SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P63058

- THA_MOUSE

UniProt

P63058 - THA_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Thyroid hormone receptor alpha
Gene
Thra, C-erba-alpha, Nr1a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. Isoform Alpha-deltaE6 does not bind DNA, inhibits the activity of isoform Alpha-1, and stimulates myoblast differentiation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei228 – 2281Thyroid hormone By similarity
Binding sitei277 – 2771Thyroid hormone; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi53 – 12775Nuclear receptor
Add
BLAST
Zinc fingeri53 – 7321NR C4-type
Add
BLAST
Zinc fingeri91 – 11525NR C4-type
Add
BLAST

GO - Molecular functioni

  1. chromatin DNA binding Source: MGI
  2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  3. protein binding Source: UniProtKB
  4. protein complex binding Source: MGI
  5. single-stranded RNA binding Source: MGI
  6. steroid hormone receptor activity Source: InterPro
  7. steroid receptor RNA activator RNA binding Source: MGI
  8. thyroid hormone binding Source: UniProtKB
  9. thyroid hormone receptor activity Source: UniProtKB
  10. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. Type I pneumocyte differentiation Source: MGI
  2. cartilage condensation Source: MGI
  3. cytoplasmic sequestering of transcription factor Source: MGI
  4. erythrocyte differentiation Source: MGI
  5. female courtship behavior Source: MGI
  6. intracellular receptor signaling pathway Source: GOC
  7. learning or memory Source: MGI
  8. negative regulation of DNA-templated transcription, initiation Source: Ensembl
  9. negative regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: Ensembl
  10. negative regulation of transcription, DNA-templated Source: MGI
  11. organ morphogenesis Source: MGI
  12. ossification Source: MGI
  13. positive regulation of female receptivity Source: MGI
  14. positive regulation of myotube differentiation Source: MGI
  15. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  16. regulation of heart contraction Source: MGI
  17. regulation of lipid catabolic process Source: MGI
  18. regulation of myeloid cell apoptotic process Source: MGI
  19. regulation of thyroid hormone mediated signaling pathway Source: MGI
  20. response to cold Source: MGI
  21. thyroid gland development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid hormone receptor alpha
Alternative name(s):
Nuclear receptor subfamily 1 group A member 1
c-erbA-1
c-erbA-alpha
Gene namesi
Name:Thra
Synonyms:C-erba-alpha, Nr1a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98742. Thra.

Subcellular locationi

Isoform Alpha-deltaE6 : Cytoplasm
Note: Sequesters isoform Alpha-1 into this compartment.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Ensembl
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Thyroid hormone receptor alpha
PRO_0000053425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRIDEiP63058.

PTM databases

PhosphoSiteiP63058.

Expressioni

Tissue specificityi

Ubiquitous (Isoform Alpha-deltaE6).1 Publication

Gene expression databases

ArrayExpressiP63058.
BgeeiP63058.
CleanExiMM_THRA.
GenevestigatoriP63058.

Interactioni

Subunit structurei

Binds DNA as a dimer; homodimer and heterodimer with RXRB. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Probably interacts with SFPQ. Interacts with AKAP13. Interacts with C1D. Interacts with TP53INP2. Interacts with PER2.3 Publications

Protein-protein interaction databases

BioGridi204183. 4 interactions.
DIPiDIP-43752N.
IntActiP63058. 1 interaction.
MINTiMINT-3374329.

Structurei

3D structure databases

ProteinModelPortaliP63058.
SMRiP63058. Positions 49-409.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5252Modulating
Add
BLAST
Regioni190 – 370181Ligand-binding
Add
BLAST

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Isoform Alpha-deltaE6 lacks the hinge region that connects the modulating domain and the DNA binding domain.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG272726.
GeneTreeiENSGT00740000114969.
HOVERGENiHBG005606.
InParanoidiQ80Y90.
KOiK05547.
OMAiWLNGPKR.
OrthoDBiEOG7TBC2V.
PhylomeDBiP63058.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Alpha-2 (identifier: P63058-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCPLKSSMS GYIPSYLDKD    50
EQCVVCGDKA TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID 100
KITRNQCQLC RFKKCIAVGM AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM 150
IRSLQQRPEP TPEEWDLIHV ATEAHRSTNA QGSHWKQRRK FLPDDIGQSP 200
IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS ELPCEDQIIL 250
LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 300
ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE 350
HYVNHRKHNI PHFWPKLLMK EREVQSSILY KGAAAEGRPG GSLGVHPEGQ 400
QLLGMHVVQG PQVRQLEQQL GEAGSLRGPV LQHQSPKSPQ QRLLELLHRS 450
GILHSRAVCG EDDSSEASSL SSSSDTEDTE VCEDQAGKAA SP 492
Length:492
Mass (Da):55,023
Last modified:January 19, 2010 - v2
Checksum:i870100FCB5C34A10
GO
Isoform Alpha-1 (identifier: P63058-2) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     371-492: EREVQSSILY...EDQAGKAASP → VTDLRMIGAC...FLEVFEDQEV

Show »
Length:410
Mass (Da):46,795
Checksum:iEC0240EF1ECF4111
GO
Isoform Alpha-3 (identifier: P63058-3) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     371-409: Missing.

Show »
Length:453
Mass (Da):50,954
Checksum:i6DE1FECA97686CAF
GO
Isoform Alpha-deltaE6 (identifier: P63058-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     121-197: AMDLVLDDSK...RRKFLPDDIG → GTSP
     371-492: EREVQSSILY...EDQAGKAASP → VTDLRMIGAC...FLEVFEDQEV

Note: Due to mismatches with the underlying genomic sequence that lie within a microexon, this isoform has been proposed to undergo RNA editing involving both base insertion and deletion.

Show »
Length:337
Mass (Da):37,926
Checksum:i27137623BED67783
GO

Sequence cautioni

The sequence CAM46188.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei121 – 19777AMDLV…PDDIG → GTSP in isoform Alpha-deltaE6.
VSP_038640Add
BLAST
Alternative sequencei371 – 492122EREVQ…KAASP → VTDLRMIGACHASRFLHMKV ECPTELFPPLFLEVFEDQEV in isoform Alpha-1 and isoform Alpha-deltaE6.
VSP_003624Add
BLAST
Alternative sequencei371 – 40939Missing in isoform Alpha-3.
VSP_003625Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061Q → H in CAA36241. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07750 mRNA. Translation: CAA30575.1.
X07751 mRNA. Translation: CAA30576.1.
X07752 mRNA. Translation: CAA30577.1.
X51983 mRNA. Translation: CAA36241.1.
AK078233 mRNA. Translation: BAC37186.1.
AL590963 Genomic DNA. Translation: CAM46188.1. Sequence problems.
AL590963 Genomic DNA. Translation: CAM46189.1.
AL590963 Genomic DNA. Translation: CAM46190.1.
CH466556 Genomic DNA. Translation: EDL16164.1.
CH466556 Genomic DNA. Translation: EDL16165.1.
BC046795 mRNA. Translation: AAH46795.1.
CCDSiCCDS25362.1. [P63058-2]
PIRiS14416.
S14417.
S14418.
S14690. QRMSA1.
RefSeqiNP_835161.1. NM_178060.3. [P63058-2]
UniGeneiMm.265917.
Mm.442648.

Genome annotation databases

EnsembliENSMUST00000064187; ENSMUSP00000068281; ENSMUSG00000058756. [P63058-1]
ENSMUST00000103139; ENSMUSP00000099428; ENSMUSG00000058756. [P63058-2]
ENSMUST00000124072; ENSMUSP00000115323; ENSMUSG00000058756.
GeneIDi21833.
KEGGimmu:21833.
UCSCiuc007lhe.1. mouse. [P63058-2]
uc007lhf.1. mouse.
uc007lhg.1. mouse. [P63058-3]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07750 mRNA. Translation: CAA30575.1 .
X07751 mRNA. Translation: CAA30576.1 .
X07752 mRNA. Translation: CAA30577.1 .
X51983 mRNA. Translation: CAA36241.1 .
AK078233 mRNA. Translation: BAC37186.1 .
AL590963 Genomic DNA. Translation: CAM46188.1 . Sequence problems.
AL590963 Genomic DNA. Translation: CAM46189.1 .
AL590963 Genomic DNA. Translation: CAM46190.1 .
CH466556 Genomic DNA. Translation: EDL16164.1 .
CH466556 Genomic DNA. Translation: EDL16165.1 .
BC046795 mRNA. Translation: AAH46795.1 .
CCDSi CCDS25362.1. [P63058-2 ]
PIRi S14416.
S14417.
S14418.
S14690. QRMSA1.
RefSeqi NP_835161.1. NM_178060.3. [P63058-2 ]
UniGenei Mm.265917.
Mm.442648.

3D structure databases

ProteinModelPortali P63058.
SMRi P63058. Positions 49-409.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204183. 4 interactions.
DIPi DIP-43752N.
IntActi P63058. 1 interaction.
MINTi MINT-3374329.

Chemistry

GuidetoPHARMACOLOGYi 588.

PTM databases

PhosphoSitei P63058.

Proteomic databases

PRIDEi P63058.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064187 ; ENSMUSP00000068281 ; ENSMUSG00000058756 . [P63058-1 ]
ENSMUST00000103139 ; ENSMUSP00000099428 ; ENSMUSG00000058756 . [P63058-2 ]
ENSMUST00000124072 ; ENSMUSP00000115323 ; ENSMUSG00000058756 .
GeneIDi 21833.
KEGGi mmu:21833.
UCSCi uc007lhe.1. mouse. [P63058-2 ]
uc007lhf.1. mouse.
uc007lhg.1. mouse. [P63058-3 ]

Organism-specific databases

CTDi 7067.
MGIi MGI:98742. Thra.

Phylogenomic databases

eggNOGi NOG272726.
GeneTreei ENSGT00740000114969.
HOVERGENi HBG005606.
InParanoidi Q80Y90.
KOi K05547.
OMAi WLNGPKR.
OrthoDBi EOG7TBC2V.
PhylomeDBi P63058.
TreeFami TF328382.

Miscellaneous databases

NextBioi 301282.
PROi P63058.
SOURCEi Search...

Gene expression databases

ArrayExpressi P63058.
Bgeei P63058.
CleanExi MM_THRA.
Genevestigatori P63058.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple sequences encoding potential thyroid hormone receptors isolated from mouse skeletal muscle cDNA libraries."
    Prost E., Koenig R.J., Moore D.D., Larsen P.R., Whalen R.G.
    Nucleic Acids Res. 16:6248-6248(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-452 (ISOFORMS ALPHA-2 AND ALPHA-3).
    Strain: C3H.
    Tissue: Muscle.
  2. "Nucleotide sequence of the murine thyroid hormone receptor (alpha-1) cDNA."
    Masuda M., Yasuhara S., Yamashita M., Shibuya M., Odaka T.
    Nucleic Acids Res. 18:3055-3055(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
    Strain: C3H.
    Tissue: Testis.
  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.
    , 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 ALPHA-1).
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 ALPHA-2).
    Strain: C57BL/6.
    Tissue: Brain.
  7. "Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex."
    Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1D.
  8. "Cloning and characterization of RAP250, a nuclear receptor coactivator."
    Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.
    J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  9. "Characterization of a novel thyroid hormone receptor alpha variant involved in the regulation of myoblast differentiation."
    Casas F., Busson M., Grandemange S., Seyer P., Carazo A., Pessemesse L., Wrutniak-Cabello C., Cabello G.
    Mol. Endocrinol. 20:749-763(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS ALPHA-1 AND ALPHA-DELTAE6), POTENTIAL RNA EDITING OF ISOFORM ALPHA-DELTAE6, FUNCTION, TISSUE SPECIFICITY.
  10. "The mammalian clock component PERIOD2 coordinates circadian output by interaction with nuclear receptors."
    Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.
    Genes Dev. 24:345-357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PER2.

Entry informationi

Entry nameiTHA_MOUSE
AccessioniPrimary (citable) accession number: P63058
Secondary accession number(s): A3KFN4
, P10685, P15827, P16416, P37241, Q542U8, Q63107, Q63195, Q63196, Q80Y90, Q99146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 19, 2010
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi