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Q9BYV2

- TRI54_HUMAN

UniProt

Q9BYV2 - TRI54_HUMAN

Protein

Tripartite motif-containing protein 54

Gene

TRIM54

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    May bind and stabilize microtubules during myotubes formation.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri26 – 8257RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri121 – 16343B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. signal transducer activity Source: UniProtKB
    2. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. microtubule-based process Source: UniProtKB
    3. multicellular organismal development Source: UniProtKB-KW
    4. negative regulation of microtubule depolymerization Source: UniProtKB
    5. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tripartite motif-containing protein 54
    Alternative name(s):
    Muscle-specific RING finger protein
    Short name:
    MuRF
    Muscle-specific RING finger protein 3
    Short name:
    MuRF-3
    Short name:
    MuRF3
    RING finger protein 30
    Gene namesi
    Name:TRIM54
    Synonyms:MURF, MURF3, RNF30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16008. TRIM54.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line By similarity
    Note: Associates with microtubules. Localizes to the Z-lines in skeletal muscles By similarity.By similarity

    GO - Cellular componenti

    1. microtubule Source: UniProtKB
    2. microtubule associated complex Source: Ensembl
    3. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34434.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Tripartite motif-containing protein 54PRO_0000056282Add
    BLAST

    Proteomic databases

    PaxDbiQ9BYV2.
    PRIDEiQ9BYV2.

    PTM databases

    PhosphoSiteiQ9BYV2.

    Expressioni

    Tissue specificityi

    Specifically expressed in heart and skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ9BYV2.
    CleanExiHS_TRIM54.
    GenevestigatoriQ9BYV2.

    Organism-specific databases

    HPAiHPA019690.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer. Interacts with tubulin By similarity. Interacts with TRIM63 and probably with TRIM55.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi121415. 28 interactions.
    IntActiQ9BYV2. 4 interactions.
    STRINGi9606.ENSP00000296098.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi127 – 1293
    Beta strandi132 – 1387
    Turni139 – 1424
    Beta strandi143 – 1464
    Helixi147 – 1515
    Turni154 – 1574
    Beta strandi160 – 1623
    Helixi164 – 1663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q1DX-ray2.15A122-168[»]
    ProteinModelPortaliQ9BYV2.
    SMRiQ9BYV2. Positions 17-85, 122-168, 220-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYV2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini271 – 32959COSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni168 – 21144Mediates microtubule-binding and homooligomerizationBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili220 – 25839Sequence AnalysisAdd
    BLAST

    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 fingeri26 – 8257RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri121 – 16343B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG310224.
    HOGENOMiHOG000231156.
    HOVERGENiHBG071242.
    KOiK10653.
    OMAiGYESMDQ.
    OrthoDBiEOG7VDXPK.
    PhylomeDBiQ9BYV2.
    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: Q9BYV2-1) [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

    MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC    50
    ANDVFQASNP LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL 100
    VENIIDIYKQ ESSRPLHSKA EQHLMCEEHE EEKINIYCLS CEVPTCSLCK 150
    VFGAHKDCEV APLPTIYKRQ KSELSDGIAM LVAGNDRVQA VITQMEEVCQ 200
    TIEDNSRRQK QLLNQRFESL CAVLEERKGE LLQALAREQE EKLQRVRGLI 250
    RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG 300
    RPEPGYESME QFTVRVEHVA EMLRTIDFQP GASGEEEEVA PDGEEGSAGP 350
    EEERPDGP 358
    Length:358
    Mass (Da):40,301
    Last modified:October 14, 2008 - v3
    Checksum:iC44B08A9871323F6
    GO
    Isoform 2 (identifier: Q9BYV2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         171-171: K → KKQDLTLLPRLECSGTNTTYCSLDLPSSSDPPILASQNTKIID

    Show »
    Length:400
    Mass (Da):44,833
    Checksum:iD4D12B4FA81A841F
    GO

    Sequence cautioni

    The sequence AAY24296.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC32841.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC32842.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1721S → N in CAC32841. (PubMed:11243782)Curated
    Sequence conflicti214 – 2141N → T in CAC32841. (PubMed:11243782)Curated
    Sequence conflicti214 – 2141N → T in CAC32842. (PubMed:11243782)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei171 – 1711K → KKQDLTLLPRLECSGTNTTY CSLDLPSSSDPPILASQNTK IID in isoform 2. 1 PublicationVSP_016061

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291714 mRNA. Translation: CAC32841.1. Different initiation.
    AJ291714 mRNA. Translation: CAC32842.1. Different initiation.
    AC013413 Genomic DNA. Translation: AAY24296.1. Different initiation.
    CH471053 Genomic DNA. Translation: EAX00606.1.
    BC141807 mRNA. Translation: AAI41808.1.
    CCDSiCCDS1745.2. [Q9BYV2-2]
    CCDS1746.2. [Q9BYV2-1]
    RefSeqiNP_115935.3. NM_032546.3. [Q9BYV2-2]
    NP_912730.2. NM_187841.2. [Q9BYV2-1]
    UniGeneiHs.516036.

    Genome annotation databases

    EnsembliENST00000296098; ENSP00000296098; ENSG00000138100. [Q9BYV2-2]
    ENST00000380075; ENSP00000369415; ENSG00000138100. [Q9BYV2-1]
    GeneIDi57159.
    KEGGihsa:57159.
    UCSCiuc002rjn.3. human. [Q9BYV2-2]
    uc002rjo.3. human. [Q9BYV2-1]

    Polymorphism databases

    DMDMi209572715.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291714 mRNA. Translation: CAC32841.1 . Different initiation.
    AJ291714 mRNA. Translation: CAC32842.1 . Different initiation.
    AC013413 Genomic DNA. Translation: AAY24296.1 . Different initiation.
    CH471053 Genomic DNA. Translation: EAX00606.1 .
    BC141807 mRNA. Translation: AAI41808.1 .
    CCDSi CCDS1745.2. [Q9BYV2-2 ]
    CCDS1746.2. [Q9BYV2-1 ]
    RefSeqi NP_115935.3. NM_032546.3. [Q9BYV2-2 ]
    NP_912730.2. NM_187841.2. [Q9BYV2-1 ]
    UniGenei Hs.516036.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q1D X-ray 2.15 A 122-168 [» ]
    ProteinModelPortali Q9BYV2.
    SMRi Q9BYV2. Positions 17-85, 122-168, 220-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121415. 28 interactions.
    IntActi Q9BYV2. 4 interactions.
    STRINGi 9606.ENSP00000296098.

    PTM databases

    PhosphoSitei Q9BYV2.

    Polymorphism databases

    DMDMi 209572715.

    Proteomic databases

    PaxDbi Q9BYV2.
    PRIDEi Q9BYV2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296098 ; ENSP00000296098 ; ENSG00000138100 . [Q9BYV2-2 ]
    ENST00000380075 ; ENSP00000369415 ; ENSG00000138100 . [Q9BYV2-1 ]
    GeneIDi 57159.
    KEGGi hsa:57159.
    UCSCi uc002rjn.3. human. [Q9BYV2-2 ]
    uc002rjo.3. human. [Q9BYV2-1 ]

    Organism-specific databases

    CTDi 57159.
    GeneCardsi GC02P027506.
    HGNCi HGNC:16008. TRIM54.
    HPAi HPA019690.
    MIMi 606474. gene.
    neXtProti NX_Q9BYV2.
    PharmGKBi PA34434.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310224.
    HOGENOMi HOG000231156.
    HOVERGENi HBG071242.
    KOi K10653.
    OMAi GYESMDQ.
    OrthoDBi EOG7VDXPK.
    PhylomeDBi Q9BYV2.
    TreeFami TF331669.

    Miscellaneous databases

    ChiTaRSi TRIM54. human.
    EvolutionaryTracei Q9BYV2.
    GenomeRNAii 57159.
    NextBioi 63157.
    PROi Q9BYV2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BYV2.
    CleanExi HS_TRIM54.
    Genevestigatori Q9BYV2.

    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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, OLIGOMERIZATION, INTERACTION WITH TRIM63 AND TRIM55.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "The B-box domain of TRIM54."
      Structural genomics consortium (SGC)
      Submitted (FEB-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 122-168 IN COMPLEX WITH ZINC IONS.

    Entry informationi

    Entry nameiTRI54_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYV2
    Secondary accession number(s): A5D8T7, Q53SY4, Q9BYV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 118 of the entry and version 3 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3