HMGN1_HUMAN
ID HMGN1_HUMAN Reviewed; 100 AA.
AC P05114; Q3KQR8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Non-histone chromosomal protein HMG-14;
DE AltName: Full=High mobility group nucleosome-binding domain-containing protein 1;
GN Name=HMGN1; Synonyms=HMG14;
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].
RX PubMed=3782107; DOI=10.1016/s0021-9258(18)66680-3;
RA Landsman D., Srikantha T., Westermann R., Bustin M.;
RT "Chromosomal protein HMG-14. Complete human cDNA sequence and evidence for
RT a multigene family.";
RL J. Biol. Chem. 261:16082-16086(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2563381; DOI=10.1016/s0021-9258(18)94084-6;
RA Landsman D., McBride O.W., Soares N., Crippa M.P., Srikantha T., Bustin M.;
RT "Chromosomal protein HMG-14. Identification, characterization, and
RT chromosome localization of a functional gene from the large human multigene
RT family.";
RL J. Biol. Chem. 264:3421-3427(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and Ovary;
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 PROTEIN SEQUENCE OF 19-31, PHOSPHORYLATION AT SER-21 AND SER-25,
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=10739259; DOI=10.1110/ps.9.1.170;
RA Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G.;
RT "Phosphorylation and subcellular redistribution of high mobility group
RT proteins 14 and 17, analyzed by mass spectrometry.";
RL Protein Sci. 9:170-179(2000).
RN [7]
RP PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), RNA EDITING, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18993075; DOI=10.1016/j.cub.2008.09.059;
RA Zougman A., Ziolkowski P., Mann M., Wisniewski J.R.;
RT "Evidence for insertional RNA editing in humans.";
RL Curr. Biol. 18:1760-1765(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89 AND SER-99, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(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., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
RP IDENTIFICATION BY 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-82, AND IDENTIFICATION
RP 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., Walther T.C.,
RA 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-86 AND SER-89, 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 [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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-86 AND SER-89, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-86 AND
RP SER-89, AND IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
RP IDENTIFICATION BY 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 [20]
RP ADP-RIBOSYLATION AT SER-7 AND SER-25.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [21]
RP INTERACTION WITH SEHBP.
RX PubMed=33468658; DOI=10.1073/pnas.2021943118;
RA Koh M., Ahmad I., Ko Y., Zhang Y., Martinez T.F., Diedrich J.K., Chu Q.,
RA Moresco J.J., Erb M.A., Saghatelian A., Schultz P.G., Bollong M.J.;
RT "A short ORF-encoded transcriptional regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Binds to the inner side of the nucleosomal DNA thus altering
CC the interaction between the DNA and the histone octamer. May be
CC involved in the process which maintains transcribable genes in a unique
CC chromatin conformation. Inhibits the phosphorylation of nucleosomal
CC histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with transcriptional regulator SEHBP.
CC {ECO:0000269|PubMed:33468658}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic enrichment
CC upon phosphorylation. The RNA edited version localizes to the nucleus.
CC -!- PTM: Phosphorylation on Ser-21 and Ser-25 weakens binding to
CC nucleosomes and increases the rate of H3 phosphorylation (By
CC similarity). Phosphorylation favors cytoplasmic localization.
CC {ECO:0000250, ECO:0000269|PubMed:10739259}.
CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=Partially edited.
CC A new initiator methionine may be created by a single uridine insertion
CC in the 5'-UTR, causing an N-terminal extension of 45 amino acids. The
CC existence of the RNA edited version is supported by direct protein
CC sequencing by MS/MS of the following peptides specific to that version:
CC 23-31 and 40-48. The RNA edited version is called ET-HMGN1.
CC {ECO:0000269|PubMed:18993075};
CC -!- MASS SPECTROMETRY: Mass=10527.8; Mass_error=0.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- MASS SPECTROMETRY: Mass=10608; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- MASS SPECTROMETRY: Mass=10688; Mass_error=1.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- MASS SPECTROMETRY: Mass=10768; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10739259};
CC -!- SIMILARITY: Belongs to the HMGN family. {ECO:0000305}.
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DR EMBL; J02621; AAA52676.1; -; mRNA.
DR EMBL; M21339; AAA52677.1; -; Genomic_DNA.
DR EMBL; BT007337; AAP36001.1; -; mRNA.
DR EMBL; AF064861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163279; CAB90453.1; -; Genomic_DNA.
DR EMBL; BC000075; AAH00075.1; -; mRNA.
DR EMBL; BC023984; AAH23984.1; -; mRNA.
DR EMBL; BC070153; AAH70153.1; -; mRNA.
DR EMBL; BC106080; AAI06081.1; -; mRNA.
DR CCDS; CCDS33559.1; -.
DR PIR; A33310; A33310.
DR RefSeq; NP_004956.5; NM_004965.6.
DR AlphaFoldDB; P05114; -.
DR BioGRID; 109393; 133.
DR IntAct; P05114; 44.
DR MINT; P05114; -.
DR STRING; 9606.ENSP00000370125; -.
DR GlyGen; P05114; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05114; -.
DR PhosphoSitePlus; P05114; -.
DR SwissPalm; P05114; -.
DR BioMuta; HMGN1; -.
DR DMDM; 123101; -.
DR CPTAC; CPTAC-1350; -.
DR EPD; P05114; -.
DR jPOST; P05114; -.
DR MassIVE; P05114; -.
DR MaxQB; P05114; -.
DR PaxDb; P05114; -.
DR PeptideAtlas; P05114; -.
DR PRIDE; P05114; -.
DR ProteomicsDB; 51800; -.
DR TopDownProteomics; P05114; -.
DR Antibodypedia; 23386; 406 antibodies from 36 providers.
DR DNASU; 3150; -.
DR Ensembl; ENST00000380749.10; ENSP00000370125.5; ENSG00000205581.11.
DR GeneID; 3150; -.
DR KEGG; hsa:3150; -.
DR MANE-Select; ENST00000380749.10; ENSP00000370125.5; NM_004965.7; NP_004956.5.
DR UCSC; uc002yxo.4; human.
DR CTD; 3150; -.
DR DisGeNET; 3150; -.
DR GeneCards; HMGN1; -.
DR HGNC; HGNC:4984; HMGN1.
DR HPA; ENSG00000205581; Low tissue specificity.
DR MIM; 163920; gene.
DR neXtProt; NX_P05114; -.
DR OpenTargets; ENSG00000205581; -.
DR PharmGKB; PA35088; -.
DR VEuPathDB; HostDB:ENSG00000205581; -.
DR eggNOG; ENOG502S7UM; Eukaryota.
DR GeneTree; ENSGT00950000182802; -.
DR HOGENOM; CLU_141985_1_0_1; -.
DR InParanoid; P05114; -.
DR OMA; CHWPEGA; -.
DR OrthoDB; 1354926at2759; -.
DR PhylomeDB; P05114; -.
DR TreeFam; TF105374; -.
DR PathwayCommons; P05114; -.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR SignaLink; P05114; -.
DR SIGNOR; P05114; -.
DR BioGRID-ORCS; 3150; 29 hits in 1045 CRISPR screens.
DR ChiTaRS; HMGN1; human.
DR GeneWiki; HMGN1; -.
DR GenomeRNAi; 3150; -.
DR Pharos; P05114; Tbio.
DR PRO; PR:P05114; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P05114; protein.
DR Bgee; ENSG00000205581; Expressed in ventricular zone and 105 other tissues.
DR ExpressionAtlas; P05114; baseline and differential.
DR Genevisible; P05114; HS.
DR GO; GO:0000785; C:chromatin; TAS:ProtInc.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; TAS:ProtInc.
DR GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; IEA:Ensembl.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IEA:Ensembl.
DR GO; GO:0040034; P:regulation of development, heterochronic; IEA:Ensembl.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; IEA:Ensembl.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Ensembl.
DR InterPro; IPR000079; HMGN_fam.
DR Pfam; PF01101; HMG14_17; 1.
DR PRINTS; PR00925; NONHISHMG17.
DR SMART; SM00527; HMG17; 1.
DR PROSITE; PS00355; HMG14_17; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; RNA editing.
FT CHAIN 1..100
FT /note="Non-histone chromosomal protein HMG-14"
FT /id="PRO_0000206691"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 21
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:10739259,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 25
FT /note="Phosphoserine; alternate; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:10739259,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18608"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18608"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 1
FT /note="M -> MLGRREEWQRQGSPVSRRLSARRGPQAPGTRLPRRHPARAFPAATM
FT (in RNA edited version)"
FT /id="VAR_054790"
SQ SEQUENCE 100 AA; 10659 MW; 8F4CB5374D51FBF3 CRC64;
MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG
KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD
