HMBX1_MOUSE
ID HMBX1_MOUSE Reviewed; 419 AA.
AC Q8BJA3; Q80WC2; Q8BWE7; Q99LV1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Homeobox-containing protein 1;
GN Name=Hmbox1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-419 (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Colon, Mammary gland, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION 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 (By
CC similarity). Associates with the telomerase complex at sites of active
CC telomere processing and positively regulates telomere elongation (By
CC similarity). Important for TERT binding to chromatin, indicating a role
CC in recruitment of the telomerase complex to telomeres
CC (PubMed:23685356). Also plays a role in the alternative lengthening of
CC telomeres (ALT) pathway in telomerase-negative cells where it promotes
CC formation and/or maintenance of ALT-associated promyelocytic leukemia
CC bodies (APBs) (By similarity). Enhances formation of telomere C-circles
CC in ALT cells, suggesting a possible role in telomere recombination (By
CC similarity). Might also be involved in the DNA damage response at
CC telomeres (By similarity). {ECO:0000250|UniProtKB:Q6NT76,
CC ECO:0000269|PubMed:23685356}.
CC -!- SUBUNIT: Associates with the telomerase holoenzyme complex. Interacts
CC with DKC1, XRCC6 and COIL. {ECO:0000250|UniProtKB:Q6NT76}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23685356}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6NT76}. Chromosome, telomere
CC {ECO:0000269|PubMed:23685356}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q6NT76}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q6NT76}. Note=Predominantly detected in
CC cytoplasm. Localizes in a dynamic manner to actively processed
CC telomeres. Localizes to the periphery of Cajal bodies. Associates with
CC PML nuclear bodies in telomerase-negative cells.
CC {ECO:0000250|UniProtKB:Q6NT76}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BJA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJA3-2; Sequence=VSP_018114, VSP_018115;
CC Name=3;
CC IsoId=Q8BJA3-3; Sequence=VSP_018116;
CC Name=4;
CC IsoId=Q8BJA3-4; Sequence=VSP_018115;
CC -!- DOMAIN: The homeobox domain is required for binding to 5'-TTAGGG-3'
CC repeats in telomeres, and for telomere localization.
CC {ECO:0000250|UniProtKB:Q6NT76}.
CC -!- CAUTION: Reported to have transcriptional repression activity in vitro.
CC However, it is unclear whether this protein has any function in
CC transcription in vivo. {ECO:0000250|UniProtKB:Q6NT76}.
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; AK052729; BAC35118.1; -; mRNA.
DR EMBL; AK089782; BAC40961.1; -; mRNA.
DR EMBL; BC002212; AAH02212.1; -; mRNA.
DR EMBL; BC051457; AAH51457.1; -; mRNA.
DR CCDS; CCDS36955.1; -. [Q8BJA3-1]
DR CCDS; CCDS84149.1; -. [Q8BJA3-2]
DR RefSeq; NP_001334555.1; NM_001347626.1.
DR RefSeq; NP_001334556.1; NM_001347627.1. [Q8BJA3-2]
DR RefSeq; NP_796312.2; NM_177338.6. [Q8BJA3-1]
DR RefSeq; XP_011243336.1; XM_011245034.2. [Q8BJA3-2]
DR RefSeq; XP_011243337.1; XM_011245035.2. [Q8BJA3-4]
DR RefSeq; XP_011243338.1; XM_011245036.2. [Q8BJA3-4]
DR AlphaFoldDB; Q8BJA3; -.
DR BMRB; Q8BJA3; -.
DR SMR; Q8BJA3; -.
DR BioGRID; 230121; 1.
DR IntAct; Q8BJA3; 9.
DR MINT; Q8BJA3; -.
DR STRING; 10090.ENSMUSP00000135372; -.
DR iPTMnet; Q8BJA3; -.
DR PhosphoSitePlus; Q8BJA3; -.
DR jPOST; Q8BJA3; -.
DR MaxQB; Q8BJA3; -.
DR PaxDb; Q8BJA3; -.
DR PRIDE; Q8BJA3; -.
DR ProteomicsDB; 269573; -. [Q8BJA3-1]
DR ProteomicsDB; 269574; -. [Q8BJA3-2]
DR ProteomicsDB; 269575; -. [Q8BJA3-3]
DR ProteomicsDB; 269576; -. [Q8BJA3-4]
DR Antibodypedia; 10471; 167 antibodies from 27 providers.
DR DNASU; 219150; -.
DR Ensembl; ENSMUST00000022544; ENSMUSP00000022544; ENSMUSG00000021972. [Q8BJA3-2]
DR Ensembl; ENSMUST00000067843; ENSMUSP00000066905; ENSMUSG00000021972. [Q8BJA3-1]
DR GeneID; 219150; -.
DR KEGG; mmu:219150; -.
DR UCSC; uc007uip.1; mouse. [Q8BJA3-4]
DR UCSC; uc007uiq.1; mouse. [Q8BJA3-2]
DR UCSC; uc007uir.1; mouse. [Q8BJA3-1]
DR CTD; 79618; -.
DR MGI; MGI:2445066; Hmbox1.
DR VEuPathDB; HostDB:ENSMUSG00000021972; -.
DR eggNOG; ENOG502QQSR; Eukaryota.
DR GeneTree; ENSGT00940000154928; -.
DR InParanoid; Q8BJA3; -.
DR OrthoDB; 1342373at2759; -.
DR PhylomeDB; Q8BJA3; -.
DR BioGRID-ORCS; 219150; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Hmbox1; mouse.
DR PRO; PR:Q8BJA3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BJA3; protein.
DR Bgee; ENSMUSG00000021972; Expressed in undifferentiated genital tubercle and 259 other tissues.
DR ExpressionAtlas; Q8BJA3; baseline and differential.
DR Genevisible; Q8BJA3; MM.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IMP:BHF-UCL.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0051972; P:regulation of telomerase activity; ISO:MGI.
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 Alternative splicing; Chromosome; Cytoplasm; DNA-binding; Homeobox;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..419
FT /note="Homeobox-containing protein 1"
FT /id="PRO_0000233288"
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 REGION 56..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..148
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:0000250|UniProtKB:Q6NT76"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NT76"
FT VAR_SEQ 343
FT /note="I -> IE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018114"
FT VAR_SEQ 375..419
FT /note="DDSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD -> SSF
FT AGALIQLERQKGPPGCQQLPVLSGLL (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018115"
FT VAR_SEQ 376..419
FT /note="DSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD -> TWQA
FT RNGEEEEERSSEGGREAEKVEEERRI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018116"
SQ SEQUENCE 419 AA; 47116 MW; 3F204060F1D0AE70 CRC64;
MLSSFPVVLL ETMSHYTDEP RFTIEQIDLL QRLRRTGMTK HEILHALETL DRLDQEHSDK
FGRRSSYGGS SYGNSTNNVP ASSSTATAST QTQHSGMSPS PSNSYDTSPL PCTTNQNGRE
NNDRLSTSNG KMSPSRYHAN SMGQRSYSFE ASEEDLDVDD KVEELMRRDS SVIKEEIKAF
LANRRISQAV VAQVTGISQS RISHWLLQQG SDLSEQKKRA FYRWYQLEKT NPGATLSMRP
APIPIEDPEW RQTPPPVSAT PGTFRLRRGS RFTWRKECLA VMESYFNENQ YPDEAKREEI
ANACNAVIQK PGKKLSDLER VTSLKVYNWF ANRRKEIKRR ANIAAILESH GIDVQSPGGH
SNSDDVDGND YSEQDDSTSH SDHQDPISLA VEMAAVNHTI LALARQGANE IKTEALDDD
