Q06455 (MTG8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein CBFA2T1

Alternative name(s):
Cyclin-D-related protein
Eight twenty one protein
Protein ETO
Protein MTG8
Zinc finger MYND domain-containing protein 2

Gene names

Name:	RUNX1T1
Synonyms:	AML1T1, CBFA2T1, CDR, ETO, MTG8, ZMYND2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription regulator that excerts its function by binding to histone deacetylases and transcription factors. Can repress transactivation mediated by TCF12. Ref.11 Ref.15
Subunit structure	Homotetramer. Heterotetramer with CBFA2T2 and CBFA2T3. Interacts with TCF12, SIN3A, HDAC1, HDAC2, HDAC3, NCOR1 and NCOR2. Interacts with ATN1 (via its N-terminus); the interaction enhances the transcriptional repression. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Nucleus. Note: Colocalizes with ATN1 in discrete nuclear dots. Ref.11
Tissue specificity	Most abundantly expressed in brain. Lower levels in lung, heart, testis and ovary.
Domain	The TAFH domain mediates interaction with transcription regulators. Ref.17
Involvement in disease	A chromosomal aberration involving RUNX1T1 is a cause of acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1/AML1. Ref.1 Ref.19 Ref.20 Ref.21 Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. Note: The disease may be caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the CBFA2T family. Contains 1 MYND-type zinc finger. Contains 1 TAFH (NHR1) domain.
Sequence caution	The sequence AAH05850.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA03247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	generation of precursor metabolites and energy Traceable author statement PubMed 9618262. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear matrix Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 9618262. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-743342,EBI-743342

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform MTG8B (identifier: Q06455-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform MTG8A (identifier: Q06455-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MISVKRNTWRALSLVIGDCRKKGNFEYCQ → MP

Isoform 3 (identifier: Q06455-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MISVKRNTWRALSLVIGDCRKKGNFEYCQ → MCHPDKAFTSDKLQCVFNEYKAAVWVPPRPRPLSRAPLPE

Isoform 4 (identifier: Q06455-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 604

604

Protein CBFA2T1

PRO_0000218299

Regions

Domain

120 – 215

96

TAFH

Zinc finger

515 – 551

37

MYND-type

Region

337 – 383

47

Important for oligomerization

Compositional bias

57 – 60

4

Poly-Pro

Compositional bias

102 – 108

7

Poly-Ser

Compositional bias

290 – 297

8

Poly-Pro

Compositional bias

408 – 413

6

Poly-Ser

Sites

Site

30 – 31

2

Breakpoint for translocation to form AML1-MTG8 in AML-M2

Amino acid modifications

Modified residue

41

1

Phosphoserine Ref.13

Modified residue

417

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

1 – 37

37

Missing in isoform 4.

VSP_045442

Alternative sequence

1 – 29

29

MISVK…FEYCQ → MCHPDKAFTSDKLQCVFNEY KAAVWVPPRPRPLSRAPLPE in isoform 3.

VSP_044558

Alternative sequence

1 – 29

29

MISVK…FEYCQ → MP in isoform MTG8A.

VSP_003327

Natural variant

386

1

R → W in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036321

Natural variant

395

1

R → W in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036322

Natural variant

471

1

A → V in a colorectal cancer sample; somatic mutation. Ref.22

VAR_036323

Experimental info

Mutagenesis

125

1

K → A or D: Loss of interaction with TCF12. Ref.15

Mutagenesis

126

1

L → A: Loss of interaction with TCF12. Ref.15

Mutagenesis

128

1

R → D: Loss of interaction with TCF12. Ref.15

Mutagenesis

129

1

F → A: Loss of interaction with TCF12. Ref.15 Ref.17

Mutagenesis

129

1

F → K: Abolishes interaction with corepressor. Ref.15 Ref.17

Mutagenesis

136

1

F → A: Abolishes interaction with corepressor. Ref.17

Mutagenesis

170

1

Q → A: Abolishes interaction with corepressor. Ref.17

Mutagenesis

173

1

T → Q: Abolishes interaction with corepressor. Ref.17

Mutagenesis

175

1

F → A: Abolishes interaction with corepressor. Ref.17

Mutagenesis

177

1

L → A: Abolishes interaction with corepressor. Ref.17

Mutagenesis

178

1

R → A or D: Loss of interaction with TCF12. Ref.15

Mutagenesis

184

1

F → A: Loss of interaction with TCF12. Ref.15

Mutagenesis

547

1

H → A: Causes unfolding of the MYND-type zinc finger domain. Ref.16

Sequence conflict

427

1

D → G in AAC26143. Ref.2

Sequence conflict

455

1

E → G in BAH12630. Ref.3

Sequence conflict

506

1

N → S in BAH12630. Ref.3

Secondary structure

1

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604

Helix Strand Turn

Details...

