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Q9C035

- TRIM5_HUMAN

UniProt

Q9C035 - TRIM5_HUMAN

Protein

Tripartite motif-containing protein 5

Gene

TRIM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV) and equine infectious anemia virus (EIAV).6 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 5945RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein homodimerization activity Source: UniProtKB
    5. signaling pattern recognition receptor activity Source: UniProtKB
    6. ubiquitin-protein transferase activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of innate immune response Source: UniProtKB
    2. defense response to virus Source: UniProtKB
    3. innate immune response Source: UniProt
    4. negative regulation of viral entry into host cell Source: UniProt
    5. negative regulation of viral release from host cell Source: UniProt
    6. pattern recognition receptor signaling pathway Source: GOC
    7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    8. positive regulation of MAPK cascade Source: UniProtKB
    9. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    10. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProt
    11. protein K63-linked ubiquitination Source: UniProtKB
    12. protein trimerization Source: UniProtKB
    13. regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    14. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tripartite motif-containing protein 5 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 88
    Gene namesi
    Name:TRIM5
    Synonyms:RNF88
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:16276. TRIM5.

    Subcellular locationi

    CytoplasmP-body 2 Publications
    Note: Closely associates with proteasomal subunits in cytoplasmic bodies By similarity. Colocalizes with SQSTM1 in cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProt
    2. cytoplasmic mRNA processing body Source: UniProtKB
    3. Golgi apparatus Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151C → A: Abolishes E3 ligase activity. 1 Publication
    Mutagenesisi332 – 3321R → A, G, H, P, Q or S: Increases strongly cell restriction against HIV-1 and SIVmac infection. 1 Publication
    Mutagenesisi332 – 3321R → D, E or L: Increases strongly cell restriction against HIV-1 infection. 1 Publication
    Mutagenesisi332 – 3321R → K: No effect on HIV-1 and SIVmac infection. 1 Publication

    Organism-specific databases

    PharmGKBiPA38109.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 493492Tripartite motif-containing protein 5PRO_0000056201Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    Degraded in a proteasome-independent fashion in the absence of viral infection but in a proteasome-dependent fashion following exposure to restriction sensitive virus.
    Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ9C035.
    PaxDbiQ9C035.
    PRIDEiQ9C035.

    PTM databases

    PhosphoSiteiQ9C035.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9C035.
    BgeeiQ9C035.
    GenevestigatoriQ9C035.

    Organism-specific databases

    HPAiCAB013497.
    HPA023420.
    HPA023422.

    Interactioni

    Subunit structurei

    Can form homodimers and homotrimers. In addition to lower-order dimerization, also exhibits a higher-order multimerization and both low- and high-order multimerizations are essential for its restriction activity. Isoform Delta interacts with BTBD1 and BTBD2. Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70 By similarity. Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with PSMC2, SQSTM1, MAP3K7/TAK1, TAB2 and TAB3.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-924214,EBI-924214
    Q2Y0803EBI-924230,EBI-924086From a different organism.
    TRIM32Q130492EBI-924214,EBI-742790

    Protein-protein interaction databases

    BioGridi124491. 45 interactions.
    IntActiQ9C035. 18 interactions.
    MINTiMINT-6631391.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni16 – 183
    Beta strandi29 – 313
    Helixi38 – 458
    Turni46 – 505
    Turni56 – 583
    Beta strandi64 – 663
    Beta strandi92 – 943
    Turni96 – 983
    Beta strandi104 – 1063
    Turni107 – 1093
    Beta strandi111 – 1133
    Helixi115 – 1184
    Turni121 – 1255

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ECVNMR-A1-78[»]
    2YRGNMR-A86-129[»]
    ProteinModelPortaliQ9C035.
    SMRiQ9C035. Positions 5-78, 87-131, 255-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9C035.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini281 – 493213B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili130 – 241112Sequence AnalysisAdd
    BLAST

    Domaini

    The B box-type zinc finger domain and the coiled-coil domain contribute to the higher and low order multimerization respectively which is essential for restriction activity.1 Publication
    The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (PubMed:22482711).1 Publication
    The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization.1 Publication

    Sequence similaritiesi

    Belongs to the TRIM/RBCC family.Curated
    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 5945RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG253216.
    HOVERGENiHBG001357.
    KOiK10648.
    OMAiSKTHITY.
    OrthoDBiEOG7RJPR6.
    PhylomeDBiQ9C035.
    TreeFamiTF338674.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR003877. SPRY_rcpt.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view]
    PRINTSiPR01407. BUTYPHLNCDUF.
    SMARTiSM00336. BBOX. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q9C035-1) [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

    MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK    50
    GESSCPVCRI SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE 100
    KLLLFCQEDG KVICWLCERS QEHRGHHTFL TEEVAREYQV KLQAALEMLR 150
    QKQQEAEELE ADIREEKASW KTQIQYDKTN VLADFEQLRD ILDWEESNEL 200
    QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ GSVMELLQGV 250
    DGVIKRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD 300
    VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG 350
    SQSITSGKHY WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW 400
    VIGLEEGVKC SAFQDSSFHT PSVPFIVPLS VIICPDRVGV FLDYEACTVS 450
    FFNITNHGFL IYKFSHCSFS QPVFPYLNPR KCGVPMTLCS PSS 493
    Length:493
    Mass (Da):56,338
    Last modified:June 1, 2001 - v1
    Checksum:i8E61AAFD508AF6C0
    GO
    Isoform Beta (identifier: Q9C035-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         390-400: NENYQPKYGYW → KRFMILLPRHT
         401-493: Missing.

    Note: Probable artifact.

    Show »
    Length:400
    Mass (Da):46,038
    Checksum:iE8AC7B014BF58488
    GO
    Isoform Gamma (identifier: Q9C035-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         299-347: VDVTVAPNNI...TFVNFNYCTG → GKEKSHYHKP...SKTHITYPSL
         348-493: Missing.

    Show »
    Length:347
    Mass (Da):40,108
    Checksum:i07B838DB840C4F55
    GO
    Isoform Delta (identifier: Q9C035-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         299-326: VDVTVAPNNISCAVISEDKRQVSSPKPQ → GWSAMARSRFTATSTSQIQAILLPQPPK
         327-493: Missing.

    Show »
    Length:326
    Mass (Da):37,685
    Checksum:iAB54B894549C8775
    GO
    Isoform Epsilon (identifier: Q9C035-5) [UniParc]FASTAAdd to Basket

    Also known as: Kappa

    The sequence of this isoform differs from the canonical sequence as follows:
         249-271: GVDGVIKRTENVTLKKPETFPKN → DGERDLEEARNFSKKSKESVSSS
         272-493: Missing.

    Show »
    Length:271
    Mass (Da):31,253
    Checksum:iC988390B71D2B74F
    GO
    Isoform Iota (identifier: Q9C035-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         249-257: GVDGVIKRT → VKSGKKPEH
         258-493: Missing.

    Note: Has dominant-negative activity against TRIM5alpha. Does not inhibit HIV-1 replication.

    Show »
    Length:257
    Mass (Da):29,677
    Checksum:i8769CFD2E659BEF5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761I → L in BAB55218. (PubMed:15249690)Curated
    Sequence conflicti130 – 1301L → P in BAB55218. (PubMed:15249690)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311G → S.1 Publication
    Corresponds to variant rs59896509 [ dbSNP | Ensembl ].
    VAR_060707
    Natural varianti43 – 431H → Y.2 Publications
    Corresponds to variant rs3740996 [ dbSNP | Ensembl ].
    VAR_017397
    Natural varianti58 – 581C → Y.1 Publication
    Corresponds to variant rs61432120 [ dbSNP | Ensembl ].
    VAR_060708
    Natural varianti110 – 1101G → E.1 Publication
    Corresponds to variant rs56348930 [ dbSNP | Ensembl ].
    VAR_060709
    Natural varianti112 – 1121V → F.1 Publication
    Corresponds to variant rs11601507 [ dbSNP | Ensembl ].
    VAR_030154
    Natural varianti136 – 1361R → Q.4 Publications
    Corresponds to variant rs10838525 [ dbSNP | Ensembl ].
    VAR_017398
    Natural varianti249 – 2491G → D.2 Publications
    Corresponds to variant rs11038628 [ dbSNP | Ensembl ].
    VAR_030155
    Natural varianti419 – 4191H → Y.1 Publication
    Corresponds to variant rs28381981 [ dbSNP | Ensembl ].
    VAR_030156
    Natural varianti467 – 4671C → S.1 Publication
    Corresponds to variant rs59218593 [ dbSNP | Ensembl ].
    VAR_060710
    Natural varianti479 – 4791P → L.1 Publication
    Corresponds to variant rs7104422 [ dbSNP | Ensembl ].
    VAR_030157

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei249 – 27123GVDGV…TFPKN → DGERDLEEARNFSKKSKESV SSS in isoform Epsilon. 2 PublicationsVSP_009016Add
    BLAST
    Alternative sequencei249 – 2579GVDGVIKRT → VKSGKKPEH in isoform Iota. CuratedVSP_044095
    Alternative sequencei258 – 493236Missing in isoform Iota. CuratedVSP_044096Add
    BLAST
    Alternative sequencei272 – 493222Missing in isoform Epsilon. 2 PublicationsVSP_009017Add
    BLAST
    Alternative sequencei299 – 34749VDVTV…NYCTG → GKEKSHYHKPPCGLSLLLSL SFRILCSLLGSCFKIYDSPS KTHITYPSL in isoform Gamma. 2 PublicationsVSP_009012Add
    BLAST
    Alternative sequencei299 – 32628VDVTV…SPKPQ → GWSAMARSRFTATSTSQIQA ILLPQPPK in isoform Delta. 1 PublicationVSP_009014Add
    BLAST
    Alternative sequencei327 – 493167Missing in isoform Delta. 1 PublicationVSP_009015Add
    BLAST
    Alternative sequencei348 – 493146Missing in isoform Gamma. 2 PublicationsVSP_009013Add
    BLAST
    Alternative sequencei390 – 40011NENYQPKYGYW → KRFMILLPRHT in isoform Beta. 1 PublicationVSP_009010Add
    BLAST
    Alternative sequencei401 – 49393Missing in isoform Beta. 1 PublicationVSP_009011Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220025 mRNA. Translation: AAG53479.1.
    AF220026 mRNA. Translation: AAG53480.1.
    AF220027 mRNA. Translation: AAG53481.1.
    AF220028 mRNA. Translation: AAG53482.1.
