ID RBBP6_HUMAN Reviewed; 1792 AA. AC Q7Z6E9; Q147T5; Q15290; Q6DKH4; Q6P4C2; Q6YNC9; Q7Z6E8; Q8N0V2; Q96PH3; AC Q9H3I8; Q9H5M5; Q9NPX4; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 185. DE RecName: Full=E3 ubiquitin-protein ligase RBBP6; DE EC=2.3.2.27; DE AltName: Full=Proliferation potential-related protein; DE AltName: Full=Protein P2P-R; DE AltName: Full=RING-type E3 ubiquitin transferase RBBP6 {ECO:0000305}; DE AltName: Full=Retinoblastoma-binding Q protein 1; DE Short=RBQ-1; DE AltName: Full=Retinoblastoma-binding protein 6; DE AltName: Full=p53-associated cellular protein of testis; GN Name=RBBP6; Synonyms=P2PR, PACT, RBQ1; ORFNames=My038; 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] (ISOFORMS 1 AND 2). RA Kudo E., Itakura M.; RT "Retinoblastoma binding protein 6 (RBBP6), mRNA."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-1727 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 1427-1792 (ISOFORMS 1/2/4). RC TISSUE=Bone, and Kidney; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-55 (ISOFORMS 1/2/3/4). RC TISSUE=Fetal brain; RA Mao Y.M., Xie Y., Zheng Z.H.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-1792 (ISOFORM 2). RC TISSUE=Spleen; RA Ma X., Qu X., Sun L., Wu S., He F.; RT "The cDNA sequence for the human PACT gene."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-1792 (ISOFORM 1). RA Camargo A.A., Moreira E.S., Simpson A.J.G.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-1146 (ISOFORM 1). RC TISSUE=Lung carcinoma; RX PubMed=8595913; DOI=10.1006/geno.1995.0017; RA Sakai Y., Saijo M., Coelho K., Kishino T., Niikawa N., Taya Y.; RT "cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 RT (RBBP6), that binds to the retinoblastoma gene product."; RL Genomics 30:98-101(1995). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1165-1792 (ISOFORMS 1/2). RC TISSUE=Hepatoma; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1264-1792 (ISOFORMS 1/2). RC TISSUE=Amygdala; 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 [10] RP SUBCELLULAR LOCATION. RX PubMed=12064457; DOI=10.1002/jcp.10084; RA Gao S., Witte M.M., Scott R.E.; RT "P2P-R protein localizes to the nucleolus of interphase cells and the RT periphery of chromosomes in mitotic cells which show maximum P2P-R RT immunoreactivity."; RL J. Cell. Physiol. 191:145-154(2002). RN [11] RP ERRATUM OF PUBMED:12064457. RA Gao S., Witte M.M., Scott R.E.; RL J. Cell. Physiol. 192:359-360(2002). RN [12] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND OVEREXPRESSION IN ESOPHAGEAL RP CANCER. RX PubMed=15475430; DOI=10.1158/1078-0432.ccr-04-0841; RA Yoshitake Y., Nakatsura T., Monji M., Senju S., Matsuyoshi H., RA Tsukamoto H., Hosaka S., Komori H., Fukuma D., Ikuta Y., Katagiri T., RA Furukawa Y., Ito H., Shinohara M., Nakamura Y., Nishimura Y.; RT "Proliferation potential-related protein, an ideal esophageal cancer RT antigen for immunotherapy, identified using complementary DNA microarray RT analysis."; RL Clin. Cancer Res. 10:6437-6448(2004). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-245; SER-246; RP SER-247; SER-360; SER-770; SER-772; SER-861; SER-1179 AND SER-1328, AND 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, 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 [15] RP INTERACTION WITH MDM2. RX PubMed=17470788; DOI=10.1073/pnas.0701916104; RA Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J., RA Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.; RT "PACT is a negative regulator of p53 and essential for cell growth and RT embryonic development."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007). RN [16] 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 [17] RP FUNCTION, AND INTERACTION WITH YBX1. RX PubMed=18851979; DOI=10.1016/j.jmb.2008.09.060; RA Chibi M., Meyer M., Skepu A., Rees D.J.G., Moolman-Smook J.C., Pugh D.J.; RT "RBBP6 interacts with multifunctional protein YB-1 through its RING finger RT domain, leading to ubiquitination and proteosomal degradation of YB-1."; RL J. Mol. Biol. 384:908-916(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-516; SER-1179; RP THR-1468; SER-1646 AND SER-1648, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1328, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-1179; SER-1277; RP SER-1328 AND SER-1648, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [22] RP SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION. RX PubMed=20873783; DOI=10.1021/pr100562w; RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., RA Paes Leme A.F., Kobarg J.; RT "Characterization of hNek6 interactome reveals an important role for its RT short N-terminal domain and colocalization with proteins at the RT centrosome."; RL J. Proteome Res. 9:6298-6316(2010). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-245; SER-246; RP SER-247; SER-516; SER-861; SER-1179 AND SER-1328, AND IDENTIFICATION BY RP 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1179 AND SER-1328, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-516; SER-768; RP SER-770; SER-772; SER-815; SER-861; SER-873; SER-957; THR-984; SER-1179; RP SER-1221; SER-1277; SER-1328; SER-1341 AND SER-1347, AND IDENTIFICATION BY RP 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 FUNCTION, AND INTERACTION WITH ZBTB38. RX PubMed=24726359; DOI=10.1016/j.celrep.2014.03.030; RA Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D., RA Debatisse M., He F., Zhang L., Defossez P.A.; RT "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile RT site stability."; RL Cell Rep. 7:575-587(2014). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-984 AND SER-1277, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1106 AND LYS-1169, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1169, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE 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 [30] RP STRUCTURE BY NMR OF 1-81. RX PubMed=16396680; DOI=10.1186/1472-6807-6-1; RA Pugh D.J.R., Ab E., Faro A., Lutya P.T., Hoffmann E., Rees D.J.G.; RT "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing RT and ubiquitin-like pathways."; RL BMC Struct. Biol. 6:1-1(2006). RN [31] RP STRUCTURE BY NMR OF 159-309. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the zinc finger CCHC domain and of the RING finger RT from the human retinoblastoma-binding protein 6 (retinoblastoma-binding Q RT protein 1, RBQ-1)."; RL Submitted (APR-2008) to the PDB data bank. RN [32] {ECO:0007744|PDB:3ZTG} RP STRUCTURE BY NMR OF 249-335, AND DOMAIN. RX PubMed=22130672; DOI=10.1074/jbc.m110.217059; RA Kappo M.A., Ab E., Hassem F., Atkinson R.A., Faro A., Muleya V., RA Mulaudzi T., Poole J.O., McKenzie J.M., Chibi M., Moolman-Smook J.C., RA Rees D.J., Pugh D.J.; RT "Solution structure of RING finger-like domain of retinoblastoma-binding RT protein-6 (RBBP6) suggests it functions as a U-box."; RL J. Biol. Chem. 287:7146-7158(2012). RN [33] {ECO:0007744|PDB:6E5X} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 554-568, INTERACTION WITH RP EBOLAVIRUS VP30 (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL INFECTION). RX PubMed=30550789; DOI=10.1016/j.cell.2018.08.044; RA Batra J., Hultquist J.F., Liu D., Shtanko O., Von Dollen J., Satkamp L., RA Jang G.M., Luthra P., Schwarz T.M., Small G.I., Arnett E., Anantpadma M., RA Reyes A., Leung D.W., Kaake R., Haas P., Schmidt C.B., Schlesinger L.S., RA LaCount D.J., Davey R.A., Amarasinghe G.K., Basler C.F., Krogan N.J.; RT "Protein Interaction Mapping Identifies RBBP6 as a Negative Regulator of RT Ebola Virus Replication."; RL Cell 175:1917-1930.e13(2018). CC -!- FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination of CC YBX1, leading to its degradation by the proteasome (PubMed:18851979). CC May play a role as a scaffold protein to promote the assembly of the CC p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated CC ubiquitination and degradation of p53/TP53; may function as negative CC regulator of p53/TP53, leading to both apoptosis and cell growth (By CC similarity). Regulates DNA-replication and the stability of chromosomal CC common fragile sites (CFSs) in a ZBTB38- and MCM10-dependent manner. CC Controls ZBTB38 protein stability and abundance via ubiquitination and CC proteasomal degradation, and ZBTB38 in turn negatively regulates the CC expression of MCM10 which plays an important role in DNA-replication CC (PubMed:24726359). {ECO:0000250|UniProtKB:P97868, CC ECO:0000269|PubMed:18851979, ECO:0000269|PubMed:24726359}. CC -!- FUNCTION: (Microbial infection) [Isoform 1]: Restricts ebolavirus CC replication probably by impairing the vp30-NP interaction, and thus CC viral transcription. {ECO:0000269|PubMed:30550789}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with p53/TP53 and RB1 (By similarity). Interacts CC also with MDM2 and YBX1 (PubMed:17470788). Interacts also with MDM2 and CC YBX1 (PubMed:18851979). Interacts with NEK6 (PubMed:20873783). CC Interacts with ZBTB38 (PubMed:24726359). {ECO:0000250|UniProtKB:P97868, CC ECO:0000269|PubMed:17470788, ECO:0000269|PubMed:18851979, CC ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:24726359}. CC -!- SUBUNIT: (Microbial infection) [Isoform 1]: Interacts with ebolavirus CC VP30. {ECO:0000269|PubMed:30550789}. CC -!- INTERACTION: CC Q7Z6E9; Q16629: SRSF7; NbExp=3; IntAct=EBI-2117026, EBI-398885; CC Q7Z6E9-3; P49821: NDUFV1; NbExp=3; IntAct=EBI-11743772, EBI-748312; CC Q7Z6E9-3; O76024: WFS1; NbExp=3; IntAct=EBI-11743772, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome. CC Note=Colocalizes with mitotic chromosomes. Colocalizes with NEK6 in the CC centrosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q7Z6E9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7Z6E9-2; Sequence=VSP_018284; CC Name=3; CC IsoId=Q7Z6E9-3; Sequence=VSP_018281, VSP_018282; CC Name=4; CC IsoId=Q7Z6E9-4; Sequence=VSP_018283; CC -!- TISSUE SPECIFICITY: Highly expressed in the placenta and testis. CC Expressed at lower levels in the brain, heart, kidney, liver and lung. CC Overexpressed in esophageal cancer. {ECO:0000269|PubMed:15475430}. CC -!- DOMAIN: Contains a N-terminus DWNN domain, a zinc-finger domain and a CC C4C4 zinc-binding RING finger domain (PubMed:22130672). The ring finger CC may indeed be a U-box domain (PubMed:22130672). CC {ECO:0000269|PubMed:22130672}. CC -!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG43155.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=AAH63524.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAL05625.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAL68925.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=CAA59445.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB112074; BAC77636.1; -; mRNA. DR EMBL; AB112075; BAC77637.1; -; mRNA. DR EMBL; CH471145; EAW55789.1; -; Genomic_DNA. DR EMBL; BC029352; AAH29352.1; -; mRNA. DR EMBL; BC063524; AAH63524.1; ALT_SEQ; mRNA. DR EMBL; BC073938; AAH73938.1; -; mRNA. DR EMBL; BC101139; AAI01140.1; -; mRNA. DR EMBL; BC101140; AAI01141.1; -; mRNA. DR EMBL; BC101141; AAI01142.1; -; mRNA. DR EMBL; BC101142; AAI01143.1; -; mRNA. DR EMBL; BC114353; AAI14354.1; -; mRNA. DR EMBL; BC114354; AAI14355.1; -; mRNA. DR EMBL; BC118667; AAI18668.1; -; mRNA. DR EMBL; BC139830; AAI39831.1; -; mRNA. DR EMBL; AF063596; AAG43155.1; ALT_SEQ; mRNA. DR EMBL; AY072922; AAL68925.1; ALT_SEQ; mRNA. DR EMBL; AF352051; AAL05625.1; ALT_FRAME; mRNA. DR EMBL; X85133; CAA59445.1; ALT_FRAME; mRNA. DR EMBL; AK026954; BAB15600.1; -; mRNA. DR EMBL; AL359564; CAB94869.1; -; mRNA. DR CCDS; CCDS10621.1; -. [Q7Z6E9-1] DR CCDS; CCDS10622.1; -. [Q7Z6E9-2] DR CCDS; CCDS45444.1; -. [Q7Z6E9-3] DR