P10242 (MYB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional activator Myb

Alternative name(s):
Proto-oncogene c-Myb

Gene names

Name:

MYB

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	640 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.
Subunit structure	Binds MYBBP1A. Interacts with HIPK2, MAF and NLK By similarity. Binds to HIPK1. Ref.15 Ref.16
Subcellular location	Nucleus Ref.16.
Domain	Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression. Ref.14
Post-translational modification	Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation Probable. Ref.15 Phosphorylated by NLK on multiple sites, which induces proteasomal degradation By similarity. Ref.16 Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels. Ref.16
Sequence similarities	Contains 3 HTH myb-type DNA-binding domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome calcium ion transport Inferred from electronic annotation. Source: Compara chromatin remodeling Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB embryonic digestive tract development Inferred from electronic annotation. Source: Compara homeostasis of number of cells Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 20531406. Source: BHF-UCL positive regulation of T-helper cell differentiation Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB positive regulation of histone H3-K4 methylation Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB positive regulation of histone H3-K9 methylation Inferred from mutant phenotype PubMed 20484083. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 20484083. Source: UniProtKB thymus development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear matrix Non-traceable author statement Ref.12. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERC2	O15083	2	EBI-298355,EBI-2684336
SUMO1	P63165	3	EBI-298355,EBI-80140
SUMO2	P61956	3	EBI-298355,EBI-473220
ZFC3H1	O60293	2	EBI-298355,EBI-746701

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10242-1)

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 2 (identifier: P10242-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-316: Missing.

Isoform 3 (identifier: P10242-3)

The sequence of this isoform differs from the canonical sequence as follows:
     317-350: TQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGE → LCGPLLNSDIFSDWAANWDGSLCFATYIVNQQRQ
     351-640: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: P10242-4)

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: S → SDSSSWCDLS...VKSLPFSPSQ

Isoform 5 (identifier: P10242-5)

The sequence of this isoform differs from the canonical sequence as follows:
     402-402: F → M
     403-640: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 6 (identifier: P10242-6)

The sequence of this isoform differs from the canonical sequence as follows:
     567-640: NILTSSVLMA...NAFSARTLVM → TGVQWHDFGS...LRFNGTSIRR

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 7 (identifier: P10242-7)

