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Q8CIG8

- ANM5_MOUSE

UniProt

Q8CIG8 - ANM5_MOUSE

Protein

Protein arginine N-methyltransferase 5

Gene

Prmt5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter.5 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].

    Enzyme regulationi

    Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei304 – 3041Peptide substrateBy similarity
    Binding sitei307 – 3071Peptide substrateBy similarity
    Binding sitei324 – 3241S-adenosyl-L-methionineBy similarity
    Sitei327 – 3271Critical for specifying symmetric addition of methyl groupsBy similarity
    Binding sitei392 – 3921S-adenosyl-L-methionineBy similarity
    Active sitei435 – 4351Proton donor/acceptorBy similarity
    Active sitei444 – 4441Proton donor/acceptorBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. core promoter sequence-specific DNA binding Source: UniProtKB
    3. histone-arginine N-methyltransferase activity Source: RefGenome
    4. methyltransferase activity Source: MGI
    5. protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. ribonucleoprotein complex binding Source: Ensembl
    8. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. circadian regulation of gene expression Source: UniProtKB
    2. endothelial cell activation Source: Ensembl
    3. histone arginine methylation Source: RefGenome
    4. histone H4-R3 methylation Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    6. peptidyl-arginine methylation Source: UniProtKB
    7. peptidyl-arginine methylation, to symmetrical-dimethyl arginine Source: RefGenome
    8. peptidyl-arginine N-methylation Source: MGI
    9. spliceosomal snRNP assembly Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    ReactomeiREACT_206812. snRNP Assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein arginine N-methyltransferase 5 (EC:2.1.1.-)
    Alternative name(s):
    Histone-arginine N-methyltransferase PRMT5 (EC:2.1.1.125)
    Jak-binding protein 1
    Shk1 kinase-binding protein 1 homolog
    Short name:
    SKB1 homolog
    Gene namesi
    Name:Prmt5
    Synonyms:Jbp1, Skb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1351645. Prmt5.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. methylosome Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 637636Protein arginine N-methyltransferase 5PRO_0000212344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8CIG8.
    PaxDbiQ8CIG8.
    PRIDEiQ8CIG8.

    PTM databases

    PhosphoSiteiQ8CIG8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8CIG8.
    BgeeiQ8CIG8.
    CleanExiMM_PRMT5.
    GenevestigatoriQ8CIG8.

    Interactioni

    Subunit structurei

    Forms, at least, homodimers and homotetramers. Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2 and SSTR1. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4 By similarity. Interacts with PRDM1. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation By similarity. Interacts with BRAF and with active RAF1 By similarity. Interacts with HOXA9 By similarity. Interacts with SRGAP2. Interacts with EPB41L3; this modulates methylation of target proteins By similarity. Found in a complex with COPRS, RUNX1 and CBFB. Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1. Interacts with IWS1 By similarity. Interacts with CRY1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ccnd1P253225EBI-2527009,EBI-847243
    ChtopQ9CY574EBI-2527009,EBI-6393116

    Protein-protein interaction databases

    BioGridi205181. 14 interactions.
    IntActiQ8CIG8. 7 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CIG8.
    SMRiQ8CIG8. Positions 13-637.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini308 – 615308SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 292280TIM barrelBy similarityAdd
    BLAST
    Regioni333 – 3342S-adenosyl-L-methionine bindingBy similarity
    Regioni419 – 4202S-adenosyl-L-methionine bindingBy similarity
    Regioni465 – 637173Beta barrelBy similarityAdd
    BLAST
    Regioni488 – 4947DimerizationBy similarity

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG291156.
    GeneTreeiENSGT00390000001141.
    HOGENOMiHOG000175933.
    HOVERGENiHBG057083.
    InParanoidiQ8CIG8.
    KOiK02516.
    OrthoDBiEOG7X6KZR.
    PhylomeDBiQ8CIG8.
    TreeFamiTF300626.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR007857. Arg_MeTrfase_PRMT5.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10738. PTHR10738. 1 hit.
    PfamiPF05185. PRMT5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015894. Skb1_MeTrfase. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8CIG8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF    50
    KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR 100
    RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM 150
    FWMRVPLVAP EDLRDDVIAN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK 200
    RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKVQ 250
    QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 300
    AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP 350
    EEEKETNVQV LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT 400
    LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL 450
    DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM 500
    PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG 550
    FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV 600
    RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL 637
    Length:637
    Mass (Da):72,680
    Last modified:January 23, 2007 - v3
    Checksum:iE8014CA172B30543
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691A → E in BAE21155. (PubMed:16141072)Curated
    Sequence conflicti169 – 1691A → E in BAE38057. (PubMed:16141072)Curated
    Sequence conflicti376 – 3761L → F in AAF04503. (PubMed:10531356)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132414 mRNA. Translation: BAE21155.1.
    AK165165 mRNA. Translation: BAE38057.1.
    BC023905 mRNA. Translation: AAH23905.1.
    AF167573 mRNA. Translation: AAF04503.1.
    CCDSiCCDS27091.1.
    RefSeqiNP_038796.2. NM_013768.3.
    UniGeneiMm.196585.

    Genome annotation databases

    EnsembliENSMUST00000023873; ENSMUSP00000023873; ENSMUSG00000023110.
    GeneIDi27374.
    KEGGimmu:27374.
    UCSCiuc007twf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK132414 mRNA. Translation: BAE21155.1 .
    AK165165 mRNA. Translation: BAE38057.1 .
    BC023905 mRNA. Translation: AAH23905.1 .
    AF167573 mRNA. Translation: AAF04503.1 .
    CCDSi CCDS27091.1.
    RefSeqi NP_038796.2. NM_013768.3.
    UniGenei Mm.196585.

    3D structure databases

    ProteinModelPortali Q8CIG8.
    SMRi Q8CIG8. Positions 13-637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205181. 14 interactions.
    IntActi Q8CIG8. 7 interactions.

    PTM databases

    PhosphoSitei Q8CIG8.

    Proteomic databases

    MaxQBi Q8CIG8.
    PaxDbi Q8CIG8.
    PRIDEi Q8CIG8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023873 ; ENSMUSP00000023873 ; ENSMUSG00000023110 .
    GeneIDi 27374.
    KEGGi mmu:27374.
    UCSCi uc007twf.2. mouse.

    Organism-specific databases

    CTDi 10419.
    MGIi MGI:1351645. Prmt5.

    Phylogenomic databases

    eggNOGi NOG291156.
    GeneTreei ENSGT00390000001141.
    HOGENOMi HOG000175933.
    HOVERGENi HBG057083.
    InParanoidi Q8CIG8.
    KOi K02516.
    OrthoDBi EOG7X6KZR.
    PhylomeDBi Q8CIG8.
    TreeFami TF300626.

    Enzyme and pathway databases

    Reactomei REACT_206812. snRNP Assembly.

    Miscellaneous databases

    NextBioi 305288.
    PROi Q8CIG8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CIG8.
    Bgeei Q8CIG8.
    CleanExi MM_PRMT5.
    Genevestigatori Q8CIG8.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025799. Arg_MeTrfase.
    IPR007857. Arg_MeTrfase_PRMT5.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10738. PTHR10738. 1 hit.
    Pfami PF05185. PRMT5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015894. Skb1_MeTrfase. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J.
      Tissue: Skin.
    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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity."
      Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.
      J. Biol. Chem. 274:31531-31542(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-637.
    4. "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
      Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
      Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN METHYLATION OF HISTONE H3.
    5. "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells."
      Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.
      Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRDM1.
    6. "Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members."
      Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.
      Genes Dev. 23:1749-1762(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN METHYLATION OF PIWI PROTEINS.
    7. Cited for: FUNCTION, INTERACTION WITH CHTOP.
    8. "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
      Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
      Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE REGULATION OF MAPK1/MAPK3 SIGNALING PATHWAY, RAF1 METHYLATION.
    9. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
      Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
      Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHTOP, SUBCELLULAR LOCATION.
    10. "The histone- and PRMT5-associated protein COPR5 is required for myogenic differentiation."
      Paul C., Sardet C., Fabbrizio E.
      Cell Death Differ. 19:900-908(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPRS, IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 AND CBFB.
    11. "Role of type II protein arginine methyltransferase 5 in the regulation of Circadian Per1 gene."
      Na J., Lee K., Kim H.G., Shin J.Y., Na W., Jeong H., Lee J.W., Cho S., Kim W.S., Ju B.G.
      PLoS ONE 7:E48152-E48152(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CRY1.

    Entry informationi

    Entry nameiANM5_MOUSE
    AccessioniPrimary (citable) accession number: Q8CIG8
    Secondary accession number(s): Q3TNN1, Q9QZS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 3 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