BBX_HUMAN
ID BBX_HUMAN Reviewed; 941 AA.
AC Q8WY36; A2RRM7; Q2TAJ1; Q7L3J8; Q7LBY8; Q8NDB0; Q8WY35; Q9H0J6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=HMG box transcription factor BBX;
DE AltName: Full=Bobby sox homolog;
DE AltName: Full=HMG box-containing protein 2;
GN Name=BBX; Synonyms=HBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=11680820; DOI=10.1007/s002940100241;
RA Sanchez-Diaz A., Blanco M.A., Jones N., Moreno S.;
RT "HBP2: a new mammalian protein that complements the fission yeast MBF
RT transcription complex.";
RL Curr. Genet. 40:110-118(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lee C.-J., Chan W.-I., Appleby V.J., Orme A.T., Scotting P.J.;
RT "BBX is expressed in developing CNS and in neuronal tumours.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Ovary, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485 AND SER-822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-704 AND SER-822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-385; LYS-573 AND LYS-696, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor that is necessary for cell cycle
CC progression from G1 to S phase. {ECO:0000269|PubMed:11680820}.
CC -!- INTERACTION:
CC Q8WY36-3; P42858: HTT; NbExp=6; IntAct=EBI-22013474, EBI-466029;
CC Q8WY36-3; O76024: WFS1; NbExp=3; IntAct=EBI-22013474, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WY36-1; Sequence=Displayed;
CC Name=2; Synonyms=BBXa;
CC IsoId=Q8WY36-2; Sequence=VSP_018006;
CC Name=3;
CC IsoId=Q8WY36-3; Sequence=VSP_054880, VSP_054881;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10904.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF276948; AAL68984.1; -; mRNA.
DR EMBL; AF276949; AAL68985.1; -; mRNA.
DR EMBL; AF454941; AAL58870.1; -; mRNA.
DR EMBL; AF454942; AAL58871.1; -; mRNA.
DR EMBL; AL136769; CAB66703.1; -; mRNA.
DR EMBL; AL834307; CAD38977.1; -; mRNA.
DR EMBL; AC068765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC072044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012837; AAH12837.2; -; mRNA.
DR EMBL; BC110903; AAI10904.1; ALT_SEQ; mRNA.
DR EMBL; BC131718; AAI31719.1; -; mRNA.
DR CCDS; CCDS2950.1; -. [Q8WY36-2]
DR CCDS; CCDS46881.1; -. [Q8WY36-1]
DR CCDS; CCDS63712.1; -. [Q8WY36-3]
DR RefSeq; NP_001136040.1; NM_001142568.2. [Q8WY36-1]
DR RefSeq; NP_001263215.1; NM_001276286.1. [Q8WY36-3]
DR RefSeq; NP_064620.2; NM_020235.6. [Q8WY36-2]
DR RefSeq; XP_005247699.1; XM_005247642.3. [Q8WY36-1]
DR RefSeq; XP_005247700.1; XM_005247643.3. [Q8WY36-1]
DR RefSeq; XP_005247701.1; XM_005247644.3. [Q8WY36-1]
DR RefSeq; XP_011511302.1; XM_011513000.1. [Q8WY36-1]
DR RefSeq; XP_011511303.1; XM_011513001.1. [Q8WY36-1]
DR RefSeq; XP_011511306.1; XM_011513004.2. [Q8WY36-2]
DR RefSeq; XP_016862370.1; XM_017006881.1. [Q8WY36-1]
DR RefSeq; XP_016862371.1; XM_017006882.1. [Q8WY36-2]
DR AlphaFoldDB; Q8WY36; -.
DR SMR; Q8WY36; -.
DR BioGRID; 121304; 111.
DR IntAct; Q8WY36; 30.
DR MINT; Q8WY36; -.
DR STRING; 9606.ENSP00000319974; -.
DR GlyGen; Q8WY36; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q8WY36; -.
DR PhosphoSitePlus; Q8WY36; -.
DR BioMuta; BBX; -.
DR DMDM; 74724044; -.
DR EPD; Q8WY36; -.
DR jPOST; Q8WY36; -.
DR MassIVE; Q8WY36; -.
DR MaxQB; Q8WY36; -.
DR PaxDb; Q8WY36; -.
DR PeptideAtlas; Q8WY36; -.
DR PRIDE; Q8WY36; -.
DR ProteomicsDB; 476; -.
DR ProteomicsDB; 75124; -. [Q8WY36-1]
DR ProteomicsDB; 75125; -. [Q8WY36-2]
DR Antibodypedia; 32337; 118 antibodies from 24 providers.
DR DNASU; 56987; -.
DR Ensembl; ENST00000325805.13; ENSP00000319974.8; ENSG00000114439.19. [Q8WY36-1]
DR Ensembl; ENST00000406780.5; ENSP00000385530.1; ENSG00000114439.19. [Q8WY36-2]
DR Ensembl; ENST00000415149.6; ENSP00000408358.2; ENSG00000114439.19. [Q8WY36-2]
DR Ensembl; ENST00000416476.6; ENSP00000403860.2; ENSG00000114439.19. [Q8WY36-3]
DR GeneID; 56987; -.
DR KEGG; hsa:56987; -.
DR MANE-Select; ENST00000325805.13; ENSP00000319974.8; NM_001142568.3; NP_001136040.1.
DR UCSC; uc003dwk.6; human. [Q8WY36-1]
DR CTD; 56987; -.
DR DisGeNET; 56987; -.
DR GeneCards; BBX; -.
DR HGNC; HGNC:14422; BBX.
DR HPA; ENSG00000114439; Low tissue specificity.
DR neXtProt; NX_Q8WY36; -.
DR OpenTargets; ENSG00000114439; -.
