Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q64127 (TIF1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription intermediary factor 1-alpha

Short name=TIF1-alpha
EC=6.3.2.-
Alternative name(s):
E3 ubiquitin-protein ligase Trim24
Tripartite motif-containing protein 24
Gene names
Name:Trim24
Synonyms:Tif1, Tif1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1051 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) By similarity. Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes. Ref.1 Ref.4 Ref.6 Ref.7 Ref.9 Ref.12 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts (via bromo domain) with histone H3 (via N-terminus), provided that it is not methylated at 'Lys-4' (H3K4me0). Does not interact with histone H3 that is methylated at 'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo domain) with histone H3 (via N-terminus) that is acetylated at 'Lys-23' (H3K23ac). Has the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac). Has very low affinity for histone H3 that is methylated at 'Lys-9' (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and 'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in vitro). Interacts with NR3C2/MCR By similarity. Interacts with the ligand-binding domain of estrogen receptors (in vitro). Interaction with DNA-bound estrogen receptors requires the presence of estradiol By similarity. Interacts with AR, CARM1, KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1. Interacts with p53/TP53 and PML. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Ref.12 Ref.13

Subcellular location

Nucleus. Cytoplasm. Note: Detected in the cytoplasm of the zygote. Translocates into the pronucleus at the time of genome activation. Colocalizes with sites of active transcription. Ref.1 Ref.4 Ref.5 Ref.6 Ref.12

Tissue specificity

Detected in embryonic and adult liver. Detected in zygote and throughout embryogenesis (at protein level). Detected in all adult tissues, with the highest expression level in testis. Ref.8 Ref.9

Induction

Before puberty, highly expressed in liver from males and females. After puberty, expression is considerably higher in liver from females compared to males. Up-regulated in males by continuous exposure to growth hormone. Ref.8

Post-translational modification

Sumoylated. Ref.5

Involvement in disease

A chromosomal aberration involving TRIM24 produces a TRIM24-BRAF (T18) oncogene originally isolated from a furfural-induced hepatoma.

Disruption phenotype

No visible phenotype during the first few months. Impaired transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes. Hepatocytes continue to proliferate throughout adulthood. High incidence hypertrophic hepatocytes with enlarged nuclei after three months. After nine months, about half of the mice have hepatocellular adenomas. Very high incidence of hepatocarcinoma in 13 to 29 month old mice, increasing from 40% to 80%. When one copy of Rara is disrupted, mice do not develop liver tumors or liver dysplasia. Ref.9 Ref.11

Sequence similarities

Contains 2 B box-type zinc fingers.

Contains 1 bromo domain.

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
Tumor suppressor
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion homeostasis

Inferred from mutant phenotype Ref.11. Source: MGI

cellular response to estrogen stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.9. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10562550Ref.9. Source: MGI

positive regulation of gene expression

Inferred from mutant phenotype Ref.9. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from genetic interaction Ref.1. Source: MGI

protein autophosphorylation

Inferred from direct assay PubMed 10562550. Source: MGI

protein catabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 10562550. Source: MGI

protein ubiquitination

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of signal transduction by p53 class mediator

Inferred from genetic interaction Ref.13. Source: MGI

regulation of vitamin D receptor signaling pathway

Inferred from mutant phenotype Ref.11. Source: MGI

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11331580. Source: MGI

nuclear euchromatin

Inferred from direct assay PubMed 10318760PubMed 10525195. Source: MGI

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

perichromatin fibrils

Inferred from direct assay PubMed 10318760. Source: MGI

   Molecular_functionchromatin binding

Inferred from direct assay PubMed 10318760. Source: MGI

estrogen response element binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyl-lysine binding

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from direct assay PubMed 15322135. Source: MGI

p53 binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 10562550. Source: MGI

sequence-specific DNA binding

Inferred from direct assay Ref.9. Source: MGI

transcription coactivator activity

Inferred from direct assay Ref.12. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.13. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q64127-1)

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 Short (identifier: Q64127-2)

The sequence of this isoform differs from the canonical sequence as follows:
     477-510: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10511051Transcription intermediary factor 1-alpha
PRO_0000056391

Regions

Domain933 – 98856Bromo
Zinc finger52 – 7726RING-type
Zinc finger158 – 21154B box-type 1
Zinc finger218 – 25942B box-type 2
Zinc finger827 – 87448PHD-type
Region755 – 78026Nuclear receptor binding site (NRBS)
Region835 – 8417Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0) By similarity
Coiled coil289 – 35971 Potential
Motif892 – 90817Nuclear localization signal Potential
Compositional bias8 – 158Poly-Ala
Compositional bias19 – 224Poly-Ala
Compositional bias344 – 3474Poly-Gln
Compositional bias583 – 5875Poly-Ser

Sites

Site332 – 3332Breakpoint for translocation to form TRIM24-BRAF oncogene
Site8281Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0) By similarity

Amino acid modifications

Modified residue971Phosphothreonine By similarity
Modified residue1101Phosphoserine By similarity
Modified residue6681Phosphoserine By similarity
Modified residue7451Phosphoserine By similarity
Modified residue7691Phosphoserine By similarity
Modified residue8091Phosphoserine By similarity
Modified residue8121Phosphoserine By similarity
Modified residue8191Phosphothreonine By similarity
Modified residue10261Phosphoserine Ref.10
Modified residue10291Phosphoserine Ref.10
Modified residue10431Phosphoserine By similarity
Cross-link724Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link742Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Alternative sequence477 – 51034Missing in isoform Short.
VSP_005773

Experimental info

Mutagenesis7241K → R: Loss of sumoylation; when associated with R-742. Ref.5
Mutagenesis7421K → R: Loss of sumoylation; when associated with R-724. Ref.5

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 610584C1C6885972

FASTA1,051116,657
        10         20         30         40         50         60 
MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD TCAVCHQNIQ 

        70         80         90        100        110        120 
SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP APAPAPAPGS PAGGPSPFAT 

       130        140        150        160        170        180 
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV 

       190        200        210        220        230        240 
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK 

       250        260        270        280        290        300 
LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ 

       310        320        330        340        350        360 
NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM 

       370        380        390        400        410        420 
HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NTTIQFHCDP SFWAQNIINL 

       430        440        450        460        470        480 
GSLVIEDKES QPQMPKQNPV VEQSSQPPGG LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ 

       490        500        510        520        530        540 
RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY 

       550        560        570        580        590        600 
SPSQNVPRQT TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY 

       610        620        630        640        650        660 
DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ PRPPSNRTVQ 

       670        680        690        700        710        720 
SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS SSKPAGADST HKVPVVMLEP 

       730        740        750        760        770        780 
IRIKQENSGP PENYDFPVVI VKQESDEESR PQNTNYPRSI LTSLLLNSSQ SSASEETVLR 

       790        800        810        820        830        840 
SDAPDSTGDQ PGLHQENSSN GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL 

       850        860        870        880        890        900 
CCEKCPKVFH LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK 

       910        920        930        940        950        960 
LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK KRLQEDYCMY 

       970        980        990       1000       1010       1020 
TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE LLKNLYPEKR FPKVEFRHEA 

      1030       1040       1050 
EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL K 

« Hide

Isoform Short [UniParc].

Checksum: 0EDAF4BC938F56B6
Show »

FASTA1,017112,844

References

« Hide 'large scale' references
[1]"The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18."
le Douarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B., Heery D., Gronemeyer H., Chambon P., Losson R.
EMBO J. 14:2020-2033(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESTROGEN RECEPTOR, SUBCELLULAR LOCATION.
Tissue: Carcinoma.
[2]"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] (ISOFORM LONG).
Strain: C57BL/6.
Tissue: Brain.
[3]"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX1 AND CBX3.
[4]"A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins."
Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H., Kalantry S., Freedman L.P., Pandolfi P.P.
Nat. Genet. 23:287-295(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
[5]"Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification."
Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A.
Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, MUTAGENESIS OF LYS-724 AND LYS-742.
[6]"Role of TIF1alpha as a modulator of embryonic transcription in the mouse zygote."
Torres-Padilla M.E., Zernicka-Goetz M.
J. Cell Biol. 174:329-338(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Transcriptional intermediary factor 1alpha mediates physical interaction and functional synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein 1 nuclear receptor coactivators."
Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.
Mol. Endocrinol. 20:1276-1286(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CARM1, IDENTIFICATION IN A COACTIVATOR COMPLEX WITH CARM1 AND NCOA2/GRIP1.
[8]"Characterization of three growth hormone-responsive transcription factors preferentially expressed in adult female liver."
Laz E.V., Holloway M.G., Chen C.S., Waxman D.J.
Endocrinology 148:3327-3337(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY.
[9]"Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity to retinoic acid receptor alpha."
Khetchoumian K., Teletin M., Tisserand J., Mark M., Herquel B., Ignat M., Zucman-Rossi J., Cammas F., Lerouge T., Thibault C., Metzger D., Chambon P., Losson R.
Nat. Genet. 39:1500-1506(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1026 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"Arterial calcifications and increased expression of vitamin D receptor targets in mice lacking TIF1alpha."
Ignat M., Teletin M., Tisserand J., Khetchoumian K., Dennefeld C., Chambon P., Losson R., Mark M.
Proc. Natl. Acad. Sci. U.S.A. 105:2598-2603(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[12]"TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AR; KAT5/TIP60 AND BRD7.
[13]"Trim24 targets endogenous p53 for degradation."
Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A., Johnson R.L., Barton M.C.
Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78221 mRNA. Translation: AAB34290.1.
S78219 mRNA. Translation: AAB34289.1.
BC056959 mRNA. Translation: AAH56959.1.
PIRS55259.
RefSeqNP_001258993.1. NM_001272064.1.
NP_001259005.1. NM_001272076.1.
NP_659542.3. NM_145076.4.
UniGeneMm.41063.

3D structure databases

ProteinModelPortalQ64127.
SMRQ64127. Positions 46-150, 159-261, 825-1013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204196. 11 interactions.
DIPDIP-31476N.
IntActQ64127. 10 interactions.
MINTMINT-4137892.

PTM databases

PhosphoSiteQ64127.

Proteomic databases

PaxDbQ64127.
PRIDEQ64127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031859; ENSMUSP00000031859; ENSMUSG00000029833. [Q64127-1]
ENSMUST00000120428; ENSMUSP00000113063; ENSMUSG00000029833. [Q64127-2]
GeneID21848.
KEGGmmu:21848.
UCSCuc009bjk.1. mouse. [Q64127-1]
uc009bjl.1. mouse. [Q64127-2]

Organism-specific databases

CTD8805.
MGIMGI:109275. Trim24.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00530000062982.
HOGENOMHOG000252971.
HOVERGENHBG054599.
InParanoidQ64127.
KOK08881.
OMAPGLHQEN.
OrthoDBEOG790FZZ.
PhylomeDBQ64127.
TreeFamTF106455.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ64127.
BgeeQ64127.
CleanExMM_TRIM24.
GenevestigatorQ64127.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 3 hits.
4.10.45.10. 1 hit.
InterProIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM24. mouse.
NextBio301326.
PROQ64127.
SOURCESearch...

Entry information

Entry nameTIF1A_MOUSE
AccessionPrimary (citable) accession number: Q64127
Secondary accession number(s): Q64126
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 139 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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