The sequence of this isoform differs from the canonical sequence as follows:
     314-316: Missing.
     401-401: S → SDSSSWCDLS...VKSLPFSPSQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 640	640	Transcriptional activator Myb		PRO_0000197048
Regions
	Domain	35 – 86	52	HTH myb-type 1
	Domain	87 – 142	56	HTH myb-type 2
	Domain	143 – 193	51	HTH myb-type 3
	DNA binding	63 – 86	24	H-T-H motif By similarity
	DNA binding	115 – 138	24	H-T-H motif By similarity
	DNA binding	166 – 189	24	H-T-H motif By similarity
	Region	90 – 193	104	Interaction with HIPK2 and NLK By similarity
	Region	275 – 327	53	Transcriptional activation domain
	Region	328 – 465	138	Negative regulatory domain By similarity
	Region	376 – 397	22	Leucine-zipper
Amino acid modifications
	Modified residue	471	1	N6-acetyllysine Ref.17
	Modified residue	480	1	N6-acetyllysine Ref.17
Natural variations
	Alternative sequence	314 – 316	3	Missing in isoform 2 and isoform 7.		VSP_003293
	Alternative sequence	317 – 350	34	TQNHT…SCLGE → LCGPLLNSDIFSDWAANWDG SLCFATYIVNQQRQ in isoform 3.		VSP_003294
	Alternative sequence	351 – 640	290	Missing in isoform 3.		VSP_003295
	Alternative sequence	401	1	S → SDSSSWCDLSSFEFFEEADF SPSQHHTGKALQLQQREGNG TKPAGEPSPRVNKRMLSESS LDPPKVLPPARHSTIPLVIL RKKRGQASPLATGDCSSFIF ADVSSSTPKRSPVKSLPFSP SQ in isoform 4 and isoform 7.		VSP_003296
	Alternative sequence	402	1	F → M in isoform 5.		VSP_003297
	Alternative sequence	403 – 640	238	Missing in isoform 5.		VSP_003298
	Alternative sequence	567 – 640	74	NILTS…RTLVM → TGVQWHDFGSLQPLPPGFKR FSCLSLPRSWDYRHPPPRPA NFEFLVETGFLHVGQAGLEL LTSGDLPASASQSARITGVS HRARPEYSYKLRFNGTSIRR in isoform 6.		VSP_003299
	Natural variant	336	1	T → I. Corresponds to variant rs2229999 [ dbSNP | Ensembl ].		VAR_050188
	Natural variant	422	1	T → N. Corresponds to variant rs2230000 [ dbSNP | Ensembl ].		VAR_050189
Experimental info
	Sequence conflict	511	1	I → F in AAA52032. Ref.1
	Sequence conflict	563	1	A → R in AAA52032. Ref.1
Isoform 4:
	Sequence conflict	433	1	L → F in CAA35503. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: FD5E6694020426ED	FASTA	640	72,341
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 370 380 390 400 410 420 PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE NSDLEMPSLT 430 440 450 460 470 480 STPLIGHKLT VTTPFHRDQT VKTQKENTVF RTPAIKRSIL ESSPRTPTPF KHALAAQEIK 490 500 510 520 530 540 YGPLKMLPQT PSHLVEDLQD VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF 550 560 570 580 590 600 FCSHHWEGDS LNTQLFTQTS PVADAPNILT SSVLMAPASE DEDNVLKAFT VPKNRSLASP 610 620 630 640 LQPCSSTWEP ASCGKMEEQM TSSSQARKYV NAFSARTLVM
	Isoform 2 [UniParc]. Checksum: 75D8144FEEC381C5	FASTA	637	72,032
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQTQNHTCS YPGWHSTTIA DHTRPHGDSA PVSCLGEHHS TPSLPADPGS 370 380 390 400 410 420 LPEESASPAR CMIVHQGTIL DNVKNLLEFA ETLQFIDSFL NTSSNHENSD LEMPSLTSTP 430 440 450 460 470 480 LIGHKLTVTT PFHRDQTVKT QKENTVFRTP AIKRSILESS PRTPTPFKHA LAAQEIKYGP 490 500 510 520 530 540 LKMLPQTPSH LVEDLQDVIK QESDESGIVA EFQENGPPLL KKIKQEVESP TDKSGNFFCS 550 560 570 580 590 600 HHWEGDSLNT QLFTQTSPVA DAPNILTSSV LMAPASEDED NVLKAFTVPK NRSLASPLQP 610 620 630 CSSTWEPASC GKMEEQMTSS SQARKYVNAF SARTLVM
	Isoform 3 [UniParc]. Checksum: 60632631CFEE51FF	FASTA	350	40,620
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 LLMSTENELK GQQVLPLCGP LLNSDIFSDW AANWDGSLCF ATYIVNQQRQ
	Isoform 4 [UniParc]. Checksum: 9D11661393B1A85B	FASTA	761	85,475
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 370 380 390 400 410 420 PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SDSSSWCDLS SFEFFEEADF 430 440 450 460 470 480 SPSQHHTGKA LQLQQREGNG TKPAGEPSPR VNKRMLSESS LDPPKVLPPA RHSTIPLVIL 490 500 510 520 530 540 RKKRGQASPL ATGDCSSFIF ADVSSSTPKR SPVKSLPFSP SQFLNTSSNH ENSDLEMPSL 550 560 570 580 590 600 TSTPLIGHKL TVTTPFHRDQ TVKTQKENTV FRTPAIKRSI LESSPRTPTP FKHALAAQEI 610 620 630 640 650 660 KYGPLKMLPQ TPSHLVEDLQ DVIKQESDES GIVAEFQENG PPLLKKIKQE VESPTDKSGN 670 680 690 700 710 720 FFCSHHWEGD SLNTQLFTQT SPVADAPNIL TSSVLMAPAS EDEDNVLKAF TVPKNRSLAS 730 740 750 760 PLQPCSSTWE PASCGKMEEQ MTSSSQARKY VNAFSARTLV M
	Isoform 5 [UniParc]. Checksum: 331FC406EC1C335C	FASTA	402	46,065
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 370 380 390 400 PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SM
	Isoform 6 [UniParc]. Checksum: BF91C8F858EA12DF	FASTA	666	75,526
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD 370 380 390 400 410 420 PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE NSDLEMPSLT 430 440 450 460 470 480 STPLIGHKLT VTTPFHRDQT VKTQKENTVF RTPAIKRSIL ESSPRTPTPF KHALAAQEIK 490 500 510 520 530 540 YGPLKMLPQT PSHLVEDLQD VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF 550 560 570 580 590 600 FCSHHWEGDS LNTQLFTQTS PVADAPTGVQ WHDFGSLQPL PPGFKRFSCL SLPRSWDYRH 610 620 630 640 650 660 PPPRPANFEF LVETGFLHVG QAGLELLTSG DLPASASQSA RITGVSHRAR PEYSYKLRFN GTSIRR
	Isoform 7 [UniParc]. Checksum: 0F2142F19B9D4E48	FASTA	758	85,166
	10 20 30 40 50 60 MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 70 80 90 100 110 120 DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 130 140 150 160 170 180 HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 190 200 210 220 230 240 IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV 250 260 270 280 290 300 NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 310 320 330 340 350 360 LLMSTENELK GQQTQNHTCS YPGWHSTTIA DHTRPHGDSA PVSCLGEHHS TPSLPADPGS 370 380 390 400 410 420 LPEESASPAR CMIVHQGTIL DNVKNLLEFA ETLQFIDSDS SSWCDLSSFE FFEEADFSPS 430 440 450 460 470 480 QHHTGKALQL QQREGNGTKP AGEPSPRVNK RMLSESSLDP PKVLPPARHS TIPLVILRKK 490 500 510 520 530 540 RGQASPLATG DCSSFIFADV SSSTPKRSPV KSLPFSPSQF LNTSSNHENS DLEMPSLTST 550 560 570 580 590 600 PLIGHKLTVT TPFHRDQTVK TQKENTVFRT PAIKRSILES SPRTPTPFKH ALAAQEIKYG 610 620 630 640 650 660 PLKMLPQTPS HLVEDLQDVI KQESDESGIV AEFQENGPPL LKKIKQEVES PTDKSGNFFC 670 680 690 700 710 720 SHHWEGDSLN TQLFTQTSPV ADAPNILTSS VLMAPASEDE DNVLKAFTVP KNRSLASPLQ 730 740 750 PCSSTWEPAS CGKMEEQMTS SSQARKYVNA FSARTLVM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human c-myb protooncogene: nucleotide sequence of cDNA and organization of the genomic locus." Majello B., Kenyon L.C., Dalla-Favera R. Proc. Natl. Acad. Sci. U.S.A. 83:9636-9640(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Alternative splicing of the human c-myb gene." Westin E.H., Gorse K.M., Clarke M.F. Oncogene 5:1117-1124(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing a quantitative trait locus for fetal hemoglobin expression in adults." Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L. BMC Genomics 5:33-33(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
[4]	"Characterization of the complete sequence structure of the human c-myb gene." Westin E.H., Gorse K.M. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6). Tissue: Liver and Placenta.
[5]	Gaillard C., Perbal B. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"Complex RNA splicing produces multiple forms of c-Myb with distinct transcriptional activities." O'Rourke J.P. Jr., Ness S.A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), ALTERNATIVE SPLICING.
[7]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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 1). Tissue: Testis.
[10]	"Identification of a second promoter in the human c-myb proto-oncogene." Jacobs S.M., Gorse K.M., Westin E.H. Oncogene 9:227-235(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-47.
[11]	"Positive autoregulation of c-myb expression via Myb binding sites in the 5' flanking region of the human c-myb gene." Nicolaides N.C., Gualdi R., Casadevall C., Manzella L., Calabretta B. Mol. Cell. Biol. 11:6166-6176(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[12]	"Studies of the human c-myb gene and its product in human acute leukemias." Slamon D.J., Boone T.C., Murdock D.C., Keith D.E., Press M.F., Larson R.A., Souza L.M. Science 233:347-351(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-640 (ISOFORM 1).
[13]	"Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences." Dasgupta P., Reddy E.P. Oncogene 4:1419-1423(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[14]	"Transcriptional activation by human c-myb and v-myb genes." Kalkbrenner F., Guehmann S., Moelling K. Oncogene 5:657-661(1990) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTION ACTIVATION DOMAIN.
[15]	"p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3." Tanikawa J., Ichikawa-Iwata E., Kanei-Ishii C., Nakai A., Matsuzawa S., Reed J.C., Ishii S. J. Biol. Chem. 275:15578-15585(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[16]	"HIPK1 interacts with c-Myb and modulates its activity through phosphorylation." Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S. Biochem. Biophys. Res. Commun. 388:150-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY HIPK1, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-480, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15024 mRNA. Translation: AAA52032.1. X52125 mRNA. Translation: CAA36371.1. AJ606319 mRNA. Translation: CAE55170.1. AJ606320 mRNA. Translation: CAE55171.1. AJ616791 mRNA. Translation: CAF04482.1. AJ616791 mRNA. Translation: CAF04479.1. U22376 Genomic DNA. Translation: AAB49034.1. U22376 Genomic DNA. Translation: AAB49035.1. U22376 Genomic DNA. Translation: AAB49036.1. U22376 Genomic DNA. Translation: AAB49037.1. U22376 Genomic DNA. Translation: AAB49038.1. U22376 Genomic DNA. Translation: AAB49039.1. AF104863 mRNA. Translation: AAC96326.1. AY787461 mRNA. No translation available. AL023693 Genomic DNA. No translation available. CH471051 Genomic DNA. Translation: EAW47969.1. CH471051 Genomic DNA. Translation: EAW47973.1. BC064955 mRNA. Translation: AAH64955.1. M13665 mRNA. Translation: AAA52030.1. M13666 mRNA. Translation: AAA52031.1. Sequence problems. X17469 mRNA. Translation: CAA35503.1.
IPI	IPI00219496. IPI00219497. IPI00420046. IPI00471985. IPI00749442. IPI00930645. IPI00983514.
PIR	TVHUMB. A26661.
RefSeq	NP_001123644.1. NM_001130172.1. NP_001123645.1. NM_001130173.1. NP_001155128.1. NM_001161656.1. NP_005366.2. NM_005375.2.
UniGene	Hs.606320.
3D structure databases
ProteinModelPortal	P10242.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1057N.
IntAct	P10242. 28 interactions.
MINT	MINT-6772664.
STRING	9606.ENSP00000339992.
PTM databases
PhosphoSite	P10242.
Polymorphism databases
DMDM	2815504.
Proteomic databases
PaxDb	P10242.
PRIDE	P10242.
Protocols and materials databases
DNASU	4602.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341911; ENSP00000339992; ENSG00000118513. ENST00000367812; ENSP00000356786; ENSG00000118513. ENST00000367814; ENSP00000356788; ENSG00000118513. ENST00000430686; ENSP00000390460; ENSG00000118513. ENST00000442647; ENSP00000410825; ENSG00000118513. ENST00000525477; ENSP00000437081; ENSG00000118513. ENST00000525514; ENSP00000435578; ENSG00000118513. ENST00000528774; ENSP00000434723; ENSG00000118513. ENST00000529586; ENSP00000437264; ENSG00000118513. ENST00000533384; ENSP00000432811; ENSG00000118513. ENST00000533808; ENSP00000435293; ENSG00000118513. ENST00000533837; ENSP00000434639; ENSG00000118513.
GeneID	4602.
KEGG	hsa:4602.
UCSC	uc003qfc.3. human. uc003qfh.3. human. uc003qfq.3. human. uc003qfu.3. human.
Organism-specific databases
CTD	4602.
GeneCards	GC06P135503.
HGNC	HGNC:7545. MYB.
HPA	CAB017704.
MIM	189990. gene.
neXtProt	NX_P10242.
Orphanet	86849. Acute basophilic leukemia. 99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKB	PA31345.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5147.
HOVERGEN	HBG007964.
KO	K09420.
OMA	HLMGFAH.
OrthoDB	EOG4H9XKD.
Enzyme and pathway databases
Pathway_Interaction_DB	il2_pi3kpathway. IL2 signaling events mediated by PI3K. il4_2pathway. IL4-mediated signaling events.
Reactome	REACT_604. Hemostasis.
SignaLink	P10242.
Gene expression databases
ArrayExpress	P10242.
Bgee	P10242.
CleanEx	HS_MYB.
Genevestigator	P10242.
GermOnline	ENSG00000118513. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.60. 3 hits.
InterPro	IPR015395. C-myb_C. IPR009057. Homeodomain-like. IPR017930. Myb_dom. IPR001005. SANT/Myb. IPR012642. Tscrpt_reg_Wos2-domain. [Graphical view]
Pfam	PF09316. Cmyb_C. 1 hit. PF07988. LMSTEN. 1 hit. PF00249. Myb_DNA-binding. 1 hit. [Graphical view]
SMART	SM00717. SANT. 3 hits. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 2 hits.
PROSITE	PS51294. HTH_MYB. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYB. human.
GenomeRNAi	4602.
NextBio	17700.
SOURCE	Search...

Entry information

Entry name

MYB_HUMAN

Accession

Primary (citable) accession number: P10242
Secondary accession number(s): E9PNL6 , P78391, P78392, P78525, P78526, Q14023, Q14024, Q708E4, Q708E7, Q9UE83

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	May 29, 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.