    AF220029 mRNA. Translation: AAG53483.1.
    AY625000 mRNA. Translation: AAT48101.1.
    DQ301444 Genomic DNA. Translation: ABC00997.1.
    DQ301445 Genomic DNA. Translation: ABC00998.1.
    DQ301446 Genomic DNA. Translation: ABC00999.1.
    DQ301447 Genomic DNA. Translation: ABC01000.1.
    DQ301448 Genomic DNA. Translation: ABC01001.1.
    DQ301449 Genomic DNA. Translation: ABC01002.1.
    DQ301450 Genomic DNA. Translation: ABC01003.1.
    DQ301451 Genomic DNA. Translation: ABC01004.1.
    DQ301452 Genomic DNA. Translation: ABC01005.1.
    DQ301453 Genomic DNA. Translation: ABC01006.1.
    DQ301454 Genomic DNA. Translation: ABC01007.1.
    DQ301455 Genomic DNA. Translation: ABC01008.1.
    DQ301456 Genomic DNA. Translation: ABC01009.1.
    DQ301457 Genomic DNA. Translation: ABC01010.1.
    DQ301458 Genomic DNA. Translation: ABC01011.1.
    DQ301459 Genomic DNA. Translation: ABC01012.1.
    DQ301460 Genomic DNA. Translation: ABC01013.1.
    DQ301461 Genomic DNA. Translation: ABC01014.1.
    DQ301462 Genomic DNA. Translation: ABC01015.1.
    DQ301463 Genomic DNA. Translation: ABC01016.1.
    DQ301464 Genomic DNA. Translation: ABC01017.1.
    DQ301465 Genomic DNA. Translation: ABC01018.1.
    DQ301466 Genomic DNA. Translation: ABC01019.1.
    DQ301467 Genomic DNA. Translation: ABC01020.1.
    DQ301468 Genomic DNA. Translation: ABC01021.1.
    DQ301469 Genomic DNA. Translation: ABC01022.1.
    DQ301470 Genomic DNA. Translation: ABC01023.1.
    DQ301471 Genomic DNA. Translation: ABC01024.1.
    DQ301472 Genomic DNA. Translation: ABC01025.1.
    DQ301473 Genomic DNA. Translation: ABC01026.1.
    DQ301474 Genomic DNA. Translation: ABC01027.1.
    DQ301475 Genomic DNA. Translation: ABC01028.1.
    DQ301476 Genomic DNA. Translation: ABC01029.1.
    DQ301477 Genomic DNA. Translation: ABC01030.1.
    DQ301478 Genomic DNA. Translation: ABC01031.1.
    DQ301479 Genomic DNA. Translation: ABC01032.1.
    DQ301480 Genomic DNA. Translation: ABC01033.1.
    DQ288685 mRNA. Translation: ABB90543.1.
    JF928461 mRNA. Translation: AEN14475.1.
    JF928462 mRNA. Translation: AEN14476.1.
    AK027593 mRNA. Translation: BAB55218.1.
    AC015691 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68771.1.
    CH471064 Genomic DNA. Translation: EAW68772.1.
    CH471064 Genomic DNA. Translation: EAW68774.1.
    CH471064 Genomic DNA. Translation: EAW68775.1.
    EU260465 Genomic DNA. Translation: ABW96352.1.
    CH471064 Genomic DNA. Translation: EAW68776.1.
    CH471064 Genomic DNA. Translation: EAW68777.1.
    BC021258 mRNA. Translation: AAH21258.1.
    CCDSiCCDS31392.1. [Q9C035-4]
    CCDS31393.1. [Q9C035-1]
    CCDS31394.1. [Q9C035-3]
    RefSeqiNP_149023.2. NM_033034.2. [Q9C035-1]
    NP_149083.2. NM_033092.2. [Q9C035-3]
    NP_149084.2. NM_033093.2. [Q9C035-4]
    XP_005253240.1. XM_005253183.1. [Q9C035-1]
    XP_005253241.1. XM_005253184.1. [Q9C035-4]
    UniGeneiHs.125300.

    Genome annotation databases

    EnsembliENST00000380027; ENSP00000369366; ENSG00000132256. [Q9C035-4]
    ENST00000380034; ENSP00000369373; ENSG00000132256. [Q9C035-1]
    ENST00000396847; ENSP00000380058; ENSG00000132256. [Q9C035-3]
    ENST00000433961; ENSP00000393052; ENSG00000132256. [Q9C035-5]
    GeneIDi85363.
    KEGGihsa:85363.
    UCSCiuc001mbm.2. human. [Q9C035-1]
    uc001mbn.3. human. [Q9C035-4]
    uc001mbp.3. human. [Q9C035-3]
    uc021qcx.1. human. [Q9C035-6]

    Polymorphism databases

    DMDMi38605459.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220025 mRNA. Translation: AAG53479.1 .
    AF220026 mRNA. Translation: AAG53480.1 .
    AF220027 mRNA. Translation: AAG53481.1 .
    AF220028 mRNA. Translation: AAG53482.1 .
    AF220029 mRNA. Translation: AAG53483.1 .
    AY625000 mRNA. Translation: AAT48101.1 .
    DQ301444 Genomic DNA. Translation: ABC00997.1 .
    DQ301445 Genomic DNA. Translation: ABC00998.1 .
    DQ301446 Genomic DNA. Translation: ABC00999.1 .
    DQ301447 Genomic DNA. Translation: ABC01000.1 .
    DQ301448 Genomic DNA. Translation: ABC01001.1 .
    DQ301449 Genomic DNA. Translation: ABC01002.1 .
    DQ301450 Genomic DNA. Translation: ABC01003.1 .
    DQ301451 Genomic DNA. Translation: ABC01004.1 .
    DQ301452 Genomic DNA. Translation: ABC01005.1 .
    DQ301453 Genomic DNA. Translation: ABC01006.1 .
    DQ301454 Genomic DNA. Translation: ABC01007.1 .
    DQ301455 Genomic DNA. Translation: ABC01008.1 .
    DQ301456 Genomic DNA. Translation: ABC01009.1 .
    DQ301457 Genomic DNA. Translation: ABC01010.1 .
    DQ301458 Genomic DNA. Translation: ABC01011.1 .
    DQ301459 Genomic DNA. Translation: ABC01012.1 .
    DQ301460 Genomic DNA. Translation: ABC01013.1 .
    DQ301461 Genomic DNA. Translation: ABC01014.1 .
    DQ301462 Genomic DNA. Translation: ABC01015.1 .
    DQ301463 Genomic DNA. Translation: ABC01016.1 .
    DQ301464 Genomic DNA. Translation: ABC01017.1 .
    DQ301465 Genomic DNA. Translation: ABC01018.1 .
    DQ301466 Genomic DNA. Translation: ABC01019.1 .
    DQ301467 Genomic DNA. Translation: ABC01020.1 .
    DQ301468 Genomic DNA. Translation: ABC01021.1 .
    DQ301469 Genomic DNA. Translation: ABC01022.1 .
    DQ301470 Genomic DNA. Translation: ABC01023.1 .
    DQ301471 Genomic DNA. Translation: ABC01024.1 .
    DQ301472 Genomic DNA. Translation: ABC01025.1 .
    DQ301473 Genomic DNA. Translation: ABC01026.1 .
    DQ301474 Genomic DNA. Translation: ABC01027.1 .
    DQ301475 Genomic DNA. Translation: ABC01028.1 .
    DQ301476 Genomic DNA. Translation: ABC01029.1 .
    DQ301477 Genomic DNA. Translation: ABC01030.1 .
    DQ301478 Genomic DNA. Translation: ABC01031.1 .
    DQ301479 Genomic DNA. Translation: ABC01032.1 .
    DQ301480 Genomic DNA. Translation: ABC01033.1 .
    DQ288685 mRNA. Translation: ABB90543.1 .
    JF928461 mRNA. Translation: AEN14475.1 .
    JF928462 mRNA. Translation: AEN14476.1 .
    AK027593 mRNA. Translation: BAB55218.1 .
    AC015691 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68771.1 .
    CH471064 Genomic DNA. Translation: EAW68772.1 .
    CH471064 Genomic DNA. Translation: EAW68774.1 .
    CH471064 Genomic DNA. Translation: EAW68775.1 .
    EU260465 Genomic DNA. Translation: ABW96352.1 .
    CH471064 Genomic DNA. Translation: EAW68776.1 .
    CH471064 Genomic DNA. Translation: EAW68777.1 .
    BC021258 mRNA. Translation: AAH21258.1 .
    CCDSi CCDS31392.1. [Q9C035-4 ]
    CCDS31393.1. [Q9C035-1 ]
    CCDS31394.1. [Q9C035-3 ]
    RefSeqi NP_149023.2. NM_033034.2. [Q9C035-1 ]
    NP_149083.2. NM_033092.2. [Q9C035-3 ]
    NP_149084.2. NM_033093.2. [Q9C035-4 ]
    XP_005253240.1. XM_005253183.1. [Q9C035-1 ]
    XP_005253241.1. XM_005253184.1. [Q9C035-4 ]
    UniGenei Hs.125300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ECV NMR - A 1-78 [» ]
    2YRG NMR - A 86-129 [» ]
    ProteinModelPortali Q9C035.
    SMRi Q9C035. Positions 5-78, 87-131, 255-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124491. 45 interactions.
    IntActi Q9C035. 18 interactions.
    MINTi MINT-6631391.

    PTM databases

    PhosphoSitei Q9C035.

    Polymorphism databases

    DMDMi 38605459.

    Proteomic databases

    MaxQBi Q9C035.
    PaxDbi Q9C035.
    PRIDEi Q9C035.

    Protocols and materials databases

    DNASUi 85363.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380027 ; ENSP00000369366 ; ENSG00000132256 . [Q9C035-4 ]
    ENST00000380034 ; ENSP00000369373 ; ENSG00000132256 . [Q9C035-1 ]
    ENST00000396847 ; ENSP00000380058 ; ENSG00000132256 . [Q9C035-3 ]
    ENST00000433961 ; ENSP00000393052 ; ENSG00000132256 . [Q9C035-5 ]
    GeneIDi 85363.
    KEGGi hsa:85363.
    UCSCi uc001mbm.2. human. [Q9C035-1 ]
    uc001mbn.3. human. [Q9C035-4 ]
    uc001mbp.3. human. [Q9C035-3 ]
    uc021qcx.1. human. [Q9C035-6 ]

    Organism-specific databases

    CTDi 85363.
    GeneCardsi GC11M005641.
    H-InvDB HIX0009393.
    HGNCi HGNC:16276. TRIM5.
    HPAi CAB013497.
    HPA023420.
    HPA023422.
    MIMi 608487. gene.
    neXtProti NX_Q9C035.
    PharmGKBi PA38109.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253216.
    HOVERGENi HBG001357.
    KOi K10648.
    OMAi SKTHITY.
    OrthoDBi EOG7RJPR6.
    PhylomeDBi Q9C035.
    TreeFami TF338674.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi TRIM5. human.
    EvolutionaryTracei Q9C035.
    GeneWikii TRIM5alpha.
    GenomeRNAii 85363.
    NextBioi 75883.
    PROi Q9C035.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9C035.
    Bgeei Q9C035.
    Genevestigatori Q9C035.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR003879. Butyrophylin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR003877. SPRY_rcpt.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00336. BBOX. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA; DELTA AND EPSILON), VARIANT GLN-136.
    2. "Trim5alpha protein restricts both HIV-1 and murine leukemia virus."
      Yap M.W., Nisole S., Lynch C., Stoye J.P.
      Proc. Natl. Acad. Sci. U.S.A. 101:10786-10791(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    3. "High-frequency persistence of an impaired allele of the retroviral defense gene TRIM5alpha in humans."
      Sawyer S.L., Wu L.I., Akey J.M., Emerman M., Malik H.S.
      Curr. Biol. 16:95-100(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA), VARIANTS TYR-43 AND ASP-249.
    4. "Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential role."
      Yamauchi K., Wada K., Tanji K., Tanaka M., Kamitani T.
      FEBS J. 275:1540-1555(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136, FUNCTION, AUTOUBIQUITINATION, UBIQUITINATION BY TRIM21, MUTAGENESIS OF CYS-15.
      Tissue: Brain.
    5. "Modulation of TRIM5alpha activity in human cells by alternatively spliced TRIM5 isoforms."
      Battivelli E., Migraine J., Lecossier D., Matsuoka S., Perez-Bercoff D., Saragosti S., Clavel F., Hance A.J.
      J. Virol. 85:7828-7835(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON), ALTERNATIVE SPLICING, FUNCTION.
    6. "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] (ISOFORM ALPHA), VARIANT GLN-136.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. NIEHS SNPs program
      Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-31; TYR-43; TYR-58; GLU-110; PHE-112; GLN-136; ASP-249; TYR-419; SER-467 AND LEU-479.
    10. "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 GAMMA).
      Tissue: Rhabdomyosarcoma.
    11. "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta."
      Xu L., Yang L., Moitra P.K., Hashimoto K., Rallabhandi P., Kaul S., Meroni G., Jensen J.P., Weissman A.M., D'Arpa P.
      Exp. Cell Res. 288:84-93(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BTBD1 AND BTBD2.
    12. "Retroviral restriction factors Fv1 and TRIM5alpha act independently and can compete for incoming virus before reverse transcription."
      Passerini L.D., Keckesova Z., Towers G.J.
