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Q969Q1

- TRI63_HUMAN

UniProt

Q969Q1 - TRI63_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM63

Gene

TRIM63

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. signal transducer activity Source: UniProtKB
    4. titin binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: Ensembl
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. muscle contraction Source: Ensembl
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    3. regulation of gene expression Source: Ensembl
    4. response to electrical stimulus involved in regulation of muscle adaptation Source: UniProtKB
    5. response to glucocorticoid Source: Ensembl
    6. response to interleukin-1 Source: Ensembl
    7. signal transduction Source: UniProtKB
    8. skeletal muscle atrophy Source: Ensembl

    Keywords - Molecular functioni

    Ligase, Muscle protein

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase TRIM63 (EC:6.3.2.-)
    Alternative name(s):
    Iris RING finger protein
    Muscle-specific RING finger protein 1
    Short name:
    MuRF-1
    Short name:
    MuRF1
    RING finger protein 28
    Striated muscle RING zinc finger protein
    Tripartite motif-containing protein 63
    Gene namesi
    Name:TRIM63
    Synonyms:IRF, MURF1, RNF28, SMRZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16007. TRIM63.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity. CytoplasmmyofibrilsarcomereM line. CytoplasmmyofibrilsarcomereZ line
    Note: Colocalizes with TNNI3 in myocytes By similarity. Localizes to the M- and Z-lines in skeletal muscle.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. M band Source: UniProtKB-SubCell
    3. microtubule Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391C → A: Loss of SUMO2-binding. 1 Publication
    Mutagenesisi41 – 411H → A: Loss of SUMO2-binding. 1 Publication
    Mutagenesisi44 – 441C → A: Loss of SUMO2-binding. 1 Publication
    Mutagenesisi47 – 471C → A: Loss of SUMO2-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA34431.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 353353E3 ubiquitin-protein ligase TRIM63PRO_0000056290Add
    BLAST

    Proteomic databases

    PaxDbiQ969Q1.
    PRIDEiQ969Q1.

    PTM databases

    PhosphoSiteiQ969Q1.

    Expressioni

    Tissue specificityi

    Muscle specific. Selectively expressed in heart and skeletal muscle. Also expressed in the iris.4 Publications

    Developmental stagei

    Expressed throughout all developmental stages.1 Publication

    Gene expression databases

    BgeeiQ969Q1.
    CleanExiHS_TRIM63.
    GenevestigatoriQ969Q1.

    Interactioni

    Subunit structurei

    Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 and TNNI3. Forms a ternary complex with GNB2L1 and PRKCE By similarity. Interacts with CKM.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCAR1Q8IX122EBI-5661333,EBI-356265
    EEF1GP266412EBI-5661333,EBI-351467
    GFM1Q96RP92EBI-5661333,EBI-2255048
    MRPL41Q8IXM32EBI-5661333,EBI-912501
    MYOZ1Q9NP982EBI-5661333,EBI-744402
    TTNQ8WZ423EBI-5661333,EBI-681210

    Protein-protein interaction databases

    BioGridi124195. 66 interactions.
    IntActiQ969Q1. 37 interactions.
    MINTiMINT-6492114.
    STRINGi9606.ENSP00000363390.

    Structurei

    Secondary structure

    1
    353
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi123 – 1253
    Beta strandi132 – 1343
    Turni135 – 1384
    Beta strandi139 – 1413
    Helixi143 – 1486
    Turni150 – 1534
    Beta strandi156 – 1583
    Helixi214 – 26754

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D8UNMR-A119-169[»]
    3DDTX-ray1.90A/B/C117-161[»]
    4M3LX-ray2.10A/B/C/D214-271[»]
    ProteinModelPortaliQ969Q1.
    SMRiQ969Q1. Positions 16-78, 117-161, 214-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ969Q1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini267 – 32559COSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni74 – 218145Interaction with TTNAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili207 – 26963Sequence AnalysisAdd
    BLAST

    Domaini

    The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus. Also required for the E3 ubiquitin ligase activity By similarity.By similarity
    The B box-type zinc finger mediates homodimerization.3 Publications

