Full text data of FTSJ3
FTSJ3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
pre-rRNA processing protein FTSJ3; 2.1.1.- (2'-O-ribose RNA methyltransferase SPB1 homolog; Protein ftsJ homolog 3; Putative rRNA methyltransferase 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
pre-rRNA processing protein FTSJ3; 2.1.1.- (2'-O-ribose RNA methyltransferase SPB1 homolog; Protein ftsJ homolog 3; Putative rRNA methyltransferase 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00217686
IPI00217686 FtsJ homolog 3 hypothetical protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00217686 FtsJ homolog 3 hypothetical protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q8IY81
ID SPB1_HUMAN Reviewed; 847 AA.
AC Q8IY81; B2RCA5; D3DU22; Q8N3A3; Q8WXX1; Q9BWM4; Q9NXT6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=pre-rRNA processing protein FTSJ3;
DE EC=2.1.1.-;
DE AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog;
DE AltName: Full=Protein ftsJ homolog 3;
DE AltName: Full=Putative rRNA methyltransferase 3;
GN Name=FTSJ3; ORFNames=SB92;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RA Zhang W., Li N., Wan T., Chen T., Cao T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RC TISSUE=Colon, and Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RC TISSUE=Placenta, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, AND VARIANT
RP CYS-424.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336
RP AND SER-347, AND MASS SPECTROMETRY.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-356; THR-371; SER-549; SER-584 AND SER-644, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-584; SER-644;
RP SER-676 AND SER-688, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP FUNCTION, INTERACTION WITH NIP7, AND SUBCELLULAR LOCATION.
RX PubMed=22195017; DOI=10.1371/journal.pone.0029174;
RA Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C.,
RA Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I.;
RT "The human nucleolar protein FTSJ3 associates with NIP7 and functions
RT in pre-rRNA processing.";
RL PLoS ONE 6:E29174-E29174(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-584 AND SER-644, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Probable methyltransferase involved in the processing of
CC the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit
CC formation.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-
CC homocysteine + rRNA containing 2'-O-methylnucleoside.
CC -!- SUBUNIT: Interacts with NIP7.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-744088, EBI-640775;
CC Q9Y6K5:OAS3; NbExp=2; IntAct=EBI-744088, EBI-6115729;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmE
CC family. SPB1 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90924.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF327355; AAL56015.1; -; mRNA.
DR EMBL; AK000069; BAA90924.1; ALT_INIT; mRNA.
DR EMBL; AK315010; BAG37502.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94273.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94274.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94275.1; -; Genomic_DNA.
DR EMBL; BC000131; AAH00131.2; -; mRNA.
DR EMBL; BC036710; AAH36710.1; -; mRNA.
DR EMBL; AL834482; CAD39141.1; -; mRNA.
DR RefSeq; NP_060117.3; NM_017647.3.
DR UniGene; Hs.463785; -.
DR ProteinModelPortal; Q8IY81; -.
DR SMR; Q8IY81; 23-199.
DR IntAct; Q8IY81; 12.
DR MINT; MINT-1468947; -.
DR STRING; 9606.ENSP00000337518; -.
DR PhosphoSite; Q8IY81; -.
DR DMDM; 296452883; -.
DR SWISS-2DPAGE; Q8IY81; -.
DR PaxDb; Q8IY81; -.
DR PRIDE; Q8IY81; -.
DR DNASU; 117246; -.
DR Ensembl; ENST00000427159; ENSP00000396673; ENSG00000108592.
DR GeneID; 117246; -.
DR KEGG; hsa:117246; -.
DR UCSC; uc002jbz.3; human.
DR CTD; 117246; -.
DR GeneCards; GC17M061896; -.
DR HGNC; HGNC:17136; FTSJ3.
DR HPA; HPA055544; -.
DR neXtProt; NX_Q8IY81; -.
DR PharmGKB; PA28419; -.
DR eggNOG; COG0293; -.
DR HOVERGEN; HBG075246; -.
DR InParanoid; Q8IY81; -.
DR KO; K14857; -.
DR OMA; LIWVFNQ; -.
DR OrthoDB; EOG7WX07S; -.
