RBBP7_HUMAN
ID RBBP7_HUMAN Reviewed; 425 AA.
AC Q16576; Q5JP00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Histone-binding protein RBBP7;
DE AltName: Full=Histone acetyltransferase type B subunit 2;
DE AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE AltName: Full=Retinoblastoma-binding protein 7;
DE Short=RBBP-7;
DE AltName: Full=Retinoblastoma-binding protein p46;
GN Name=RBBP7; Synonyms=RBAP46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RB1.
RX PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
RA Qian Y.-W., Lee E.Y.-H.P.;
RT "Dual retinoblastoma-binding proteins with properties related to a negative
RT regulator of ras in yeast.";
RL J. Biol. Chem. 270:25507-25513(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=9150135; DOI=10.1016/s0092-8674(00)80216-0;
RA Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Histone deacetylases and SAP18, a novel polypeptide, are components of a
RT human Sin3 complex.";
RL Cell 89:357-364(1997).
RN [6]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=9790534; DOI=10.1016/s0092-8674(00)81758-4;
RA Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.;
RT "The dermatomyositis-specific autoantigen Mi2 is a component of a complex
RT containing histone deacetylase and nucleosome remodeling activities.";
RL Cell 95:279-289(1998).
RN [7]
RP INTERACTION WITH HAT1 AND HISTONE H4.
RX PubMed=9427644; DOI=10.1016/s0960-9822(98)70040-5;
RA Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
RT "Nucleosomal DNA regulates the core-histone-binding subunit of the human
RT Hat1 acetyltransferase.";
RL Curr. Biol. 8:96-108(1998).
RN [8]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=9651585; DOI=10.1016/s1097-2765(00)80102-1;
RA Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
RA Hampsey M., Reinberg D.;
RT "SAP30, a novel protein conserved between human and yeast, is a component
RT of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [9]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=10444591; DOI=10.1101/gad.13.15.1924;
RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.;
RT "Analysis of the NuRD subunits reveals a histone deacetylase core complex
RT and a connection with DNA methylation.";
RL Genes Dev. 13:1924-1935(1999).
RN [10]
RP INTERACTION WITH BRCA1 AND RB1.
RX PubMed=10220405; DOI=10.1073/pnas.96.9.4983;
RA Yarden R.I., Brody L.C.;
RT "BRCA1 interacts with components of the histone deacetylase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH CREBBP.
RX PubMed=10866654; DOI=10.1128/mcb.20.14.4970-4978.2000;
RA Zhang Q., Vo N., Goodman R.H.;
RT "Histone binding protein RbAp48 interacts with a complex of CREB binding
RT protein and phosphorylated CREB.";
RL Mol. Cell. Biol. 20:4970-4978(2000).
RN [12]
RP IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [13]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=11118440; DOI=10.1074/jbc.m007664200;
RA Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M.,
RA Hauser C.A., Gu W., Gudkov A.V., Qin J.;
RT "Differential association of products of alternative transcripts of the
RT candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional
RT corepressor complex.";
RL J. Biol. Chem. 276:8734-8739(2001).
RN [14]
RP IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND
RP SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12435631; DOI=10.1101/gad.1035902;
RA Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Histone methyltransferase activity associated with a human multiprotein
RT complex containing the Enhancer of Zeste protein.";
RL Genes Dev. 16:2893-2905(2002).
RN [15]
RP IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
RX PubMed=11784859; DOI=10.1128/mcb.22.3.835-848.2002;
RA Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Role of the Sin3-histone deacetylase complex in growth regulation by the
RT candidate tumor suppressor p33(ING1).";
RL Mol. Cell. Biol. 22:835-848(2002).
RN [16]
RP IDENTIFICATION IN THE NURF-1 COMPLEX, INTERACTION WITH SMARCA1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14609955; DOI=10.1093/emboj/cdg582;
RA Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
RA Shiekhattar R.;
RT "Isolation of human NURF: a regulator of Engrailed gene expression.";
RL EMBO J. 22:6089-6100(2003).
RN [17]
RP IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
RX PubMed=12920132; DOI=10.1074/jbc.m302955200;
RA Yao Y.-L., Yang W.-M.;
RT "The metastasis-associated proteins 1 and 2 form distinct protein complexes
RT with histone deacetylase activity.";
RL J. Biol. Chem. 278:42560-42568(2003).
RN [18]
RP IDENTIFICATION IN COMPLEXES WITH SMARCA1, AND INTERACTION WITH SMARCA1.
RX PubMed=15310751; DOI=10.1074/jbc.m406212200;
RA Barak O., Lazzaro M.A., Cooch N.S., Picketts D.J., Shiekhattar R.;
RT "A tissue-specific, naturally occurring human SNF2L variant inactivates
RT chromatin remodeling.";
RL J. Biol. Chem. 279:45130-45138(2004).
RN [19]
RP INTERACTION WITH MBD3L1.
