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P54843 (MAF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Maf
Alternative name(s):
Proto-oncogene c-Maf
V-maf musculoaponeurotic fibrosarcoma oncogene homolog
Gene names
Name:Maf
Synonyms:Maf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters By similarity. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf-responsive element binding. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Homodimer or heterodimer with other bHLH-Zip transcription factors. Binds DNA as a homodimer or as a heterodimer. Heterotetramer of two MAF and two USF2. Interacts with PAX6; the interaction is direct. Interacts with MYB; interaction takes place weakly in normal T-cells and increases in T-cells following stimulation through the TCR engagement. Interacts with MYB; the ternary complex formed with MYB and the CD13 promoter is regulated in response to differentiating signals. Interacts with USF2; the interaction inhibits its DNA-binding activity on the L7 promoter. Interacts with CREBBP, EP300 and ETS1 By similarity. Ref.5 Ref.6 Ref.11 Ref.14 Ref.16

Subcellular location

Nucleus.

Tissue specificity

Expressed in tubules of the renal cortex and hepatocytes. Expressed in the lens (at protein level). Expressed in pancreatic islets and endothelial cells. Ref.13 Ref.15 Ref.16

Developmental stage

Expressed in the floor of the diencephalon at 10 dpc (at protein level). Expressed in the midline of the forebrain and in the eye region at 9 dpc. Expressed in the head ectoderm destined to become the lens vesicle at 9 and 10 dpc. Expressed in the lens placode at 10.5 dpc. Expressed in the lens vesicle in both epithelial and fiber cells at 11 dpc. Expressed in secondary fiber cells at the equatorial region that divides the lens into anterior and posterior hemispheres between 11 and 14 dpc. Expressed in the neural tube and in primary fiber cells of the lens at 11.5 dpc. Expressed in proximal tubules of the cortex in the kidney at 16 and 17 dpc. Expressed in hypertrophic chondrocytes at 14.5 to 18.5 dpc. Expressed in the pancreas at 12.5 dpc until the adult stage. Ref.8 Ref.10 Ref.12 Ref.13 Ref.16

Post-translational modification

Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by glucocorticoids By similarity.

Phosphorylated by GSK3 and MAPK13 on serine and threonine residues By similarity. The phosphorylation status can serve to either stimulate or inhibit transcription.

Disruption phenotype

Knockout mice lacking this gene exhibit small eyes or microphthalmia with an absence of normal lens structures, an abnormal chondrocyte development, with terminal differentiation of hypertrophic chondrocytes initially delayed, followed by a subsequent expansion of the hypertrophic chondrocyte domain in the growth plates of embryonic and postnatal long bones. They also show a lack of IL4 production. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Sequence similarities

Belongs to the bZIP family. Maf subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
Tumor suppressor
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell development

Inferred from mutant phenotype Ref.10. Source: MGI

cytokine production

Inferred from direct assay PubMed 15790681. Source: MGI

inner ear development

Inferred from direct assay PubMed 21795542. Source: MGI

lens development in camera-type eye

Inferred from mutant phenotype Ref.8Ref.10PubMed 12835653. Source: MGI

lens fiber cell differentiation

Inferred from mutant phenotype Ref.8PubMed 12835653. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19623612. Source: MGI

positive regulation of gene expression

Inferred from direct assay PubMed 21460847. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12381733PubMed 12835653. Source: MGI

regulation of chondrocyte differentiation

Inferred from mutant phenotype Ref.12. Source: MGI

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.7. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.13. Source: MGI

nucleus

Inferred from direct assay Ref.13. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12381733. Source: MGI

protein binding

Inferred from physical interaction PubMed 16675956. Source: IntAct

sequence-specific DNA binding

Inferred from direct assay Ref.10. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12835653. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smarca5Q91ZW32EBI-3842521,EBI-927547

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54843-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54843-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     370-370: M → MCVCVCALFIL
Note: No experimental confirmation available.
Isoform 3 (identifier: P54843-3)

The sequence of this isoform differs from the canonical sequence as follows:
     370-370: M → MYPRDSSTSVM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Transcription factor Maf
PRO_0000076492

Regions

Domain285 – 34864bZIP
Region126 – 370245Represses ARE-mediated transcription By similarity
Region285 – 31026Basic motif By similarity
Region313 – 33422Leucine-zipper By similarity
Compositional bias126 – 251126Gly-rich
Compositional bias132 – 22493Ala-rich
Compositional bias180 – 19415His-rich

Natural variations

Alternative sequence3701M → MCVCVCALFIL in isoform 2.
VSP_036408
Alternative sequence3701M → MYPRDSSTSVM in isoform 3.
VSP_036409

Experimental info

Mutagenesis151S → A: Inhibition on transcriptional activation on CD13 proximal promoter in endothelial cells. Ref.15
Mutagenesis701S → A: No effect on transcriptional activation on CD13 proximal promoter. Increases liver specific transactivation on the IL-4 promoter. Ref.15
Mutagenesis3341L → P: Abolishes interaction with USF2. Ref.5
Sequence conflict2021A → T in AAB32820. Ref.1
Sequence conflict208 – 2114ASAS → SSSN in AAB32820. Ref.1
Sequence conflict223 – 2242SA → NT in AAB32820. Ref.1
Sequence conflict2311G → D in AAB32820. Ref.1
Sequence conflict2481A → S in AAB32820. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 1E8722C8287AAAC9

FASTA37038,435
        10         20         30         40         50         60 
MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM 

        70         80         90        100        110        120 
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN 

       130        140        150        160        170        180 
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH 

       190        200        210        220        230        240 
YHHHHHHAAG HHHHPTAGAP GAAGGASASA SGAGGAGGGG PASAGGGGGG GGGGGTAGAG 

       250        260        270        280        290        300 
GALHPHHAAG GLHFDDRFSD EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ 

       310        320        330        340        350        360 
SCRFKRVQQR HVLESEKNQL LQQVDHLKQE ISRLVRERDA YKEKYEKLVS NGFRENGSSS 

       370 
DNPSSPEFFM 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: 8A86683B08071901
Show »

FASTA38039,501
Isoform 3 [UniParc].