DR PhylomeDB; Q8IY81; -.
DR ChiTaRS; FTSJ3; human.
DR GeneWiki; FTSJ3; -.
DR GenomeRNAi; 117246; -.
DR NextBio; 80174; -.
DR PRO; PR:Q8IY81; -.
DR ArrayExpress; Q8IY81; -.
DR Bgee; Q8IY81; -.
DR CleanEx; HS_FTSJ3; -.
DR Genevestigator; Q8IY81; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR HAMAP; MF_01547; RNA_methyltr_E; 1; -.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1; -.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_Spb1_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR028589; Spb1.
DR PANTHER; PTHR10920; PTHR10920; 1.
DR PANTHER; PTHR10920:SF13; PTHR10920:SF13; 1.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Methyltransferase; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 847 pre-rRNA processing protein FTSJ3.
FT /FTId=PRO_0000155577.
FT COILED 355 407 Potential.
FT COILED 739 777 Potential.
FT ACT_SITE 157 157 Proton acceptor (By similarity).
FT BINDING 56 56 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 58 58 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 76 76 S-adenosyl-L-methionine (By similarity).
FT BINDING 92 92 S-adenosyl-L-methionine (By similarity).
FT BINDING 117 117 S-adenosyl-L-methionine (By similarity).
FT MOD_RES 333 333 Phosphoserine.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 336 336 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 356 356 Phosphoserine.
FT MOD_RES 371 371 Phosphothreonine.
FT MOD_RES 549 549 Phosphoserine.
FT MOD_RES 584 584 Phosphoserine.
FT MOD_RES 644 644 Phosphoserine.
FT MOD_RES 676 676 Phosphoserine.
FT MOD_RES 688 688 Phosphoserine.
FT VARIANT 91 91 Q -> E (in dbSNP:rs2584625).
FT /FTId=VAR_023284.
FT VARIANT 424 424 S -> C (in dbSNP:rs2727288).
FT /FTId=VAR_023285.
FT CONFLICT 278 278 E -> I (in Ref. 1; AAL56015 and 2;
FT BAA90924).
SQ SEQUENCE 847 AA; 96558 MW; 06B2F4D28A48026F CRC64;
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE
EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM
FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG
VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED
DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG
TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH
RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG
KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA
QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ
KKKHKRK
//
ID SPB1_HUMAN Reviewed; 847 AA.
AC Q8IY81; B2RCA5; D3DU22; Q8N3A3; Q8WXX1; Q9BWM4; Q9NXT6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=pre-rRNA processing protein FTSJ3;
DE EC=2.1.1.-;
DE AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog;
DE AltName: Full=Protein ftsJ homolog 3;
DE AltName: Full=Putative rRNA methyltransferase 3;
GN Name=FTSJ3; ORFNames=SB92;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RA Zhang W., Li N., Wan T., Chen T., Cao T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RC TISSUE=Colon, and Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND
RP CYS-424.
RC TISSUE=Placenta, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, AND VARIANT
RP CYS-424.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336
RP AND SER-347, AND MASS SPECTROMETRY.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-356; THR-371; SER-549; SER-584 AND SER-644, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-584; SER-644;
RP SER-676 AND SER-688, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP FUNCTION, INTERACTION WITH NIP7, AND SUBCELLULAR LOCATION.
RX PubMed=22195017; DOI=10.1371/journal.pone.0029174;
RA Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C.,
RA Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I.;
RT "The human nucleolar protein FTSJ3 associates with NIP7 and functions
RT in pre-rRNA processing.";
RL PLoS ONE 6:E29174-E29174(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-584 AND SER-644, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Probable methyltransferase involved in the processing of
CC the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit
CC formation.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-
CC homocysteine + rRNA containing 2'-O-methylnucleoside.
CC -!- SUBUNIT: Interacts with NIP7.
CC -!- INTERACTION:
CC P19525:EIF2AK2; NbExp=2; IntAct=EBI-744088, EBI-640775;
CC Q9Y6K5:OAS3; NbExp=2; IntAct=EBI-744088, EBI-6115729;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmE
CC family. SPB1 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90924.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF327355; AAL56015.1; -; mRNA.
DR EMBL; AK000069; BAA90924.1; ALT_INIT; mRNA.
DR EMBL; AK315010; BAG37502.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94273.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94274.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94275.1; -; Genomic_DNA.
DR EMBL; BC000131; AAH00131.2; -; mRNA.
DR EMBL; BC036710; AAH36710.1; -; mRNA.
DR EMBL; AL834482; CAD39141.1; -; mRNA.
DR RefSeq; NP_060117.3; NM_017647.3.
DR UniGene; Hs.463785; -.
DR ProteinModelPortal; Q8IY81; -.
DR SMR; Q8IY81; 23-199.
DR IntAct; Q8IY81; 12.
DR MINT; MINT-1468947; -.
DR STRING; 9606.ENSP00000337518; -.
DR PhosphoSite; Q8IY81; -.
DR DMDM; 296452883; -.
DR SWISS-2DPAGE; Q8IY81; -.
DR PaxDb; Q8IY81; -.
DR PRIDE; Q8IY81; -.
DR DNASU; 117246; -.
DR Ensembl; ENST00000427159; ENSP00000396673; ENSG00000108592.
DR GeneID; 117246; -.
DR KEGG; hsa:117246; -.
DR UCSC; uc002jbz.3; human.
DR CTD; 117246; -.
DR GeneCards; GC17M061896; -.
DR HGNC; HGNC:17136; FTSJ3.
DR HPA; HPA055544; -.
DR neXtProt; NX_Q8IY81; -.
DR PharmGKB; PA28419; -.
DR eggNOG; COG0293; -.
DR HOVERGEN; HBG075246; -.
DR InParanoid; Q8IY81; -.
DR KO; K14857; -.
DR OMA; LIWVFNQ; -.
DR OrthoDB; EOG7WX07S; -.
DR PhylomeDB; Q8IY81; -.
DR ChiTaRS; FTSJ3; human.
DR GeneWiki; FTSJ3; -.
DR GenomeRNAi; 117246; -.
DR NextBio; 80174; -.
DR PRO; PR:Q8IY81; -.
DR ArrayExpress; Q8IY81; -.
DR Bgee; Q8IY81; -.
DR CleanEx; HS_FTSJ3; -.
DR Genevestigator; Q8IY81; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR HAMAP; MF_01547; RNA_methyltr_E; 1; -.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1; -.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_Spb1_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR028589; Spb1.
DR PANTHER; PTHR10920; PTHR10920; 1.
DR PANTHER; PTHR10920:SF13; PTHR10920:SF13; 1.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Methyltransferase; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 847 pre-rRNA processing protein FTSJ3.
FT /FTId=PRO_0000155577.
FT COILED 355 407 Potential.
FT COILED 739 777 Potential.
FT ACT_SITE 157 157 Proton acceptor (By similarity).
FT BINDING 56 56 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 58 58 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT BINDING 76 76 S-adenosyl-L-methionine (By similarity).
FT BINDING 92 92 S-adenosyl-L-methionine (By similarity).
FT BINDING 117 117 S-adenosyl-L-methionine (By similarity).
FT MOD_RES 333 333 Phosphoserine.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 336 336 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 356 356 Phosphoserine.
FT MOD_RES 371 371 Phosphothreonine.
FT MOD_RES 549 549 Phosphoserine.
FT MOD_RES 584 584 Phosphoserine.
FT MOD_RES 644 644 Phosphoserine.
FT MOD_RES 676 676 Phosphoserine.
FT MOD_RES 688 688 Phosphoserine.
FT VARIANT 91 91 Q -> E (in dbSNP:rs2584625).
FT /FTId=VAR_023284.
FT VARIANT 424 424 S -> C (in dbSNP:rs2727288).
FT /FTId=VAR_023285.
FT CONFLICT 278 278 E -> I (in Ref. 1; AAL56015 and 2;
FT BAA90924).
SQ SEQUENCE 847 AA; 96558 MW; 06B2F4D28A48026F CRC64;
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE
EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM
FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG
VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED
DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG
TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH
RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG
KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA
QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ
KKKHKRK
//