Helix

121 – 123

3

Helix

125 – 135

11

Helix

137 – 140

4

Helix

142 – 156

15

Helix

162 – 172

11

Beta strand

173 – 176

4

Beta strand

179 – 181

3

Helix

182 – 186

5

Helix

189 – 199

11

Helix

200 – 202

3

Helix

209 – 212

4

Helix

347 – 399

53

Helix

444 – 465

22

Beta strand

512 – 514

3

Beta strand

516 – 518

3

Beta strand

524 – 526

3

Turn

527 – 529

3

Beta strand

533 – 536

4

Helix

537 – 542

6

Helix

544 – 547

4

Turn

548 – 550

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform MTG8B [UniParc]. Last modified November 1, 1997. Version 2. Checksum: C3D2452F96E65679	FASTA	604	67,566
	10 20 30 40 50 60 MISVKRNTWR ALSLVIGDCR KKGNFEYCQD RTEKHSTMPD SPVDVKTQSR LTPPTMPPPP 70 80 90 100 110 120 TTQGAPRTSS FTPTTLTNGT SHSPTALNGA PSPPNGFSNG PSSSSSSSLA NQQLPPACGA 130 140 150 160 170 180 RQLSKLKRFL TTLQQFGNDI SPEIGERVRT LVLGLVNSTL TIEEFHSKLQ EATNFPLRPF 190 200 210 220 230 240 VIPFLKANLP LLQRELLHCA RLAKQNPAQY LAQHEQLLLD ASTTSPVDSS ELLLDVNENG 250 260 270 280 290 300 KRRTPDRTKE NGFDREPLHS EHPSKRPCTI SPGQRYSPNN GLSYQPNGLP HPTPPPPQHY 310 320 330 340 350 360 RLDDMAIAHH YRDSYRHPSH RDLRDRNRPM GLHGTRQEEM IDHRLTDREW AEEWKHLDHL 370 380 390 400 410 420 LNCIMDMVEK TRRSLTVLRR CQEADREELN YWIRRYSDAE DLKKGGGSSS SHSRQQSPVN 430 440 450 460 470 480 PDPVALDAHR EFLHRPASGY VPEEIWKKAE EAVNEVKRQA MTELQKAVSE AERKAHDMIT 490 500 510 520 530 540 TERAKMERTV AEAKRQAAED ALAVINQQED SSESCWNCGR KASETCSGCN TARYCGSFCQ 550 560 570 580 590 600 HKDWEKHHHI CGQTLQAQQQ GDTPAVSSSV TPNSGAGSPM DTPPAATPRS TTPGTPSTIE TTPR
	Isoform MTG8A [UniParc]. Checksum: 70E84F0120C11C3B	FASTA	577	64,396
	10 20 30 40 50 60 MPDRTEKHST MPDSPVDVKT QSRLTPPTMP PPPTTQGAPR TSSFTPTTLT NGTSHSPTAL 70 80 90 100 110 120 NGAPSPPNGF SNGPSSSSSS SLANQQLPPA CGARQLSKLK RFLTTLQQFG NDISPEIGER 130 140 150 160 170 180 VRTLVLGLVN STLTIEEFHS KLQEATNFPL RPFVIPFLKA NLPLLQRELL HCARLAKQNP 190 200 210 220 230 240 AQYLAQHEQL LLDASTTSPV DSSELLLDVN ENGKRRTPDR TKENGFDREP LHSEHPSKRP 250 260 270 280 290 300 CTISPGQRYS PNNGLSYQPN GLPHPTPPPP QHYRLDDMAI AHHYRDSYRH PSHRDLRDRN 310 320 330 340 350 360 RPMGLHGTRQ EEMIDHRLTD REWAEEWKHL DHLLNCIMDM VEKTRRSLTV LRRCQEADRE 370 380 390 400 410 420 ELNYWIRRYS DAEDLKKGGG SSSSHSRQQS PVNPDPVALD AHREFLHRPA SGYVPEEIWK 430 440 450 460 470 480 KAEEAVNEVK RQAMTELQKA VSEAERKAHD MITTERAKME RTVAEAKRQA AEDALAVINQ 490 500 510 520 530 540 QEDSSESCWN CGRKASETCS GCNTARYCGS FCQHKDWEKH HHICGQTLQA QQQGDTPAVS 550 560 570 SSVTPNSGAG SPMDTPPAAT PRSTTPGTPS TIETTPR
	Isoform 3 [UniParc]. Checksum: 4FB11B0FAEC56B07	FASTA	615	68,746
	10 20 30 40 50 60 MCHPDKAFTS DKLQCVFNEY KAAVWVPPRP RPLSRAPLPE DRTEKHSTMP DSPVDVKTQS 70 80 90 100 110 120 RLTPPTMPPP PTTQGAPRTS SFTPTTLTNG TSHSPTALNG APSPPNGFSN GPSSSSSSSL 130 140 150 160 170 180 ANQQLPPACG ARQLSKLKRF LTTLQQFGND ISPEIGERVR TLVLGLVNST LTIEEFHSKL 190 200 210 220 230 240 QEATNFPLRP FVIPFLKANL PLLQRELLHC ARLAKQNPAQ YLAQHEQLLL DASTTSPVDS 250 260 270 280 290 300 SELLLDVNEN GKRRTPDRTK ENGFDREPLH SEHPSKRPCT ISPGQRYSPN NGLSYQPNGL 310 320 330 340 350 360 PHPTPPPPQH YRLDDMAIAH HYRDSYRHPS HRDLRDRNRP MGLHGTRQEE MIDHRLTDRE 370 380 390 400 410 420 WAEEWKHLDH LLNCIMDMVE KTRRSLTVLR RCQEADREEL NYWIRRYSDA EDLKKGGGSS 430 440 450 460 470 480 SSHSRQQSPV NPDPVALDAH REFLHRPASG YVPEEIWKKA EEAVNEVKRQ AMTELQKAVS 490 500 510 520 530 540 EAERKAHDMI TTERAKMERT VAEAKRQAAE DALAVINQQE DSSESCWNCG RKASETCSGC 550 560 570 580 590 600 NTARYCGSFC QHKDWEKHHH ICGQTLQAQQ QGDTPAVSSS VTPNSGAGSP MDTPPAATPR 610 STTPGTPSTI ETTPR
	Isoform 4 [UniParc]. Checksum: 44AADF2EC7032050	FASTA	567	63,212
	10 20 30 40 50 60 MPDSPVDVKT QSRLTPPTMP PPPTTQGAPR TSSFTPTTLT NGTSHSPTAL NGAPSPPNGF 70 80 90 100 110 120 SNGPSSSSSS SLANQQLPPA CGARQLSKLK RFLTTLQQFG NDISPEIGER VRTLVLGLVN 130 140 150 160 170 180 STLTIEEFHS KLQEATNFPL RPFVIPFLKA NLPLLQRELL HCARLAKQNP AQYLAQHEQL 190 200 210 220 230 240 LLDASTTSPV DSSELLLDVN ENGKRRTPDR TKENGFDREP LHSEHPSKRP CTISPGQRYS 250 260 270 280 290 300 PNNGLSYQPN GLPHPTPPPP QHYRLDDMAI AHHYRDSYRH PSHRDLRDRN RPMGLHGTRQ 310 320 330 340 350 360 EEMIDHRLTD REWAEEWKHL DHLLNCIMDM VEKTRRSLTV LRRCQEADRE ELNYWIRRYS 370 380 390 400 410 420 DAEDLKKGGG SSSSHSRQQS PVNPDPVALD AHREFLHRPA SGYVPEEIWK KAEEAVNEVK 430 440 450 460 470 480 RQAMTELQKA VSEAERKAHD MITTERAKME RTVAEAKRQA AEDALAVINQ QEDSSESCWN 490 500 510 520 530 540 CGRKASETCS GCNTARYCGS FCQHKDWEKH HHICGQTLQA QQQGDTPAVS SSVTPNSGAG 550 560 SPMDTPPAAT PRSTTPGTPS TIETTPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript." Miyoshi H., Kozu T., Shimizu K., Enomoto K., Maseki N., Kaneko Y., Kamada N., Ohki M. EMBO J. 12:2715-2721(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MTG8B), VARIANT AML1-MTG8/ETO FUSION IN AML-M2. Tissue: Fetal brain.
[2]	"Structure and expression of the human MTG8/ETO gene." Wolford J.K., Prochazka M. Gene 212:103-109(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MTG8B).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MTG8A).
[6]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Muscle.
[9]	"The ETO portion of acute myeloid leukemia t(8;21) fusion transcript encodes a highly evolutionarily conserved putative transcription factor." Erickson P.F., Robinson M., Owens G., Drabkin H.A. Cancer Res. 54:1782-1786(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-604.
[10]	"Alternative, out-of-frame runt/MTG8 transcripts are encoded by the derivative (8) chromosome in the t(8;21) of acute myeloid leukemia M2." Tighe J.E., Calabi F. Blood 84:2115-2121(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-432, VARIANT AML1-MTG8/ETO FUSION.
[11]	"Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription." Wood J.D., Nucifora F.C. Jr., Duan K., Zhang C., Wang J., Kim Y., Schilling G., Sacchi N., Liu J.M., Ross C.A. J. Cell Biol. 150:939-948(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATN1, SUBCELLULAR LOCATION, FUNCTION.
[12]	"The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t(16; 21)-positive myeloid malignancies." Hoogeveen A.T., Rossetti S., Stoyanova V., Schonkeren J., Fenaroli A., Schiaffonati L., van Unen L., Sacchi N. Oncogene 21:6703-6712(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-417, MASS SPECTROMETRY.
[14]	"The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity." Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D., Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H. Cancer Cell 9:249-260(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 335-403, SUBUNIT, INTERACTION WITH HDAC1; HDAC2; HDAC3; TCF12; NCOR1; NCOR2; SIN3A; CBFA2T2 AND CBFA2T3.
[15]	"The acute myeloid leukemia fusion protein AML1-ETO targets E proteins via a paired amphipathic helix-like TBP-associated factor homology domain." Plevin M.J., Zhang J., Guo C., Roeder R.G., Ikura M. Proc. Natl. Acad. Sci. U.S.A. 103:10242-10247(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 120-222, INTERACTION WITH TCF12, FUNCTION, MUTAGENESIS OF LYS-125; LEU-126; ARG-128; PHE-129; ARG-178 AND PHE-184.
[16]	"Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity." Liu Y., Chen W., Gaudet J., Cheney M.D., Roudaia L., Cierpicki T., Klet R.C., Hartman K., Laue T.M., Speck N.A., Bushweller J.H. Cancer Cell 11:483-497(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 510-559 IN COMPLEX WITH ZINC IONS AND NCOR2, MUTAGENESIS OF HIS-547, INTERACTION WITH NCOR 1 AND NCOR2.
[17]	"A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription." Wei Y., Liu S., Lausen J., Woodrell C., Cho S., Biris N., Kobayashi N., Wei Y., Yokoyama S., Werner M.H. Nat. Struct. Mol. Biol. 14:653-661(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 119-225, INTERACTION WITH NCOR1 AND TCF12, MUTAGENESIS OF PHE-129; PHE-136; GLN-170; THR-173; PHE-175 AND LEU-177, DOMAIN.
[18]	"Solution structure of ZF-MYND domain of protein CBFA2TI (protein MTG8)." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 505-551.
[19]	"Identification of two transcripts of AML1/ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells." Era T., Asou N., Kunisada T., Yamasaki H., Asou H., Kamada N., Nishikawa S., Yamaguchi K., Takatsuki K. Genes Chromosomes Cancer 13:25-33(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
[20]	"Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction." Kozu T., Miyoshi H., Shimizu K., Maseki N., Kaneko Y., Asou H., Kamada N., Ohki M. Blood 82:1270-1276(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
[21]	"Transcriptionally active chimeric gene derived from the fusion of the AML1 gene and a novel gene on chromosome 8 in t(8;21) leukemic cells." Nisson P.E., Watkins P.C., Sacchi N. Cancer Genet. Cytogenet. 63:81-88(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
[22]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-386; TRP-395 AND VAL-471.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D14821 mRNA. Translation: BAA03558.1.
D13979 mRNA. Translation: BAA03089.1. Sequence problems.
D14289 mRNA. Translation: BAA03247.1. Different initiation.
AF018282 , AF018271, AF018272, AF018273, AF018274, AF018275, AF018276, AF018277, AF018278, AF018279, AF018281 Genomic DNA. Translation: AAC28932.1.
AF018282 , AF018270, AF018272, AF018273, AF018274, AF018275, AF018276, AF018277, AF018278, AF018279, AF018281 Genomic DNA. Translation: AAC28931.1.
AF018283 mRNA. Translation: AAC26143.1.
AK297616 mRNA. Translation: BAH12630.1.
BT009871 mRNA. Translation: AAP88873.1.
CR456792 mRNA. Translation: CAG33073.1.
AC103680 Genomic DNA. No translation available.
AC104339 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91685.1.
BC005850 mRNA. Translation: AAH05850.1. Different initiation.
BC067078 mRNA. Translation: AAH67078.2.
AF181450 Genomic DNA. No translation available.
D43638 mRNA. Translation: BAA07755.1.
X79990 mRNA. Translation: CAA56311.1.
S74096 Genomic DNA. Translation: AAB32126.1.
S74092 Genomic DNA. No translation available.
S78158 mRNA. Translation: AAB34819.2. Sequence problems.
S78159 mRNA. Translation: AAB34820.2. Sequence problems.
D14822 mRNA. Translation: BAA03559.1. Sequence problems.
D14823 mRNA. Translation: BAA03560.1. Sequence problems.
S50186 Genomic DNA. No translation available.

IPI

IPI00333194.
IPI00465350.
IPI00975673.

PIR

A57784.
C57784.

RefSeq

NP_001185554.1. NM_001198625.1.
NP_001185555.1. NM_001198626.1.
NP_001185556.1. NM_001198627.1.
NP_001185557.1. NM_001198628.1.
NP_001185558.1. NM_001198629.1.
NP_001185559.1. NM_001198630.1.
NP_001185560.1. NM_001198631.1.
NP_001185561.1. NM_001198632.1.
NP_001185562.1. NM_001198633.1.
NP_001185563.1. NM_001198634.1.
NP_001185608.1. NM_001198679.1.
NP_004340.1. NM_004349.3.
NP_783552.1. NM_175634.2.
NP_783553.1. NM_175635.2.
NP_783554.1. NM_175636.2.

UniGene

Hs.368431.
Hs.739194.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WQ6	X-ray	2.00	A/B	335-403	[»]
2DJ8	NMR	-	A	505-551	[»]
2H7B	NMR	-	A	120-222	[»]
2KNH	NMR	-	A	119-216	[»]
2KYG	NMR	-	C	437-467	[»]
2OD1	NMR	-	A	510-559	[»]
2ODD	NMR	-	A	510-559	[»]
2PP4	NMR	-	A	119-225	[»]

ProteinModelPortal

Q06455.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29401N.

IntAct

Q06455. 9 interactions.

MINT

MINT-2857382.

PTM databases

PhosphoSite

Q06455.

Polymorphism databases

DMDM

2498595.

Proteomic databases

PaxDb

Q06455.

PRIDE

Q06455.

Protocols and materials databases

DNASU

862.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265814; ENSP00000265814; ENSG00000079102.
ENST00000360348; ENSP00000353504; ENSG00000079102.
ENST00000396218; ENSP00000379520; ENSG00000079102.
ENST00000422361; ENSP00000390137; ENSG00000079102.
ENST00000436581; ENSP00000402257; ENSG00000079102.
ENST00000518844; ENSP00000430728; ENSG00000079102.
ENST00000520724; ENSP00000428742; ENSG00000079102.
ENST00000523629; ENSP00000428543; ENSG00000079102.

GeneID

862.

KEGG

hsa:862.

UCSC

uc003yfb.2. human.
uc003yfc.2. human.

Organism-specific databases

CTD

862.

GeneCards

GC08M093041.

HGNC

HGNC:1535. RUNX1T1.

MIM

114500. phenotype.
133435. gene.

neXtProt

NX_Q06455.

Orphanet

102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.

PharmGKB

PA26111.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG79810.

HOVERGEN

HBG000169.

KO

K10053.

OMA

MITSERA.

OrthoDB

EOG4TB4B6.

PhylomeDB

Q06455.

Gene expression databases

ArrayExpress

Q06455.

Bgee

Q06455.

Genevestigator

Q06455.

GermOnline

ENSG00000079102. Homo sapiens.

Family and domain databases

InterPro

IPR013289. ETO.
IPR013290. MTG8.
IPR014896. NHR2.
IPR003894. TAFH_NHR1.
IPR002893. Znf_MYND.
[Graphical view]

PANTHER

PTHR10379:SF5. PTHR10379:SF5. 1 hit.

Pfam

PF08788. NHR2. 1 hit.
PF07531. TAFH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]

PRINTS

PR01875. ETOFAMILY.
PR01876. MTG8PROTEIN.

SMART

SM00549. TAFH. 1 hit.
[Graphical view]

PROSITE

PS51119. TAFH. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RUNX1T1. human.

EvolutionaryTrace

Q06455.

GenomeRNAi

862.

NextBio

3586.

SOURCE

Search...

Entry information

Entry name

MTG8_HUMAN

Accession

Primary (citable) accession number: Q06455
Secondary accession number(s): B7Z4P4 , E7EPN4, O14784, Q06456, Q14873, Q16239, Q16346, Q16347, Q6IBL1, Q6NXH1, Q7Z4J5, Q92479, Q9BRZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.