Q08874 (MITF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microphthalmia-associated transcription factor

Gene names

Name:	Mitf
Synonyms:	Bw, Mi, Vit

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium.
Subunit structure	Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA in the form of homodimer or heterodimer with either TFE3, TFEB or TFEC. Identified in a complex with HINT1 and CTNNB1 By similarity. Interacts with KARS. Ref.8
Subcellular location	Nucleus Ref.7.
Tissue specificity	In the adult, expressed at high levels in the heart, skin, skeletal muscle, intestine, stomach, kidney, ovary, lung, spleen and brain. In the embryo, expressed in developing eye, ear, skin and heart. Isoform M is expressed in melanocytes and also in the embryonic and adult heart while isoform A and isoform H are more widely expressed. Ref.1
Post-translational modification	Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter. Phosphorylated at Ser-180 and Ser-516 following KIT signaling, trigerring a short live activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and RPS6KA1, respectively, activate the transcription factor activity but also promote ubiquitination and subsequent degradation by the proteasome By similarity. Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome. Deubiquitinated by USP13, preventing its degradation By similarity.
Involvement in disease	Defects in Mitf are the cause of microphthalmia (mi), a condition characterized by loss of pigmentation; reduced eye size; failure of secondary bone resorption; reduced numbers of mast cells; early onset of deafness, and which gives rise to a number of different phenotypes. Among them, microphthalmia-eyeless white (mi-ew) has a normal appearance at the heterozygous state, but shows white coat; eyes almost absent and eyelids never open at homozygosity. Microphthalmia-black and white spot (mi-bws) is normal at heterozygosity, and presents white spots and black eyes at homozygous state. Microphthalmia-white (mi-wh) has reduced coat color and eye pigmentation; spots on toes, tail and belly; inner ear defects at heterozygosity, and at homozygosity shows white coat; eyes small and inner iris slightly pigmented; spinal ganglia, adrenal medulla and dermis smaller than normal, and inner ear defects. Microphthalmia-vitiligo (mi-vi) has normal phenotype at heterozygosity, but shows gradual depigmentation of coat, skin and eyes; and retinal degeneration at homozygosity. Microphthalmia-spotted (mi-sp) shows normal phenotype; at homozygosity, however, tyrosinase activity in skin is reduced. Microphthalmia-defective irism (mi-di) has reduced retinal pigmentation at heterozygosity and shows white coat; eyes of reduced sized and possible mild osteoporosis at homozygosity. Microphthalmia-cloudy eyed (mi-ce) has a normal appearance at the heterozygous state, but shows white coat; eyes of reduced size and unpigmented at homozygosity. Microphthalmia-red-eyed white (mi-rw) has a normal appearance at the homozygous state, but shows white coat with one or more pigmented spots around the head/and or tail; eyes are small and red at heterozygosity. Microphthalmia-black-eyed white (mi-bw) shows a white coat but normal sized eyes which reamin black at homozygosity.
Sequence similarities	Belongs to the MiT/TFE family. Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Deafness Disease mutation
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from direct assay PubMed 12235125. Source: MGI bone remodeling Inferred from mutant phenotype PubMed 12086670. Source: MGI camera-type eye development Inferred from genetic interaction PubMed 15576400. Source: MGI cell fate commitment Inferred from mutant phenotype PubMed 15576400. Source: MGI melanocyte differentiation Inferred from mutant phenotype PubMed 12086670PubMed 2379821. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 12086670. Source: MGI osteoclast differentiation Inferred from mutant phenotype PubMed 12086670. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15304486. Source: BHF-UCL regulation of cell proliferation Inferred from direct assay PubMed 12235125. Source: MGI regulation of osteoclast differentiation Inferred from mutant phenotype PubMed 11930005. Source: MGI
Cellular_component	nucleus Inferred from direct assay PubMed 12235125. Source: MGI
Molecular_function	RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 15729346. Source: MGI chromatin binding Inferred from direct assay PubMed 15729346. Source: MGI sequence-specific DNA binding Inferred from sequence alignment PubMed 12086670. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q08874-1)

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 A1 (identifier: Q08874-2)

The sequence of this isoform differs from the canonical sequence as follows:
     139-194: Missing.

