PHRF1_HUMAN
ID PHRF1_HUMAN Reviewed; 1649 AA.
AC Q9P1Y6; A6H8W1; B7ZM64; B9EGP0; C9JS82; Q6PJP2; Q8IVY2; Q8N2Y7; Q9BSM2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PHD and RING finger domain-containing protein 1;
GN Name=PHRF1; Synonyms=KIAA1542;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-1449.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1094-1649 (ISOFORM 2), AND VARIANT ALA-1449.
RC TISSUE=Brain, Lymph, and Uterus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991 AND SER-1202, AND
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-867; SER-1128 AND
RP SER-1202, AND 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330; SER-915; THR-917;
RP SER-936; SER-1359; SER-1360; SER-1371 AND THR-1404, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-991, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867 AND SER-1360, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-814; SER-846; SER-867;
RP SER-915; SER-936; SER-973; SER-991; SER-1124; SER-1202; SER-1229; SER-1360
RP AND SER-1371, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-814; SER-845; SER-915;
RP SER-973; SER-1202; SER-1229 AND SER-1360, AND IDENTIFICATION BY MASS
RP 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).
CC -!- SUBUNIT: Interacts with POLR2A (via the C-terminal domain).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P1Y6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P1Y6-2; Sequence=VSP_023247, VSP_023248;
CC Name=3;
CC IsoId=Q9P1Y6-3; Sequence=VSP_039187;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB040975; BAA96066.1; ALT_INIT; mRNA.
DR EMBL; AP006284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004950; AAH04950.1; -; mRNA.
DR EMBL; BC013381; AAH13381.1; -; mRNA.
DR EMBL; BC029651; AAH29651.1; -; mRNA.
DR EMBL; BC041631; AAH41631.1; -; mRNA.
DR EMBL; BC136615; AAI36616.1; -; mRNA.
DR EMBL; BC144293; AAI44294.1; -; mRNA.
DR EMBL; BC146771; AAI46772.1; -; mRNA.
DR CCDS; CCDS44507.1; -. [Q9P1Y6-3]
DR CCDS; CCDS65988.1; -. [Q9P1Y6-1]
DR RefSeq; NP_001273510.1; NM_001286581.1. [Q9P1Y6-1]
DR RefSeq; NP_001273511.1; NM_001286582.1.
DR RefSeq; NP_001273512.1; NM_001286583.1.
DR RefSeq; NP_065952.2; NM_020901.3. [Q9P1Y6-3]
DR AlphaFoldDB; Q9P1Y6; -.
DR SMR; Q9P1Y6; -.
DR BioGRID; 121694; 57.
DR IntAct; Q9P1Y6; 16.
DR STRING; 9606.ENSP00000264555; -.
DR GlyGen; Q9P1Y6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P1Y6; -.
DR PhosphoSitePlus; Q9P1Y6; -.
DR BioMuta; PHRF1; -.
DR DMDM; 296439275; -.
DR EPD; Q9P1Y6; -.
DR jPOST; Q9P1Y6; -.
DR MassIVE; Q9P1Y6; -.
DR MaxQB; Q9P1Y6; -.
DR PaxDb; Q9P1Y6; -.
DR PeptideAtlas; Q9P1Y6; -.
DR PRIDE; Q9P1Y6; -.
DR ProteomicsDB; 83679; -. [Q9P1Y6-1]
DR ProteomicsDB; 83680; -. [Q9P1Y6-2]
DR ProteomicsDB; 83681; -. [Q9P1Y6-3]
DR Antibodypedia; 5345; 22 antibodies from 10 providers.
DR DNASU; 57661; -.
DR Ensembl; ENST00000264555.10; ENSP00000264555.5; ENSG00000070047.13. [Q9P1Y6-1]
DR Ensembl; ENST00000416188.3; ENSP00000410626.2; ENSG00000070047.13. [Q9P1Y6-3]
DR Ensembl; ENST00000534320.5; ENSP00000435360.1; ENSG00000070047.13. [Q9P1Y6-2]
DR Ensembl; ENST00000616346.2; ENSP00000483129.1; ENSG00000274780.2.
DR GeneID; 57661; -.
DR KEGG; hsa:57661; -.
DR MANE-Select; ENST00000264555.10; ENSP00000264555.5; NM_001286581.2; NP_001273510.1.
DR UCSC; uc001lqe.5; human. [Q9P1Y6-1]
DR CTD; 57661; -.
DR DisGeNET; 57661; -.
DR GeneCards; PHRF1; -.
DR HGNC; HGNC:24351; PHRF1.
DR HPA; ENSG00000070047; Low tissue specificity.
DR MIM; 611780; gene.
DR neXtProt; NX_Q9P1Y6; -.
DR OpenTargets; ENSG00000070047; -.
DR PharmGKB; PA164718737; -.
DR PharmGKB; PA164724459; -.
DR VEuPathDB; HostDB:ENSG00000070047; -.
DR eggNOG; KOG0825; Eukaryota.
DR GeneTree; ENSGT00950000183205; -.
DR InParanoid; Q9P1Y6; -.
DR OMA; GHIFEDF; -.
DR PhylomeDB; Q9P1Y6; -.
DR TreeFam; TF332183; -.
DR PathwayCommons; Q9P1Y6; -.
DR SignaLink; Q9P1Y6; -.
DR BioGRID-ORCS; 57661; 12 hits in 1114 CRISPR screens.
DR ChiTaRS; PHRF1; human.