    Sequence similaritiesi

    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
    Contains 1 COS domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG310224.
    HOGENOMiHOG000231156.
    HOVERGENiHBG071242.
    InParanoidiQ969Q1.
    KOiK10655.
    OMAiDGNPMEN.
    OrthoDBiEOG7VDXPK.
    PhylomeDBiQ969Q1.
    TreeFamiTF331669.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProiIPR017903. COS_domain.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00643. zf-B_box. 1 hit.
    [Graphical view]
    SMARTiSM00336. BBOX. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS51262. COS. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q969Q1-1) [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

    MDYKSSLIQD GNPMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND    50
    IFQAANPYWT SRGSSVSMSG GRFRCPTCRH EVIMDRHGVY GLQRNLLVEN 100
    IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSMCKVFGI 150
    HKACEVAPLQ SVFQGQKTEL NNCISMLVAG NDRVQTIITQ LEDSRRVTKE 200
    NSHQVKEELS QKFDTLYAIL DEKKSELLQR ITQEQEKKLS FIEALIQQYQ 250
    EQLDKSTKLV ETAIQSLDEP GGATFLLTAK QLIKSIVEAS KGCQLGKTEQ 300
    GFENMDFFTL DLEHIADALR AIDFGTDEEE EEFIEEEDQE EEESTEGKEE 350
    GHQ 353
    Length:353
    Mass (Da):40,248
    Last modified:December 1, 2001 - v1
    Checksum:i9BE4B1505039BC86
    GO
    Isoform 2 (identifier: Q969Q1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-131: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:325
    Mass (Da):36,950
    Checksum:iB03213D38E2063B0
    GO

    Sequence cautioni

    The sequence AAK52497.1 differs from that shown. Reason: Sequencing errors.
    The sequence AAK52497.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence CAC33173.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti237 – 2371K → E.2 Publications
    Corresponds to variant rs2275950 [ dbSNP | Ensembl ].
    VAR_020116

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei104 – 13128Missing in isoform 2. 1 PublicationVSP_055443Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291713 mRNA. Translation: CAC33173.1. Different initiation.
    AF353673 mRNA. Translation: AAK39519.1.
    AJ276484 mRNA. Translation: CAC81706.1.
    AF361946 mRNA. Translation: AAK52497.1. Sequence problems.
    AK056942 mRNA. Translation: BAB71318.1.
    AK297820 mRNA. Translation: BAG60157.1.
    AL391650 Genomic DNA. Translation: CAI17133.1.
    BC080529 mRNA. Translation: AAH80529.1.
    CCDSiCCDS273.1.
    RefSeqiNP_115977.2. NM_032588.3.
    UniGeneiHs.279709.

    Genome annotation databases

    EnsembliENST00000374272; ENSP00000363390; ENSG00000158022. [Q969Q1-1]
    GeneIDi84676.
    KEGGihsa:84676.
    UCSCiuc001bli.2. human.

    Polymorphism databases

    DMDMi21362898.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291713 mRNA. Translation: CAC33173.1 . Different initiation.
    AF353673 mRNA. Translation: AAK39519.1 .
    AJ276484 mRNA. Translation: CAC81706.1 .
    AF361946 mRNA. Translation: AAK52497.1 . Sequence problems.
    AK056942 mRNA. Translation: BAB71318.1 .
    AK297820 mRNA. Translation: BAG60157.1 .
    AL391650 Genomic DNA. Translation: CAI17133.1 .
    BC080529 mRNA. Translation: AAH80529.1 .
    CCDSi CCDS273.1.
    RefSeqi NP_115977.2. NM_032588.3.
    UniGenei Hs.279709.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D8U NMR - A 119-169 [» ]
    3DDT X-ray 1.90 A/B/C 117-161 [» ]
    4M3L X-ray 2.10 A/B/C/D 214-271 [» ]
    ProteinModelPortali Q969Q1.
    SMRi Q969Q1. Positions 16-78, 117-161, 214-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124195. 66 interactions.
    IntActi Q969Q1. 37 interactions.
    MINTi MINT-6492114.
    STRINGi 9606.ENSP00000363390.