DR PharmGKB; PA25280; -.
DR VEuPathDB; HostDB:ENSG00000114439; -.
DR eggNOG; KOG2746; Eukaryota.
DR GeneTree; ENSGT00940000158592; -.
DR HOGENOM; CLU_435423_0_0_1; -.
DR InParanoid; Q8WY36; -.
DR OMA; LAEAKMC; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; Q8WY36; -.
DR TreeFam; TF106402; -.
DR PathwayCommons; Q8WY36; -.
DR SignaLink; Q8WY36; -.
DR BioGRID-ORCS; 56987; 25 hits in 1120 CRISPR screens.
DR ChiTaRS; BBX; human.
DR GeneWiki; BBX_(gene); -.
DR GenomeRNAi; 56987; -.
DR Pharos; Q8WY36; Tbio.
DR PRO; PR:Q8WY36; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WY36; protein.
DR Bgee; ENSG00000114439; Expressed in corpus epididymis and 213 other tissues.
DR ExpressionAtlas; Q8WY36; baseline and differential.
DR Genevisible; Q8WY36; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR019102; TF_HMG_box_BBX_DUF2028.
DR Pfam; PF09667; DUF2028; 2.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..941
FT /note="HMG box transcription factor BBX"
FT /id="PRO_0000232885"
FT DNA_BIND 80..148
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 326..370
FT /evidence="ECO:0000255"
FT COMPBIAS 40..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBW5"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 303..628
FT /note="MCLASEGMKMEESKLIKAKESDGGRIKELEKGKEEKEIKMEKTDETRLQKEA
FT EFEKSAKENLRDSKELRNFEALQIDDIMAIKMEDPKEIRKEELEEDHKCSHFPDFSYSA
FT SSKIIISDVPSRKDHMCHPHGIMIIEDPAALNKPEKLKKKKKKSKMDRHGNDKSTPKKT
FT CKKRQSSESDIESVIYTIEAVAKGDWGIEKLGDTPRKKVRTSSSGKGSILDAKPPKKKV
FT KSREKKMSKEKSSDTTKESRPPDFISISASKNISGETPEGIKAEPLTPMEDALPPSLSG
FT QAKPEDSDCHRKIETCGSRKSERSCKGALYKTLVSEGM -> ENEAQEKETPLIMKGVG
FT MKKAGHLVRVGPVGARSSRRQSQKKTVSLAPQSWMKNLKKNSTASLNIVLLHLTGNVYL
FT SQEKRRRLEMCPQNRLKPAKVLSSLRKRTYSTKLSANISTKRRSPMFRKKEVGINGQTS
FT NSSWMPFTLQKPYFQKTETPWSLFIRLKISHPFSTLQSQQQRKNLWWAAKREKQGKPRL
FT HTLSGQQMAGYHQQEVLWMTNQRNNCRGVSLKQLRQTAMTNAHTTPRSGRRGAVLQKCL
FT PCLRSLASLRWLKWQPWKMCTEVRGQLRSPMMDSQKKCRRLLYLFPALTSEAPFHCKTL
FT CFTYYPSLVFTEGC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054880"
FT VAR_SEQ 629..941
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054881"
FT VAR_SEQ 735..764
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.2"
FT /id="VSP_018006"
FT VARIANT 576
FT /note="P -> S (in dbSNP:rs59781647)"
FT /id="VAR_061264"
SQ SEQUENCE 941 AA; 105130 MW; E45B359A602B5D8D CRC64;
MKGSNRNKDH SAEGEGVGKR PKRKCLQWHP LLAKKLLDFS EEEEEEDEEE DIDKVQLLGA
DGLEQDVGET EDDESPEQRA RRPMNAFLLF CKRHRSLVRQ EHPRLDNRGA TKILADWWAV
LDPKEKQKYT DMAKEYKDAF MKANPGYKWC PTTNKPVKSP TPTVNPRKKL WAFPSDSSRD
LPSPKKAKTE EMPQLNFGMA DPTQMGGLSM LLLAGEHALG TPEVSSGTCR PDVSESPELR
QKSPLFQFAE ISSSTSHSDA STKQCQTSAL FQFAEISSNT SQLGGAEPVK RCGKSALFQL
AEMCLASEGM KMEESKLIKA KESDGGRIKE LEKGKEEKEI KMEKTDETRL QKEAEFEKSA
KENLRDSKEL RNFEALQIDD IMAIKMEDPK EIRKEELEED HKCSHFPDFS YSASSKIIIS
DVPSRKDHMC HPHGIMIIED PAALNKPEKL KKKKKKSKMD RHGNDKSTPK KTCKKRQSSE
SDIESVIYTI EAVAKGDWGI EKLGDTPRKK VRTSSSGKGS ILDAKPPKKK VKSREKKMSK
EKSSDTTKES RPPDFISISA SKNISGETPE GIKAEPLTPM EDALPPSLSG QAKPEDSDCH
RKIETCGSRK SERSCKGALY KTLVSEGMLT SLRANVDRGK RSSGKGNSSD HEGCWNEESW
TFSQSGTSGS KKFKKTKPKE DCLLGSAKLD EEFEKKFNSL PQYSPVTFDR KCVPVPRKKK
KTGNVSSEPT KTSKGPFQSQ KKNLFHKIVS KYKHKKEKPN VPEKGSGDKW SNKQLFLDAI
HPTEAIFSED RNTMEPVHKV KNIPSIFNTP EPTTTQEPLV GSQKRKARKT KITHLVRTAD
GRVSPAGGTL DDKPKEQLQR SLPKATETDC NDKCSHNTEV GETRSSTPEM PAVSAFFSLA
ALAEVAAMEN VHRGQRSTPL THDGQPKEMP QAPVLISCAD Q
