GenomeNet

Database: UniProt
Entry: Q06330
LinkDB: Q06330
Original site: Q06330 
ID   SUH_HUMAN               Reviewed;         500 AA.
AC   Q06330; B4DY22; Q5XKH9; Q6P1N3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 3.
DT   17-JUN-2020, entry version 199.
DE   RecName: Full=Recombining binding protein suppressor of hairless;
DE   AltName: Full=CBF-1;
DE   AltName: Full=J kappa-recombination signal-binding protein;
DE   AltName: Full=RBP-J kappa;
DE            Short=RBP-J;
DE            Short=RBP-JK;
DE   AltName: Full=Renal carcinoma antigen NY-REN-30;
GN   Name=RBPJ {ECO:0000312|HGNC:HGNC:5724};
GN   Synonyms=IGKJRB, IGKJRB1, RBPJK, RBPSUH;
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 APCR-1; APCR-2 AND APCR-3), AND
RP   VARIANT VAL-456.
RC   TISSUE=Placenta;
RX   PubMed=8406481; DOI=10.1006/geno.1993.1326;
RA   Amakawa R., Jing W., Ozawa K., Matsunami N., Hamaguchi Y., Matsuda F.,
RA   Kawaichi M., Honjo T.;
RT   "Human Jk recombination signal binding protein gene (IGKJRB): comparison
RT   with its mouse homologue.";
RL   Genomics 17:306-315(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC   TISSUE=Eye;
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   [5]
RP   INTERACTION WITH EBV EBNA2.
RX   PubMed=8016657; DOI=10.1126/science.8016657;
RA   Henkel T., Ling P.D., Hayward S.D., Peterson M.G.;
RT   "Mediation of Epstein-Barr virus EBNA2 transactivation by recombination
RT   signal-binding protein J kappa.";
RL   Science 265:92-95(1994).
RN   [6]
RP   INTERACTION WITH EBV EBNA3; EBV EBNA4 AND EBV EBNA6.
RX   PubMed=8627785;
RA   Robertson E.S., Lin J., Kieff E.;
RT   "The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B,
RT   and 3C interact with RBPJ(kappa).";
RL   J. Virol. 70:3068-3074(1996).
RN   [7]
RP   IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-cell
RT   carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [8]
RP   INTERACTION WITH CIR1, AND SUBCELLULAR LOCATION.
RX   PubMed=9874765; DOI=10.1073/pnas.96.1.23;
RA   Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.;
RT   "CIR, a corepressor linking the DNA binding factor CBF1 to the histone
RT   deacetylase complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999).
RN   [9]
RP   INTERACTION WITH SNW1.
RX   PubMed=10644367; DOI=10.1128/jvi.74.4.1939-1947.2000;
RA   Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
RT   "A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
RL   J. Virol. 74:1939-1947(2000).
RN   [10]
RP   INTERACTION WITH NOTCH1.
RX   PubMed=10637481; DOI=10.1038/sj.leu.2401630;
RA   Callahan J., Aster J., Sklar J., Kieff E., Robertson E.S.;
RT   "Intracellular forms of human NOTCH1 interact at distinctly different
RT   levels with RBP-jkappa in human B and T cells.";
RL   Leukemia 14:84-92(2000).
RN   [11]
RP   INTERACTION WITH MINT.
RX   PubMed=12374742; DOI=10.1093/emboj/cdf549;
RA   Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K.,
RA   Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S.,
RA   Schmid R.M.;
RT   "SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway.";
RL   EMBO J. 21:5417-5426(2002).
RN   [12]
RP   INTERACTION WITH C12ORF52, AND SUBCELLULAR LOCATION.
RX   PubMed=21102556; DOI=10.1038/emboj.2010.289;
RA   Wacker S.A., Alvarado C., von Wichert G., Knippschild U., Wiedenmann J.,
RA   Clauss K., Nienhaus G.U., Hameister H., Baumann B., Borggrefe T.,
RA   Knochel W., Oswald F.;
RT   "RITA, a novel modulator of Notch signalling, acts via nuclear export of
RT   RBP-J.";
RL   EMBO J. 30:43-56(2011).
RN   [13]
RP   FUNCTION, AND METHYLATED DNA-BINDING.
RX   PubMed=21991380; DOI=10.1371/journal.pone.0025884;
RA   Bartels S.J., Spruijt C.G., Brinkman A.B., Jansen P.W., Vermeulen M.,
RA   Stunnenberg H.G.;
RT   "A SILAC-based screen for Methyl-CpG binding proteins identifies RBP-J as a
RT   DNA methylation and sequence-specific binding protein.";
RL   PLoS ONE 6:E25884-E25884(2011).
RN   [14]
RP   INTERACTION WITH BEND6.
RX   PubMed=23571214; DOI=10.1242/dev.087502;
RA   Dai Q., Andreu-Agullo C., Insolera R., Wong L.C., Shi S.H., Lai E.C.;
RT   "BEND6 is a nuclear antagonist of Notch signaling during self-renewal of
RT   neural stem cells.";
RL   Development 140:1892-1902(2013).
RN   [15]
RP   FUNCTION IN COX4I2 TRANSCRIPTION, AND INTERACTION WITH CHCHD2 AND CXXC5.
RX   PubMed=23303788; DOI=10.1093/nar/gks1454;
RA   Aras S., Pak O., Sommer N., Finley R. Jr., Huttemann M., Weissmann N.,
RA   Grossman L.I.;
RT   "Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene
RT   expression is mediated by transcription factors RBPJ, CXXC5 and CHCHD2.";
RL   Nucleic Acids Res. 41:2255-2266(2013).
RN   [16]
RP   INTERACTION WITH ZMIZ1.
RX   PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
RA   Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y., Alarcon A.S.,
RA   Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S., Maillard I.,
RA   Samuelson L.C., Cierpicki T., Chiang M.Y.;
RT   "The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
RT   Notch1 in T cell development and leukemia.";
RL   Immunity 43:870-883(2015).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA; MAML1
RP   AND NOTCH1.
RX   PubMed=16530044; DOI=10.1016/j.cell.2005.12.037;
RA   Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.;
RT   "Structural basis for cooperativity in recruitment of MAML coactivators to
RT   Notch transcription complexes.";
RL   Cell 124:973-983(2006).
RN   [18]
RP   VARIANTS AOS3 GLY-63 AND GLU-169, AND CHARACTERIZATION OF VARIANTS AOS3
RP   GLY-63 AND GLU-169.
RX   PubMed=22883147; DOI=10.1016/j.ajhg.2012.07.005;
RA   Hassed S.J., Wiley G.B., Wang S., Lee J.Y., Li S., Xu W., Zhao Z.J.,
RA   Mulvihill J.J., Robertson J., Warner J., Gaffney P.M.;
RT   "RBPJ mutations identified in two families affected by Adams-Oliver
RT   syndrome.";
RL   Am. J. Hum. Genet. 91:391-395(2012).
CC   -!- FUNCTION: Transcriptional regulator that plays a central role in Notch
CC       signaling, a signaling pathway involved in cell-cell communication that
CC       regulates a broad spectrum of cell-fate determinations. Acts as a
CC       transcriptional repressor when it is not associated with Notch
CC       proteins. When associated with some NICD product of Notch proteins
CC       (Notch intracellular domain), it acts as a transcriptional activator
CC       that activates transcription of Notch target genes. Probably represses
CC       or activates transcription via the recruitment of chromatin remodeling
CC       complexes containing histone deacetylase or histone acetylase proteins,
CC       respectively. Specifically binds to the immunoglobulin kappa-type J
CC       segment recombination signal sequence. Binds specifically to methylated
CC       DNA (PubMed:21991380). Binds to the oxygen responsive element of COX4I2
CC       and activates its transcription under hypoxia conditions (4% oxygen)
CC       (PubMed:23303788). Negatively regulates the phagocyte oxidative burst
CC       in response to bacterial infection by repressing transcription of NADPH
CC       oxidase subunits (By similarity). {ECO:0000250|UniProtKB:P31266,
CC       ECO:0000269|PubMed:21991380, ECO:0000269|PubMed:23303788}.
CC   -!- SUBUNIT: Interacts with activated NOTCH1, NOTCH2 or NOTCH3. Interacts
CC       with MINT/SHARP. This interaction may mediate the recruitment of large
CC       corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2,
CC       SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A.
CC       Interacts with Epstein-Barr virus EBNA2, EBNA3, EBNA4 and EBNA6.
CC       Interacts with RITA1/C12orf52, leading to nuclear export, prevent the
CC       interaction between RBPJ and NICD product and subsequent down-
CC       regulation of the Notch signaling pathway. Interacts with SNW1.
CC       Interacts with CHCHD2 and CXXC5 (PubMed:23303788). Interacts with BEND6
CC       (via BEN domain). Interacts with NKAPL (By similarity). Interacts with
CC       ZMIZ1. Interacts with RBM15 (By similarity).
CC       {ECO:0000250|UniProtKB:P31266, ECO:0000269|PubMed:10637481,
CC       ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:12374742,
CC       ECO:0000269|PubMed:16530044, ECO:0000269|PubMed:21102556,
CC       ECO:0000269|PubMed:23303788, ECO:0000269|PubMed:23571214,
CC       ECO:0000269|PubMed:26522984, ECO:0000269|PubMed:8016657,
CC       ECO:0000269|PubMed:8627785, ECO:0000269|PubMed:9874765}.
CC   -!- INTERACTION:
CC       Q06330; P54253: ATXN1; NbExp=7; IntAct=EBI-632552, EBI-930964;
CC       Q06330; P0C7T5: ATXN1L; NbExp=7; IntAct=EBI-632552, EBI-8624731;
CC       Q06330; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-632552, EBI-2506081;
CC       Q06330; O60341: KDM1A; NbExp=4; IntAct=EBI-632552, EBI-710124;
CC       Q06330; Q9Y618: NCOR2; NbExp=3; IntAct=EBI-632552, EBI-80830;
CC       Q06330; P46531: NOTCH1; NbExp=12; IntAct=EBI-632552, EBI-636374;
CC       Q06330; Q9UPP1: PHF8; NbExp=2; IntAct=EBI-632552, EBI-1560800;
CC       Q06330; Q96K30: RITA1; NbExp=10; IntAct=EBI-632552, EBI-2836148;
CC       Q06330; P51532: SMARCA4; NbExp=2; IntAct=EBI-632552, EBI-302489;
CC       Q06330; Q13573: SNW1; NbExp=2; IntAct=EBI-632552, EBI-632715;
CC       Q06330; Q96T58: SPEN; NbExp=2; IntAct=EBI-632552, EBI-765739;
CC       Q06330; P04637: TP53; NbExp=5; IntAct=EBI-632552, EBI-366083;
CC       Q06330; P12978: EBNA2; Xeno; NbExp=2; IntAct=EBI-632552, EBI-8052923;
CC       Q06330; P12977: EBNA3; Xeno; NbExp=4; IntAct=EBI-632552, EBI-993115;
CC       Q06330; P03203: EBNA4; Xeno; NbExp=4; IntAct=EBI-632552, EBI-9346250;
CC       Q06330; P03204: EBNA6; Xeno; NbExp=3; IntAct=EBI-632552, EBI-9255985;
CC       Q06330; Q01705: Notch1; Xeno; NbExp=3; IntAct=EBI-632552, EBI-1392707;
CC       Q06330; P0CJ62: rita1; Xeno; NbExp=2; IntAct=EBI-632552, EBI-8517225;
CC       Q06330-6; P46531: NOTCH1; NbExp=6; IntAct=EBI-12599287, EBI-636374;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear, upon
CC       interaction with RITA/C12orf52, translocates to the cytoplasm, down-
CC       regulating the Notch signaling pathway.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=APCR-2;
CC         IsoId=Q06330-1; Sequence=Displayed;
CC       Name=APCR-1;
CC         IsoId=Q06330-2; Sequence=VSP_002717;
CC       Name=APCR-3;
CC         IsoId=Q06330-3; Sequence=VSP_002718, VSP_002719;
CC       Name=4;
CC         IsoId=Q06330-4; Sequence=VSP_021573;
CC       Name=5;
CC         IsoId=Q06330-5; Sequence=VSP_021572;
CC       Name=6;
CC         IsoId=Q06330-6; Sequence=VSP_021574;
CC       Name=7;
CC         IsoId=Q06330-7; Sequence=VSP_042637;
CC   -!- DISEASE: Adams-Oliver syndrome 3 (AOS3) [MIM:614814]: An autosomal
CC       dominant form of Adams-Oliver syndrome, a disorder characterized by the
CC       congenital absence of skin (aplasia cutis congenita) in combination
CC       with transverse limb defects. Aplasia cutis congenita can be located
CC       anywhere on the body, but in the vast majority of the cases, it is
CC       present on the posterior parietal region where it is often associated
CC       with an underlying defect of the parietal bones. Limb abnormalities are
CC       typically limb truncation defects affecting the distal phalanges or
CC       entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals
CC       or more proximal limb structures are also affected. Apart from
CC       transverse limb defects, syndactyly, most commonly of second and third
CC       toes, can also be observed. The clinical features are highly variable
CC       and can also include cardiovascular malformations, brain abnormalities
CC       and vascular defects such as cutis marmorata and dilated scalp veins.
CC       AOS3 patients manifest characteristic vertex scalp defects and terminal
CC       limb defects, but without congenital heart defects, other associated
CC       defects, or immune defects. {ECO:0000269|PubMed:22883147}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
CC   -!- CAUTION: Despite some similarity with the 'phage' integrase family, it
CC       has no recombinase activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA16254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; L07872; AAA60258.1; -; mRNA.
DR   EMBL; L07874; AAA16253.1; -; mRNA.
DR   EMBL; L07875; AAA16254.1; ALT_INIT; mRNA.
DR   EMBL; L07876; AAA16356.1; -; mRNA.
DR   EMBL; AK302230; BAG63584.1; -; mRNA.
DR   EMBL; AC093637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC097109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC097714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020780; AAH20780.1; -; mRNA.
DR   EMBL; BC053531; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC064976; AAH64976.1; -; mRNA.
DR   CCDS; CCDS33969.1; -. [Q06330-6]
DR   CCDS; CCDS3436.1; -. [Q06330-4]
DR   CCDS; CCDS3437.1; -. [Q06330-1]
DR   CCDS; CCDS43219.1; -. [Q06330-7]
DR   CCDS; CCDS87214.1; -. [Q06330-5]
DR   PIR; A47214; A47214.
DR   RefSeq; NP_005340.2; NM_005349.3. [Q06330-1]
DR   RefSeq; NP_056958.3; NM_015874.4. [Q06330-7]
DR   RefSeq; NP_976028.1; NM_203283.2. [Q06330-4]
DR   RefSeq; NP_976029.1; NM_203284.2. [Q06330-6]
DR   RefSeq; XP_005248218.1; XM_005248161.3.
DR   RefSeq; XP_011512142.1; XM_011513840.2. [Q06330-6]
DR   RefSeq; XP_016863661.1; XM_017008172.1.
DR   RefSeq; XP_016863662.1; XM_017008173.1.
DR   RefSeq; XP_016863663.1; XM_017008174.1. [Q06330-6]
DR   RefSeq; XP_016863664.1; XM_017008175.1. [Q06330-6]
DR   PDB; 2F8X; X-ray; 3.25 A; C=23-449.
DR   PDB; 3NBN; X-ray; 3.45 A; A/D=23-448.
DR   PDB; 3V79; X-ray; 3.85 A; C=23-449.
DR   PDB; 6PY8; X-ray; 3.75 A; C/E=23-466.
DR   PDBsum; 2F8X; -.
DR   PDBsum; 3NBN; -.
DR   PDBsum; 3V79; -.
DR   PDBsum; 6PY8; -.
DR   SMR; Q06330; -.
DR   BioGRID; 109736; 139.
DR   CORUM; Q06330; -.
DR   DIP; DIP-33326N; -.
DR   ELM; Q06330; -.
DR   IntAct; Q06330; 120.
DR   MINT; Q06330; -.
DR   STRING; 9606.ENSP00000345206; -.
DR   BindingDB; Q06330; -.
DR   ChEMBL; CHEMBL4105709; -.
DR   iPTMnet; Q06330; -.
DR   PhosphoSitePlus; Q06330; -.
DR   BioMuta; RBPJ; -.
DR   DMDM; 338817983; -.
DR   EPD; Q06330; -.
DR   jPOST; Q06330; -.
DR   MassIVE; Q06330; -.
DR   MaxQB; Q06330; -.
DR   PaxDb; Q06330; -.
DR   PeptideAtlas; Q06330; -.
DR   PRIDE; Q06330; -.
DR   ProteomicsDB; 58432; -. [Q06330-1]
DR   ProteomicsDB; 58433; -. [Q06330-2]
DR   ProteomicsDB; 58434; -. [Q06330-3]
DR   ProteomicsDB; 58435; -. [Q06330-4]
DR   ProteomicsDB; 58436; -. [Q06330-5]
DR   ProteomicsDB; 58437; -. [Q06330-6]
DR   ProteomicsDB; 58438; -. [Q06330-7]
DR   TopDownProteomics; Q06330-3; -. [Q06330-3]
DR   Antibodypedia; 10265; 349 antibodies.
DR   DNASU; 3516; -.
DR   Ensembl; ENST00000342295; ENSP00000345206; ENSG00000168214. [Q06330-1]
DR   Ensembl; ENST00000342320; ENSP00000340124; ENSG00000168214. [Q06330-6]
DR   Ensembl; ENST00000345843; ENSP00000305815; ENSG00000168214. [Q06330-4]
DR   Ensembl; ENST00000348160; ENSP00000339699; ENSG00000168214. [Q06330-7]
DR   Ensembl; ENST00000355476; ENSP00000347659; ENSG00000168214. [Q06330-6]
DR   Ensembl; ENST00000361572; ENSP00000354528; ENSG00000168214. [Q06330-1]
DR   Ensembl; ENST00000507561; ENSP00000423907; ENSG00000168214. [Q06330-5]
DR   GeneID; 3516; -.
DR   KEGG; hsa:3516; -.
DR   UCSC; uc003grx.3; human. [Q06330-1]
DR   CTD; 3516; -.
DR   DisGeNET; 3516; -.
DR   EuPathDB; HostDB:ENSG00000168214.20; -.
DR   GeneCards; RBPJ; -.
DR   GeneReviews; RBPJ; -.
DR   HGNC; HGNC:5724; RBPJ.
DR   HPA; ENSG00000168214; Low tissue specificity.
DR   MalaCards; RBPJ; -.
DR   MIM; 147183; gene.
DR   MIM; 614814; phenotype.
DR   neXtProt; NX_Q06330; -.
DR   OpenTargets; ENSG00000168214; -.
DR   Orphanet; 974; Adams-Oliver syndrome.
DR   PharmGKB; PA34292; -.
DR   eggNOG; KOG3743; Eukaryota.
DR   eggNOG; ENOG410XV7K; LUCA.
DR   GeneTree; ENSGT00390000005197; -.
DR   HOGENOM; CLU_022207_2_1_1; -.
DR   InParanoid; Q06330; -.
DR   KO; K06053; -.
DR   OMA; DMPHFGL; -.
DR   OrthoDB; 444988at2759; -.
DR   PhylomeDB; Q06330; -.
DR   TreeFam; TF314117; -.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR   Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR   Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR   SignaLink; Q06330; -.
DR   SIGNOR; Q06330; -.
DR   BioGRID-ORCS; 3516; 14 hits in 791 CRISPR screens.
DR   ChiTaRS; RBPJ; human.
DR   EvolutionaryTrace; Q06330; -.
DR   GeneWiki; RBPJ; -.
DR   GenomeRNAi; 3516; -.
DR   Pharos; Q06330; Tbio.
DR   PRO; PR:Q06330; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q06330; protein.
DR   Bgee; ENSG00000168214; Expressed in corpus callosum and 241 other tissues.
DR   ExpressionAtlas; Q06330; baseline and differential.
DR   Genevisible; Q06330; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:CAFA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:CAFA.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:CAFA.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL.
DR   GO; GO:0003176; P:aortic valve development; IEA:Ensembl.
DR   GO; GO:0060844; P:arterial endothelial cell fate commitment; IEA:Ensembl.
DR   GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:0097101; P:blood vessel endothelial cell fate specification; ISS:BHF-UCL.
DR   GO; GO:0072554; P:blood vessel lumenization; ISS:BHF-UCL.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060486; P:club cell differentiation; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0009957; P:epidermal cell fate specification; IEA:Ensembl.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
DR   GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
DR   GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
DR   GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; ISS:BHF-UCL.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IC:BHF-UCL.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:BHF-UCL.
DR   GO; GO:1901297; P:positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; IEA:Ensembl.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR   GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
DR   GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:1901186; P:positive regulation of ERBB signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:UniProtKB.
DR   GO; GO:0003177; P:pulmonary valve development; IEA:Ensembl.
DR   GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
DR   GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
DR   GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
DR   CDD; cd01176; IPT_RBP-Jkappa; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1450; -; 1.
DR   IDEAL; IID00380; -.
DR   InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR   InterPro; IPR036358; BTD_sf.
DR   InterPro; IPR040159; CLS_fam.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR   InterPro; IPR037095; RBP-J/Cbf11/Cbf12_DNA-bd_sf.
DR   InterPro; IPR038007; RBP-Jkappa_IPT.
DR   PANTHER; PTHR10665; PTHR10665; 1.
DR   Pfam; PF09270; BTD; 1.
DR   Pfam; PF09271; LAG1-DNAbind; 1.
DR   SMART; SM01268; BTD; 1.
DR   SMART; SM01267; LAG1_DNAbind; 1.
DR   SUPFAM; SSF110217; SSF110217; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW   Disease mutation; DNA-binding; Notch signaling pathway; Nucleus;
KW   Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..500
FT                   /note="Recombining binding protein suppressor of hairless"
FT                   /id="PRO_0000208567"
FT   DOMAIN          355..445
FT                   /note="IPT/TIG"
FT   DNA_BIND        58..65
FT   DNA_BIND        192..201
FT   DNA_BIND        265..297
FT   MOD_RES         175
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P31266"
FT   VAR_SEQ         1..89
FT                   /note="Missing (in isoform APCR-3)"
FT                   /evidence="ECO:0000303|PubMed:8406481"
FT                   /id="VSP_002718"
FT   VAR_SEQ         1..75
FT                   /note="Missing (in isoform APCR-1)"
FT                   /evidence="ECO:0000303|PubMed:8406481"
FT                   /id="VSP_002717"
FT   VAR_SEQ         1..35
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021572"
FT   VAR_SEQ         1..20
FT                   /note="MDHTEGSPAEEPPAHAPSPG -> MGGCR (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021573"
FT   VAR_SEQ         1..20
FT                   /note="MDHTEGSPAEEPPAHAPSPG -> MAWIKR (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021574"
FT   VAR_SEQ         1..19
FT                   /note="MDHTEGSPAEEPPAHAPSP -> MAPVVT (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042637"
FT   VAR_SEQ         90..95
FT                   /note="DGCSEQ -> MAWIKR (in isoform APCR-3)"
FT                   /evidence="ECO:0000303|PubMed:8406481"
FT                   /id="VSP_002719"
FT   VARIANT         63
FT                   /note="E -> G (in AOS3; shows decreased binding to the HES1
FT                   promoter compared to wild-type; dbSNP:rs387907270)"
FT                   /evidence="ECO:0000269|PubMed:22883147"
FT                   /id="VAR_068929"
FT   VARIANT         169
FT                   /note="K -> E (in AOS3; shows decreased binding to the HES1
FT                   promoter compared to wild-type; dbSNP:rs387907271)"
FT                   /evidence="ECO:0000269|PubMed:22883147"
FT                   /id="VAR_068930"
FT   VARIANT         291
FT                   /note="K -> E (in dbSNP:rs1064372)"
FT                   /id="VAR_028994"
FT   VARIANT         334
FT                   /note="D -> H (in dbSNP:rs1064376)"
FT                   /id="VAR_028995"
FT   VARIANT         408
FT                   /note="I -> V (in dbSNP:rs1064381)"
FT                   /id="VAR_057244"
FT   VARIANT         419
FT                   /note="R -> Q (in dbSNP:rs1064384)"
FT                   /id="VAR_028996"
FT   VARIANT         425
FT                   /note="P -> S (in dbSNP:rs1064387)"
FT                   /id="VAR_028997"
FT   VARIANT         456
FT                   /note="A -> V (in dbSNP:rs1064402)"
FT                   /evidence="ECO:0000269|PubMed:8406481"
FT                   /id="VAR_028998"
FT   CONFLICT        7
FT                   /note="S -> L (in Ref. 1; AAA60258/AAA16253/AAA16254)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140..141
FT                   /note="ML -> IF (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="G -> V (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="V -> C (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="R -> M (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="Q -> H (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="R -> P (in Ref. 1; AAA60258)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..41
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          50..57
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          72..74
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   HELIX           79..88
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   TURN            89..91
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   TURN            94..96
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          102..105
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          118..121
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   STRAND          137..139
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          141..146
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          152..157
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          161..166
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          174..176
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          178..180
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          185..191
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   HELIX           193..195
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   TURN            197..199
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          204..206
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          209..211
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          220..225
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          231..234
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          246..255
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          262..268
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          271..275
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          284..289
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          291..295
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          297..299
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   STRAND          302..306
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          319..321
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          328..336
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          343..345
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   STRAND          356..362
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   HELIX           366..368
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          370..377
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          382..386
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          389..391
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          393..397
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          400..404
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   HELIX           408..411
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          412..414
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          426..430
FT                   /evidence="ECO:0000244|PDB:2F8X"
FT   STRAND          431..433
FT                   /evidence="ECO:0000244|PDB:3NBN"
FT   STRAND          435..437
FT                   /evidence="ECO:0000244|PDB:2F8X"
SQ   SEQUENCE   500 AA;  55637 MW;  91E50D2DE9087EDA CRC64;
     MDHTEGSPAE EPPAHAPSPG KFGERPPPKR LTREAMRNYL KERGDQTVLI LHAKVAQKSY
     GNEKRFFCPP PCVYLMGSGW KKKKEQMERD GCSEQESQPC AFIGIGNSDQ EMQQLNLEGK
     NYCTAKTLYI SDSDKRKHFM LSVKMFYGNS DDIGVFLSKR IKVISKPSKK KQSLKNADLC
     IASGTKVALF NRLRSQTVST RYLHVEGGNF HASSQQWGAF FIHLLDDDES EGEEFTVRDG
     YIHYGQTVKL VCSVTGMALP RLIIRKVDKQ TALLDADDPV SQLHKCAFYL KDTERMYLCL
     SQERIIQFQA TPCPKEPNKE MINDGASWTI ISTDKAEYTF YEGMGPVLAP VTPVPVVESL
     QLNGGGDVAM LELTGQNFTP NLRVWFGDVE AETMYRCGES MLCVVPDISA FREGWRWVRQ
     PVQVPVTLVR NDGIIYSTSL TFTYTPEPGP RPHCSAAGAI LRANSSQVPP NESNTNSEGS
     YTNASTNSTS VTSSTATVVS
//
DBGET integrated database retrieval system