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O75030 (MITF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microphthalmia-associated transcription factor
Alternative name(s):
Class E basic helix-loop-helix protein 32
Short name=bHLHe32
Gene names
Name:MITF
Synonyms:BHLHE32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.11 Ref.19

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. Interacts with KARS. Identified in a complex with HINT1 and CTNNB1. Ref.12 Ref.19

Subcellular location

Nucleus.

Tissue specificity

Isoform Mis exclusively expressed in melanocytes and melanoma cells. Isoform Aand isoform Hare widely expressed in many cell types including melanocytes and retinal pigment epithelium (RPE). Isoform Cis expressed in many cell types including RPE but not in melanocyte-lineage cells. Isoform Mdel is widely expressed in melanocytes, melanoma cell lines and tissues, but almost undetectable in non-melanoma cell lines. Ref.3

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. Ref.10 Ref.11

Ubiquitinated following phosphorylation at Ser-180, leading to subsequent degradation by the proteasome. Deubiquitinated by USP13, preventing its degradation. Ref.10

Involvement in disease

Waardenburg syndrome 2A (WS2A) [MIM:193510]: WS2 is a genetically heterogeneous, autosomal dominant disorder characterized by sensorineural deafness, pigmentary disturbances, and absence of dystopia canthorum. The frequency of deafness is higher in WS2 than in WS1.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Waardenburg syndrome 2, with ocular albinism, autosomal recessive (WS2-OA) [MIM:103470]: A disorder characterized by the association of features typical of Waardenburg syndrome type 2 with ocular albinism. Patients manifest reduced visual acuity, albinotic fundus, deafness, hypomelanosis.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Tietz syndrome (TIETZS) [MIM:103500]: Autosomal dominant disorder characterized by generalized hypopigmentation and profound, congenital, bilateral deafness. Penetrance is complete.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Melanoma, cutaneous malignant 8 (CMM8) [MIM:614456]: A malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but also may involve other sites.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.17 Ref.18

Sequence similarities

Belongs to the MiT/TFE family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAlbinism
Deafness
Disease mutation
Waardenburg syndrome
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone remodeling

Inferred from electronic annotation. Source: Ensembl

camera-type eye development

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell fate commitment

Inferred from electronic annotation. Source: Ensembl

melanocyte differentiation

Non-traceable author statement Ref.1. Source: UniProtKB

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20530484PubMed 21209915. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

protein complex assembly

Inferred from direct assay PubMed 20530484. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Non-traceable author statement Ref.9Ref.1. Source: UniProtKB

   Cellular_componentnucleus

Non-traceable author statement Ref.9Ref.1. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 20530484. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 20530484. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 20530484PubMed 21811243. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Note: The X2-type isoforms differ from the X1-type isoforms by the absence of a 6 residue insert.
Isoform A1 (identifier: O75030-1)

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 A2 (identifier: O75030-2)

The sequence of this isoform differs from the canonical sequence as follows:
     294-299: Missing.
Isoform B1 (identifier: O75030-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MLYAFWFSH
Isoform B2 (identifier: O75030-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MLYAFWFSH
     294-299: Missing.
Isoform C1 (identifier: O75030-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MGHLENTSVVFPRAIFSLCEKETRKLTLCLFSR
Isoform C2 (identifier: O75030-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS → MGHLENTSVVFPRAIFSLCEKETRKLTLCLFSR
     294-299: Missing.
Isoform H1 (identifier: O75030-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRVQMFMPCSFESLYL
Isoform H2 (identifier: O75030-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS → MEALRVQMFMPCSFESLYL
     294-299: Missing.
Isoform M1 (identifier: O75030-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: MQSESGIVPD...ATQVPMEVLK → MLEMLEYNHYQ
Isoform M2 (identifier: O75030-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: MQSESGIVPD...ATQVPMEVLK → MLEMLEYNHYQ
     294-299: Missing.
Isoform Mdel (identifier: O75030-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: MQSESGIVPD...ATQVPMEVLK → MLEMLEYNHYQ
     139-194: Missing.
     293-298: Missing.
Isoform 12 (identifier: O75030-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     293-298: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Microphthalmia-associated transcription factor
PRO_0000127276

Regions

Domain311 – 36454bHLH
Region224 – 29572Transactivation
Region374 – 39522Leucine-zipper
Region401 – 43131DNA binding regulation

