P41212 (ETV6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor ETV6

Alternative name(s):
ETS translocation variant 6
ETS-related protein Tel1
Short name=Tel

Gene names

Name:	ETV6
Synonyms:	TEL, TEL1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'.
Subunit structure	Can form homodimers or heterodimers with TEL2 or FLI1. Interacts with L3MBTL1 and HDAC9. Ref.14 Ref.15
Subcellular location	Nucleus.
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylation of Ser-257 by MAPK14 (p38) inhibits ETV6 transcriptional repression.
Involvement in disease	Note=A chromosomal aberration involving ETV6 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with PDGFRB. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML). Ref.12 Note=Chromosomal aberrations involving ETV6 are found in a form of acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with MN1; translocation t(4;12)(q12;p13) with CHIC2. Ref.7 Ref.8 Ref.16 Note=Chromosomal aberrations involving ETV6 are found in childhood acute lymphoblastic leukemia (ALL). Translocations t(12;21)(p12;q22) and t(12;21)(p13;q22) with RUNX1/AML1. Note=A chromosomal aberration involving ETV6 is found in a form of pre-B acute myeloid leukemia. Translocation t(9;12)(p24;p13) with JAK2. Note=A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS) with basophilia. Translocation t(5;12)(q31;p13) with ACSL6. Note=A chromosomal aberration involving ETV6 is found in acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ACSL6. Note=A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS). Translocation t(1;12)(p36.1;p13) with MDS2. Defects in ETV6 are a cause of myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]. A hematologic disorder characterized by malignant eosinophils proliferation. Note=A chromosomal aberration involving ETV6 is found in many instances of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;12) with PDGFRB on chromosome 5 creating an ETV6-PDGFRB fusion protein. Defects in ETV6 are a cause of acute myelogenous leukemia (AML) [MIM:601626]. AML is a malignant disease in which hematopoietic precursors are arrested in an early stage of development. Ref.7 Ref.8 Ref.16 Note=A chromosomal aberration involving ETV6 is found in acute lymphoblastic leukemia. Translocation t(9;12)(p13;p13) with PAX5.
Sequence similarities	Belongs to the ETS family. Contains 1 ETS DNA-binding domain. Contains 1 PNT (pointed) domain.
Sequence caution	The sequence ABI30005.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Disease mutation Proto-oncogene
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein domain specific binding Inferred from physical interaction Ref.14. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC9	Q9UKV0-3	3	EBI-1372759,EBI-765476

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Transcription factor ETV6

PRO_0000204121

Regions

Domain

40 – 124

85

PNT

DNA binding

339 – 420

82

ETS

Sites

Site

11 – 12

2

Breakpoint for translocation to form CHIC2-ETV6 in AML

Site

54 – 55

2

Breakpoint for translocation to form ETV6-MDS2 in MDS

Site

55 – 56

2

Breakpoint for translocation to form PAX5-ETV6

Site

336 – 337

2

Breakpoint for translocation to form ETV6-AML1 in ALL

Amino acid modifications

Modified residue

11

1

N6-acetyllysine Ref.20

Modified residue

16

1

Phosphoserine Ref.18 Ref.19

Modified residue

18

1

Phosphothreonine Ref.17 Ref.19

Modified residue

22

1

Phosphoserine Ref.11 Ref.17 Ref.18 Ref.19

Modified residue

213

1

Phosphoserine Ref.18

Modified residue

257

1

Phosphoserine; by MAPK14 Ref.11

Modified residue

302

1

N6-acetyllysine Ref.20

Natural variations

Natural variant

344

1

Y → YG in one individual with AML; somatic mutation; unable to repress transcription. Ref.16

VAR_034600

Experimental info

Mutagenesis

22

1

S → A: No effect.

Mutagenesis

213

1

S → A: No effect. Ref.11

Mutagenesis

238

1

S → A: No effect. Ref.11

Mutagenesis

257

1

S → A: No phosphorylation by MAPK14. Ref.11

Secondary structure

1

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452

Helix Strand Turn

Details...

