ZN106_HUMAN
ID ZN106_HUMAN Reviewed; 1883 AA.
AC Q9H2Y7; B4DZ40; E9PE29; Q6NSD9; Q6PEK1; Q86T43; Q86T45; Q86T50; Q86T58;
AC Q86TA9; Q96M37; Q9H7B8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 106;
DE Short=Zfp-106;
DE AltName: Full=Zinc finger protein 474;
GN Name=ZNF106; Synonyms=SH3BP3, ZFP106, ZNF474;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Mashima H., Horikawa Y., Cox N.J., Bell G.I.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 256-1033 AND 1604-1883 (ISOFORM 1).
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1883 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-861; SER-864;
RP SER-937; THR-1021; SER-1025; SER-1026; SER-1031; SER-1279 AND SER-1328, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590; SER-861; SER-1025;
RP SER-1026; SER-1370 AND THR-1372, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861; SER-893; SER-1025;
RP SER-1026; SER-1279; SER-1328 AND SER-1370, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025; SER-1026; SER-1031;
RP SER-1279; SER-1284; SER-1302; SER-1328 AND SER-1370, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-641; SER-661;
RP SER-861; SER-864; SER-893; SER-937; THR-1021; SER-1025; SER-1026; SER-1249;
RP SER-1279; SER-1302; SER-1328; SER-1370; THR-1372 AND SER-1468, AND
RP 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 [13]
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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-371; LYS-775; LYS-911
RP AND LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1737, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356; LYS-371; LYS-775; LYS-911;
RP LYS-1265 AND LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-371; LYS-911; LYS-1265 AND
RP LYS-1737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-76; LYS-133; LYS-243;
RP LYS-287; LYS-305; LYS-356; LYS-365; LYS-371; LYS-417; LYS-451; LYS-461;
RP LYS-477; LYS-492; LYS-505; LYS-515; LYS-525; LYS-539; LYS-557; LYS-603;
RP LYS-671; LYS-684; LYS-705; LYS-721; LYS-741; LYS-775; LYS-807; LYS-905;
RP LYS-911; LYS-953; LYS-1265; LYS-1299; LYS-1324; LYS-1380; LYS-1392;
RP LYS-1395; LYS-1454; LYS-1486; LYS-1504; LYS-1585; LYS-1737 AND LYS-1864,
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-37 (ISOFORM 2), 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: RNA-binding protein. Specifically binds to 5'-GGGGCC-3'
CC sequence repeats in RNA. Essential for maintenance of peripheral motor
CC neuron and skeletal muscle function. Required for normal expression
CC and/or alternative splicing of a number of genes in spinal cord and
CC skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also
CC contributes to normal mitochondrial respiratory function in motor
CC neurons, via an unknown mechanism. {ECO:0000250|UniProtKB:O88466}.
CC -!- SUBUNIT: Interacts with KNOP1. Interacts with TARDBP and NUP107.
CC Interacts (via N-terminus) with RBM39. Interacts with the SH3 domains
CC of FYN and GRB2. {ECO:0000250|UniProtKB:O88466}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O88466}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O88466}. Note=Colocalizes with RBM39 in nuclear
CC speckles. Inhibition of RNA synthesis, or overexpression of KNOP1,
CC induces translocation from nuclear speckles to the nucleolus.
CC {ECO:0000250|UniProtKB:O88466}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2Y7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2Y7-2; Sequence=VSP_057120, VSP_057121;
CC -!- PTM: Phosphorylated by FYN in vitro. {ECO:0000250|UniProtKB:O88466}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58023.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH70244.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB14976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD91134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF205632; AAG35666.1; -; mRNA.
DR EMBL; AF209502; AAL40184.1; -; Genomic_DNA.
DR EMBL; AK024726; BAB14976.1; ALT_INIT; mRNA.
DR EMBL; AK057410; BAB71475.1; -; mRNA.
DR EMBL; AK302735; BAG63952.1; -; mRNA.
DR EMBL; AC012651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058023; AAH58023.1; ALT_SEQ; mRNA.
DR EMBL; BC070244; AAH70244.1; ALT_SEQ; mRNA.
DR EMBL; AL832455; CAD89926.1; -; mRNA.
DR EMBL; AL831983; CAD91134.1; ALT_INIT; mRNA.
DR EMBL; AL833301; CAD91142.1; -; mRNA.
DR EMBL; AL832014; CAD91147.1; -; mRNA.
DR EMBL; AL832352; CAD91149.1; -; mRNA.
DR CCDS; CCDS32208.1; -. [Q9H2Y7-1]
DR CCDS; CCDS61603.1; -. [Q9H2Y7-2]
DR RefSeq; NP_001271235.1; NM_001284306.1.
DR RefSeq; NP_001271236.1; NM_001284307.1. [Q9H2Y7-2]
DR RefSeq; NP_071918.1; NM_022473.2. [Q9H2Y7-1]
DR AlphaFoldDB; Q9H2Y7; -.
DR SMR; Q9H2Y7; -.
DR BioGRID; 122154; 66.
DR IntAct; Q9H2Y7; 33.
DR MINT; Q9H2Y7; -.
DR STRING; 9606.ENSP00000263805; -.
DR GlyGen; Q9H2Y7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2Y7; -.
DR PhosphoSitePlus; Q9H2Y7; -.
DR BioMuta; ZNF106; -.
DR DMDM; 51702191; -.
DR EPD; Q9H2Y7; -.
DR jPOST; Q9H2Y7; -.
DR MassIVE; Q9H2Y7; -.
DR MaxQB; Q9H2Y7; -.
DR PaxDb; Q9H2Y7; -.
DR PeptideAtlas; Q9H2Y7; -.
DR PRIDE; Q9H2Y7; -.
DR ProteomicsDB; 19800; -.
DR ProteomicsDB; 80634; -. [Q9H2Y7-1]
DR Antibodypedia; 10821; 105 antibodies from 24 providers.
DR DNASU; 64397; -.
DR Ensembl; ENST00000263805.8; ENSP00000263805.4; ENSG00000103994.18. [Q9H2Y7-1]
DR Ensembl; ENST00000565380.5; ENSP00000455674.1; ENSG00000103994.18. [Q9H2Y7-2]
DR GeneID; 64397; -.
DR KEGG; hsa:64397; -.
DR UCSC; uc001zpv.5; human. [Q9H2Y7-1]
DR CTD; 64397; -.
DR DisGeNET; 64397; -.
DR GeneCards; ZNF106; -.
DR HGNC; HGNC:12886; ZNF106.
DR HPA; ENSG00000103994; Tissue enhanced (skeletal muscle, tongue).
DR neXtProt; NX_Q9H2Y7; -.
DR OpenTargets; ENSG00000103994; -.
DR PharmGKB; PA166048944; -.
DR VEuPathDB; HostDB:ENSG00000103994; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157336; -.
DR HOGENOM; CLU_001566_0_0_1; -.
DR InParanoid; Q9H2Y7; -.
DR PhylomeDB; Q9H2Y7; -.
DR TreeFam; TF105569; -.
DR PathwayCommons; Q9H2Y7; -.
DR SignaLink; Q9H2Y7; -.
DR BioGRID-ORCS; 64397; 22 hits in 1084 CRISPR screens.
DR ChiTaRS; ZNF106; human.
DR GeneWiki; ZFP106; -.
DR GenomeRNAi; 64397; -.
DR Pharos; Q9H2Y7; Tbio.
DR PRO; PR:Q9H2Y7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H2Y7; protein.
DR Bgee; ENSG00000103994; Expressed in skeletal muscle tissue of rectus abdominis and 204 other tissues.
DR ExpressionAtlas; Q9H2Y7; baseline and differential.
DR Genevisible; Q9H2Y7; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR DisProt; DP02007; -.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR042622; Znf106.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14435; PTHR14435; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..1883
FT /note="Zinc finger protein 106"
FT /id="PRO_0000051467"
FT REPEAT 1529..1568
FT /note="WD 1"
FT REPEAT 1570..1611
FT /note="WD 2"
FT REPEAT 1654..1695
FT /note="WD 3"
FT REPEAT 1698..1737
FT /note="WD 4"
FT REPEAT 1738..1775
FT /note="WD 5"
FT REPEAT 1778..1815
FT /note="WD 6"
FT ZN_FING 20..44
FT /note="C2H2-type 1; atypical"
FT ZN_FING 1813..1838
FT /note="C2H2-type 2; atypical"
FT REGION 39..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1021
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88466"
FT MOD_RES 1284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1372
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 451
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 525
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 603
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 671
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 705
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 905
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 911
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 953
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1395
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1864
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..38
FT /note="MPVGRIECPSSPSFPRDISHECRVCGVTEVGLSAYAKH -> MVRERKCILC
FT HIVYSSKKEMDEHMRSMLHHRELENLKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057120"
FT VAR_SEQ 39..810
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057121"
FT VARIANT 103
FT /note="W -> R (in dbSNP:rs12440118)"
FT /id="VAR_053440"
FT VARIANT 646
FT /note="I -> T (in dbSNP:rs12101559)"
FT /id="VAR_053441"
FT VARIANT 656
FT /note="M -> V (in dbSNP:rs34792942)"
FT /id="VAR_053442"
FT VARIANT 1162
FT /note="P -> T (in dbSNP:rs34983340)"
FT /id="VAR_053443"
FT CONFLICT 475
FT /note="N -> D (in Ref. 2; BAB71475)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="D -> G (in Ref. 5; CAD91147)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="I -> V (in Ref. 2; BAB71475)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="E -> G (in Ref. 5; CAD91142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509
FT /note="S -> P (in Ref. 2; BAG63952)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="R -> L (in Ref. 2; BAB14976)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q9H2Y7-2:6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9H2Y7-2:37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1883 AA; 208883 MW; 7D1CBD6193F8888C CRC64;
MPVGRIECPS SPSFPRDISH ECRVCGVTEV GLSAYAKHIS GQLHKDNVDA QEREDDGKGE
EEEEDYFDKE LIQLIKQRKE QSRQDEPSNS NQEINSDDRR PQWRREDRIP YQDRESYSQP
AWHHRGPPQR DWKWEKDGFN NTRKNSFPHS LRNGGGPRGR SGWHKGVAGG SSTWFHNHSN
SGGGWLSNSG AVDWNHNGTG RNSSWLSEGT GGFSSWHMNN SNGNWKSSVR STNNWNYSGP
GDKFQPGRNR NSNCQMEDMT MLWNKKSNKS NKYSHDRYNW QRQENDKLGT VATYRGPSEG
FTSDKFPSEG LLDFNFEQLE SQTTKQADTA TSKVSGKNGS AAREKPRRWT PYPSQKTLDL
QSGLKDITGN KSEMIEKPLF DFSLITTGIQ EPQTDETRNS PTQKTQKEIH TGSLNHKASS
DSAASFEVVR QCPTAEKPEQ EHTPNKMPSL KSPLLPCPAT KSLSQKQDPK NISKNTKTNF
FSPGEHSNPS NKPTVEDNHG PYISKLRSSC PHVLKGNKST FGSQKQSGDN LNDTLRKAKE
VLQCHESLQN PLLSTSKSTR NYAKASRNVE ESEKGSLKIE FQVHALEDES DGETSDTEKH
GTKIGTLGSA TTELLSGSTR TADEKEEDDR ILKTSRELST SPCNPIVRQK ESELQMTSAA
SPHPGLLLDL KTSLEDAQVD DSIKSHVSYE TEGFESASLD AELQKSDISQ PSGPLLPELS
KLGFPASLQR DLTRHISLKS KTGVHLPEPN LNSARRIRNI SGHRKSETEK ESGLKPTLRQ
ILNASRRNVN WEQVIQQVTK KKQELGKGLP RFGIEMVPLV QNEQEALDLD GEPDLSSLEG
FQWEGVSISS SPGLARKRSL SESSVIMDRA PSVYSFFSEE GTGKENEPQQ MVSPSNSLRA
GQSQKATMHL KQEVTPRAAS LRTGERAENV ATQRRHSAQL SSDHIIPLMH LAKDLNSQER
SIPPSENQNS QESNGEGNCL SSSASSALAI SSLADAATDS SCTSGAEQND GQSIRKKRRA
TGDGSSPELP SLERKNKRRK IKGKKERSQV DQLLNISLRE EELSKSLQCM DNNLLQARAA
LQTAYVEVQR LLMLKQQITM EMSALRTHRI QILQGLQETY EPSEHPDQVP CSLTRERRNS
RSQTSIDAAL LPTPFFPLFL EPPSSHVSPS PTGASLQITT SPTFQTHGSV PAPDSSVQIK
QEPMSPEQDE NVNAVPPSSA CNVSKELLEA NREISDSCPV YPVITARLSL PESTESFHEP
SQELKFSVEQ RNTRNRENSP SSQSAGLSSI NKEGEEPTKG NSGSEACTSS FLRLSFASET
PLEKEPHSPA DQPEQQAEST LTSAETRGSK KKKKLRKKKS LRAAHVPENS DTEQDVLTVK
PVRKVKAGKL IKGGKVTTST WEDSRTGREQ ESVRDEPDSD SSLEVLEIPN PQLEVVAIDS
SESGEEKPDS PSKKDIWNST EQNPLETSRS GCDEVSSTSE IGTRYKDGIP VSVAETQTVI
SSIKGSKNSS EISSEPGDDD EPTEGSFEGH QAAVNAIQIF GNLLYTCSAD KTVRVYNLVS
RKCIGVFEGH TSKVNCLLVT QTSGKNAALY TGSSDHTIRC YNVKSRECVE QLQLEDRVLC
LHSRWRILYA GLANGTVVTF NIKNNKRLEI FECHGPRAVS CLATAQEGAR KLLVVGSYDC
TISVRDARNG LLLRTLEGHS KTILCMKVVN DLVFSGSSDQ SVHAHNIHTG ELVRIYKGHN
HAVTVVNILG KVMVTACLDK FVRVYELQSH DRLQVYGGHK DMIMCMTIHK SMIYTGCYDG
SIQAVRLNLM QNYRCWWHGC SLIFGVVDHL KQHLLTDHTN PNFQTLKCRW KNCDAFFTAR
KGSKQDAAGH IERHAEDDSK IDS