    PTM databases

    PhosphoSitei Q969Q1.

    Polymorphism databases

    DMDMi 21362898.

    Proteomic databases

    PaxDbi Q969Q1.
    PRIDEi Q969Q1.

    Protocols and materials databases

    DNASUi 84676.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374272 ; ENSP00000363390 ; ENSG00000158022 . [Q969Q1-1 ]
    GeneIDi 84676.
    KEGGi hsa:84676.
    UCSCi uc001bli.2. human.

    Organism-specific databases

    CTDi 84676.
    GeneCardsi GC01M026377.
    HGNCi HGNC:16007. TRIM63.
    MIMi 606131. gene.
    neXtProti NX_Q969Q1.
    PharmGKBi PA34431.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310224.
    HOGENOMi HOG000231156.
    HOVERGENi HBG071242.
    InParanoidi Q969Q1.
    KOi K10655.
    OMAi DGNPMEN.
    OrthoDBi EOG7VDXPK.
    PhylomeDBi Q969Q1.
    TreeFami TF331669.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi TRIM63. human.
    EvolutionaryTracei Q969Q1.
    GeneWikii TRIM63.
    GenomeRNAii 84676.
    NextBioi 74699.
    PROi Q969Q1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q969Q1.
    CleanExi HS_TRIM63.
    Genevestigatori Q969Q1.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi IPR017903. COS_domain.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    SMARTi SM00336. BBOX. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS51262. COS. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain."
      Centner T., Yano J., Kimura E., McElhinny A.S., Pelin K., Witt C.C., Bang M.-L., Trombitas K., Granzier H., Gregorio C.C., Sorimachi H., Labeit S.
      J. Mol. Biol. 306:717-726(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-237, INTERACTION WITH TTN; TRIM54 AND TRIM55, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    2. "Expressed sequence tag analysis of adult human iris for the NEIBank project: steroid-response factors and similarities with retinal pigment epithelium."
      Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A., Touchman J.W., Bouffard G., Smith D., Peterson K.
      Mol. Vis. 8:185-195(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Iris.
    3. "Characterisation of MURF2, a new muscle-specific RING finger protein of the RBCC family that associates with microtubules."
      Stanchi F.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    4. "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain."
      Dai K.-S., Liew C.-C.
      J. Biol. Chem. 276:23992-23999(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SUMO2, MUTAGENESIS OF CYS-39; HIS-41; CYS-44 AND CYS-47, DOMAIN.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Heart and Skeletal muscle.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1), VARIANT GLU-237.
      Tissue: Skin.
    8. Cited for: TISSUE SPECIFICITY.
    9. "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1."
      McElhinny A.S., Kakinuma K., Sorimachi H., Labeit S., Gregorio C.C.
      J. Cell Biol. 157:125-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN, FUNCTION, INTERACTION WITH GMEB1.
    10. "MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies."
      Hirner S., Krohne C., Schuster A., Hoffmann S., Witt S., Erber R., Sticht C., Gasch A., Labeit S., Labeit D.
      J. Mol. Biol. 379:666-677(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis."
      Koyama S., Hata S., Witt C.C., Ono Y., Lerche S., Ojima K., Chiba T., Doi N., Kitamura F., Tanaka K., Abe K., Witt S.H., Rybin V., Gasch A., Franz T., Labeit S., Sorimachi H.
      J. Mol. Biol. 376:1224-1236(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CKM, FUNCTION.
    12. "Solution structure of the B-box domain of the human tripartite motif-containing 63 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 119-169.
    13. "Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold."
      Mrosek M., Meier S., Ucurum-Fotiadis Z., von Castelmur E., Hedbom E., Lustig A., Grzesiek S., Labeit D., Labeit S., Mayans O.
      Biochemistry 47:10722-10730(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 117-161 IN COMPLEX WITH ZINC IONS, DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiTRI63_HUMAN
    AccessioniPrimary (citable) accession number: Q969Q1
    Secondary accession number(s): B4DN95
    , Q5T2I1, Q96BD3, Q96KD9, Q9BYV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3