Helix

52 – 54

3

Helix

58 – 60

3

Helix

63 – 76

14

Turn

84 – 87

4

Helix

91 – 94

4

Helix

99 – 105

7

Turn

107 – 109

3

Helix

110 – 122

13

Helix

341 – 350

10

Helix

352 – 354

3

Turn

355 – 357

3

Beta strand

358 – 362

5

Helix

363 – 365

3

Beta strand

367 – 371

5

Helix

373 – 383

11

Helix

391 – 403

13

Beta strand

406 – 408

3

Beta strand

411 – 419

9

Helix

424 – 426

3

Beta strand

430 – 432

3

Helix

434 – 438

5

Sequences

	Sequence		Length	Mass (Da)
	P41212 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: DEC45682ECADECBB	FASTA	452	53,000
	10 20 30 40 50 60 MSETPAQCSI KQERISYTPP ESPVPSYASS TPLHVPVPRA LRMEEDSIRL PAHLRLQPIY 70 80 90 100 110 120 WSRDDVAQWL KWAENEFSLR PIDSNTFEMN GKALLLLTKE DFRYRSPHSG DVLYELLQHI 130 140 150 160 170 180 LKQRKPRILF SPFFHPGNSI HTQPEVILHQ NHEEDNCVQR TPRPSVDNVH HNPPTIELLH 190 200 210 220 230 240 RSRSPITTNH RPSPDPEQRP LRSPLDNMIR RLSPAERAQG PRPHQENNHQ ESYPLSVSPM 250 260 270 280 290 300 ENNHCPASSE SHPKPSSPRQ ESTRVIQLMP SPIMHPLILN PRHSVDFKQS RLSEDGLHRE 310 320 330 340 350 360 GKPINLSHRE DLAYMNHIMV SVSPPEEHAM PIGRIADCRL LWDYVYQLLS DSRYENFIRW 370 380 390 400 410 420 EDKESKIFRI VDPNGLARLW GNHKNRTNMT YEKMSRALRH YYKLNIIRKE PGQRLLFRFM 430 440 450 KTPDEIMSGR TDRLEHLESQ ELDEQIYQED EC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation." Golub T.R., Barker G.F., Lovett M., Gilliland D.G. Cell 77:307-316(1994) [PubMed: 8168137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Urinary bladder.
[3]	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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"Genomic organization of TEL: the human ETS-variant gene 6." Baens M., Peeters P., Guo C., Aerssens J., Marynen P. Genome Res. 6:404-413(1996) [PubMed: 8743990] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-109; 111-336 AND 338-452.
[6]	"Genome-wide analysis of genetic alterations in acute lymphoblastic leukaemia." Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E., Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H., Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R. Nature 446:758-764(2007) [PubMed: 17344859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-452, CHROMOSOMAL TRANSLOCATION WITH PAX5.
[7]	"Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute lymphoblastic leukemia." Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C., Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G. Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995) [PubMed: 7761424] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH AML1.
[8]	"The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene fusion." Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D., Berger R., Bernard O.A. Blood 85:3662-3670(1995) [PubMed: 7780150] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH AML1.
[9]	"Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13)." Yagasaki F., Jinnai I., Yoshida S., Yokoyama Y., Matsuda A., Kusumoto S., Kobayashi H., Terasaki H., Ohyashiki K., Asou N., Murohashi I., Bessho M., Hirashima K. Genes Chromosomes Cancer 26:192-202(1999) [PubMed: 10502316] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ACSL6.
[10]	"Fusion of a novel gene, BTL, to ETV6 in acute myeloid leukemias with a t(4;12)(q11-q12;p13)." Cools J., Bilhou-Nabera C., Wlodarska I., Cabrol C., Talmant P., Bernard P., Hagemeijer A., Marynen P. Blood 94:1820-1824(1999) [PubMed: 10477709] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CHIC2.
[11]	"Functional regulation of TEL by p38-induced phosphorylation." Arai H., Maki K., Waga K., Sasaki K., Nakamura Y., Imai Y., Kurokawa M., Hirai H., Mitani K. Biochem. Biophys. Res. Commun. 299:116-125(2002) [PubMed: 12435397] [Abstract] Cited for: PHOSPHORYLATION AT SER-22 AND SER-257, MUTAGENESIS OF SER-213; SER-238 AND SER-257.
[12]	"A novel gene, MDS2, is fused to ETV6/TEL in a t(1;12)(p36.1;p13) in a patient with myelodysplastic syndrome." Odero M.D., Vizmanos J.L., Roman J.P., Lahortiga I., Panizo C., Calasanz M.J., Zeleznik-Le N.J., Rowley J.D., Novo F.J. Genes Chromosomes Cancer 35:11-19(2002) [PubMed: 12203785] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MDS2.
[13]	"Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor beta." Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J., Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E., Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E., Silberman S., Schultheis B., Cross N.C.P., Goldman J.M. N. Engl. J. Med. 347:481-487(2002) [PubMed: 12181402] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
[14]	"The human L(3)MBT Polycomb group protein is a transcriptional repressor and interacts physically and functionally with TEL (ETV6)." Boccuni P., MacGrogan D., Scandura J.M., Nimer S.D. J. Biol. Chem. 278:15412-15420(2003) [PubMed: 12588862] [Abstract] Cited for: INTERACTION WITH L3MBTL1.
[15]	"The histone deacetylase 9 gene encodes multiple protein isoforms." Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M., Zelent A. J. Biol. Chem. 278:16059-16072(2003) [PubMed: 12590135] [Abstract] Cited for: INTERACTION WITH HDAC9.
[16]	"Somatic heterozygous mutations in ETV6 (TEL) and frequent absence of ETV6 protein in acute myeloid leukemia." Barjesteh van Waalwijk van Doorn-Khosrovani S., Spensberger D., de Knegt Y., Tang M., Loewenberg B., Delwel R. Oncogene 24:4129-4137(2005) [PubMed: 15806161] [Abstract] Cited for: INVOLVEMENT IN AML, VARIANT GLY-344 INS, CHARACTERIZATION OF VARIANT GLY-344 INS.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-22, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-22 AND SER-213, MASS SPECTROMETRY.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-18 AND SER-22, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-302, MASS SPECTROMETRY.
[21]	"Solution structure of ets domain transcriptional factor ETV6 protein." RIKEN structural genomics initiative (RSGI) Submitted (DEC-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 338-442.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U11732 mRNA. Translation: AAA19786.1.
AK289441 mRNA. Translation: BAF82130.1.
CH471094 Genomic DNA. Translation: EAW96240.1.
BC043399 mRNA. Translation: AAH43399.1.
U61375 Genomic DNA. Translation: AAC50690.1.
U63312 Genomic DNA. Translation: AAB17134.1.
U63313 Genomic DNA. Translation: AAB17135.1.
DQ841178 mRNA. Translation: ABI30005.1. Different initiation.

IPI

IPI00013159.

RefSeq

NP_001978.1. NM_001987.4.

UniGene

Hs.504765.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JI7	X-ray	1.45	A/B/C	47-123	[»]
1LKY	X-ray	2.30	A/B/C/D/E/F	47-123	[»]
2DAO	NMR	-	A	338-442	[»]
2QAR	X-ray	2.40	A/B/D/E	47-124	[»]
2QB0	X-ray	2.56	A/C	47-123	[»]
2QB1	X-ray	2.61	A/B	47-121	[»]

ProteinModelPortal

P41212.

SMR

P41212. Positions 21-125, 338-442.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17028N.

IntAct

P41212. 7 interactions.

STRING

P41212.

PTM databases

PhosphoSite

P41212.

Polymorphism databases

DMDM

730927.

Proteomic databases

PeptideAtlas

P41212.

PRIDE

P41212.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266427; ENSP00000266427; ENSG00000139083.

GeneID

2120.

KEGG

hsa:2120.

UCSC

uc001qzz.1. human.

Organism-specific databases

CTD

2120.

GeneCards

GC12P011703.

H-InvDB

HIX0026395.

HGNC

HGNC:3495. ETV6.

HPA

HPA000264.

MIM

131440. phenotype.
600618. gene.
601626. phenotype.

neXtProt

NX_P41212.

Orphanet

2030. Fibrosarcoma.
99860. Precursor B-cell acute lymphoblastic leukemia.

PharmGKB

PA27909.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG716146.

HOVERGEN

HBG005617.

InParanoid

P41212.

OMA

NPRHSMD.

OrthoDB

EOG4ZS938.

PhylomeDB

P41212.

Gene expression databases

ArrayExpress

P41212.

Bgee

P41212.

CleanEx

HS_ETV6.

Genevestigator

P41212.

GermOnline

ENSG00000139083. Homo sapiens.

Family and domain databases

InterPro

IPR000418. Ets.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.150.50. SAM_type. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K03211.

Pfam

PF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]

PRINTS

PR00454. ETSDOMAIN.

SMART

SM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS00345. ETS_DOMAIN_1. False negative.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

8571.

SOURCE

Search...

Entry information

Entry name

ETV6_HUMAN

Accession

Primary (citable) accession number: P41212
Secondary accession number(s): A3QVP6 , A8K076, Q9UMF6, Q9UMF7, Q9UMG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 130 of the entry and version 1 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.