; -.
DR InParanoid; Q9ULU4; -.
DR OMA; MPVQRFN; -.
DR OrthoDB; 369818at2759; -.
DR PhylomeDB; Q9ULU4; -.
DR TreeFam; TF317221; -.
DR PathwayCommons; Q9ULU4; -.
DR SignaLink; Q9ULU4; -.
DR SIGNOR; Q9ULU4; -.
DR BioGRID-ORCS; 23613; 210 hits in 1103 CRISPR screens.
DR ChiTaRS; ZMYND8; human.
DR GeneWiki; ZMYND8; -.
DR GenomeRNAi; 23613; -.
DR Pharos; Q9ULU4; Tbio.
DR PRO; PR:Q9ULU4; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9ULU4; protein.
DR Bgee; ENSG00000101040; Expressed in corpus epididymis and 215 other tissues.
DR ExpressionAtlas; Q9ULU4; baseline and differential.
DR Genevisible; Q9ULU4; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR CDD; cd05508; Bromo_RACK7; 1.
DR CDD; cd05841; BS69_related; 1.
DR CDD; cd15538; PHD_PRKCBP1; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR044075; PRKCBP1_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR037967; RACK7_Bromo_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR021931; ZMYND8.
DR InterPro; IPR035505; ZMYND8/11_PWWP.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12064; DUF3544; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; Cytoplasm;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1186
FT /note="Protein kinase C-binding protein 1"
FT /id="PRO_0000211209"
FT DOMAIN 165..235
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 277..327
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 88..133
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1028..1062
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..406
FT /note="Interaction with histone H3K14ac"
FT /evidence="ECO:0000269|PubMed:27477906"
FT REGION 75..268
FT /note="Interaction with histone H3K4me0"
FT /evidence="ECO:0000269|PubMed:27477906"
FT REGION 412..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1186
FT /note="Interaction with PRKCB1"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:28966017,
FT ECO:0007744|PDB:5Y1Z"
FT BINDING 1028
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1031
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1039
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1046
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1058
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 1062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 413
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 495
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 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 530
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11003709"
FT /id="VSP_000566"
FT VAR_SEQ 1..376
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11149944"
FT /id="VSP_000565"
FT VAR_SEQ 1..145
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11149944,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000564"
FT VAR_SEQ 1
FT /note="M -> MVFLEEFEARSCLAEEEIKTEQEVVEGM (in isoform 19)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054810"
FT VAR_SEQ 1
FT /note="M -> MFSSLQKSFNLAEEEIKTEQEVVEGM (in isoform 20)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054811"
FT VAR_SEQ 1
FT /note="M -> MHPQSLAEEEIKTEQEVVEGM (in isoform 5, isoform 7,
FT isoform 8, isoform 10, isoform 12, isoform 13, isoform 14,
FT isoform 15, isoform 16, isoform 17, isoform 18 and isoform
FT 22)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_000563"
FT VAR_SEQ 58..82
FT /note="Missing (in isoform 5, isoform 14, isoform 15,
FT isoform 16, isoform 17, isoform 18, isoform 20, isoform 21
FT and isoform 23)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_000567"
FT VAR_SEQ 132..169
FT /note="Missing (in isoform 23)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054812"
FT VAR_SEQ 474..520
FT /note="Missing (in isoform 15 and isoform 18)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_053400"
FT VAR_SEQ 742..868
FT /note="Missing (in isoform 8 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_017096"
FT VAR_SEQ 823..869
FT /note="SKFQTSSQKWHMQKMQRQQQQQQQQNQQQQPQSSQGTRYQTRQAVKA -> T
FT (in isoform 2, isoform 3, isoform 4, isoform 6, isoform 9,
FT isoform 12, isoform 13, isoform 14, isoform 15, isoform 16,
FT isoform 21, isoform 22 and isoform 23)"
FT /evidence="ECO:0000303|PubMed:11003709,
FT ECO:0000303|PubMed:11149944, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.4"
FT /id="VSP_000568"
FT VAR_SEQ 933..959
FT /note="Missing (in isoform 22)"
FT /evidence="ECO:0000305"
FT /id="VSP_054814"
FT VAR_SEQ 1142
FT /note="D -> VSKRCDKQPAYAPTTTDHQPHPNYPAQKY (in isoform 6,
FT isoform 7, isoform 8, isoform 9, isoform 11, isoform 13,
FT isoform 16, isoform 19, isoform 22 and isoform 23)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_000570"
FT VARIANT 752
FT /note="V -> A (in dbSNP:rs2275801)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_055559"
FT MUTAGEN 76
FT /note="D->A: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 79
FT /note="D->A: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 84
FT /note="D->A: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 88
FT /note="D->A: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 89
FT /note="F->D: Increases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 104
FT /note="E->A: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 227..228
FT /note="YN->AA: Decreases interaction with histone H3K4me0."
FT /evidence="ECO:0000269|PubMed:27477906"
FT MUTAGEN 240
FT /note="V->Q: Decreases binding to DBN1."
FT /evidence="ECO:0000269|PubMed:28966017"
FT MUTAGEN 311
FT /note="H->A: Loss of binding to DBN1. Loss of cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:28966017"
FT MUTAGEN 312
FT /note="D->R: Loss of binding to DBN1."
FT /evidence="ECO:0000269|PubMed:28966017"
FT CONFLICT 119
FT /note="S -> P (in Ref. 6; BAH11794)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> T (in Ref. 6; BAH12176)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> F (in Ref. 6; BAH12176)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="I -> V (in Ref. 2; AAL50790)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="L -> P (in Ref. 6; BAH11794)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="D -> G (in Ref. 6; BAH11794)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="E -> G (in Ref. 6; BAG53824)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="P -> A (in Ref. 2; AAG34905/AAL50790)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="I -> T (in Ref. 7; CAE46008)"
FT /evidence="ECO:0000305"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4COS"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:7CWH"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7CWH"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4COS"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 210..228
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4COS"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:4COS"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5Y1Z"
FT HELIX 336..357
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4COS"
FT HELIX 953..972
FT /evidence="ECO:0007829|PDB:5MQ4"
FT HELIX 975..1023
FT /evidence="ECO:0007829|PDB:5MQ4"
FT TURN 1029..1031
FT /evidence="ECO:0007829|PDB:5MQ4"
FT STRAND 1037..1040
FT /evidence="ECO:0007829|PDB:5MQ4"
FT STRAND 1043..1047
FT /evidence="ECO:0007829|PDB:5MQ4"
FT HELIX 1048..1058
FT /evidence="ECO:0007829|PDB:5MQ4"
FT HELIX 1059..1061
FT /evidence="ECO:0007829|PDB:5MQ4"
FT CONFLICT Q9ULU4-2:297
FT /note="T -> S (in Ref. 1; AAF71262)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q9ULU4-5:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-7:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-8:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-10:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-12:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-13:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-14:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-15:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-16:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-17:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-18:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9ULU4-22:12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1186 AA; 131692 MW; BAE8CDEF240E647A CRC64;
MDISTRSKDP GSAERTAQKR KFPSPPHSSN GHSPQDTSTS PIKKKKKPGL LNSNNKEQSE
LRHGPFYYMK QPLTTDPVDV VPQDGRNDFY CWVCHREGQV LCCELCPRVY HAKCLRLTSE
PEGDWFCPEC EKITVAECIE TQSKAMTMLT IEQLSYLLKF AIQKMKQPGT DAFQKPVPLE
QHPDYAEYIF HPMDLCTLEK NAKKKMYGCT EAFLADAKWI LHNCIIYNGG NHKLTQIAKV
VIKICEHEMN EIEVCPECYL AACQKRDNWF CEPCSNPHPL VWAKLKGFPF WPAKALRDKD
GQVDARFFGQ HDRAWVPINN CYLMSKEIPF SVKKTKSIFN SAMQEMEVYV ENIRRKFGVF
NYSPFRTPYT PNSQYQMLLD PTNPSAGTAK IDKQEKVKLN FDMTASPKIL MSKPVLSGGT
GRRISLSDMP RSPMSTNSSV HTGSDVEQDA EKKATSSHFS ASEESMDFLD KSTASPASTK
TGQAGSLSGS PKPFSPQLSA PITTKTDKTS TTGSILNLNL DRSKAEMDLK ELSESVQQQS
TPVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV YTAVEHSDSE DSEKSDSSDS
EYISDDEQKS KNEPEDTEDK EGCQMDKEPS AVKKKPKPTN PVEIKEELKS TSPASEKADP
GAVKDKASPE PEKDFSEKAK PSPHPIKDKL KGKDETDSPT VHLGLDSDSE SELVIDLGED
HSGREGRKNK KEPKEPSPKQ DVVGKTPPST TVGSHSPPET PVLTRSSAQT SAAGATATTS
TSSTVTVTAP APAATGSPVK KQRPLLPKET APAVQRVVWN SSSKFQTSSQ KWHMQKMQRQ
QQQQQQQNQQ QQPQSSQGTR YQTRQAVKAV QQKEITQSPS TSTITLVTST QSSPLVTSSG
SMSTLVSSVN ADLPIATASA DVAADIAKYT SKMMDAIKGT MTEIYNDLSK NTTGSTIAEI
RRLRIEIEKL QWLHQQELSE MKHNLELTMA EMRQSLEQER DRLIAEVKKQ LELEKQQAVD
ETKKKQWCAN CKKEAIFYCC WNTSYCDYPC QQAHWPEHMK SCTQSATAPQ QEADAEVNTE
TLNKSSQGSS SSTQSAPSET ASASKEKETS AEKSKESGST LDLSGSRETP SSILLGSNQG
SDHSRSNKSS WSSSDEKRGS TRSDHNTSTS TKSLLPKESR LDTFWD
