TRIM5
entrez
85363
canonical
uniprot
Q9C035
canonical
ensembl
ENSG00000132256
resolver
ensp
ENSP00000369366
resolver
ensp
ENSP00000369373
resolver
ensp
ENSP00000380058
resolver
ensp
ENSP00000506742
resolver
ensp
ENSP00000507420
resolver
ensp
ENSP00000655490
resolver
ensp
ENSP00000655491
resolver
ensp
ENSP00000655492
resolver
ensp
ENSP00000704692
resolver
enst
ENST00000682968
resolver
genesymbol
TRIM5
resolver
genesymbol_syn
RNF88
resolver
hgnc
HGNC:16276
resolver
uniprot
A0A804HHS7
resolver
uniprot
A6NGQ1
resolver
uniprot
A8WFA8
resolver
uniprot
D3DQS8
resolver
uniprot
D3DQS9
resolver
uniprot
G3GJY1
resolver
uniprot
Q2MLV4
resolver
uniprot
Q2MLV8
resolver
uniprot
Q2MLV9
resolver
uniprot
Q2MLW1
resolver
uniprot
Q2MLW3
resolver
uniprot
Q2MLW4
resolver
uniprot
Q2MLW6
resolver
uniprot
Q2MLW7
resolver
uniprot
Q2MLX1
resolver
uniprot
Q2MLX2
resolver
uniprot
Q2MLX3
resolver
uniprot
Q2MLX5
resolver
uniprot
Q2MLY3
resolver
uniprot
Q2MLY4
resolver
uniprot
Q2V6Q6
resolver
uniprot
Q6GX26
resolver
uniprot
Q8WU46
resolver
uniprot
Q96SR5
resolver
uniprot
Q9C031
resolver
uniprot
Q9C032
resolver
uniprot
Q9C033
resolver
uniprot
Q9C034
resolver
uniprot_entry
A0A804HHS7_HUMAN
resolver
uniprot_entry
TRIM5_HUMAN
resolver
uniprot_sec
A6NGQ1
resolver
uniprot_sec
A8WFA8
resolver
uniprot_sec
D3DQS8
resolver
uniprot_sec
D3DQS9
resolver
uniprot_sec
G3GJY1
resolver
uniprot_sec
Q2MLV4
resolver
uniprot_sec
Q2MLV8
resolver
uniprot_sec
Q2MLV9
resolver
uniprot_sec
Q2MLW1
resolver
uniprot_sec
Q2MLW3
resolver
uniprot_sec
Q2MLW4
resolver
uniprot_sec
Q2MLW6
resolver
uniprot_sec
Q2MLW7
resolver
uniprot_sec
Q2MLX1
resolver
uniprot_sec
Q2MLX2
resolver
uniprot_sec
Q2MLX3
resolver
uniprot_sec
Q2MLX5
resolver
uniprot_sec
Q2MLY3
resolver
uniprot_sec
Q2MLY4
resolver
uniprot_sec
Q2V6Q6
resolver
uniprot_sec
Q6GX26
resolver
uniprot_sec
Q8WU46
resolver
uniprot_sec
Q96SR5
resolver
uniprot_sec
Q9C031
resolver
uniprot_sec
Q9C032
resolver
uniprot_sec
Q9C033
resolver
uniprot_sec
Q9C034
resolver
amino_acid_sequence
MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: 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), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057). {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:18312418, ECO:0000269|PubMed:21035162, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21632761, ECO:0000269|PubMed:22291694, ECO:0000269|PubMed:25127057}.
uniprot
proteins
mass_dalton
56338
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="C->A: Abolishes E3 ligase activity."; /evidence="ECO:0000269|PubMed:18312418"; MUTAGEN 332; /note="R->A,G,H,P,Q,S: Increases strongly cell restriction against HIV-1 and SIVmac infection."; /evidence="ECO:0000269|PubMed:16809279"; MUTAGEN 332; /note="R->D,E,L: Increases strongly cell restriction against HIV-1 infection."; /evidence="ECO:0000269|PubMed:16809279"; MUTAGEN 332; /note="R->K: No effect on HIV-1 and SIVmac infection."; /evidence="ECO:0000269|PubMed:16809279
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Degraded in a proteasome-independent fashion in the absence of viral infection but in a proteasome-dependent fashion following exposure to restriction sensitive virus.; PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation. {ECO:0000269|PubMed:18312418}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
11331580
uniprot
proteins
pubmed
12878161
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15249690
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16401428
uniprot
proteins
pubmed
16474118
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16643975
uniprot
proteins
pubmed
16809279
uniprot
proteins
pubmed
16956947
uniprot
proteins
pubmed
17156811
uniprot
proteins
pubmed
18312418
uniprot
proteins
pubmed
20053985
uniprot
proteins
pubmed
20357094
uniprot
proteins
pubmed
21035162
uniprot
proteins
pubmed
21247355
uniprot
proteins
pubmed
21512569
uniprot
proteins
pubmed
21512573
uniprot
proteins
pubmed
21572451
uniprot
proteins
pubmed
21575904
uniprot
proteins
pubmed
21632761
uniprot
proteins
pubmed
21680743
uniprot
proteins
pubmed
21734049
uniprot
proteins
pubmed
21866272
uniprot
proteins
pubmed
22078707
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22291694
uniprot
proteins
pubmed
22482711
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25127057
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25127057}. Nucleus {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in cytoplasmic bodies (PubMed:12878161, PubMed:20357094). Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27 (By similarity). In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1 (By similarity). {ECO:0000250|UniProtKB:Q0PF16, ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:25127057}.
uniprot
proteins