RBBP6_HUMAN
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 03-AUG-2022, entry version 176.
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; P46937: YAP1; NbExp=2; IntAct=EBI-2117026, EBI-1044059;
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 SMR; Q7Z6E9; -.
DR BioGRID; 111865; 208.
DR DIP; DIP-46897N; -.
DR IntAct; Q7Z6E9; 52.
DR MINT; Q7Z6E9; -.
DR STRING; 9606.ENSP00000317872; -.
DR GlyGen; Q7Z6E9; 3 sites, 1 O-linked glycan (3 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; Q7Z6E9; -.
DR PeptideAtlas; Q7Z6E9; -.
DR PRIDE; Q7Z6E9; -.
DR ProteomicsDB; 69396; -. [Q7Z6E9-1]
DR ProteomicsDB; 69397; -. [Q7Z6E9-2]
DR ProteomicsDB; 69398; -. [Q7Z6E9-3]
DR ProteomicsDB; 69399; -. [Q7Z6E9-4]
DR Antibodypedia; 26070; 364 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 CTD; 5930; -.
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; DYDNQHP; -.
DR OrthoDB; 81368at2759; -.
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 UniPathway; UPA00143; -.
DR BioGRID-ORCS; 5930; 771 hits in 1131 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 201 other tissues.
DR ExpressionAtlas; Q7Z6E9; baseline and differential.
DR Genevisible; Q7Z6E9; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:cellular response to DNA damage stimulus; 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:0006397; P:mRNA processing; IEA:InterPro.
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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR033489; RBBP6.
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; PTHR15439; 2.
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; SSF57756; 1.
DR PROSITE; PS51282; DWNN; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
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
