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Q08874 (MITF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Mitf
Synonyms:Bw, Mi, Vit
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt 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

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from direct assay PubMed 12235125. Source: MGI

cell differentiation

Inferred from mutant phenotype PubMed 9199364. 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

pigmentation

Inferred from mutant phenotype PubMed 12086670PubMed 2379821. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14575687. Source: MGI

regulation of cell proliferation

Inferred from direct assay PubMed 12235125. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 12086670. Source: MGI

regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 11930005. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12235125. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15729346. Source: GOC

   Cellular_componentnucleus

Inferred from direct assay PubMed 12235125. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 14575687. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 23980096. Source: MGI

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

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12235125PubMed 14575687. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Microphthalmia-associated transcription factor
PRO_0000127277

Regions

Domain311 – 36454bHLH
Region224 – 29168Transactivation By similarity
Region374 – 39522Leucine-zipper
Region401 – 43131DNA binding regulation By similarity

Amino acid modifications

Modified residue1801Phosphoserine; by MAPK By similarity
Modified residue4051Phosphoserine; by GSK3 By similarity
Modified residue4141Phosphoserine By similarity
Modified residue4911Phosphoserine By similarity
Modified residue5161Phosphoserine; by RPS6KA1 By similarity
Cross-link289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 118118MQSES…MEVLK → MLEMLEYSHYQ in isoform M and isoform M1.
VSP_002130
Alternative sequence1 – 3535MQSES…PLKSS → MEALRFEMLIPCSFESLCL in isoform H, isoform H1, isoform H2 and isoform H3.
VSP_002129
Alternative sequence119 – 254136Missing in isoform H1 and isoform H2.
VSP_002132
Alternative sequence119 – 222104Missing in isoform A2.
VSP_002131
Alternative sequence139 – 19456Missing in isoform A1 and isoform H3.
VSP_002133
Alternative sequence294 – 31926ACIFP…NHNLI → V in isoform H2.
VSP_002135
Alternative sequence294 – 2996Missing in isoform A2 and isoform M1.
VSP_002134
Alternative sequence318 – 3192LI → LSKFV in isoform A2.
VSP_002136
Natural variant36 – 11883Missing in microphthalmia-red-eyed white/mi-rw.
Natural variant119 – 254136Missing in microphthalmia-white spot/mi-ws.
Natural variant139 – 19456Missing in microphthalmia-black and white spot/mi-bws.
Natural variant294 – 31926ACIFP…NHNLI → V in microphthalmia-eyeless-white/mi-ew.
Natural variant294 – 2996Missing in microphthalmia-spotted/mi-sp.
Natural variant3191I → N in microphthalmia-white/mi-wh.
Natural variant3231Missing in microphthalmia/mi.
Natural variant3291D → N in microphthalmia-vitiligo/mi-vi.
Natural variant370 – 526157Missing in microphthalmia-cloudy-eyed/mi-ce and microphthalmia-defective iris/mi-di.

Experimental info

Sequence conflict411P → S in AAF81266. Ref.2
Sequence conflict411P → S in AAF81267. Ref.2
Sequence conflict411P → S in AAF81268. Ref.2
Sequence conflict411P → S in AAF81269. Ref.2
Sequence conflict411P → S in AAF81270. Ref.2
Sequence conflict411P → S in AAF81271. Ref.2
Sequence conflict411P → S in AAF81272. Ref.2
Sequence conflict481I → L in AAF81266. Ref.2
Sequence conflict481I → L in AAF81267. Ref.2
Sequence conflict481I → L in AAF81268. Ref.2
Sequence conflict481I → L in AAF81269. Ref.2
Sequence conflict481I → L in AAF81270. Ref.2
Sequence conflict481I → L in AAF81271. Ref.2
Sequence conflict481I → L in AAF81272. Ref.2
Sequence conflict521S → T in AAF81266. Ref.2
Sequence conflict521S → T in AAF81267. Ref.2
Sequence conflict521S → T in AAF81268. Ref.2
Sequence conflict521S → T in AAF81269. Ref.2
Sequence conflict521S → T in AAF81270. Ref.2
Sequence conflict521S → T in AAF81271. Ref.2
Sequence conflict521S → T in AAF81272. Ref.2

Secondary structure

....... 526
Helix Strand Turn

Details...