RX PubMed=15456747; DOI=10.1074/jbc.m409149200;
RA Jiang C.-L., Jin S.-G., Pfeifer G.P.;
RT "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-
RT binding protein 2 (MBD2) and components of the NuRD complex.";
RL J. Biol. Chem. 279:52456-52464(2004).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
RP AT SER-13 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], 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 [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-10 AND SER-354, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-159, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [31]
RP INTERACTION WITH CENPA.
RX PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
RA Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S., Cui L.,
RA Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G., Zhang X.,
RA Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
RT "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-
RT dependent deposition at centromeres.";
RL Dev. Cell 32:68-81(2015).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-101; LYS-155 AND LYS-159,
RP AND IDENTIFICATION BY MASS 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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE H4,
RP AND DOMAINS WD REPEATS.
RX PubMed=18571423; DOI=10.1016/j.str.2008.05.006;
RA Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J.,
RA Pratap J.V., McLaughlin S.H., Ben-Shahar T.R., Verreault A., Luisi B.F.,
RA Laue E.D.;
RT "Structural basis for the recognition of histone H4 by the histone-
RT chaperone RbAp46.";
RL Structure 16:1077-1085(2008).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC remodeling factors, histone acetyltransferases and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of several complexes which regulate
CC chromatin metabolism. These include the type B histone
CC acetyltransferase (HAT) complex, which is required for chromatin
CC assembly following DNA replication; the core histone deacetylase (HDAC)
CC complex, which promotes histone deacetylation and consequent
CC transcriptional repression; the nucleosome remodeling and histone
CC deacetylase complex (the NuRD complex), which promotes transcriptional
CC repression by histone deacetylation and nucleosome remodeling; and the
CC PRC2/EED-EZH2 complex, which promotes repression of homeotic genes
CC during development; and the NURF (nucleosome remodeling factor)
CC complex. {ECO:0000269|PubMed:10866654}.
CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a
CC region that is not accessible when H4 is in chromatin
CC (PubMed:18571423). Subunit of the type B histone acetyltransferase
CC (HAT) complex, composed of RBBP7 and HAT1. Subunit of the core histone
CC deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4
CC and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180,
CC SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to
CC form the SIN3 HDAC complex. The core HDAC complex may also associate
CC with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and
CC histone deacetylase complex (the NuRD complex). The NuRD complex may
CC also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of
CC the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2,
CC RBBP4, RBBP7 and SUZ12 (PubMed:12435631). The PRC2/EED-EZH2 complex may
CC also associate with HDAC1. Component of the NURF-1 ISWI chromatin
CC remodeling complex (also called the nucleosome-remodeling factor (NURF)
CC complex) at least composed of SMARCA1 (isoform 2), BPTF, RBBP4 and
CC RBBP7 (PubMed:14609955, PubMed:15310751). Within the complex interacts
CC with isoform 2 of SMARCA1 (PubMed:14609955, PubMed:15310751). Component
CC of the BPFT-SMARCA1 complex at least composed of SMARCA1 (isoform 1),
CC BPFT, RBBP4 and RBBP7; the complex is catalytically inactive and does
CC not remodel chromatin (PubMed:15310751). Within the complex interacts
CC with isoform 1 of SMARCA1 (PubMed:15310751). Interacts with the viral
CC protein-binding domain of the retinoblastoma protein (RB1)
CC (PubMed:7503932, PubMed:10220405). Interacts with CREBBP, and this
CC interaction may be enhanced by the binding of phosphorylated CREB1 to
CC CREBBP. Interacts with BRCA1, HDAC7 and SUV39H1. Interacts with CENPA
CC (PubMed:25556658). Interacts with PWWP2B (By similarity).
CC {ECO:0000250|UniProtKB:Q60973, ECO:0000269|PubMed:10220405,
CC ECO:0000269|PubMed:10444591, ECO:0000269|PubMed:10866654,
CC ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11118440,
CC ECO:0000269|PubMed:11784859, ECO:0000269|PubMed:12435631,
CC ECO:0000269|PubMed:12920132, ECO:0000269|PubMed:14609955,
CC ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15456747,
CC ECO:0000269|PubMed:18571423, ECO:0000269|PubMed:25556658,
CC ECO:0000269|PubMed:7503932, ECO:0000269|PubMed:9150135,
CC ECO:0000269|PubMed:9427644, ECO:0000269|PubMed:9651585,
CC ECO:0000269|PubMed:9790534}.
CC -!- INTERACTION:
CC Q16576; P62805: H4C9; NbExp=9; IntAct=EBI-352227, EBI-302023;
CC Q16576; Q13547: HDAC1; NbExp=7; IntAct=EBI-352227, EBI-301834;
CC Q16576; O94776: MTA2; NbExp=11; IntAct=EBI-352227, EBI-1783035;
CC Q16576; Q17R98: ZNF827; NbExp=2; IntAct=EBI-352227, EBI-5564776;
CC Q16576; P62799; Xeno; NbExp=2; IntAct=EBI-352227, EBI-302085;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16576-2; Sequence=VSP_043016;
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBBP7ID42065chXp22.html";
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DR EMBL; U35143; AAC50231.1; -; mRNA.
DR EMBL; X72841; CAA51360.1; -; mRNA.
DR EMBL; AK091911; BAG52439.1; -; mRNA.
DR EMBL; AL929302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14179.1; -. [Q16576-1]
DR CCDS; CCDS56598.1; -. [Q16576-2]
DR PIR; I39181; I39181.
DR RefSeq; NP_001185648.1; NM_001198719.1. [Q16576-2]
DR RefSeq; NP_002884.1; NM_002893.3. [Q16576-1]
DR PDB; 3CFS; X-ray; 2.40 A; B=1-411.
DR PDB; 3CFV; X-ray; 2.60 A; A/B=1-411.
DR PDB; 7M3X; X-ray; 1.46 A; A=6-411.
DR PDBsum; 3CFS; -.
DR PDBsum; 3CFV; -.
DR PDBsum; 7M3X; -.
DR AlphaFoldDB; Q16576; -.
DR SMR; Q16576; -.
DR BioGRID; 111866; 294.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-688; NuRF chromatin remodeling complex.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q16576; -.
DR DIP; DIP-436N; -.
DR IntAct; Q16576; 145.
DR MINT; Q16576; -.
DR STRING; 9606.ENSP00000369424; -.
DR ChEMBL; CHEMBL3301388; -.
DR GlyGen; Q16576; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16576; -.
DR MetOSite; Q16576; -.
DR PhosphoSitePlus; Q16576; -.
DR SwissPalm; Q16576; -.
DR BioMuta; RBBP7; -.
DR DMDM; 2494891; -.
DR EPD; Q16576; -.
DR jPOST; Q16576; -.
DR MassIVE; Q16576; -.
DR PaxDb; Q16576; -.
DR PeptideAtlas; Q16576; -.
DR PRIDE; Q16576; -.
DR ProteomicsDB; 60926; -. [Q16576-1]
DR ProteomicsDB; 60927; -. [Q16576-2]
DR Antibodypedia; 24054; 396 antibodies from 31 providers.
DR DNASU; 5931; -.
DR Ensembl; ENST00000380084.8; ENSP00000369424.4; ENSG00000102054.18. [Q16576-2]
DR Ensembl; ENST00000380087.7; ENSP00000369427.3; ENSG00000102054.18. [Q16576-1]
DR GeneID; 5931; -.
DR KEGG; hsa:5931; -.
DR MANE-Select; ENST00000380087.7; ENSP00000369427.3; NM_002893.4; NP_002884.1.
DR UCSC; uc004cxs.3; human. [Q16576-1]
DR CTD; 5931; -.
DR DisGeNET; 5931; -.
DR GeneCards; RBBP7; -.
DR HGNC; HGNC:9890; RBBP7.
DR HPA; ENSG00000102054; Low tissue specificity.
DR MIM; 300825; gene.
DR neXtProt; NX_Q16576; -.
DR OpenTargets; ENSG00000102054; -.
DR PharmGKB; PA34254; -.
DR VEuPathDB; HostDB:ENSG00000102054; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000154748; -.
DR InParanoid; Q16576; -.
DR OMA; PITDFNW; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q16576; -.
DR TreeFam; TF106485; -.
DR PathwayCommons; Q16576; -.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; Q16576; -.
DR SIGNOR; Q16576; -.
DR BioGRID-ORCS; 5931; 36 hits in 709 CRISPR screens.
DR ChiTaRS; RBBP7; human.
DR EvolutionaryTrace; Q16576; -.
DR GeneWiki; RBBP7; -.
DR GenomeRNAi; 5931; -.
DR Pharos; Q16576; Tbio.
DR PRO; PR:Q16576; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16576; protein.
DR Bgee; ENSG00000102054; Expressed in oocyte and 203 other tissues.
DR ExpressionAtlas; Q16576; baseline and differential.
DR Genevisible; Q16576; HS.
DR GO; GO:1904949; C:ATPase complex; IDA:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0016589; C:NURF complex; IPI:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IC:ComplexPortal.
DR GO; GO:0070370; P:cellular heat acclimation; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR DisProt; DP01282; -.
DR Gene3D; 2.130.10.10; -; 1.
DR IDEAL; IID00084; -.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Chromatin regulator; Direct protein sequencing; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT CHAIN 2..425
FT /note="Histone-binding protein RBBP7"
FT /id="PRO_0000051195"
FT REPEAT 47..122
FT /note="WD 1"
FT REPEAT 128..173
FT /note="WD 2"
FT REPEAT 181..217
FT /note="WD 3"
FT REPEAT 228..269
FT /note="WD 4"
FT REPEAT 275..312
FT /note="WD 5"
FT REPEAT 318..369
FT /note="WD 6"
FT REPEAT 376..403
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60973"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60973"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..6
FT /note="MASKEM -> MAAEAGVVGAGASPDGDWRDQACGLLLHVHLSSRLGRAAPVR
FT TGRHLRTV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043016"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:7M3X"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:7M3X"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3CFV"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:7M3X"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:7M3X"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:7M3X"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:7M3X"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:7M3X"
FT INIT_MET Q16576-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q16576-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q16576-2:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 425 AA; 47820 MW; 1A4B4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL
EGQGS