Isoform A2 (identifier: Q08874-3)

The sequence of this isoform differs from the canonical sequence as follows:
     119-222: Missing.
     294-299: Missing.
     318-319: LI → LSKFV

Isoform H (identifier: Q08874-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRFEMLIPCSFESLCL

Isoform H1 (identifier: Q08874-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRFEMLIPCSFESLCL
     119-254: Missing.

Isoform H2 (identifier: Q08874-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRFEMLIPCSFESLCL
     119-254: Missing.
     294-319: ACIFPTESEARALAKERQKKDNHNLI → V

Isoform H3 (identifier: Q08874-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRFEMLIPCSFESLCL
     139-194: Missing.

Isoform M (identifier: Q08874-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: MQSESGIVPD...ATQVPMEVLK → MLEMLEYSHYQ

Isoform M1 (identifier: Q08874-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: MQSESGIVPD...ATQVPMEVLK → MLEMLEYSHYQ
     294-299: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 526

526

Microphthalmia-associated transcription factor

PRO_0000127277

Regions

Domain

311 – 364

54

bHLH

Region

224 – 291

68

Transactivation By similarity

Region

374 – 395

22

Leucine-zipper

Region

401 – 431

31

DNA binding regulation By similarity

Amino acid modifications

Modified residue

180

1

Phosphoserine; by MAPK By similarity

Modified residue

405

1

Phosphoserine; by GSK3 By similarity

Modified residue

414

1

Phosphoserine Ref.9

Modified residue

491

1

Phosphoserine By similarity

Modified residue

516

1

Phosphoserine; by RPS6KA1 By similarity

Cross-link

289

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

423

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 118

118

MQSES…MEVLK → MLEMLEYSHYQ in isoform M and isoform M1.

VSP_002130

Alternative sequence

1 – 35

35

MQSES…PLKSS → MEALRFEMLIPCSFESLCL in isoform H, isoform H1, isoform H2 and isoform H3.

VSP_002129

Alternative sequence

119 – 254

136

Missing in isoform H1 and isoform H2.

VSP_002132

Alternative sequence

119 – 222

104

Missing in isoform A2.

VSP_002131

Alternative sequence

139 – 194

56

Missing in isoform A1 and isoform H3.

VSP_002133

Alternative sequence

294 – 319

26

ACIFP…NHNLI → V in isoform H2.

VSP_002135

Alternative sequence

294 – 299

6

Missing in isoform A2 and isoform M1.

VSP_002134

Alternative sequence

318 – 319

2

LI → LSKFV in isoform A2.

VSP_002136

Natural variant

36 – 118

83

Missing in microphthalmia-red-eyed white/mi-rw.

Natural variant

119 – 254

136

Missing in microphthalmia-white spot/mi-ws.

Natural variant

139 – 194

56

Missing in microphthalmia-black and white spot/mi-bws.

Natural variant

294 – 319

26

ACIFP…NHNLI → V in microphthalmia-eyeless-white/mi-ew.

Natural variant

294 – 299

6

Missing in microphthalmia-spotted/mi-sp.

Natural variant

319

1

I → N in microphthalmia-white/mi-wh.

Natural variant

323

1

Missing in microphthalmia/mi.

Natural variant

329

1

D → N in microphthalmia-vitiligo/mi-vi.

Natural variant

370 – 526

157

Missing in microphthalmia-cloudy-eyed/mi-ce and microphthalmia-defective iris/mi-di.

Experimental info

Sequence conflict

41

1

P → S in AAF81266. Ref.2

Sequence conflict

41

1

P → S in AAF81267. Ref.2

Sequence conflict

41

1

P → S in AAF81268. Ref.2

Sequence conflict

41

1

P → S in AAF81269. Ref.2

Sequence conflict

41

1

P → S in AAF81270. Ref.2

Sequence conflict

41

1

P → S in AAF81271. Ref.2

Sequence conflict

41

1

P → S in AAF81272. Ref.2

Sequence conflict

48

1

I → L in AAF81266. Ref.2

Sequence conflict

48

1

I → L in AAF81267. Ref.2

Sequence conflict

48

1

I → L in AAF81268. Ref.2

Sequence conflict

48

1

I → L in AAF81269. Ref.2

Sequence conflict

48

1

I → L in AAF81270. Ref.2

Sequence conflict

48

1

I → L in AAF81271. Ref.2

Sequence conflict

48

1

I → L in AAF81272. Ref.2

Sequence conflict

52

1

S → T in AAF81266. Ref.2

Sequence conflict

52

1

S → T in AAF81267. Ref.2

Sequence conflict

52

1

S → T in AAF81268. Ref.2

Sequence conflict

52

1

S → T in AAF81269. Ref.2

Sequence conflict

52

1

S → T in AAF81270. Ref.2

Sequence conflict

52

1

S → T in AAF81271. Ref.2

Sequence conflict

52

1

S → T in AAF81272. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

526

Helix Strand Turn

Details...

Helix

324 – 337

14

Helix

350 – 366

17

Helix

368 – 401

34

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified February 21, 2001. Version 3. Checksum: 46F759A85ECC4B73	FASTA	526	58,627
	10 20 30 40 50 60 MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR 70 80 90 100 110 120 QQLMREQMQE QERREQQQKL QAAQFMQQRV AVSQTPAINV SVPTTLPSAT QVPMEVLKVQ 130 140 150 160 170 180 THLENPTKYH IQQAQRHQVK QYLSTTLANK HASQVLSSPC PNQPGDHAMP PVPGSSAPNS 190 200 210 220 230 240 PMAMLTLNSN CEKEAFYKFE EQSRAESECP GMNTHSRASC MQMDDVIDDI ISLESSYNEE 250 260 270 280 290 300 ILGLMDPALQ MANTLPVSGN LIDLYSNQGL PPPGLTISNS CPANLPNIKR ELTACIFPTE 310 320 330 340 350 360 SEARALAKER QKKDNHNLIE RRRRFNINDR IKELGTLIPK SNDPDMRWNK GTILKASVDY 370 380 390 400 410 420 IRKLQREQQR AKDLENRQKK LEHANRHLLL RVQELEMQAR AHGLSLIPST GLCSPDLVNR 430 440 450 460 470 480 IIKQEPVLEN CSQELVQHQA DLTCTTTLDL TDGTITFTNN LGTMPESSPA YSIPRKMGSN 490 500 510 520 LEDILMDDAL SPVGVTDPLL SSVSPGASKT SSRRSSMSAE ETEHAC
	Isoform A1 [UniParc]. Checksum: A355DD0C45BC9E31	FASTA	470	52,768
	10 20 30 40 50 60 MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR 70 80 90 100 110 120 QQLMREQMQE QERREQQQKL QAAQFMQQRV AVSQTPAINV SVPTTLPSAT QVPMEVLKVQ 130 140 150 160 170 180 THLENPTKYH IQQAQRHQAF YKFEEQSRAE SECPGMNTHS RASCMQMDDV IDDIISLESS 190 200 210 220 230 240 YNEEILGLMD PALQMANTLP VSGNLIDLYS NQGLPPPGLT ISNSCPANLP NIKRELTACI 250 260 270 280 290 300 FPTESEARAL AKERQKKDNH NLIERRRRFN INDRIKELGT LIPKSNDPDM RWNKGTILKA 310 320 330 340 350 360 SVDYIRKLQR EQQRAKDLEN RQKKLEHANR HLLLRVQELE MQARAHGLSL IPSTGLCSPD 370 380 390 400 410 420 LVNRIIKQEP VLENCSQELV QHQADLTCTT TLDLTDGTIT FTNNLGTMPE SSPAYSIPRK 430 440 450 460 470 MGSNLEDILM DDALSPVGVT DPLLSSVSPG ASKTSSRRSS MSAEETEHAC
	Isoform A2 [UniParc]. Checksum: 99F18E2972927452	FASTA	419	46,837
	10 20 30 40 50 60 MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR 70 80 90 100 110 120 QQLMREQMQE QERREQQQKL QAAQFMQQRV AVSQTPAINV SVPTTLPSAT QVPMEVLKMD 130 140 150 160 170 180 DVIDDIISLE SSYNEEILGL MDPALQMANT LPVSGNLIDL YSNQGLPPPG LTISNSCPAN 190 200 210 220 230 240 LPNIKRELTE SEARALAKER QKKDNHNLSK FVERRRRFNI NDRIKELGTL IPKSNDPDMR 250 260 270 280 290 300 WNKGTILKAS VDYIRKLQRE QQRAKDLENR QKKLEHANRH LLLRVQELEM QARAHGLSLI 310 320 330 340 350 360 PSTGLCSPDL VNRIIKQEPV LENCSQELVQ HQADLTCTTT LDLTDGTITF TNNLGTMPES 370 380 390 400 410 SPAYSIPRKM GSNLEDILMD DALSPVGVTD PLLSSVSPGA SKTSSRRSSM SAEETEHAC
	Isoform H [UniParc]. Checksum: 57F10FE5A4A95175	FASTA	510	56,814
	10 20 30 40 50 60 MEALRFEMLI PCSFESLCLS SAEHPGASKP PISSSSMTSR ILLRQQLMRE QMQEQERREQ 70 80 90 100 110 120 QQKLQAAQFM QQRVAVSQTP AINVSVPTTL PSATQVPMEV LKVQTHLENP TKYHIQQAQR 130 140 150 160 170 180 HQVKQYLSTT LANKHASQVL SSPCPNQPGD HAMPPVPGSS APNSPMAMLT LNSNCEKEAF 190 200 210 220 230 240 YKFEEQSRAE SECPGMNTHS RASCMQMDDV IDDIISLESS YNEEILGLMD PALQMANTLP 250 260 270 280 290 300 VSGNLIDLYS NQGLPPPGLT ISNSCPANLP NIKRELTACI FPTESEARAL AKERQKKDNH 310 320 330 340 350 360 NLIERRRRFN INDRIKELGT LIPKSNDPDM RWNKGTILKA SVDYIRKLQR EQQRAKDLEN 370 380 390 400 410 420 RQKKLEHANR HLLLRVQELE MQARAHGLSL IPSTGLCSPD LVNRIIKQEP VLENCSQELV 430 440 450 460 470 480 QHQADLTCTT TLDLTDGTIT FTNNLGTMPE SSPAYSIPRK MGSNLEDILM DDALSPVGVT 490 500 510 DPLLSSVSPG ASKTSSRRSS MSAEETEHAC
	Isoform H1 [UniParc]. Checksum: A18701591F5D55D9	FASTA	374	41,769
	10 20 30 40 50 60 MEALRFEMLI PCSFESLCLS SAEHPGASKP PISSSSMTSR ILLRQQLMRE QMQEQERREQ 70 80 90 100 110 120 QQKLQAAQFM QQRVAVSQTP AINVSVPTTL PSATQVPMEV LKLPVSGNLI DLYSNQGLPP 130 140 150 160 170 180 PGLTISNSCP ANLPNIKREL TACIFPTESE ARALAKERQK KDNHNLIERR RRFNINDRIK 190 200 210 220 230 240 ELGTLIPKSN DPDMRWNKGT ILKASVDYIR KLQREQQRAK DLENRQKKLE HANRHLLLRV 250 260 270 280 290 300 QELEMQARAH GLSLIPSTGL CSPDLVNRII KQEPVLENCS QELVQHQADL TCTTTLDLTD 310 320 330 340 350 360 GTITFTNNLG TMPESSPAYS IPRKMGSNLE DILMDDALSP VGVTDPLLSS VSPGASKTSS 370 RRSSMSAEET EHAC
	Isoform H2 [UniParc]. Checksum: 686DEC9758924B01	FASTA	349	38,902
	10 20 30 40 50 60 MEALRFEMLI PCSFESLCLS SAEHPGASKP PISSSSMTSR ILLRQQLMRE QMQEQERREQ 70 80 90 100 110 120 QQKLQAAQFM QQRVAVSQTP AINVSVPTTL PSATQVPMEV LKLPVSGNLI DLYSNQGLPP 130 140 150 160 170 180 PGLTISNSCP ANLPNIKREL TVERRRRFNI NDRIKELGTL IPKSNDPDMR WNKGTILKAS 190 200 210 220 230 240 VDYIRKLQRE QQRAKDLENR QKKLEHANRH LLLRVQELEM QARAHGLSLI PSTGLCSPDL 250 260 270 280 290 300 VNRIIKQEPV LENCSQELVQ HQADLTCTTT LDLTDGTITF TNNLGTMPES SPAYSIPRKM 310 320 330 340 GSNLEDILMD DALSPVGVTD PLLSSVSPGA SKTSSRRSSM SAEETEHAC
	Isoform H3 [UniParc]. Checksum: 9859C4B41D4CAA00	FASTA	454	50,954
	10 20 30 40 50 60 MEALRFEMLI PCSFESLCLS SAEHPGASKP PISSSSMTSR ILLRQQLMRE QMQEQERREQ 70 80 90 100 110 120 QQKLQAAQFM QQRVAVSQTP AINVSVPTTL PSATQVPMEV LKVQTHLENP TKYHIQQAQR 130 140 150 160 170 180 HQAFYKFEEQ SRAESECPGM NTHSRASCMQ MDDVIDDIIS LESSYNEEIL GLMDPALQMA 190 200 210 220 230 240 NTLPVSGNLI DLYSNQGLPP PGLTISNSCP ANLPNIKREL TACIFPTESE ARALAKERQK 250 260 270 280 290 300 KDNHNLIERR RRFNINDRIK ELGTLIPKSN DPDMRWNKGT ILKASVDYIR KLQREQQRAK 310 320 330 340 350 360 DLENRQKKLE HANRHLLLRV QELEMQARAH GLSLIPSTGL CSPDLVNRII KQEPVLENCS 370 380 390 400 410 420 QELVQHQADL TCTTTLDLTD GTITFTNNLG TMPESSPAYS IPRKMGSNLE DILMDDALSP 430 440 450 VGVTDPLLSS VSPGASKTSS RRSSMSAEET EHAC
	Isoform M [UniParc]. Checksum: 2620A6F93CDED178	FASTA	419	46,769
	10 20 30 40 50 60 MLEMLEYSHY QVQTHLENPT KYHIQQAQRH QVKQYLSTTL ANKHASQVLS SPCPNQPGDH 70 80 90 100 110 120 AMPPVPGSSA PNSPMAMLTL NSNCEKEAFY KFEEQSRAES ECPGMNTHSR ASCMQMDDVI 130 140 150 160 170 180 DDIISLESSY NEEILGLMDP ALQMANTLPV SGNLIDLYSN QGLPPPGLTI SNSCPANLPN 190 200 210 220 230 240 IKRELTACIF PTESEARALA KERQKKDNHN LIERRRRFNI NDRIKELGTL IPKSNDPDMR 250 260 270 280 290 300 WNKGTILKAS VDYIRKLQRE QQRAKDLENR QKKLEHANRH LLLRVQELEM QARAHGLSLI 310 320 330 340 350 360 PSTGLCSPDL VNRIIKQEPV LENCSQELVQ HQADLTCTTT LDLTDGTITF TNNLGTMPES 370 380 390 400 410 SPAYSIPRKM GSNLEDILMD DALSPVGVTD PLLSSVSPGA SKTSSRRSSM SAEETEHAC
	Isoform M1 [UniParc]. Checksum: C1A44A4D643E435B	FASTA	413	46,136
	10 20 30 40 50 60 MLEMLEYSHY QVQTHLENPT KYHIQQAQRH QVKQYLSTTL ANKHASQVLS SPCPNQPGDH 70 80 90 100 110 120 AMPPVPGSSA PNSPMAMLTL NSNCEKEAFY KFEEQSRAES ECPGMNTHSR ASCMQMDDVI 130 140 150 160 170 180 DDIISLESSY NEEILGLMDP ALQMANTLPV SGNLIDLYSN QGLPPPGLTI SNSCPANLPN 190 200 210 220 230 240 IKRELTESEA RALAKERQKK DNHNLIERRR RFNINDRIKE LGTLIPKSND PDMRWNKGTI 250 260 270 280 290 300 LKASVDYIRK LQREQQRAKD LENRQKKLEH ANRHLLLRVQ ELEMQARAHG LSLIPSTGLC 310 320 330 340 350 360 SPDLVNRIIK QEPVLENCSQ ELVQHQADLT CTTTLDLTDG TITFTNNLGT MPESSPAYSI 370 380 390 400 410 PRKMGSNLED ILMDDALSPV GVTDPLLSSV SPGASKTSSR RSSMSAEETE HAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations at the mouse microphthalmia locus are associated with defects in a gene encoding a novel basic-helix-loop-helix-zipper protein." Hodgkinson C.A., Moore K.J., Nakayama A., Steingrimsson E., Copeland N.G., Jenkins N.A., Arnheiter H. Cell 74:395-404(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS M AND M1), VARIANTS MI AND MI-WS, TISSUE SPECIFICITY. Tissue: Melanocyte.
[2]	"Genomic, transcriptional and mutational analysis of the mouse microphthalmia locus." Hallsson J.H., Favor J., Hodgkinson C., Glaser T., Lamoreux M.L., Magnusdottir R., Gunnarsson G.J., Sweet H.O., Copeland N.G., Jenkins N.A., Steingrimsson E. Genetics 155:291-300(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, MUTAGENESIS. Strain: 129/Sv. Tissue: Heart.
[3]	Hallsson J.H., Favor J., Hodgkinson C., Glaser T., Lamoreux M.L., Magnusdottir R., Gunnarsson G.J., Sweet H.O., Copeland N.G., Jenkins N.A., Steingrimsson E. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 41; 48; 52 AND 91.
[4]	"Molecular basis of mouse microphthalmia (mi) mutations helps explain their developmental and phenotypic consequences." Steingrimsson E., Moore K.J., Lamoreux M.L., Ferre-D'Amare A.R., Burley S.K., Sanders Zimring D.C., Skow L.C., Hodgkinson C.A., Arnheiter H., Copeland N.G., Jenkins N.A. Nat. Genet. 8:256-263(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND M), VARIANTS. Strain: C57BL/6. Tissue: Heart and Melanocyte.
[5]	"A helix-loop-helix transcription factor-like gene is located at the mi locus." Hughes M.J., Lingrel J.B., Krakowsky J.M., Anderson K.P. J. Biol. Chem. 268:20687-20690(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 345-392. Strain: C57BL/6. Tissue: Heart.
[6]	"Identification of a novel isoform of microphthalmia-associated transcription factor that is enriched in retinal pigment epithelium." Amae S., Fuse N., Yasumoto K., Sato S., Yajima I., Yamamoto H., Udono T., Durlu Y.K., Tamai M., Takahashi K., Shibahara S. Biochem. Biophys. Res. Commun. 247:710-715(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[7]	"The recessive phenotype displayed by a dominant negative microphthalmia-associated transcription factor mutant is a result of impaired nucleation potential." Takebayashi K., Chida K., Tsukamoto I., Morii E., Munakata H., Arnheiter H., Kuroki T., Kitamura Y., Nomura S. Mol. Cell. Biol. 16:1203-1211(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells." Lee Y.N., Nechushtan H., Figov N., Razin E. Immunity 20:145-151(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KARS.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"An L1 element intronic insertion in the black-eyed white (Mitfmi-bw) gene: the loss of a single Mitf isoform responsible for the pigmentary defect and inner ear deafness." Yajima I., Sato S., Kimura T., Yasumoto K., Shibahara S., Goding C.R., Yamamoto H. Hum. Mol. Genet. 8:1431-1441(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MI-BW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z23066 mRNA. Translation: CAA80600.1.
AF222344 Genomic DNA. Translation: AAF63466.1.
AF222959 , AF222949, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81266.2.
AF222959 , AF222950, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81267.2.
AF222959 , AF222950, AF222951, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81268.2.
AF222959 , AF222950, AF222951, AF222956, AF222958 Genomic DNA. Translation: AAF81269.2.
AF222959 , AF222950, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81270.2.
AF222959 , AF222949, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81271.2.
AF222959 , AF222949, AF222951, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81272.2.
AF222952 Genomic DNA. No translation available.
U19874 mRNA. Translation: AAC52155.1.
U19875 mRNA. Translation: AAC52156.1.
L22958 mRNA. Translation: AAB47773.1.
AB009397 mRNA. Translation: BAA32329.1.

IPI

IPI00125758.
IPI00230195.
IPI00230196.
IPI00230197.
IPI00230198.
IPI00230199.
IPI00230200.
IPI00230201.
IPI00230202.

PIR

A40728.
I49244.
PD0026.

RefSeq

NP_032627.1. NM_008601.3.

UniGene

Mm.333284.
Mm.454504.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4ATH	X-ray	1.95	A/B	324-403	[»]
4ATI	X-ray	2.60	A/B	287-403	[»]
4ATK	X-ray	2.95	A/B	287-403	[»]

ProteinModelPortal

Q08874.

SMR

Q08874. Positions 324-402.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08874. 1 interaction.

PTM databases

PhosphoSite

Q08874.

Proteomic databases

PaxDb

Q08874.

PRIDE

Q08874.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000043628; ENSMUSP00000044459; ENSMUSG00000035158.

GeneID

17342.

KEGG

mmu:17342.

Organism-specific databases

CTD

4286.

MGI

MGI:104554. Mitf.

Phylogenomic databases

eggNOG

NOG251286.

HOVERGEN

HBG006768.

InParanoid

Q08874.

KO

K09455.

OrthoDB

EOG495ZRR.

Gene expression databases

ArrayExpress

Q08874.

Bgee

Q08874.

CleanEx

MM_MITF.
MM_VIT.

Genevestigator

Q08874.

GermOnline

ENSMUSG00000035158. Mus musculus.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
IPR024097. bHLH_ZIP_TF.
IPR021802. bHLH_ZIP_TF_MiT/TFE.
[Graphical view]

PANTHER

PTHR10014. PTHR10014. 1 hit.

Pfam

PF11851. DUF3371. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075142.

ChiTaRS

MITF. mouse.

NextBio

291916.

SOURCE

Search...

Entry information

Entry name

MITF_MOUSE

Accession

Primary (citable) accession number: Q08874
Secondary accession number(s): O08885 , O88203, Q08843, Q60781, Q60782, Q9JIJ0, Q9JIJ1, Q9JIJ2, Q9JIJ3, Q9JIJ4, Q9JIJ5, Q9JIJ6, Q9JKX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	May 1, 2013
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program