Amino acid modifications

Modified residue1801Phosphoserine; by MAPK Ref.10
Modified residue4051Phosphoserine; by GSK3 Ref.11
Modified residue4141Phosphoserine Ref.14 Ref.15
Modified residue4911Phosphoserine Ref.16
Modified residue5161Phosphoserine; by RPS6KA1 Ref.10
Cross-link289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence1 – 118118MQSES…MEVLK → MLEMLEYNHYQ in isoform M1, isoform M2 and isoform Mdel.
VSP_002127
Alternative sequence1 – 5252Missing in isoform 12.
VSP_046438
Alternative sequence1 – 3535MQSES…PLKSS → MEALRVQMFMPCSFESLYL in isoform H1 and isoform H2.
VSP_002126
Alternative sequence1 – 3434MQSES…QPLKS → MLYAFWFSH in isoform B1 and isoform B2.
VSP_002124
Alternative sequence1 – 3434MQSES…QPLKS → MGHLENTSVVFPRAIFSLCE KETRKLTLCLFSR in isoform C1 and isoform C2.
VSP_002125
Alternative sequence139 – 19456Missing in isoform Mdel.
VSP_045178
Alternative sequence293 – 2986Missing in isoform Mdel and isoform 12.
VSP_045179
Alternative sequence294 – 2996Missing in isoform A2, isoform B2, isoform C2, isoform H2 and isoform M2.
VSP_002128
Natural variant3101R → K in WS2A; unknown pathological significance. Ref.20
VAR_010297
Natural variant3171N → K in TIETZS. Ref.21
VAR_010298
Natural variant3241Missing in WS2A. Ref.20
VAR_010299
Natural variant3571S → P in WS2A. Ref.20
VAR_010300
Natural variant3851N → D in WS2A. Ref.20
VAR_010301
Natural variant4051S → P in WS2A. Ref.20
VAR_010302
Natural variant4251E → K May be associated with susceptibility to CMM8; has increased frequency in individuals with melanoma or renal cell carcinoma compared to controls; affects sumoylation. Ref.17 Ref.18
Corresponds to variant rs149617956 [ dbSNP | Ensembl ].
VAR_067367

Experimental info

Mutagenesis1801S → A: Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-516. Ref.10
Mutagenesis2891K → R: Loss of sumoylation; when associated with R-423. Ref.13
Mutagenesis4051S → A or P: Loss of phosphorylation and function. Ref.11
Mutagenesis4231K → R: Loss of sumoylation; when associated with R-289. Ref.13
Mutagenesis5161S → A: Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-180. Ref.10
Sequence conflict2411I → T in BAG58874. Ref.5

Secondary structure

... 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 136EBED3044C1986

FASTA52658,795
        10         20         30         40         50         60 
MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR 

        70         80         90        100        110        120 
QQLMREQMQE QERREQQQKL QAAQFMQQRV PVSQTPAINV SVPTTLPSAT QVPMEVLKVQ 

       130        140        150        160        170        180 
THLENPTKYH IQQAQRQQVK QYLSTTLANK HANQVLSLPC PNQPGDHVMP PVPGSSAPNS 

       190        200        210        220        230        240 
PMAMLTLNSN CEKEGFYKFE EQNRAESECP GMNTHSRASC MQMDDVIDDI ISLESSYNEE 

       250        260        270        280        290        300 
ILGLMDPALQ MANTLPVSGN LIDLYGNQGL PPPGLTISNS CPANLPNIKR ELTACIFPTE 

       310        320        330        340        350        360 
SEARALAKER QKKDNHNLIE RRRRFNINDR IKELGTLIPK SNDPDMRWNK GTILKASVDY 

       370        380        390        400        410        420 
IRKLQREQQR AKELENRQKK LEHANRHLLL RIQELEMQAR AHGLSLIPST GLCSPDLVNR 

       430        440        450        460        470        480 
IIKQEPVLEN CSQDLLQHHA DLTCTTTLDL TDGTITFNNN LGTGTEANQA YSVPTKMGSK 

       490        500        510        520 
LEDILMDDTL SPVGVTDPLL SSVSPGASKT SSRRSSMSME ETEHTC 

« Hide

Isoform A2 [UniParc].

Checksum: DEE08CB1E59B9511
Show »

FASTA52058,163
Isoform B1 [UniParc].