DR GenomeRNAi; 57661; -.
DR Pharos; Q9P1Y6; Tbio.
DR PRO; PR:Q9P1Y6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P1Y6; protein.
DR Bgee; ENSG00000070047; Expressed in sural nerve and 94 other tissues.
DR ExpressionAtlas; Q9P1Y6; baseline and differential.
DR Genevisible; Q9P1Y6; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1649
FT /note="PHD and RING finger domain-containing protein 1"
FT /id="PRO_0000278266"
FT ZN_FING 108..149
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 183..233
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1549..1579
FT /evidence="ECO:0000255"
FT COMPBIAS 50..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..385
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1015
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1086
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63625"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 917
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1404
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 446
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039187"
FT VAR_SEQ 1473..1494
FT /note="VYSPGLPPAPAQPSSIPPCALV -> PQSQPVKPLQPATRRRRPRPPG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023247"
FT VAR_SEQ 1495..1649
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023248"
FT VARIANT 1231
FT /note="E -> A (in dbSNP:rs7116027)"
FT /id="VAR_030727"
FT VARIANT 1374
FT /note="A -> V (in dbSNP:rs7123948)"
FT /id="VAR_030728"
FT VARIANT 1449
FT /note="V -> A (in dbSNP:rs11246212)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030729"
FT CONFLICT 167
FT /note="R -> K (in Ref. 1; BAA96066 and 3; AAI46772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1649 AA; 178666 MW; D9B8F1454C000D65 CRC64;
MDDDSLDELV ARSPGPDGHP QVGPADPAGD FEESSVGSSG DSGDDSDSEH GDGTDGEDEG
ASEEEDLEDR SGSEDSEDDG ETLLEVAGTQ GKLEAAGSFN SDDDAESCPI CLNAFRDQAV
GTPENCAHYF CLDCIVEWSK NANSCPVDRT LFKCICIRAQ FGGKILRKIP VENTKASEEE
EDPTFCEVCG RSDREDRLLL CDGCDAGYHM ECLDPPLQEV PVDEWFCPEC AAPGVVLAAD
AGPVSEEEVS LLLADVVPTT SRLRPRAGRT RAIARTRQSE RVRATVNRNR ISTARRVQHT
PGRLGSSLLD EAIEAVATGL STAVYQRPLT PRTPARRKRK TRRRKKVPGR KKTPSGPSAK
SKSSATRSKK RQHRVKKRRG KKVKSEATTR SRIARTLGLR RPVHSSCIPS VLKPVEPSLG
LLRADIGAAS LSLFGDPYEL DPFDSSEELS ANPLSPLSAK RRALSRSALQ SHQPVARPVS
VGLSRRRLPA AVPEPDLEEE PVPDLLGSIL SGQSLLMLGS SDVIIHRDGS LSAKRAAPVS
FQRNSGSLSR GEEGFKGCLQ PRALPSGSPA QGPSGNRPQS TGLSCQGRSR TPARTAGAPV
RLDLPAAPGA VQARNLSNGS VPGFRQSHSP WFNGTNKHTL PLASAASKIS SRDSKPPCRS
VVPGPPLKPA PRRTDISELP RIPKIRRDDG GGRRDAAPAH GQSIEIPSAC ISRLTGREGT
GQPGRGTRAE SEASSRVPRE PGVHTGSSRP PAPSSHGSLA PLGPSRGKGV GSTFESFRIN
IPGNMAHSSQ LSSPGFCNTF RPVDDKEQRK ENPSPLFSIK KTKQLRSEVY DPSDPTGSDS
SAPGSSPERS GPGLLPSEIT RTISINSPKA QTVQAVRCVT SYTVESIFGT EPEPPLGPSS
AMSKLRGAVA AEGASDTERE EPTESQGLAA RLRRPSPPEP WDEEDGASCS TFFGSEERTV
TCVTVVEPEA PPSPDVLQAA THRVVELRPP SRSRSTSSSR SRKKAKRKRV SREHGRTRSG
TRSESRDRSS RSASPSVGEE RPRRQRSKAK SRRSSSDRSS SRERAKRKKA KDKSREHRRG
PWGHSRRTSR SRSGSPGSSS YEHYESRKKK KRRSASRPRG RECSPTSSLE RLCRHKHQRE
RSHERPDRKE SVAWPRDRRK RRSRSPSSEH RAREHRRPRS REKWPQTRSH SPERKGAVRE
ASPAPLAQGE PGREDLPTRL PALGEAHVSP EVATADKAPL QAPPVLEVAA ECEPDDLDLD
YGDSVEAGHV FDDFSSDAVF IQLDDMSSPP SPESTDSSPE RDFPLKPALP PASLAVAAIQ
REVSLMHDED PSQPPPLPEG TQEPHLLRPD AAEKAEAPSS PDVAPAGKED SPSASGRVQE
AARPEEVVSQ TPLLRSRALV KRVTWNLQES ESSAPAEDRA PRAPLHRPQK PREGAWDMED
VAPTGVRQVF SELPFPSHVL PEPGFPDTDP SQVYSPGLPP APAQPSSIPP CALVSQPTVQ
FILQGSLPLV GCGAAQTLAP VPAALTPASE PASQATAASN SEEKTPAPRL AAEKTKKEEY
MKKLHMQERA VEEVKLAIKP FYQKREVTKE EYKDILRKAV QKICHSKSGE INPVKVANLV
KAYVDKYRHM RRHKKPEAGE EPPTQGAEG