Sequences

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

Last modified February 21, 2001. Version 3.
Checksum: 46F759A85ECC4B73

FASTA52658,627
        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 

« Hide

Isoform A1 [UniParc].

Checksum: A355DD0C45BC9E31
Show »

FASTA47052,768
Isoform A2 [UniParc].

Checksum: 99F18E2972927452
Show »

FASTA41946,837
Isoform H [UniParc].

Checksum: 57F10FE5A4A95175
Show »

FASTA51056,814
Isoform H1 [UniParc].

Checksum: A18701591F5D55D9
Show »

FASTA37441,769
Isoform H2 [UniParc].

Checksum: 686DEC9758924B01
Show »

FASTA34938,902
Isoform H3 [UniParc].

Checksum: 9859C4B41D4CAA00
Show »

FASTA45450,954
Isoform M [UniParc].

Checksum: 2620A6F93CDED178
Show »

FASTA41946,769
Isoform M1 [UniParc].

Checksum: C1A44A4D643E435B
Show »

FASTA41346,136

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]"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 expand/collapse EMBL AC list , AF222949, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81266.2.
AF222959 expand/collapse EMBL AC list , AF222950, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81267.2.
AF222959 expand/collapse EMBL AC list , AF222950, AF222951, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81268.2.
AF222959 expand/collapse EMBL AC list , AF222950, AF222951, AF222956, AF222958 Genomic DNA. Translation: AAF81269.2.
AF222959 expand/collapse EMBL AC list , AF222950, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81270.2.
AF222959 expand/collapse EMBL AC list , AF222949, AF222951, AF222953, AF222954, AF222955, AF222956, AF222957, AF222958 Genomic DNA. Translation: AAF81271.2.
AF222959 expand/collapse EMBL AC list , 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.
CCDSCCDS20385.1. [Q08874-8]
CCDS51861.1. [Q08874-1]
CCDS51862.1. [Q08874-4]
PIRA40728.
I49244.
PD0026.
RefSeqNP_032627.1. NM_008601.3. [Q08874-8]
XP_006505758.1. XM_006505695.1. [Q08874-9]
UniGeneMm.333284.
Mm.454504.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ATHX-ray1.95A/B324-403[»]
4ATIX-ray2.60A/B287-403[»]
4ATKX-ray2.95A/B287-403[»]
ProteinModelPortalQ08874.
SMRQ08874. Positions 324-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201427. 9 interactions.
IntActQ08874. 1 interaction.

Chemistry

ChEMBLCHEMBL1075142.

PTM databases

PhosphoSiteQ08874.

Proteomic databases

PaxDbQ08874.
PRIDEQ08874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043628; ENSMUSP00000044459; ENSMUSG00000035158. [Q08874-8]
GeneID17342.
KEGGmmu:17342.
UCSCuc009dbe.2. mouse. [Q08874-1]

Organism-specific databases

CTD4286.
MGIMGI:104554. Mitf.

Phylogenomic databases

eggNOGNOG251286.
HOVERGENHBG006768.
InParanoidQ08874.
KOK09455.
PhylomeDBQ08874.

Gene expression databases

ArrayExpressQ08874.
BgeeQ08874.
CleanExMM_MITF.
MM_VIT.
GenevestigatorQ08874.

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

ChiTaRSMITF. mouse.
NextBio291916.
PROQ08874.
SOURCESearch...

Entry information

Entry nameMITF_MOUSE
AccessionPrimary (citable) accession number: Q08874
Secondary accession number(s): O08885 expand/collapse secondary AC list , 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: July 9, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot