SUH_HUMAN
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 03-AUG-2022, entry version 209.
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; DOI=10.1128/jvi.70.5.3068-3074.1996;
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 variants 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};
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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; -. [Q06330-5]
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.
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 AlphaFoldDB; Q06330; -.
DR SMR; Q06330; -.
DR BioGRID; 109736; 160.
DR CORUM; Q06330; -.
DR DIP; DIP-33326N; -.
DR ELM; Q06330; -.
DR IntAct; Q06330; 127.
DR MINT; Q06330; -.
DR STRING; 9606.ENSP00000345206; -.
DR BindingDB; Q06330; -.
DR ChEMBL; CHEMBL4105709; -.
DR GlyGen; Q06330; 1 site, 1 O-linked glycan (1 site).
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; 448 antibodies from 41 providers.
DR DNASU; 3516; -.
DR Ensembl; ENST00000342295.6; ENSP00000345206.1; ENSG00000168214.22. [Q06330-1]
DR Ensembl; ENST00000342320.8; ENSP00000340124.4; ENSG00000168214.22. [Q06330-6]
DR Ensembl; ENST00000345843.8; ENSP00000305815.6; ENSG00000168214.22. [Q06330-5]
DR Ensembl; ENST00000348160.9; ENSP00000339699.5; ENSG00000168214.22. [Q06330-6]
DR Ensembl; ENST00000355476.8; ENSP00000347659.4; ENSG00000168214.22. [Q06330-7]
DR Ensembl; ENST00000361572.10; ENSP00000354528.6; ENSG00000168214.22. [Q06330-1]
DR Ensembl; ENST00000504423.2; ENSP00000421804.2; ENSG00000168214.22. [Q06330-5]
DR Ensembl; ENST00000505958.6; ENSP00000426872.2; ENSG00000168214.22. [Q06330-6]
DR Ensembl; ENST00000507561.5; ENSP00000423907.1; ENSG00000168214.22. [Q06330-5]
DR Ensembl; ENST00000512671.6; ENSP00000423644.2; ENSG00000168214.22. [Q06330-1]
DR Ensembl; ENST00000680928.1; ENSP00000505493.1; ENSG00000168214.22. [Q06330-6]
DR Ensembl; ENST00000681093.1; ENSP00000504964.1; ENSG00000168214.22. [Q06330-6]
DR Ensembl; ENST00000681264.1; ENSP00000505255.1; ENSG00000168214.22. [Q06330-5]
DR Ensembl; ENST00000681484.1; ENSP00000505636.1; ENSG00000168214.22. [Q06330-5]
DR GeneID; 3516; -.
DR KEGG; hsa:3516; -.
DR MANE-Select; ENST00000355476.8; ENSP00000347659.4; NM_015874.6; NP_056958.3. [Q06330-7]
DR UCSC; uc003grx.3; human. [Q06330-1]
DR CTD; 3516; -.
DR DisGeNET; 3516; -.
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 VEuPathDB; HostDB:ENSG00000168214; -.
DR eggNOG; KOG3743; Eukaryota.
DR GeneTree; ENSGT00390000005197; -.
DR HOGENOM; CLU_022207_2_1_1; -.
DR InParanoid; Q06330; -.
DR OMA; ISEVQWN; -.
DR OrthoDB; 444988at2759; -.
DR PhylomeDB; Q06330; -.
DR TreeFam; TF314117; -.
DR PathwayCommons; Q06330; -.
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; 30 hits in 1086 CRISPR screens.
DR ChiTaRS; RBPJ; human.
DR EvolutionaryTrace; Q06330; -.
DR GeneWiki; RBPJ; -.
DR GenomeRNAi; 3516; -.
DR Pharos; Q06330; Tchem.
DR PRO; PR:Q06330; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q06330; protein.
DR Bgee; ENSG00000168214; Expressed in inferior olivary complex and 209 other tissues.
DR ExpressionAtlas; Q06330; baseline and differential.
DR Genevisible; Q06330; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
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:0017053; C:transcription 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:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA 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:0060379; P:cardiac muscle cell myoblast differentiation; 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:0050673; P:epithelial cell proliferation; 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: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: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:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
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; IMP: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:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
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: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:2000241; P:regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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:0072089; P:stem cell proliferation; IEA:Ensembl.
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_DNA-bd_sf.
DR InterPro; IPR038007; RBP-Jkappa_IPT.
DR PANTHER; PTHR10665; PTHR10665; 2.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR Pfam; PF20144; TIG_SUH; 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 variant; DNA-binding; Notch signaling pathway; Nucleus;
KW 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 REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..67
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:16530044"
FT REGION 165..170
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:16530044"
FT REGION 192..197
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:16530044"
FT REGION 465..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:2F8X"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3NBN"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:2F8X"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3NBN"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3NBN"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2F8X"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2F8X"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3NBN"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3NBN"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:2F8X"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:2F8X"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2F8X"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3NBN"
FT STRAND 435..437
FT /evidence="ECO:0007829|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