Checksum: 79A6165D907C017B
Show »

FASTA38039,560

References

« Hide 'large scale' references
[1]"The maf proto-oncogene stimulates transcription from multiple sites in a promoter that directs Purkinje neuron-specific gene expression."
Kurschner C., Morgan J.I.
Mol. Cell. Biol. 15:246-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Cerebellum.
[2]"Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene expression."
Cui W., Tomarev S.I., Piatigorsky J., Chepelinsky A.B., Duncan M.K.
J. Biol. Chem. 279:11088-11095(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Head.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity."
Kurschner C., Morgan J.I.
Biochem. Biophys. Res. Commun. 231:333-339(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HETEROTETRAMER, INTERACTION WITH USF2, MUTAGENESIS OF LEU-334.
[6]"c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation."
Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.
Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ETS1 AND MYB.
[7]"The transcription factor c-Maf controls the production of interleukin-4 but not other Th2 cytokines."
Kim J.I., Ho I.-C., Grusby M.J., Glimcher L.H.
Immunity 10:745-751(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"Regulation of lens fiber cell differentiation by transcription factor c-Maf."
Kawauchi S., Takahashi S., Nakajima O., Ogino H., Morita M., Nishizawa M., Yasuda K., Yamamoto M.
J. Biol. Chem. 274:19254-19260(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[9]"Requirement for the c-Maf transcription factor in crystallin gene regulation and lens development."
Kim J.I., Li T., Ho I.C., Grusby M.J., Glimcher L.H.
Proc. Natl. Acad. Sci. U.S.A. 96:3781-3785(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Regulation of mouse lens fiber cell development and differentiation by the Maf gene."
Ring B.Z., Cordes S.P., Overbeek P.A., Barsh G.S.
Development 127:307-317(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[11]"CREB-binding protein/p300 co-activation of crystallin gene expression."
Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.
J. Biol. Chem. 277:24081-24089(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CREBBP AND EP300.
[12]"Absence of transcription factor c-maf causes abnormal terminal differentiation of hypertrophic chondrocytes during endochondral bone development."
MacLean H.E., Kim J.I., Glimcher M.J., Wang J., Kronenberg H.M., Glimcher L.H.
Dev. Biol. 262:51-63(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[13]"Developmental contribution of c-maf in the kidney: distribution and developmental study of c-maf mRNA in normal mice kidney and histological study of c-maf knockout mice kidney and liver."
Imaki J., Tsuchiya K., Mishima T., Onodera H., Kim J.I., Yoshida K., Ikeda H., Sakai M.
Biochem. Biophys. Res. Commun. 320:1323-1327(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[14]"c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase apoptosis in peripheral CD4 cells."
Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.
Eur. J. Immunol. 37:2868-2880(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYB.
[15]"CD13/APN transcription is regulated by the proto-oncogene c-Maf via an atypical response element."
Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.
Gene 403:178-187(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-15 AND SER-70, DNA-BINDING, TISSUE SPECIFICITY.
[16]"Pax-6 and c-Maf functionally interact with the alpha-cell-specific DNA element G1 in vivo to promote glucagon gene expression."
Gosmain Y., Avril I., Mamin A., Philippe J.
J. Biol. Chem. 282:35024-35034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PAX6, DNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[17]"A new MAFia in cancer."
Eychene A., Rocques N., Pouponnot C.
Nat. Rev. Cancer 8:683-693(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74567 mRNA. Translation: AAB32820.1.
AY560005 mRNA. Translation: AAY81957.1.
AK132165 mRNA. Translation: BAE21007.1.
AC113301 Genomic DNA. No translation available.
CCDSCCDS40486.1. [P54843-1]
RefSeqNP_001020748.2. NM_001025577.2. [P54843-1]
UniGeneMm.275549.
Mm.439772.
Mm.488377.

3D structure databases

ProteinModelPortalP54843.
SMRP54843. Positions 257-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201281. 2 interactions.
IntActP54843. 2 interactions.
MINTMINT-1131204.

PTM databases

PhosphoSiteP54843.

Proteomic databases

MaxQBP54843.
PRIDEP54843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069009; ENSMUSP00000067704; ENSMUSG00000055435. [P54843-3]
ENSMUST00000109104; ENSMUSP00000104732; ENSMUSG00000055435. [P54843-1]
GeneID17132.
KEGGmmu:17132.
UCSCuc009noe.2. mouse. [P54843-3]
uc009nof.1. mouse. [P54843-1]

Organism-specific databases

CTD4094.
MGIMGI:96909. Maf.

Phylogenomic databases

eggNOGNOG241084.
GeneTreeENSGT00550000074549.
HOGENOMHOG000261683.
HOVERGENHBG000313.
InParanoidQ3V1Z2.
KOK09035.
OMADRSINQC.
OrthoDBEOG7BGHMQ.
PhylomeDBP54843.
TreeFamTF325689.

Gene expression databases

BgeeP54843.
GenevestigatorP54843.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028573. MafF.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF9. PTHR10129:SF9. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAF. mouse.
NextBio291332.
PROP54843.
SOURCESearch...

Entry information

Entry nameMAF_MOUSE
AccessionPrimary (citable) accession number: P54843
Secondary accession number(s): Q3V1Z2, Q4QY62
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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

MGD cross-references

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