Checksum: 57BB6D9C60C50A76
Show »

FASTA50156,038
Isoform B2 [UniParc].

Checksum: 8D10FAE2E7A855FD
Show »

FASTA49555,405
Isoform C1 [UniParc].

Checksum: E9976026708CA76E
Show »

FASTA52558,664
Isoform C2 [UniParc].

Checksum: 90083765F3F0AA7C
Show »

FASTA51958,031
Isoform H1 [UniParc].

Checksum: 19568959E6CBC288
Show »

FASTA51057,045
Isoform H2 [UniParc].

Checksum: B5EE812DB5750430
Show »

FASTA50456,412
Isoform M1 [UniParc].

Checksum: 81B2DAF59F3C26D8
Show »

FASTA41946,938
Isoform M2 [UniParc].

Checksum: D1BE704770F24258
Show »

FASTA41346,305
Isoform Mdel [UniParc].

Checksum: C4072E16DBABBD76
Show »

FASTA35740,365
Isoform 12 [UniParc].

Checksum: 3608D0683C05C79D
Show »

FASTA46852,527

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-35 (ISOFORMS H1/H2).
Tissue: Kidney.
[2]"Cloning of MITF, the human homolog of the mouse microphthalmia gene and assignment to chromosome 3p14.1-p12.3."
Tachibana M., Perez-Jurado L.A., Nakayama A., Hodgkinson C.A., Li X., Schneider M., Miki T., Fex J., Francke U., Arnheiter H.
Hum. Mol. Genet. 3:553-557(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M1).
Tissue: Skin.
[3]"Mitf-Mdel, a novel melanocyte/melanoma-specific isoform of microphthalmia-associated transcription factor-M, as a candidate biomarker for melanoma."
Wang Y., Radfar S., Liu S., Riker A.I., Khong H.T.
BMC Med. 8:14-14(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDEL), TISSUE SPECIFICITY.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A2).
Tissue: Uterus.
[5]"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. expand/collapse author list , 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 12).
Tissue: Thalamus.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS M1 AND M2).
Tissue: Skin.
[8]"Structural organization of the human microphthalmia-associated transcription factor gene containing four alternative promoters."
Udono T., Yasumoto K., Takeda K., Amae S., Watanabe K., Saito H., Fuse N., Tachibana M., Takahashi K., Tamai M., Shibahara S.
Biochim. Biophys. Acta 1491:205-219(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1/A2; B1/B2; H1/H2 AND M1/M2).
[9]"Molecular cloning of cDNA encoding a novel microphthalmia-associated transcription factor isoform with a distinct amino-terminus."
Fuse N., Yasumoto K., Takeda K., Amae S., Yoshizawa M., Udono T., Takahashi K., Tamai M., Tomita Y., Tachibana M., Shibahara S.
J. Biochem. 126:1043-1051(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM C1/C2).
Tissue: Kidney.
[10]"c-Kit triggers dual phosphorylations, which couple activation and degradation of the essential melanocyte factor Mi."
Wu M., Hemesath T.J., Takemoto C.M., Horstmann M.A., Wells A.G., Price E.R., Fisher D.Z., Fisher D.E.
Genes Dev. 14:301-312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-180 AND SER-516, UBIQUITINATION, MUTAGENESIS OF SER-180 AND SER-516.
[11]"Ser298 of MITF, a mutation site in Waardenburg syndrome type 2, is a phosphorylation site with functional significance."
Takeda K., Takemoto C., Kobayashi I., Watanabe A., Nobukuni Y., Fisher D.E., Tachibana M.
Hum. Mol. Genet. 9:125-132(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-405, PHOSPHORYLATION AT SER-405.
[12]"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.
[13]"Sumoylation of MITF and its related family members TFE3 and TFEB."
Miller A.J., Levy C., Davis I.J., Razin E., Fisher D.E.
J. Biol. Chem. 280:146-155(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-289 AND LYS-423, MUTAGENESIS OF LYS-289 AND LYS-423.
[14]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A SUMOylation-defective MITF germline mutation predisposes to melanoma and renal carcinoma."
Bertolotto C., Lesueur F., Giuliano S., Strub T., de Lichy M., Bille K., Dessen P., d'Hayer B., Mohamdi H., Remenieras A., Maubec E., de la Fouchardiere A., Molinie V., Vabres P., Dalle S., Poulalhon N., Martin-Denavit T., Thomas L. expand/collapse author list , Andry-Benzaquen P., Dupin N., Boitier F., Rossi A., Perrot J.L., Labeille B., Robert C., Escudier B., Caron O., Brugieres L., Saule S., Gardie B., Gad S., Richard S., Couturier J., Teh B.T., Ghiorzo P., Pastorino L., Puig S., Badenas C., Olsson H., Ingvar C., Rouleau E., Lidereau R., Bahadoran P., Vielh P., Corda E., Blanche H., Zelenika D., Galan P., Aubin F., Bachollet B., Becuwe C., Berthet P., Bignon Y.J., Bonadona V., Bonafe J.L., Bonnet-Dupeyron M.N., Cambazard F., Chevrant-Breton J., Coupier I., Dalac S., Demange L., d'Incan M., Dugast C., Faivre L., Vincent-Fetita L., Gauthier-Villars M., Gilbert B., Grange F., Grob J.J., Humbert P., Janin N., Joly P., Kerob D., Lasset C., Leroux D., Levang J., Limacher J.M., Livideanu C., Longy M., Lortholary A., Stoppa-Lyonnet D., Mansard S., Mansuy L., Marrou K., Mateus C., Maugard C., Meyer N., Nogues C., Souteyrand P., Venat-Bouvet L., Zattara H., Chaudru V., Lenoir G.M., Lathrop M., Davidson I., Avril M.F., Demenais F., Ballotti R., Bressac-de Paillerets B.
Nature 480:94-98(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CMM8, VARIANT LYS-425.
[18]"A novel recurrent mutation in MITF predisposes to familial and sporadic melanoma."
Yokoyama S., Woods S.L., Boyle G.M., Aoude L.G., MacGregor S., Zismann V., Gartside M., Cust A.E., Haq R., Harland M., Taylor J.C., Duffy D.L., Holohan K., Dutton-Regester K., Palmer J.M., Bonazzi V., Stark M.S., Symmons J. expand/collapse author list , Law M.H., Schmidt C., Lanagan C., O'Connor L., Holland E.A., Schmid H., Maskiell J.A., Jetann J., Ferguson M., Jenkins M.A., Kefford R.F., Giles G.G., Armstrong B.K., Aitken J.F., Hopper J.L., Whiteman D.C., Pharoah P.D., Easton D.F., Dunning A.M., Newton-Bishop J.A., Montgomery G.W., Martin N.G., Mann G.J., Bishop D.T., Tsao H., Trent J.M., Fisher D.E., Hayward N.K., Brown K.M.
Nature 480:99-103(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CMM8, VARIANT LYS-425, CHARACTERIZATION OF VARIANT LYS-425.
[19]"The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional activity in melanoma cells."
Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A., Sgambato A.
Cell Cycle 11:2206-2215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1 AND CTNNB1, FUNCTION.
[20]"The mutational spectrum in Waardenburg syndrome."
Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D., Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W., Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R., Read A.P.
Hum. Mol. Genet. 4:2131-2137(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WS2A LYS-310; ARG-324 DEL; PRO-357; ASP-385 AND PRO-405.
[21]"Tietz syndrome (hypopigmentation/deafness) caused by mutation of MITF."
Smith S.D., Kelley P.M., Kenyon J.B., Hoover D.
J. Med. Genet. 37:446-448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TIETZS LYS-317.
Tissue: Blood.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006909 mRNA. Translation: BAA32288.1.
AB006989 mRNA. No translation available.
Z29678 mRNA. Translation: CAA82775.1.
GU355676 mRNA. Translation: ADB90411.1.
AL110195 mRNA. Translation: CAB53672.1.
AK296129 mRNA. Translation: BAG58874.1.
AC099326 Genomic DNA. No translation available.
AC104445 Genomic DNA. No translation available.
AC104449 Genomic DNA. No translation available.
AC124915 Genomic DNA. No translation available.
BC026961 mRNA. Translation: AAH26961.1.
BC065243 mRNA. Translation: AAH65243.1.
AF034755 Genomic DNA. Translation: AAC39639.1.
AB032359 Genomic DNA. Translation: BAA95208.1.
AB032358 Genomic DNA. Translation: BAA95207.1.
AB032357 Genomic DNA. Translation: BAA95206.1.
AB009608 Genomic DNA. Translation: BAA95209.1. Different termination.
CCDSCCDS2913.1. [O75030-9]
CCDS43106.1. [O75030-2]
CCDS43107.1. [O75030-10]
CCDS46865.1. [O75030-8]
CCDS46866.2. [O75030-11]
CCDS54607.1. [O75030-12]
PIRI38024.
T14752.
RefSeqNP_000239.1. NM_000248.3. [O75030-9]
NP_001171896.1. NM_001184967.1. [O75030-12]
NP_006713.1. NM_006722.2. [O75030-6]
NP_937801.1. NM_198158.2. [O75030-10]
NP_937802.1. NM_198159.2. [O75030-2]
NP_937820.1. NM_198177.2. [O75030-8]
NP_937821.2. NM_198178.2. [O75030-11]
XP_005264811.1. XM_005264754.1. [O75030-1]
XP_005264812.1. XM_005264755.1. [O75030-7]
UniGeneHs.166017.
Hs.618266.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4C7NX-ray2.10A357-403[»]
ProteinModelPortalO75030.
SMRO75030. Positions 312-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110432. 23 interactions.
DIPDIP-59573N.
IntActO75030. 4 interactions.
MINTMINT-7997258.
STRING9606.ENSP00000295600.

Chemistry

ChEMBLCHEMBL1741165.

PTM databases

PhosphoSiteO75030.

Proteomic databases

MaxQBO75030.
PaxDbO75030.
PRIDEO75030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314557; ENSP00000324246; ENSG00000187098. [O75030-10]
ENST00000314589; ENSP00000324443; ENSG00000187098. [O75030-8]
ENST00000328528; ENSP00000327867; ENSG00000187098. [O75030-6]
ENST00000352241; ENSP00000295600; ENSG00000187098. [O75030-2]
ENST00000394351; ENSP00000377880; ENSG00000187098. [O75030-9]
ENST00000394355; ENSP00000377884; ENSG00000187098. [O75030-4]
ENST00000448226; ENSP00000391803; ENSG00000187098. [O75030-1]
ENST00000472437; ENSP00000418845; ENSG00000187098. [O75030-12]
ENST00000531774; ENSP00000435909; ENSG00000187098. [O75030-11]
GeneID4286.
KEGGhsa:4286.
UCSCuc003dnz.3. human. [O75030-2]
uc003doa.3. human. [O75030-6]
uc003dob.3. human. [O75030-8]
uc003doe.3. human. [O75030-10]
uc003dof.3. human. [O75030-9]
uc021xam.1. human.

Organism-specific databases

CTD4286.
GeneCardsGC03P069788.
HGNCHGNC:7105. MITF.
HPACAB002578.
HPA003259.
MIM103470. phenotype.
103500. phenotype.
156845. gene.
193510. phenotype.
614456. phenotype.
neXtProtNX_O75030.
Orphanet319276. Clear cell renal carcinoma.
293822. MITF-related melanoma and renal cell carcinoma predisposition syndrome.
352740. Ocular albinism with congenital sensorineural deafness.
319298. Papillary renal cell carcinoma.
42665. Tietz syndrome.
895. Waardenburg syndrome type 2.
PharmGKBPA30823.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251286.
HOGENOMHOG000231368.
HOVERGENHBG006768.
InParanoidO75030.
KOK09455.
OMAYSNQGLP.
OrthoDBEOG72G182.
PhylomeDBO75030.
TreeFamTF317174.

Enzyme and pathway databases

SignaLinkO75030.

Gene expression databases

ArrayExpressO75030.
BgeeO75030.
CleanExHS_MITF.
GenevestigatorO75030.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR021802. bHLH_ZIP_TF_MiT/TFE.
[Graphical view]
PfamPF11851. DUF3371. 1 hit.
PF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMicrophthalmia-associated_transcription_factor.
GenomeRNAi4286.
NextBio16861.
PMAP-CutDBO75030.
PROO75030.
SOURCESearch...

Entry information

Entry nameMITF_HUMAN
AccessionPrimary (citable) accession number: O75030
Secondary accession number(s): B4DJL2 expand/collapse secondary AC list , D3K197, E9PFN0, Q14841, Q9P2V0, Q9P2V1, Q9P2V2, Q9P2Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM