HMBX1_HUMAN
ID HMBX1_HUMAN Reviewed; 420 AA.
AC Q6NT76; A4K385; A8K3R8; B4DHY5; D3DSU0; Q3Y6P1; Q96GS5; Q9H701;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Homeobox-containing protein 1 {ECO:0000303|PubMed:16825764};
DE AltName: Full=Homeobox telomere-binding protein 1 {ECO:0000303|PubMed:23685356};
DE AltName: Full=Telomere-associated homeobox-containing protein 1 {ECO:0000303|PubMed:23813958};
GN Name=HMBOX1 {ECO:0000303|PubMed:16825764};
GN Synonyms=HOT1 {ECO:0000303|PubMed:23685356},
GN TAH1 {ECO:0000303|PubMed:23813958};
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=16825764; DOI=10.1159/000093328;
RA Chen S., Saiyin H., Zeng X., Xi J., Liu X., Li X., Yu L.;
RT "Isolation and functional analysis of human HMBOX1, a homeobox containing
RT protein with transcriptional repressor activity.";
RL Cytogenet. Genome Res. 114:131-136(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19757162; DOI=10.1007/s11033-009-9815-9;
RA Zhang M., Chen S., Li Q., Ling Y., Zhang J., Yu L.;
RT "Characterization of a novel human HMBOX1 splicing variant lacking the
RT homeodomain and with attenuated transcription repressor activity.";
RL Mol. Biol. Rep. 37:2767-2772(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Caudate nucleus, and Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-420 (ISOFORM 3).
RA Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Tang Z., Wen S., Lin L., Yang S.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19728927; DOI=10.1038/cmi.2009.35;
RA Dai J., Wu L., Zhang C., Zheng X., Tian Z., Zhang J.;
RT "Recombinant expression of a novel human transcriptional repressor HMBOX1
RT and preparation of anti-HMBOX1 monoclonal antibody.";
RL Cell. Mol. Immunol. 6:261-268(2009).
RN [8]
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 [9]
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 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23813958; DOI=10.1242/jcs.128512;
RA Feng X., Luo Z., Jiang S., Li F., Han X., Hu Y., Wang D., Zhao Y., Ma W.,
RA Liu D., Huang J., Songyang Z.;
RT "The telomere-associated homeobox-containing protein TAH1/HMBOX1
RT participates in telomere maintenance in ALT cells.";
RL J. Cell Sci. 126:3982-3989(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-170, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-174; LYS-217 AND
RP LYS-413, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-131; LYS-161; LYS-174;
RP LYS-217; LYS-310 AND LYS-413, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [18]
RP STRUCTURE BY NMR OF 268-350.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the homeobox domain of the human hypothetical
RT protein FLJ21616.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 233-345 IN COMPLEX WITH DNA,
RP FUNCTION, ASSOCIATION WITH THE TELOMERASE COMPLEX, INTERACTION WITH DKC1;
RP XRCC6 AND COIL, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ARG-271;
RP LYS-325; TYR-327; ARG-334; LYS-335; LYS-338 AND ARG-339, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=23685356; DOI=10.1038/emboj.2013.105;
RA Kappei D., Butter F., Benda C., Scheibe M., Draskovic I., Stevense M.,
RA Novo C.L., Basquin C., Araki M., Araki K., Krastev D.B., Kittler R.,
RA Jessberger R., Londono-Vallejo J.A., Mann M., Buchholz F.;
RT "HOT1 is a mammalian direct telomere repeat-binding protein contributing to
RT telomerase recruitment.";
RL EMBO J. 32:1681-1701(2013).
CC -!- FUNCTION: Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA
CC (PubMed:23813958, PubMed:23685356). Associates with the telomerase
CC complex at sites of active telomere processing and positively regulates
CC telomere elongation (PubMed:23685356). Important for TERT binding to
CC chromatin, indicating a role in recruitment of the telomerase complex
CC to telomeres (By similarity). Also plays a role in the alternative
CC lengthening of telomeres (ALT) pathway in telomerase-negative cells
CC where it promotes formation and/or maintenance of ALT-associated
CC promyelocytic leukemia bodies (APBs) (PubMed:23813958). Enhances
CC formation of telomere C-circles in ALT cells, suggesting a possible
CC role in telomere recombination (PubMed:23813958). Might also be
CC involved in the DNA damage response at telomeres (PubMed:23813958).
CC {ECO:0000250|UniProtKB:Q8BJA3, ECO:0000269|PubMed:23685356,
CC ECO:0000269|PubMed:23813958}.
CC -!- SUBUNIT: Associates with the telomerase holoenzyme complex. Interacts
CC with DKC1, XRCC6 and COIL. {ECO:0000269|PubMed:23685356}.
CC -!- INTERACTION:
CC Q6NT76; Q9NX38: ABITRAM; NbExp=6; IntAct=EBI-2549423, EBI-9105722;
CC Q6NT76; Q6ZN18-2: AEBP2; NbExp=6; IntAct=EBI-2549423, EBI-10255023;
CC Q6NT76; A1A5B0: ANKRD36; NbExp=3; IntAct=EBI-2549423, EBI-14100900;
CC Q6NT76; Q9H672: ASB7; NbExp=3; IntAct=EBI-2549423, EBI-3916346;
CC Q6NT76; Q9H672-2: ASB7; NbExp=3; IntAct=EBI-2549423, EBI-12104328;
CC Q6NT76; P48047: ATP5PO; NbExp=3; IntAct=EBI-2549423, EBI-355815;
CC Q6NT76; A0A0A0MR97: BAZ2B; NbExp=3; IntAct=EBI-2549423, EBI-11985607;
CC Q6NT76; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2549423, EBI-10181188;
CC Q6NT76; O95696: BRD1; NbExp=3; IntAct=EBI-2549423, EBI-714754;
CC Q6NT76; Q13895: BYSL; NbExp=8; IntAct=EBI-2549423, EBI-358049;
CC Q6NT76; Q9H7E9: C8orf33; NbExp=6; IntAct=EBI-2549423, EBI-715389;
CC Q6NT76; Q9H257: CARD9; NbExp=3; IntAct=EBI-2549423, EBI-751319;
CC Q6NT76; Q9HC52: CBX8; NbExp=8; IntAct=EBI-2549423, EBI-712912;
CC Q6NT76; P51959: CCNG1; NbExp=3; IntAct=EBI-2549423, EBI-3905829;
CC Q6NT76; O00311: CDC7; NbExp=3; IntAct=EBI-2549423, EBI-374980;
CC Q6NT76; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-2549423, EBI-979174;
CC Q6NT76; Q07002: CDK18; NbExp=3; IntAct=EBI-2549423, EBI-746238;
CC Q6NT76; O75553: DAB1; NbExp=3; IntAct=EBI-2549423, EBI-7875264;
CC Q6NT76; O60832: DKC1; NbExp=2; IntAct=EBI-2549423, EBI-713091;
CC Q6NT76; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-2549423, EBI-2795449;
CC Q6NT76; P63167: DYNLL1; NbExp=5; IntAct=EBI-2549423, EBI-349105;
CC Q6NT76; Q96FJ2: DYNLL2; NbExp=4; IntAct=EBI-2549423, EBI-742371;
CC Q6NT76; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2549423, EBI-744099;
CC Q6NT76; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-2549423, EBI-751248;
CC Q6NT76; Q3B820: FAM161A; NbExp=6; IntAct=EBI-2549423, EBI-719941;
CC Q6NT76; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-2549423, EBI-19153639;
CC Q6NT76; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-2549423, EBI-10247271;
CC Q6NT76; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2549423, EBI-6658203;
CC Q6NT76; O95363: FARS2; NbExp=3; IntAct=EBI-2549423, EBI-2513774;
CC Q6NT76; Q92914: FGF11; NbExp=3; IntAct=EBI-2549423, EBI-11987787;
CC Q6NT76; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-2549423, EBI-744935;
CC Q6NT76; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-2549423, EBI-741729;
CC Q6NT76; P51116: FXR2; NbExp=3; IntAct=EBI-2549423, EBI-740459;
CC Q6NT76; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-2549423, EBI-7960826;
CC Q6NT76; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-2549423, EBI-746682;
CC Q6NT76; O15499: GSC2; NbExp=3; IntAct=EBI-2549423, EBI-19954058;
CC Q6NT76; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-2549423, EBI-2549423;
CC Q6NT76; Q9C086: INO80B; NbExp=3; IntAct=EBI-2549423, EBI-715611;
CC Q6NT76; O94829: IPO13; NbExp=3; IntAct=EBI-2549423, EBI-747310;
CC Q6NT76; Q92993: KAT5; NbExp=6; IntAct=EBI-2549423, EBI-399080;
CC Q6NT76; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2549423, EBI-8472129;
CC Q6NT76; P25800: LMO1; NbExp=3; IntAct=EBI-2549423, EBI-8639312;
CC Q6NT76; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2549423, EBI-11742507;
CC Q6NT76; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2549423, EBI-739832;
CC Q6NT76; Q9H213: MAGEH1; NbExp=3; IntAct=EBI-2549423, EBI-473834;
CC Q6NT76; Q96EZ8: MCRS1; NbExp=8; IntAct=EBI-2549423, EBI-348259;
CC Q6NT76; P50221: MEOX1; NbExp=3; IntAct=EBI-2549423, EBI-2864512;
CC Q6NT76; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2549423, EBI-16439278;
CC Q6NT76; P55081: MFAP1; NbExp=6; IntAct=EBI-2549423, EBI-1048159;
CC Q6NT76; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-2549423, EBI-14086479;
CC Q6NT76; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-2549423, EBI-399246;
CC Q6NT76; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-2549423, EBI-10288852;
CC Q6NT76; Q15014: MORF4L2; NbExp=3; IntAct=EBI-2549423, EBI-399257;
CC Q6NT76; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-2549423, EBI-5453723;
CC Q6NT76; Q13084: MRPL28; NbExp=3; IntAct=EBI-2549423, EBI-723426;
CC Q6NT76; E9PJI5: NPIPA7; NbExp=3; IntAct=EBI-2549423, EBI-10177044;
CC Q6NT76; Q02548: PAX5; NbExp=3; IntAct=EBI-2549423, EBI-296331;
CC Q6NT76; P26367: PAX6; NbExp=3; IntAct=EBI-2549423, EBI-747278;
CC Q6NT76; O75928-2: PIAS2; NbExp=3; IntAct=EBI-2549423, EBI-348567;
CC Q6NT76; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2549423, EBI-79165;
CC Q6NT76; P78356: PIP4K2B; NbExp=5; IntAct=EBI-2549423, EBI-947090;
CC Q6NT76; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-2549423, EBI-10276663;
CC Q6NT76; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-2549423, EBI-10320765;
CC Q6NT76; Q13131: PRKAA1; NbExp=3; IntAct=EBI-2549423, EBI-1181405;
CC Q6NT76; P54646: PRKAA2; NbExp=3; IntAct=EBI-2549423, EBI-1383852;
CC Q6NT76; Q99633: PRPF18; NbExp=3; IntAct=EBI-2549423, EBI-2798416;
CC Q6NT76; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-2549423, EBI-1504830;
CC Q6NT76; Q96HR9: REEP6; NbExp=3; IntAct=EBI-2549423, EBI-750345;
CC Q6NT76; P32969: RPL9P9; NbExp=6; IntAct=EBI-2549423, EBI-358122;
CC Q6NT76; P62851: RPS25; NbExp=3; IntAct=EBI-2549423, EBI-353054;
CC Q6NT76; Q9HAJ7: SAP30L; NbExp=3; IntAct=EBI-2549423, EBI-2340040;
CC Q6NT76; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2549423, EBI-748391;
CC Q6NT76; O00560: SDCBP; NbExp=3; IntAct=EBI-2549423, EBI-727004;
CC Q6NT76; Q9H788: SH2D4A; NbExp=6; IntAct=EBI-2549423, EBI-747035;
CC Q6NT76; P08579: SNRPB2; NbExp=3; IntAct=EBI-2549423, EBI-1053651;
CC Q6NT76; Q13573: SNW1; NbExp=3; IntAct=EBI-2549423, EBI-632715;
CC Q6NT76; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-2549423, EBI-10246152;
CC Q6NT76; Q32MN6: TBP; NbExp=3; IntAct=EBI-2549423, EBI-10239991;
CC Q6NT76; Q15560: TCEA2; NbExp=3; IntAct=EBI-2549423, EBI-710310;
CC Q6NT76; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-2549423, EBI-954696;
CC Q6NT76; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2549423, EBI-10241197;
CC Q6NT76; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-2549423, EBI-12261790;
CC Q6NT76; P26368-2: U2AF2; NbExp=3; IntAct=EBI-2549423, EBI-11097439;
CC Q6NT76; A0AVT1: UBA6; NbExp=3; IntAct=EBI-2549423, EBI-5282516;
CC Q6NT76; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2549423, EBI-10180829;
CC Q6NT76; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-2549423, EBI-720977;
CC Q6NT76; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-2549423, EBI-12227803;
CC Q6NT76; Q15906: VPS72; NbExp=3; IntAct=EBI-2549423, EBI-399189;
CC Q6NT76; P19544-6: WT1; NbExp=3; IntAct=EBI-2549423, EBI-11745701;
CC Q6NT76; P12956: XRCC6; NbExp=2; IntAct=EBI-2549423, EBI-353208;
CC Q6NT76; O43167: ZBTB24; NbExp=3; IntAct=EBI-2549423, EBI-744471;
CC Q6NT76; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-2549423, EBI-3918996;
CC Q6NT76; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-2549423, EBI-8656416;
CC Q6NT76; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-2549423, EBI-2682299;
CC Q6NT76; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-2549423, EBI-17634549;
CC Q6NT76; P15622-3: ZNF250; NbExp=3; IntAct=EBI-2549423, EBI-10177272;
CC Q6NT76; Q9Y3M9: ZNF337; NbExp=3; IntAct=EBI-2549423, EBI-714987;
CC Q6NT76; Q8TAU3: ZNF417; NbExp=6; IntAct=EBI-2549423, EBI-740727;
CC Q6NT76; Q9P0T4: ZNF581; NbExp=6; IntAct=EBI-2549423, EBI-745520;
CC Q6NT76; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-2549423, EBI-6427977;
CC Q6NT76; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-2549423, EBI-16429014;
CC Q6NT76-2; P51116: FXR2; NbExp=3; IntAct=EBI-10212206, EBI-740459;
CC Q6NT76-2; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-10212206, EBI-399246;
CC Q6NT76-2; Q96HR9: REEP6; NbExp=3; IntAct=EBI-10212206, EBI-750345;
CC Q6NT76-2; Q86XK3: SFR1; NbExp=3; IntAct=EBI-10212206, EBI-1104535;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16825764,
CC ECO:0000269|PubMed:19728927}. Cytoplasm {ECO:0000269|PubMed:16825764,
CC ECO:0000269|PubMed:19728927}. Chromosome, telomere
CC {ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:23813958}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:23685356}. Nucleus, PML body
CC {ECO:0000269|PubMed:23813958}. Note=Predominantly detected in cytoplasm
CC (PubMed:16825764, PubMed:19728927). Localizes in a dynamic manner to
CC actively processed telomeres (PubMed:23685356). Localizes to the
CC periphery of Cajal bodies (PubMed:23685356). Associates with PML
CC nuclear bodies in telomerase-negative cells (PubMed:23813958).
CC {ECO:0000269|PubMed:16825764, ECO:0000269|PubMed:19728927,
CC ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:23813958}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus
CC {ECO:0000269|PubMed:19757162}. Cytoplasm {ECO:0000269|PubMed:19757162}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=HMBOX1A;
CC IsoId=Q6NT76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NT76-2; Sequence=VSP_018112, VSP_018113;
CC Name=3;
CC IsoId=Q6NT76-3; Sequence=VSP_018111;
CC Name=4; Synonyms=HMBOX1b;
CC IsoId=Q6NT76-4; Sequence=VSP_038983, VSP_038984;
CC Name=5;
CC IsoId=Q6NT76-5; Sequence=VSP_018112, VSP_038985;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in pancreas, brain, spleen,
CC placenta, prostate, thymus, liver, heart, bone marrow, skeletal muscle,
CC stomach, uterus, testis, kidney, ovary, colon, lung, cardiac muscle and
CC thyroid gland. {ECO:0000269|PubMed:16825764,
CC ECO:0000269|PubMed:19728927, ECO:0000269|PubMed:19757162}.
CC -!- DOMAIN: The homeobox domain is required for binding to 5'-TTAGGG-3'
CC repeats in telomeres, and for telomere localization.
CC {ECO:0000269|PubMed:23685356, ECO:0000269|PubMed:23813958}.
CC -!- CAUTION: Reported to have transcriptional repression activity in vitro
CC (PubMed:16825764, PubMed:19757162). However, it is unclear whether this
CC protein has any function in transcription in vivo.
CC {ECO:0000269|PubMed:16825764, ECO:0000269|PubMed:19757162,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15099.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY522342; AAS76643.1; -; mRNA.
DR EMBL; DQ269478; ABB82947.1; -; mRNA.
DR EMBL; AK025269; BAB15099.1; ALT_INIT; mRNA.
DR EMBL; AK290683; BAF83372.1; -; mRNA.
DR EMBL; AK295320; BAG58297.1; -; mRNA.
DR EMBL; CH471080; EAW63496.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63499.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63500.1; -; Genomic_DNA.
DR EMBL; BC009259; AAH09259.2; -; mRNA.
DR EMBL; BC069242; AAH69242.1; -; mRNA.
DR EMBL; DQ153248; AAZ81565.1; -; mRNA.
DR CCDS; CCDS6071.1; -. [Q6NT76-1]
DR CCDS; CCDS83273.1; -. [Q6NT76-5]
DR CCDS; CCDS83274.1; -. [Q6NT76-2]
DR RefSeq; NP_001129198.1; NM_001135726.2. [Q6NT76-1]
DR RefSeq; NP_001311311.1; NM_001324382.1. [Q6NT76-1]
DR RefSeq; NP_001311312.1; NM_001324383.1.
DR RefSeq; NP_001311313.1; NM_001324384.1.
DR RefSeq; NP_001311314.1; NM_001324385.1.
DR RefSeq; NP_001311315.1; NM_001324386.1.
DR RefSeq; NP_001311316.1; NM_001324387.1. [Q6NT76-3]
DR RefSeq; NP_001311317.1; NM_001324388.1. [Q6NT76-3]
DR RefSeq; NP_001311318.1; NM_001324389.1.
DR RefSeq; NP_001311319.1; NM_001324390.1.
DR RefSeq; NP_001311320.1; NM_001324391.1. [Q6NT76-2]
DR RefSeq; NP_001311321.1; NM_001324392.1. [Q6NT76-2]
DR RefSeq; NP_001311322.1; NM_001324393.1.
DR RefSeq; NP_001311323.1; NM_001324394.1.
DR RefSeq; NP_001311324.1; NM_001324395.1.
DR RefSeq; NP_001317427.1; NM_001330498.1. [Q6NT76-5]
DR RefSeq; NP_078843.2; NM_024567.4. [Q6NT76-1]
DR RefSeq; XP_016869314.1; XM_017013825.1. [Q6NT76-4]
DR PDB; 2CUF; NMR; -; A=268-350.
DR PDB; 4J19; X-ray; 2.90 A; A/B=233-345.
DR PDBsum; 2CUF; -.
DR PDBsum; 4J19; -.
DR AlphaFoldDB; Q6NT76; -.
DR BMRB; Q6NT76; -.
DR SMR; Q6NT76; -.
DR BioGRID; 122750; 130.
DR IntAct; Q6NT76; 122.
DR MINT; Q6NT76; -.
DR STRING; 9606.ENSP00000380516; -.
DR GlyGen; Q6NT76; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6NT76; -.
DR PhosphoSitePlus; Q6NT76; -.
DR BioMuta; HMBOX1; -.
DR DMDM; 74758116; -.
DR EPD; Q6NT76; -.
DR jPOST; Q6NT76; -.
DR MassIVE; Q6NT76; -.
DR MaxQB; Q6NT76; -.
DR PaxDb; Q6NT76; -.
DR PeptideAtlas; Q6NT76; -.
DR PRIDE; Q6NT76; -.
DR ProteomicsDB; 66662; -. [Q6NT76-1]
DR ProteomicsDB; 66663; -. [Q6NT76-2]
DR ProteomicsDB; 66664; -. [Q6NT76-3]
DR ProteomicsDB; 66665; -. [Q6NT76-4]
DR ProteomicsDB; 66666; -. [Q6NT76-5]
DR TopDownProteomics; Q6NT76-4; -. [Q6NT76-4]
DR Antibodypedia; 10471; 167 antibodies from 27 providers.
DR DNASU; 79618; -.
DR Ensembl; ENST00000287701.15; ENSP00000287701.10; ENSG00000147421.18. [Q6NT76-1]
DR Ensembl; ENST00000397358.7; ENSP00000380516.3; ENSG00000147421.18. [Q6NT76-1]
DR Ensembl; ENST00000521516.5; ENSP00000430238.1; ENSG00000147421.18. [Q6NT76-4]
DR Ensembl; ENST00000524238.3; ENSP00000430110.1; ENSG00000147421.18. [Q6NT76-5]
DR Ensembl; ENST00000558662.5; ENSP00000453211.1; ENSG00000147421.18. [Q6NT76-2]
DR GeneID; 79618; -.
DR KEGG; hsa:79618; -.
DR MANE-Select; ENST00000287701.15; ENSP00000287701.10; NM_001135726.3; NP_001129198.1.
DR UCSC; uc003xhd.5; human. [Q6NT76-1]
DR CTD; 79618; -.
DR DisGeNET; 79618; -.
DR GeneCards; HMBOX1; -.
DR HGNC; HGNC:26137; HMBOX1.
DR HPA; ENSG00000147421; Low tissue specificity.
DR MIM; 618610; gene.
DR neXtProt; NX_Q6NT76; -.
DR OpenTargets; ENSG00000147421; -.
DR PharmGKB; PA143485490; -.
DR VEuPathDB; HostDB:ENSG00000147421; -.
DR eggNOG; ENOG502QQSR; Eukaryota.
DR GeneTree; ENSGT00940000154928; -.
DR HOGENOM; CLU_052355_1_0_1; -.
DR InParanoid; Q6NT76; -.
DR OMA; PXAAILE; -.
DR OrthoDB; 1342373at2759; -.
DR PhylomeDB; Q6NT76; -.
DR TreeFam; TF320327; -.
DR PathwayCommons; Q6NT76; -.
DR SignaLink; Q6NT76; -.
DR SIGNOR; Q6NT76; -.
DR BioGRID-ORCS; 79618; 14 hits in 1100 CRISPR screens.
DR ChiTaRS; HMBOX1; human.
DR EvolutionaryTrace; Q6NT76; -.
DR GenomeRNAi; 79618; -.
DR Pharos; Q6NT76; Tbio.
DR PRO; PR:Q6NT76; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6NT76; protein.
DR Bgee; ENSG00000147421; Expressed in colonic epithelium and 199 other tissues.
DR ExpressionAtlas; Q6NT76; baseline and differential.
DR Genevisible; Q6NT76; HS.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; ISS:BHF-UCL.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0051972; P:regulation of telomerase activity; IDA:BHF-UCL.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR040363; HMBOX1.
DR InterPro; IPR006899; HNF-1_N.
DR InterPro; IPR044869; HNF-1_POU.
DR InterPro; IPR044866; HNF_P1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR PANTHER; PTHR14618; PTHR14618; 1.
DR Pfam; PF04814; HNF-1_N; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS51937; HNF_P1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51936; POU_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm; DNA-binding;
KW Homeobox; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Telomere; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..420
FT /note="Homeobox-containing protein 1"
FT /id="PRO_0000233287"
FT DOMAIN 18..49
FT /note="HNF-p1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01286"
FT DOMAIN 145..241
FT /note="POU-specific atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01285"
FT DNA_BIND 267..341
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000269|PubMed:23685356"
FT REGION 56..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 335
FT /note="Critical for recognition and binding of 5'-TTAGGG-3'
FT motifs in telomeric DNA"
FT /evidence="ECO:0000269|PubMed:23685356"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
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 VAR_SEQ 284..304
FT /note="SYFNENQYPDEAKREEIANAC -> RNTWSPERRMEENKWKLLSAG (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:19757162"
FT /id="VSP_038983"
FT VAR_SEQ 305..420
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19757162"
FT /id="VSP_038984"
FT VAR_SEQ 344..345
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_018111"
FT VAR_SEQ 344
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_018112"
FT VAR_SEQ 375
FT /note="Q -> QDTWQVRNGEEEEGRSSEGGREAEK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038985"
FT VAR_SEQ 377..420
FT /note="DSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD -> TWQV
FT RNGEEEEGRSSEGGREAEKVEEERRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018113"
FT MUTAGEN 271
FT /note="R->A: Abolishes binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 325
FT /note="K->E: Abolishes binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 327
FT /note="Y->A: Impairs binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 334
FT /note="R->A: Impairs binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 335
FT /note="K->A: Abolishes binding to telomeric 5'-TTAGGG-3'
FT motif. Confers binding to the non-telomeric 5'-GTGAGT-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 338
FT /note="K->A: Impairs binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT MUTAGEN 339
FT /note="R->A: Abolishes binding to telomeric 5'-TTAGGG-3'
FT motif."
FT /evidence="ECO:0000269|PubMed:23685356"
FT CONFLICT 167
FT /note="R -> G (in Ref. 6; AAZ81565)"
FT /evidence="ECO:0000305"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:4J19"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:4J19"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:4J19"
FT HELIX 323..343
FT /evidence="ECO:0007829|PDB:4J19"
SQ SEQUENCE 420 AA; 47278 MW; BB47AB7DE3B96996 CRC64;
MLSSFPVVLL ETMSHYTDEP RFTIEQIDLL QRLRRTGMTK HEILHALETL DRLDQEHSDK
FGRRSSYGGS SYGNSTNNVP ASSSTATAST QTQHSGMSPS PSNSYDTSPQ PCTTNQNGRE
NNERLSTSNG KMSPTRYHAN SMGQRSYSFE ASEEDLDVDD KVEELMRRDS SVIKEEIKAF
LANRRISQAV VAQVTGISQS RISHWLLQQG SDLSEQKKRA FYRWYQLEKT NPGATLSMRP
APIPIEDPEW RQTPPPVSAT SGTFRLRRGS RFTWRKECLA VMESYFNENQ YPDEAKREEI
ANACNAVIQK PGKKLSDLER VTSLKVYNWF ANRRKEIKRR ANIEAAILES HGIDVQSPGG
HSNSDDVDGN DYSEQDDSTS HSDHQDPISL AVEMAAVNHT ILALARQGAN EIKTEALDDD
