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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};
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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
 
 
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