      J. Virol. 80:2100-2105(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM ALPHA).
    13. "Removal of arginine 332 allows human TRIM5alpha to bind human immunodeficiency virus capsids and to restrict infection."
      Li Y., Li X., Stremlau M., Lee M., Sodroski J.
      J. Virol. 80:6738-6744(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-332.
    14. "Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha restriction of HIV-1."
      Stremlau M., Song B., Javanbakht H., Perron M., Sodroski J.
      Virology 351:112-120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM ALPHA).
    15. "Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection."
      Luban J.
      J. Virol. 81:1054-1061(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
      Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
      J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPA1A/B.
    17. "p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha."
      O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J., Campbell E.M.
      J. Virol. 84:5997-6006(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
    18. "Recent insights into the mechanism and consequences of TRIM5alpha retroviral restriction."
      Sastri J., Campbell E.M.
      AIDS Res. Hum. Retroviruses 27:231-238(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, PROTEASOMAL DEGRADATION.
    19. Cited for: REVIEW.
    20. "Immunology: TRIM5 does double duty."
      Aiken C., Joyce S.
      Nature 472:305-306(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    21. Cited for: FUNCTION, INTERACTION WITH MAP3K7/TAK1; TAB2 AND TAB3.
    22. "Antiviral immunity: TRIM5 moonlights as a pattern recognition receptor."
      Jermy A.
      Nat. Rev. Microbiol. 9:398-398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    23. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
      Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
      Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMC2.
    24. "Human Trim5alpha has additional activities that are uncoupled from retroviral capsid recognition."
      Tareen S.U., Emerman M.
      Virology 409:113-120(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "TRIM5 acts as more than a retroviral restriction factor."
      de Silva S., Wu L.
      Viruses 3:1204-1209(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    26. "TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling."
      Gruetter M.G., Luban J.
      Curr. Opin. Virol. 2:142-150(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    27. "TRIM5alpha and species tropism of HIV/SIV."
      Nakayama E.E., Shioda T.
      Front. Microbiol. 3:13-13(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, FUNCTION.
    28. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    29. "Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by TRIM5alpha(rh): structure of the RING domain of TRIM5alpha."
      Lienlaf M., Hayashi F., Di Nunzio F., Tochio N., Kigawa T., Yokoyama S., Diaz-Griffero F.
      J. Virol. 85:8725-8737(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-78.
    30. "Solution structure of the b-box domain from tripartite motif-containing protein 5."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 86-129.

    Entry informationi

    Entry nameiTRIM5_HUMAN
    AccessioniPrimary (citable) accession number: Q9C035
    Secondary accession number(s): A6NGQ1
    , A8WFA8, D3DQS8, D3DQS9, G3GJY1, Q2MLV4, Q2MLV8, Q2MLV9, Q2MLW1, Q2MLW3, Q2MLW4, Q2MLW6, Q2MLW7, Q2MLX1, Q2MLX2, Q2MLX3, Q2MLX5, Q2MLY3, Q2MLY4, Q2V6Q6, Q6GX26, Q8WU46, Q96SR5, Q9C031, Q9C032, Q9C033, Q9C034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 138 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 11
      Human chromosome 11: 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