PIR; A57640; A57640. DR PIR; T50609; T50609. DR RefSeq; NP_008841.2; NM_006910.4. [Q7Z6E9-1] DR RefSeq; NP_061173.1; NM_018703.3. [Q7Z6E9-2] DR RefSeq; NP_116015.2; NM_032626.5. [Q7Z6E9-3] DR PDB; 2C7H; NMR; -; A=1-81. DR PDB; 2YSA; NMR; -; A=159-206. DR PDB; 2YUR; NMR; -; A=249-309. DR PDB; 3ZTG; NMR; -; A/B=249-335. DR PDB; 6E5X; X-ray; 1.50 A; B=554-568. DR PDBsum; 2C7H; -. DR PDBsum; 2YSA; -. DR PDBsum; 2YUR; -. DR PDBsum; 3ZTG; -. DR PDBsum; 6E5X; -. DR AlphaFoldDB; Q7Z6E9; -. DR BMRB; Q7Z6E9; -. DR EMDB; EMD-14185; -. DR SMR; Q7Z6E9; -. DR BioGRID; 111865; 242. DR DIP; DIP-46897N; -. DR IntAct; Q7Z6E9; 53. DR MINT; Q7Z6E9; -. DR STRING; 9606.ENSP00000317872; -. DR GlyCosmos; Q7Z6E9; 3 sites, 1 glycan. DR GlyGen; Q7Z6E9; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q7Z6E9; -. DR MetOSite; Q7Z6E9; -. DR PhosphoSitePlus; Q7Z6E9; -. DR BioMuta; RBBP6; -. DR DMDM; 74762440; -. DR EPD; Q7Z6E9; -. DR jPOST; Q7Z6E9; -. DR MassIVE; Q7Z6E9; -. DR MaxQB; Q7Z6E9; -. DR PaxDb; 9606-ENSP00000317872; -. DR PeptideAtlas; Q7Z6E9; -. DR ProteomicsDB; 69396; -. [Q7Z6E9-1] DR ProteomicsDB; 69397; -. [Q7Z6E9-2] DR ProteomicsDB; 69398; -. [Q7Z6E9-3] DR ProteomicsDB; 69399; -. [Q7Z6E9-4] DR Pumba; Q7Z6E9; -. DR Antibodypedia; 26070; 388 antibodies from 30 providers. DR DNASU; 5930; -. DR Ensembl; ENST00000319715.10; ENSP00000317872.4; ENSG00000122257.20. [Q7Z6E9-1] DR Ensembl; ENST00000348022.6; ENSP00000316291.4; ENSG00000122257.20. [Q7Z6E9-2] DR Ensembl; ENST00000381039.7; ENSP00000370427.3; ENSG00000122257.20. [Q7Z6E9-4] DR Ensembl; ENST00000452655.6; ENSP00000390537.2; ENSG00000122257.20. [Q7Z6E9-3] DR GeneID; 5930; -. DR KEGG; hsa:5930; -. DR MANE-Select; ENST00000319715.10; ENSP00000317872.4; NM_006910.5; NP_008841.2. DR UCSC; uc002dmg.4; human. [Q7Z6E9-1] DR AGR; HGNC:9889; -. DR DisGeNET; 5930; -. DR GeneCards; RBBP6; -. DR HGNC; HGNC:9889; RBBP6. DR HPA; ENSG00000122257; Tissue enhanced (bone). DR MIM; 600938; gene. DR neXtProt; NX_Q7Z6E9; -. DR OpenTargets; ENSG00000122257; -. DR PharmGKB; PA34253; -. DR VEuPathDB; HostDB:ENSG00000122257; -. DR eggNOG; KOG0314; Eukaryota. DR GeneTree; ENSGT00940000157561; -. DR HOGENOM; CLU_239162_0_0_1; -. DR InParanoid; Q7Z6E9; -. DR OMA; NPPWVAP; -. DR OrthoDB; 150979at2759; -. DR PhylomeDB; Q7Z6E9; -. DR TreeFam; TF350543; -. DR PathwayCommons; Q7Z6E9; -. DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q7Z6E9; -. DR SIGNOR; Q7Z6E9; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 5930; 802 hits in 1209 CRISPR screens. DR ChiTaRS; RBBP6; human. DR EvolutionaryTrace; Q7Z6E9; -. DR GeneWiki; RBBP6; -. DR GenomeRNAi; 5930; -. DR Pharos; Q7Z6E9; Tbio. DR PRO; PR:Q7Z6E9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q7Z6E9; Protein. DR Bgee; ENSG00000122257; Expressed in buccal mucosa cell and 203 other cell types or tissues. DR ExpressionAtlas; Q7Z6E9; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR GO; GO:0061053; P:somite development; IEA:Ensembl. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR CDD; cd16620; vRING-HC-C4C4_RBBP6; 1. DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR014891; DWNN_domain. DR InterPro; IPR003613; Ubox_domain. DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C. DR InterPro; IPR001878; Znf_CCHC. DR InterPro; IPR036875; Znf_CCHC_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR15439:SF29; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN 1-RELATED; 1. DR PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1. DR Pfam; PF08783; DWNN; 1. DR Pfam; PF04564; U-box; 1. DR Pfam; PF13696; zf-CCHC_2; 1. DR SMART; SM01180; DWNN; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00343; ZnF_C2HC; 1. DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51282; DWNN; 1. DR PROSITE; PS50158; ZF_CCHC; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q7Z6E9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromosome; Cytoplasm; KW Cytoskeleton; DNA damage; DNA replication; Host-virus interaction; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT CHAIN 1..1792 FT /note="E3 ubiquitin-protein ligase RBBP6" FT /id="PRO_0000234354" FT DOMAIN 4..76 FT /note="DWNN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00612" FT ZN_FING 159..176 FT /note="CCHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT ZN_FING 259..300 FT /note="RING-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 326..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..410 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..601 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 549..571 FT /note="(Microbial infection) Interaction with Ebolavirus FT VP30" FT /evidence="ECO:0000269|PubMed:30550789" FT REGION 621..640 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 645..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 847..1290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 982..1139 FT /note="Interaction with RB1" FT /evidence="ECO:0000250" FT REGION 1321..1348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1360..1665 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1433..1544 FT /note="Interaction with p53" FT /evidence="ECO:0000250" FT REGION 1682..1792 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 560..565 FT /note="PPxPxY" FT /evidence="ECO:0000269|PubMed:30550789" FT COMPBIAS 553..601 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 645..685 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 686..729 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 735..766 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..786 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 904..929 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 982..1029 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1036..1070 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1083..1165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1175..1217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1218..1233 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1234..1255 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1256..1279 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1361..1434 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1448..1579 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1597..1625 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1647..1665 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1683..1722 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1729..1750 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1774..1792 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P97868" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 768 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163" FT MOD_RES 772 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163" FT MOD_RES 780 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 815 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 861 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 873 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 957 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 984 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1221 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1271 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P97868" FT MOD_RES 1277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1341 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1347 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1468 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1646 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 1651 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97868" FT CROSSLNK 1106 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297" FT CROSSLNK 1169 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 102..117 FT /note="IDDSSASISLAQLTKT -> VCKNTISHFFYTLLLPL (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018281" FT VAR_SEQ 118..1792 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018282" FT VAR_SEQ 431..1270 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_018283" FT VAR_SEQ 652..685 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.5" FT /id="VSP_018284" FT VARIANT 43 FT /note="D -> H (in dbSNP:rs16973796)" FT /id="VAR_051306" FT VARIANT 555 FT /note="V -> A (in dbSNP:rs16973840)" FT /id="VAR_026216" FT VARIANT 1208 FT /note="K -> I (in dbSNP:rs3743968)" FT /id="VAR_051307" FT CONFLICT 223 FT /note="I -> T (in Ref. 5; AAL68925)" FT /evidence="ECO:0000305" FT CONFLICT 1633 FT /note="D -> H (in Ref. 5; AAL68925)" FT /evidence="ECO:0000305" FT STRAND 1..8 FT /evidence="ECO:0007829|PDB:2C7H" FT STRAND 12..25 FT /evidence="ECO:0007829|PDB:2C7H" FT HELIX 26..37 FT /evidence="ECO:0007829|PDB:2C7H" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:2C7H" FT STRAND 44..53 FT /evidence="ECO:0007829|PDB:2C7H" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:2C7H" FT STRAND 70..76 FT /evidence="ECO:0007829|PDB:2C7H" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:2YSA" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:2YSA" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:2YSA" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:2YSA" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:2YUR" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:2YUR" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:2YUR" FT HELIX 283..290 FT /evidence="ECO:0007829|PDB:2YUR" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:2YUR" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:2YUR" FT TURN 306..309 FT /evidence="ECO:0007829|PDB:2YUR" FT HELIX 313..326 FT /evidence="ECO:0007829|PDB:3ZTG" SQ SEQUENCE 1792 AA; 201564 MW; 550F7BBA5125DA06 CRC64; MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK AIDDSSASIS LAQLTKTANL AEANASEEDK IKAMMSQSGH EYDPINYMKK PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK NFESGPRIKK STGIPRSFMM EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP EEPSSSSEED DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI QRNLQPLMRS PISRQQDPLM IPVTSSSTHP APSISSLTSN QSSLAPPVSG NPSSAPAPVP DITATVSISV HSEKSDGPFR DSDNKILPAA ALASEHSKGT SSIAITALME EKGYQVPVLG TPSLLGQSLL HGQLIPTTGP VRINTARPGG GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE RSQRTQGPSL PATPVFVPVP PPPLYPPPPH TLPLPPGVPP PQFSPQFPPG QPPPAGYSVP PPGFPPAPAN LSTPWVSSGV QTAHSNTIPT TQAPPLSREE FYREQRRLKE EEKKKSKLDE FTNDFAKELM EYKKIQKERR RSFSRSKSPY SGSSYSRSSY TYSKSRSGST RSRSYSRSFS RSHSRSYSRS PPYPRRGRGK SRNYRSRSRS HGYHRSRSRS PPYRRYHSRS RSPQAFRGQS PNKRNVPQGE TEREYFNRYR EVPPPYDMKA YYGRSVDFRD PFEKERYREW ERKYREWYEK YYKGYAAGAQ PRPSANRENF SPERFLPLNI RNSPFTRGRR EDYVGGQSHR SRNIGSNYPE KLSARDGHNQ KDNTKSKEKE SENAPGDGKG NKHKKHRKRR KGEESEGFLN PELLETSRKS REPTGVEENK TDSLFVLPSR DDATPVRDEP MDAESITFKS VSEKDKRERD KPKAKGDKTK RKNDGSAVSK KENIVKPAKG PQEKVDGERE RSPRSEPPIK KAKEETPKTD NTKSSSSSQK DEKITGTPRK AHSKSAKEHQ ETKPVKEEKV KKDYSKDVKS EKLTTKEEKA KKPNEKNKPL DNKGEKRKRK TEEKGVDKDF ESSSMKISKL EVTEIVKPSP KRKMEPDTEK MDRTPEKDKI SLSAPAKKIK LNRETGKKIG STENISNTKE PSEKLESTSS KVKQEKVKGK VRRKVTGTEG SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN NDNTAPAEDV IIMIQVPQSK WDKDDFESEE EDVKSTQPIS SVGKPASVIK NVSTKPSNIV KYPEKESEPS EKIQKFTKDV SHEIIQHEVK SSKNSASSEK GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF KSLSQSSKEA RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD TKRPNEETKS VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK EQITGQIDKS TVKPKPQLSH SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEESSGN ISKDLKDKIV EKAKESLDTA AVVQVGISRN QSHSSPSVSP SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK HKKHKKHKKH AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV //