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Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)

 RUNX2_HUMAN             Reviewed;         521 AA.
Q13950; O14614; O14615; O95181;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
05-DEC-2018, entry version 189.
RecName: Full=Runt-related transcription factor 2;
AltName: Full=Acute myeloid leukemia 3 protein;
AltName: Full=Core-binding factor subunit alpha-1;
Short=CBF-alpha-1;
AltName: Full=Oncogene AML-3;
AltName: Full=Osteoblast-specific transcription factor 2;
Short=OSF-2;
AltName: Full=Polyomavirus enhancer-binding protein 2 alpha A subunit;
Short=PEA2-alpha A;
Short=PEBP2-alpha A;
AltName: Full=SL3-3 enhancer factor 1 alpha A subunit;
AltName: Full=SL3/AKV core-binding factor alpha A subunit;
Name=RUNX2; Synonyms=AML3, CBFA1, OSF2, PEBP2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANT CLCD
ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-84 INS, VARIANT 78-ALA--ALA-83
DEL, AND INVOLVEMENT IN CLCD.
PubMed=9182765; DOI=10.1016/S0092-8674(00)80260-3;
Mundlos S., Otto F., Mundlos C., Mulliken J.B., Aylsworth A.S.,
Albright S., Lindhout D., Cole W.G., Henn W., Knoll J.H.M., Owen M.J.,
Mertelsmann R., Zabel B.U., Olsen B.R.;
"Mutations involving the transcription factor CBFA1 cause
cleidocranial dysplasia.";
Cell 89:773-779(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 3).
PubMed=9434946; DOI=10.1007/s003359900679;
Geoffroy V., Corral D.A., Zhou L., Lee B., Karsenty G.;
"Genomic organization, expression of the human CBFA1 gene, and
evidence for an alternative splicing event affecting protein
function.";
Mamm. Genome 9:54-57(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-19 (ISOFORM 1).
PubMed=9651525; DOI=10.1016/S0378-1119(98)00227-3;
Xiao Z.S., Thomas R., Hinson T.K., Quarles L.D.;
"Genomic structure and isoform expression of the mouse, rat and human
Cbfa1/Osf2 transcription factor.";
Gene 214:187-197(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 60-521 (ISOFORM 3).
PubMed=9233771; DOI=10.1038/sj.onc.1201352;
Zhang Y.-W., Bae S.-C., Takahashi E., Ito Y.;
"The cDNA cloning of the transcripts of human PEBP2alphaA/CBFA1 mapped
to 6p12.3-p21.1, the locus for cleidocranial dysplasia.";
Oncogene 15:367-371(1997).
[6]
INTERACTION WITH XRCC5 AND XRCC6.
TISSUE=Osteoblast;
PubMed=12145306; DOI=10.1074/jbc.M206482200;
Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S.,
Ornitz D.M., Towler D.A.;
"Regulation of osteocalcin gene expression by a novel Ku antigen
transcription factor complex.";
J. Biol. Chem. 277:37280-37291(2002).
[7]
INTERACTION WITH KAT6A AND KAT6B, AND FUNCTION.
PubMed=11965546; DOI=10.1038/sj.onc.1205367;
Pelletier N., Champagne N., Stifani S., Yang X.-J.;
"MOZ and MORF histone acetyltransferases interact with the Runt-domain
transcription factor Runx2.";
Oncogene 21:2729-2740(2002).
[8]
INTERACTION WITH CCNB1, PHOSPHORYLATION AT SER-451 BY CDK1, AND
MUTAGENESIS OF SER-451.
PubMed=16407259; DOI=10.1074/jbc.M508162200;
Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.;
"Cell cycle-dependent phosphorylation of the RUNX2 transcription
factor by cdc2 regulates endothelial cell proliferation.";
J. Biol. Chem. 281:7118-7128(2006).
[9]
INTERACTION WITH FOXP3.
PubMed=17377532; DOI=10.1038/nature05673;
Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T.,
Miyachi Y., Tsukada T., Sakaguchi S.;
"Foxp3 controls regulatory T-cell function by interacting with
AML1/Runx1.";
Nature 446:685-689(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
INVOLVEMENT IN MDMHB.
PubMed=23290074; DOI=10.1016/j.ajhg.2012.12.001;
FORGE Canada Consortium;
Moffatt P., Ben Amor M., Glorieux F.H., Roschger P., Klaushofer K.,
Schwartzentruber J.A., Paterson A.D., Hu P., Marshall C.,
Fahiminiya S., Majewski J., Beaulieu C.L., Boycott K.M., Rauch F.;
"Metaphyseal dysplasia with maxillary hypoplasia and brachydactyly is
caused by a duplication in RUNX2.";
Am. J. Hum. Genet. 92:252-258(2013).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[13]
VARIANTS CLCD ARG-175 AND ASN-191.
PubMed=9207800; DOI=10.1038/ng0797-307;
Lee B., Thirunavukkarasu K., Zhou L., Pastore L., Baldini A.,
Hecht J., Geoffroy V., Ducy P., Karsenty G.;
"Missense mutations abolishing DNA binding of the osteoblast-specific
transcription factor OSF2/CBFA1 in cleidocranial dysplasia.";
Nat. Genet. 16:307-310(1997).
[14]
VARIANTS CLCD ARG-113; ARG-118; CYS-121; ARG-123; ARG-205; GLN-225 AND
TRP-225, AND VARIANT SER-511.
PubMed=10521292; DOI=10.1086/302622;
Quack I., Vonderstrass B., Stock M., Aylsworth A.S., Becker A.,
Brueton L., Lee P.J., Majewski F., Mulliken J.B., Suri M., Zenker M.,
Mundlos S., Otto F.;
"Mutation analysis of core binding factor A1 in patients with
cleidocranial dysplasia.";
Am. J. Hum. Genet. 65:1268-1278(1999).
[15]
VARIANTS CLCD ASN-133 DEL; GLN-169; ARG-175; GLN-190; ASN-191;
CYS-193; PHE-199; ALA-200; ARG-209 AND GLN-225.
PubMed=10545612; DOI=10.1093/hmg/8.12.2311;
Zhou G., Chen Y., Zhou L., Thirunavukkarasu K., Hecht J., Chitayat D.,
Gelb B.D., Pirinen S., Berry S.A., Greenberg C.R., Karsenty G.,
Lee B.;
"CBFA1 mutation analysis and functional correlation with phenotypic
variability in cleidocranial dysplasia.";
Hum. Mol. Genet. 8:2311-2316(1999).
[16]
VARIANT CLCD SER-197.
PubMed=10689183; DOI=10.1016/S0378-1119(99)00558-2;
Zhang Y.-W., Yasui N., Kakazu N., Abe T., Takada K., Imai S., Sato M.,
Nomura S., Ochi T., Okuzumi S., Nogami H., Nagai T., Ohashi H.,
Ito Y.;
"PEBP2alphaA/CBFA1 mutations in Japanese cleidocranial dysplasia
patients.";
Gene 244:21-28(2000).
[17]
VARIANT CLCD TRP-190.
PubMed=10980549;
DOI=10.1002/1098-1004(200009)16:3<277::AID-HUMU25>3.0.CO;2-V;
Giannotti A., Tessa A., Patrono C., De Florio L., Velardo M.,
Dionisi-Vici C., Bertini E., Santorelli F.M.;
"A novel CBFA1 mutation (R190W) in an Italian family with
cleidocranial dysplasia.";
Hum. Mutat. 16:277-277(2000).
[18]
VARIANTS CLCD TRP-190; SER-197; ASN-218; ILE-220; TRP-225 AND GLN-225,
AND CHARACTERIZATION OF VARIANTS CLCD TRP-190; SER-197; ASN-218;
ILE-220; TRP-225 AND GLN-225.
PubMed=12196916; DOI=10.1086/342717;
Yoshida T., Kanegane H., Osato M., Yanagida M., Miyawaki T., Ito Y.,
Shigesada K.;
"Functional analysis of RUNX2 mutations in Japanese patients with
cleidocranial dysplasia demonstrates novel genotype-phenotype
correlations.";
Am. J. Hum. Genet. 71:724-738(2002).
[19]
VARIANT CLCD LEU-53.
PubMed=12081718; DOI=10.1034/j.1399-0004.2002.610505.x;
Machuca-Tzili L., Monroy-Jaramillo N., Gonzalez-del Angel A.,
Kofman-Alfaro S.;
"New mutations in the CBFA1 gene in two Mexican patients with
cleidocranial dysplasia.";
Clin. Genet. 61:349-353(2002).
[20]
VARIANT CLCD PRO-169.
PubMed=12424590; DOI=10.1007/s00431-002-0977-x;
Morava E., Karteszi J., Weisenbach J., Caliebe A., Mundlos S.,
Mehes K.;
"Cleidocranial dysplasia with decreased bone density and biochemical
findings of hypophosphatasia.";
Eur. J. Pediatr. 161:619-622(2002).
[21]
VARIANTS CLCD GLY-156; PRO-169; TRP-190; LYS-201; TRP-225; GLN-225 AND
VAL-362.
PubMed=11857736; DOI=10.1002/humu.10043;
Otto F., Kanegane H., Mundlos S.;
"Mutations in the RUNX2 gene in patients with cleidocranial
dysplasia.";
Hum. Mutat. 19:209-216(2002).
[22]
VARIANTS CLCD GLY-131 AND GLN-225.
PubMed=16270353; DOI=10.1002/jcp.20552;
Kim H.-J., Nam S.-H., Kim H.-J., Park H.-S., Ryoo H.-M., Kim S.-Y.,
Cho T.-J., Kim S.-G., Bae S.-C., Kim I.-S., Stein J.L.,
van Wijnen A.J., Stein G.S., Lian J.B., Choi J.-Y.;
"Four novel RUNX2 mutations including a splice donor site result in
the cleidocranial dysplasia phenotype.";
J. Cell. Physiol. 207:114-122(2006).
[23]
VARIANT CLCD ILE-420.
PubMed=20082269; DOI=10.4238/vol9-1gmr685;
Wang G.X., Sun R.P., Song F.L.;
"A novel RUNX2 mutation (T420I) in Chinese patients with cleidocranial
dysplasia.";
Genet. Mol. Res. 9:41-47(2010).
[24]
VARIANTS CLCD ASN-118; SER-131; CYS-131; PRO-136; ASP-156; VAL-175;
LYS-175; SER-187; GLN-193; ILE-200; HIS-209; PRO-211; GLN-218;
GLU-218; LEU-225; GLY-228; ARG-233; ASN-287 AND ASN-420.
PubMed=20648631; DOI=10.1002/humu.21298;
Ott C.E., Leschik G., Trotier F., Brueton L., Brunner H.G.,
Brussel W., Guillen-Navarro E., Haase C., Kohlhase J., Kotzot D.,
Lane A., Lee-Kirsch M.A., Morlot S., Simon M.E.H.,
Steichen-Gersdorf E., Tegay D.H., Peters H., Mundlos S., Klopocki E.;
"Deletions of the RUNX2 gene are present in about 10% of individuals
with cleidocranial dysplasia.";
Hum. Mutat. 31:E1587-E1593(2010).
[25]
VARIANT CLCD TRP-225.
PubMed=19744171; DOI=10.1111/j.1601-0825.2009.01623.x;
Ryoo H.M., Kang H.Y., Lee S.K., Lee K.E., Kim J.W.;
"RUNX2 mutations in cleidocranial dysplasia patients.";
Oral Dis. 16:55-60(2010).
[26]
VARIANT CLCD CYS-131.
PubMed=24984680;
Callea M., Bellacchio E., Di Stazio M., Fattori F., Bertini E.,
Yavuz I., Clarich G., Gunay A.;
"A case of cleidocranial dysplasia with peculiar dental features:
pathogenetic role of the RUNX2 mutation and long term follow-up.";
Oral Health Dent. Manag. 13:548-551(2014).
[27]
VARIANTS CLCD ARG-175; GLN-190; GLN-225 AND 462-GLY--TYR-521 DEL,
CHARACTERIZATION OF VARIANT CLCD 462-GLY--TYR-521 DEL, AND FUNCTION.
PubMed=28703881; DOI=10.1002/jcb.26283;
Jung Y.J., Bae H.S., Ryoo H.M., Baek S.H.;
"A novel RUNX2 mutation in exon 8, G462X, in a patient with
Cleidocranial Dysplasia.";
J. Cell. Biochem. 119:1152-1162(2018).
[28]
VARIANTS CLCD GLY-193 AND 400-TYR--TYR-521 DEL, CHARACTERIZATION OF
VARIANTS CLCD GLY-193 AND 400-TYR--TYR-521 DEL, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=28505335; DOI=10.1093/mutage/gex012;
Zeng L., Wei J., Han D., Liu H., Liu Y., Zhao N., Sun S., Wang Y.,
Feng H.;
"Functional analysis of novel RUNX2 mutations in cleidocranial
dysplasia.";
Mutagenesis 32:437-443(2017).
[29]
VARIANTS CLCD 67-GLN--TYR-521 DEL; ARG-113; THR-186 AND TRP-225,
CHARACTERIZATION OF VARIANTS CLCD 67-GLN--TYR-521 DEL; ARG-113;
THR-186 AND TRP-225, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=28738062; DOI=10.1371/journal.pone.0181653;
Zhang X., Liu Y., Wang X., Sun X., Zhang C., Zheng S.;
"Analysis of novel RUNX2 mutations in Chinese patients with
cleidocranial dysplasia.";
PLoS ONE 12:E0181653-E0181653(2017).
-!- FUNCTION: Transcription factor involved in osteoblastic
differentiation and skeletal morphogenesis (PubMed:28505335,
PubMed:28738062, PubMed:28703881). Essential for the maturation of
osteoblasts and both intramembranous and endochondral
ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a
number of enhancers and promoters, including murine leukemia
virus, polyomavirus enhancer, T-cell receptor enhancers,
osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen,
LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports
transcription activation: synergizes with SPEN/MINT to enhance
FGFR2-mediated activation of the osteocalcin FGF-responsive
element (OCFRE) (By similarity). Inhibits KAT6B-dependent
transcriptional activation. {ECO:0000250,
ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:28505335,
ECO:0000269|PubMed:28703881, ECO:0000269|PubMed:28738062}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit binds DNA as a monomer and through the Runt domain. DNA-
binding is increased by heterodimerization. Interacts with XRCC6
(Ku70) and XRCC5 (Ku80). Interacts with HIVEP3. Interacts with
IFI204. Interaction with SATB2; the interaction results in
enhanced DNA binding and transactivation by these transcription
factors. Binds to HIPK3. Interacts (isoform 3) with DDX5.
Interacts with FOXO1 (via a C-terminal region); the interaction
inhibits RUNX2 transcriptional activity towards BGLAP. This
interaction is prevented on insulin or IGF1 stimulation as FOXO1
is exported from the nucleus (By similarity). Interacts with
CCNB1, KAT6A and KAT6B. Interacts with FOXP3. Interacts with
TMEM119 (By similarity). Interacts with OLFM2 (By similarity).
{ECO:0000250|UniProtKB:Q08775, ECO:0000250|UniProtKB:Q9Z2J9,
ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12145306,
ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:17377532}.
-!- INTERACTION:
Q13526:PIN1; NbExp=7; IntAct=EBI-976402, EBI-714158;
O15297:PPM1D; NbExp=4; IntAct=EBI-976402, EBI-1551512;
O43541:SMAD6; NbExp=3; IntAct=EBI-976402, EBI-976374;
O15350:TP73; NbExp=3; IntAct=EBI-976402, EBI-389606;
P17480:UBTF; NbExp=4; IntAct=EBI-976402, EBI-396235;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28505335,
ECO:0000269|PubMed:28738062}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Cbfa1a;
IsoId=Q13950-1; Sequence=Displayed;
Name=2;
IsoId=Q13950-2; Sequence=VSP_005937;
Name=3; Synonyms=Cbfa1b;
IsoId=Q13950-3; Sequence=VSP_005938;
Note=Contains a phosphoserine at position 340.
{ECO:0000244|PubMed:18220336};
-!- TISSUE SPECIFICITY: Specifically expressed in osteoblasts.
-!- DOMAIN: A proline/serine/threonine rich region at the C-terminus
is necessary for transcriptional activation of target genes and
contains the phosphorylation sites.
-!- PTM: Phosphorylated; probably by MAP kinases (MAPK).
Phosphorylation by HIPK3 is required for the SPEN/MINT and FGF2
transactivation during osteoblastic differentiation (By
similarity). Phosphorylation at Ser-451 by CDK1 promotes
endothelial cell proliferation required for tumor angiogenesis
probably by facilitating cell cycle progression. Isoform 3 is
phosphorylated on Ser-340. {ECO:0000250,
ECO:0000269|PubMed:16407259}.
-!- DISEASE: Cleidocranial dysplasia (CLCD) [MIM:119600]: Autosomal
dominant skeletal disorder with high penetrance and variable
expressivity. It is due to defective endochondral and
intramembranous bone formation. Typical features include
hypoplasia/aplasia of clavicles, patent fontanelles, wormian bones
(additional cranial plates caused by abnormal ossification of the
calvaria), supernumerary teeth, short stature, and other skeletal
changes. In some cases defects in RUNX2 are exclusively associated
with dental anomalies. {ECO:0000269|PubMed:10521292,
ECO:0000269|PubMed:10545612, ECO:0000269|PubMed:10689183,
ECO:0000269|PubMed:10980549, ECO:0000269|PubMed:11857736,
ECO:0000269|PubMed:12081718, ECO:0000269|PubMed:12196916,
ECO:0000269|PubMed:12424590, ECO:0000269|PubMed:16270353,
ECO:0000269|PubMed:19744171, ECO:0000269|PubMed:20082269,
ECO:0000269|PubMed:20648631, ECO:0000269|PubMed:24984680,
ECO:0000269|PubMed:28505335, ECO:0000269|PubMed:28703881,
ECO:0000269|PubMed:28738062, ECO:0000269|PubMed:9182765,
ECO:0000269|PubMed:9207800}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Metaphyseal dysplasia with maxillary hypoplasia with or
without brachydactyly (MDMHB) [MIM:156510]: An autosomal dominant
bone dysplasia characterized by metaphyseal flaring of long bones,
enlargement of the medial halves of the clavicles, maxillary
hypoplasia, variable brachydactyly, and dystrophic teeth.
{ECO:0000269|PubMed:23290074}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Analysis
for copy-number variations revealed that a 105 kb duplication
within RUNX2 segregated with the MDMHB phenotype in a region with
maximum linkage. Real-time PCR for copy-number variation in
genomic DNA in eight samples, as well as sequence analysis of
fibroblast cDNA from one subject with MDMHB confirmed that
affected family members were heterozygous for the presence of an
intragenic duplication encompassing exons 3 to 5 of RUNX2. These
three exons code for the Q/A domain and the functionally essential
DNA-binding Runt domain of RUNX2. The RUNX2 duplication found in
individuals with MDMHB leads to a gain of function
(PubMed:23290074). {ECO:0000269|PubMed:23290074}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RUNX2ID42183ch6p21.html";
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EMBL; AF001450; AAB65159.2; -; Genomic_DNA.
EMBL; AF001443; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001444; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001445; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001446; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001447; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001448; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001449; AAB65159.2; JOINED; Genomic_DNA.
EMBL; AF001450; AAB65158.1; -; Genomic_DNA.
EMBL; AF001444; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AF001445; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AF001446; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AF001447; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AF001448; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AF001449; AAB65158.1; JOINED; Genomic_DNA.
EMBL; AL161907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL358135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF053952; AAC78624.1; -; mRNA.
EMBL; AF053949; AAC77441.1; -; Genomic_DNA.
EMBL; L40992; AAA89072.1; -; mRNA.
CCDS; CCDS43467.2; -. [Q13950-1]
CCDS; CCDS43468.2; -. [Q13950-3]
RefSeq; NP_001015051.3; NM_001015051.3. [Q13950-3]
RefSeq; NP_001019801.3; NM_001024630.3. [Q13950-1]
UniGene; Hs.535845; -.
ProteinModelPortal; Q13950; -.
SMR; Q13950; -.
BioGrid; 107308; 46.
CORUM; Q13950; -.
DIP; DIP-36707N; -.
ELM; Q13950; -.
IntAct; Q13950; 18.
MINT; Q13950; -.
STRING; 9606.ENSP00000360493; -.
iPTMnet; Q13950; -.
PhosphoSitePlus; Q13950; -.
SwissPalm; Q13950; -.
BioMuta; RUNX2; -.
DMDM; 17368460; -.
EPD; Q13950; -.
MaxQB; Q13950; -.
PaxDb; Q13950; -.
PeptideAtlas; Q13950; -.
PRIDE; Q13950; -.
ProteomicsDB; 59767; -.
ProteomicsDB; 59768; -. [Q13950-2]
ProteomicsDB; 59769; -. [Q13950-3]
DNASU; 860; -.
Ensembl; ENST00000359524; ENSP00000352514; ENSG00000124813. [Q13950-2]
Ensembl; ENST00000371432; ENSP00000360486; ENSG00000124813. [Q13950-3]
Ensembl; ENST00000371436; ENSP00000360491; ENSG00000124813. [Q13950-3]
Ensembl; ENST00000371438; ENSP00000360493; ENSG00000124813. [Q13950-1]
Ensembl; ENST00000465038; ENSP00000420707; ENSG00000124813. [Q13950-1]
Ensembl; ENST00000647337; ENSP00000495497; ENSG00000124813. [Q13950-1]
GeneID; 860; -.
KEGG; hsa:860; -.
UCSC; uc003oxt.5; human. [Q13950-1]
CTD; 860; -.
DisGeNET; 860; -.
EuPathDB; HostDB:ENSG00000124813.20; -.
GeneCards; RUNX2; -.
GeneReviews; RUNX2; -.
HGNC; HGNC:10472; RUNX2.
HPA; CAB008374; -.
HPA; CAB062561; -.
HPA; CAB068226; -.
HPA; HPA022040; -.
MalaCards; RUNX2; -.
MIM; 119600; phenotype.
MIM; 156510; phenotype.
MIM; 600211; gene.
neXtProt; NX_Q13950; -.
OpenTargets; ENSG00000124813; -.
Orphanet; 1452; Cleidocranial dysplasia.
Orphanet; 2504; Metaphyseal dysplasia-maxillary hypoplasia-brachydacty syndrome.
PharmGKB; PA34885; -.
eggNOG; KOG3982; Eukaryota.
eggNOG; ENOG4111J4Y; LUCA.
GeneTree; ENSGT00940000160171; -.
HOGENOM; HOG000045616; -.
HOVERGEN; HBG060268; -.
InParanoid; Q13950; -.
KO; K09278; -.
OMA; SDPRQFT; -.
PhylomeDB; Q13950; -.
TreeFam; TF321496; -.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8941284; RUNX2 regulates chondrocyte maturation.
Reactome; R-HSA-8941326; RUNX2 regulates bone development.
Reactome; R-HSA-8941332; RUNX2 regulates genes involved in cell migration.
Reactome; R-HSA-8941333; RUNX2 regulates genes involved in differentiation of myeloid cells.
SignaLink; Q13950; -.
SIGNOR; Q13950; -.
ChiTaRS; RUNX2; human.
GeneWiki; RUNX2; -.
GenomeRNAi; 860; -.
PRO; PR:Q13950; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124813; Expressed in 166 organ(s), highest expression level in tibia.
CleanEx; HS_RUNX2; -.
ExpressionAtlas; Q13950; baseline and differential.
Genevisible; Q13950; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0070491; F:repressing transcription factor binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; ISS:BHF-UCL.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0071773; P:cellular response to BMP stimulus; ISS:BHF-UCL.
GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001503; P:ossification; TAS:UniProtKB.
GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.770.10; -; 1.
InterPro; IPR000040; AML1_Runt.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
InterPro; IPR013524; Runt_dom.
InterPro; IPR027384; Runx_central_dom_sf.
InterPro; IPR013711; RunxI_C_dom.
InterPro; IPR016554; TF_Runt-rel_RUNX.
PANTHER; PTHR11950; PTHR11950; 1.
Pfam; PF00853; Runt; 1.
Pfam; PF08504; RunxI; 1.
PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
PRINTS; PR00967; ONCOGENEAML1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51062; RUNT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Differentiation;
Disease mutation; DNA-binding; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 521 Runt-related transcription factor 2.
/FTId=PRO_0000174659.
DOMAIN 101 229 Runt. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
REGION 242 258 Required for interaction with FOXO1.
{ECO:0000250}.
REGION 336 439 Interaction with KAT6A. {ECO:0000250}.
REGION 374 468 Interaction with KAT6B.
{ECO:0000269|PubMed:11965546}.
COMPBIAS 49 71 Poly-Gln.
COMPBIAS 73 89 Poly-Ala.
COMPBIAS 237 521 Pro/Ser/Thr-rich.
MOD_RES 267 267 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q08775}.
MOD_RES 451 451 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:16407259}.
CROSSLNK 238 238 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 19 MASNSLFSTVTPCQQNFFW -> MRIPV (in isoform
2). {ECO:0000305}.
/FTId=VSP_005937.
VAR_SEQ 341 362 Missing (in isoform 3).
{ECO:0000303|PubMed:9233771}.
/FTId=VSP_005938.
VARIANT 53 53 Q -> L (in CLCD).
{ECO:0000269|PubMed:12081718}.
/FTId=VAR_064081.
VARIANT 67 521 Missing (in CLCD; decreased subcellular
localization in the nucleus; decreased
transactivation activity).
{ECO:0000269|PubMed:28738062}.
/FTId=VAR_079576.
VARIANT 78 83 Missing. {ECO:0000269|PubMed:9182765}.
/FTId=VAR_012131.
VARIANT 84 84 A -> AAAAAAAAAAA (in CLCD; the patient
also shows brachydactyly of hands and
feet). {ECO:0000269|PubMed:9182765}.
/FTId=VAR_012130.
VARIANT 113 113 L -> R (in CLCD; unchanged subcellular
localization; decreased transactivation
activity). {ECO:0000269|PubMed:10521292,
ECO:0000269|PubMed:28738062}.
/FTId=VAR_012132.
VARIANT 118 118 S -> N (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064082.
VARIANT 118 118 S -> R (in CLCD).
{ECO:0000269|PubMed:10521292}.
/FTId=VAR_012133.
VARIANT 121 121 F -> C (in CLCD).
{ECO:0000269|PubMed:10521292}.
/FTId=VAR_012134.
VARIANT 123 123 C -> R (in CLCD).
{ECO:0000269|PubMed:10521292}.
/FTId=VAR_012135.
VARIANT 131 131 R -> C (in CLCD).
{ECO:0000269|PubMed:20648631,
ECO:0000269|PubMed:24984680}.
/FTId=VAR_064083.
VARIANT 131 131 R -> G (in CLCD).
{ECO:0000269|PubMed:16270353}.
/FTId=VAR_064084.
VARIANT 131 131 R -> S (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064085.
VARIANT 133 133 Missing (in CLCD).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012136.
VARIANT 136 136 L -> P (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064086.
VARIANT 156 156 V -> D (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064087.
VARIANT 156 156 V -> G (in CLCD).
{ECO:0000269|PubMed:11857736}.
/FTId=VAR_064088.
VARIANT 169 169 R -> P (in CLCD; dbSNP:rs104893995).
{ECO:0000269|PubMed:11857736,
ECO:0000269|PubMed:12424590}.
/FTId=VAR_064089.
VARIANT 169 169 R -> Q (in CLCD; dbSNP:rs104893995).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012137.
VARIANT 175 175 M -> K (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064090.
VARIANT 175 175 M -> R (in CLCD; abolishes DNA binding;
dbSNP:rs104893989).
{ECO:0000269|PubMed:10545612,
ECO:0000269|PubMed:28703881,
ECO:0000269|PubMed:9207800}.
/FTId=VAR_012138.
VARIANT 175 175 M -> V (in CLCD; dbSNP:rs201647225).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064091.
VARIANT 186 186 R -> T (in CLCD; unchanged subcellular
localization; decreased transactivation
activity). {ECO:0000269|PubMed:28738062}.
/FTId=VAR_079577.
VARIANT 187 187 F -> S (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064092.
VARIANT 190 190 R -> Q (in CLCD; abolishes DNA binding;
dbSNP:rs1057521068).
{ECO:0000269|PubMed:10545612,
ECO:0000269|PubMed:28703881}.
/FTId=VAR_012139.
VARIANT 190 190 R -> W (in CLCD; has severely impaired
DNA binding and transactivation).
{ECO:0000269|PubMed:10980549,
ECO:0000269|PubMed:11857736,
ECO:0000269|PubMed:12196916}.
/FTId=VAR_012140.
VARIANT 191 191 S -> N (in CLCD; abolishes DNA binding;
dbSNP:rs104893990).
{ECO:0000269|PubMed:10545612,
ECO:0000269|PubMed:9207800}.
/FTId=VAR_012141.
VARIANT 193 193 R -> C (in CLCD).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012142.
VARIANT 193 193 R -> G (in CLCD; unchanged subcellular
localization; decreased transactivation
activity). {ECO:0000269|PubMed:28505335}.
/FTId=VAR_079578.
VARIANT 193 193 R -> Q (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064093.
VARIANT 197 197 F -> S (in CLCD; retains
heterodimerization activity together with
a trace potential for DNA binding;
retains a low but still substantial
transactivation activity).
{ECO:0000269|PubMed:10689183,
ECO:0000269|PubMed:12196916}.
/FTId=VAR_012143.
VARIANT 199 199 L -> F (in CLCD; abolishes DNA binding).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012144.
VARIANT 200 200 T -> A (in CLCD; mild; associated also
with isolated dental anomalies; normal
DNA binding; dbSNP:rs104893993).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012145.
VARIANT 200 200 T -> I (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064094.
VARIANT 201 201 I -> K (in CLCD).
{ECO:0000269|PubMed:11857736}.
/FTId=VAR_064095.
VARIANT 205 205 T -> R (in CLCD).
{ECO:0000269|PubMed:10521292}.
/FTId=VAR_012146.
VARIANT 209 209 Q -> H (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064096.
VARIANT 209 209 Q -> R (in CLCD).
{ECO:0000269|PubMed:10545612}.
/FTId=VAR_012147.
VARIANT 211 211 A -> P (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064097.
VARIANT 218 218 K -> E (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064098.
VARIANT 218 218 K -> N (in CLCD; has severely impaired
DNA binding and transactivation;
dbSNP:rs752933596).
{ECO:0000269|PubMed:12196916}.
/FTId=VAR_064099.
VARIANT 218 218 K -> Q (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064100.
VARIANT 220 220 T -> I (in CLCD; has severely impaired
DNA binding and transactivation).
{ECO:0000269|PubMed:12196916}.
/FTId=VAR_064101.
VARIANT 225 225 R -> L (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064102.
VARIANT 225 225 R -> Q (in CLCD; interferes with nuclear
localization; abolishes DNA binding;
dbSNP:rs104893991).
{ECO:0000269|PubMed:10521292,
ECO:0000269|PubMed:10545612,
ECO:0000269|PubMed:11857736,
ECO:0000269|PubMed:12196916,
ECO:0000269|PubMed:16270353,
ECO:0000269|PubMed:28703881}.
/FTId=VAR_012148.
VARIANT 225 225 R -> W (in CLCD; interferes with nuclear
localization; has severely impaired DNA
binding and transactivation;
dbSNP:rs104893992).
{ECO:0000269|PubMed:10521292,
ECO:0000269|PubMed:11857736,
ECO:0000269|PubMed:12196916,
ECO:0000269|PubMed:19744171,
ECO:0000269|PubMed:28738062}.
/FTId=VAR_012149.
VARIANT 228 228 R -> G (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064103.
VARIANT 233 233 K -> R (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064104.
VARIANT 287 287 D -> N (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064105.
VARIANT 362 362 A -> V (in CLCD).
{ECO:0000269|PubMed:11857736}.
/FTId=VAR_064106.
VARIANT 400 521 Missing (in CLCD; unchanged subcellular
localization; decreased transactivation
activity). {ECO:0000269|PubMed:28505335}.
/FTId=VAR_079579.
VARIANT 420 420 T -> I (in CLCD).
{ECO:0000269|PubMed:20082269}.
/FTId=VAR_064107.
VARIANT 420 420 T -> N (in CLCD).
{ECO:0000269|PubMed:20648631}.
/FTId=VAR_064108.
VARIANT 462 521 Missing (in CLCD; decreased protein
stability; decreased transactivation
activity; decreased osteoblast
differentiation).
{ECO:0000269|PubMed:28703881}.
/FTId=VAR_079580.
VARIANT 511 511 G -> S (in dbSNP:rs11498198).
{ECO:0000269|PubMed:10521292}.
/FTId=VAR_012150.
MUTAGEN 451 451 S->A: Reduced DNA-binding and impaired
phosphorylation.
{ECO:0000269|PubMed:16407259}.
CONFLICT 16 16 N -> S (in Ref. 4; AAC77441).
{ECO:0000305}.
SEQUENCE 521 AA; 56648 MW; 44C4F3867D6F3EB1 CRC64;
MASNSLFSTV TPCQQNFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ
QQQQQQQQQQ QEAAAAAAAA AAAAAAAAAV PRLRPPHDNR TMVEIIADHP AELVRTDSPN
FLCSVLPSHW RCNKTLPVAF KVVALGEVPD GTVVTVMAGN DENYSAELRN ASAVMKNQVA
RFNDLRFVGR SGRGKSFTLT ITVFTNPPQV ATYHRAIKVT VDGPREPRRH RQKLDDSKPS
LFSDRLSDLG RIPHPSMRVG VPPQNPRPSL NSAPSPFNPQ GQSQITDPRQ AQSSPPWSYD
QSYPSYLSQM TSPSIHSTTP LSSTRGTGLP AITDVPRRIS DDDTATSDFC LWPSTLSKKS
QAGASELGPF SDPRQFPSIS SLTESRFSNP RMHYPATFTY TPPVTSGMSL GMSATTHYHT
YLPPPYPGSS QSQSGPFQTS STPYLYYGTS SGSYQFPMVP GGDRSPSRML PPCTTTSNGS
TLLNPNLPNQ NDGVDADGSH SSSPTVLNSS GRMDESVWRP Y


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18-003-43025 GA-binding protein alpha chain - GABP-subunit alpha; Transcription factor E4TF1-60; Nuclear respiratory factor 2 subunit alpha Polyclonal 0.1 mg Protein A
20-372-60120 transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha) - Mouse monoclonal anti-human TFAP2A antibody; AP2-alpha; Activating enhancer-binding protein 2 alpha; AP-2 transcription 0.1 mg
EIAAB27106 CAAT box DNA-binding protein subunit A,CBF-B,CCAAT-binding transcription factor subunit B,Nfya,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha,Rat,Rattus no
18-003-43308 Transcription factor AP-2 alpha - AP2-alpha; Activating enhancer-binding protein 2 alpha; AP-2 transcription factor; Activator protein 2; AP-2 Polyclonal 0.1 mg Protein A
28-784 Core binding factor (CBF) is a heterodimeric transcription factor that binds to the core element of many enhancers and promoters. RUNX1 is the alpha subunit of CBF and is thought to be involved in the 0.05 mg
EIAAB41099 General transcription factor IIF 74 kDa subunit,General transcription factor IIF subunit 1,GTF2F1,Homo sapiens,Human,RAP74,TFIIF-alpha,Transcription initiation factor IIF subunit alpha,Transcription i
EIAAB41095 General transcription factor IIE 56 kDa subunit,General transcription factor IIE subunit 1,GTF2E1,Homo sapiens,Human,TF2E1,TFIIE-alpha,Transcription initiation factor IIE subunit alpha
EIAAB27107 CAAT box DNA-binding protein subunit A,Homo sapiens,Human,NFYA,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha


 

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