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Protein

Tripartite motif-containing protein 5

Gene

TRIM5

Organism
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2.By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 60RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri92 – 133B box-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processAntiviral defense, Autophagy, Immunity, Innate immunity, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 5 (EC:2.3.2.27)
Alternative name(s):
RING-type E3 ubiquitin transferase TRIM5Curated
TRIM5alpha
Gene namesi
Name:TRIM5
OrganismiChlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Taxonomic identifieri9534 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeChlorocebus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002734532 – 515Tripartite motif-containing protein 5Add BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei87PhosphoserineBy similarity1

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.By similarity
Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ587N7

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. Interacts with BTBD1 and BTBD2. Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70. Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with PSMC2, MAP3K7/TAK1, TAB2 and TAB3. Interacts with SQSTM1. Interacts with TRIM6 and TRIM34. Interacts with ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3C and BECN1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ587N7
SMRiQ587N7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini283 – 515B30.2/SPRYPROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 200Required for interaction with GABARAP and for autophagyBy similarityAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili137 – 225Sequence analysisAdd BLAST89

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. The coiled coil domain is important for higher order multimerization by promoting the initial dimerization.By similarity
The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (By similarity).By similarity
The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization.By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 60RING-typePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri92 – 133B box-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

HOVERGENiHBG001357

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR003879 Butyrophylin_SPRY
IPR013320 ConA-like_dom_sf
IPR003877 SPRY_dom
IPR032917 TRIM5
IPR027370 Znf-RING_LisH
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR24103:SF426 PTHR24103:SF426, 2 hits
PfamiView protein in Pfam
PF00622 SPRY, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR01407 BUTYPHLNCDUF
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit
SM00449 SPRY, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS50119 ZF_BBOX, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q587N7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGILLNVK EEVTCPICLE LLTEPLSLPC GHSFCQACIT ANHKESMLYK
60 70 80 90 100
EEERSCPVCR ISYQPENIQP NRHVANIVEK LREVKLSPEE GQKVDHCARH
110 120 130 140 150
GEKLLLFCQE DSKVICWLCE RSQEHRGHHT FLMEEVAQEY HVKLQTALEM
160 170 180 190 200
LRQKQQEAEK LEADIREEKA SWKIQIDYDK TNVSADFEQL REILDWEESN
210 220 230 240 250
ELQNLEKEEE DILKSLTKSE TEMVQQTQYM RELISDLEHR LQGSMMELLQ
260 270 280 290 300
GVDGIIKRVE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RELTDVRRYW
310 320 330 340 350
VDVTLAPNNI SHAVIAEDKR QVSYQNPQIM YQAPGSSFGS LTNFNYCTGV
360 370 380 390 400
LGSQSITSRK LTNFNYCTGV LGSQSITSGK HYWEVDVSKK SAWILGVCAG
410 420 430 440 450
FQPDATYNIE QNENYQPKYG YWVIGLQEGD KYSVFQDSSS HTPFAPFIVP
460 470 480 490 500
LSVIICPDRV GVFVDYEACT VSFFNITNHG FLIYKFSQCS FSKPVFPYLN
510
PRKCTVPMTL CSPSS
Length:515
Mass (Da):59,262
Last modified:May 10, 2005 - v1
Checksum:i4C81FB3BB63ED581
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7L → V in AAT81167 (PubMed:15249685).Curated1
Sequence conflicti7L → V in AAT48103 (PubMed:15249690).Curated1
Sequence conflicti7L → V in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti259V → I in AAT81167 (PubMed:15249685).Curated1
Sequence conflicti259V → I in BAD93337 (PubMed:15994780).Curated1
Sequence conflicti259V → I in AAV91975 (PubMed:15689398).Curated1
Sequence conflicti325Q → R in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti333A → S in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti337S → L in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti337S → L in BAD93337 (PubMed:15994780).Curated1
Sequence conflicti345N → S in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti351L → P in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti351L → R in BAD93337 (PubMed:15994780).Curated1
Sequence conflicti359R → G in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti359R → G in BAD93337 (PubMed:15994780).Curated1
Sequence conflicti438S → G in AAT81167 (PubMed:15249685).Curated1
Sequence conflicti438S → G in AAT48104 (PubMed:15249690).Curated1
Sequence conflicti438S → G in BAD93337 (PubMed:15994780).Curated1
Sequence conflicti469C → R in AAT81167 (PubMed:15249685).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY669399 mRNA Translation: AAT81167.1
AY625002 mRNA Translation: AAT48103.1
AY625003 mRNA Translation: AAT48104.1
AB210050 mRNA Translation: BAD93337.1
AB210051 mRNA Translation: BAD93338.1
AY843504 Genomic DNA Translation: AAV91975.1

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

TRIM5alpha entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY669399 mRNA Translation: AAT81167.1
AY625002 mRNA Translation: AAT48103.1
AY625003 mRNA Translation: AAT48104.1
AB210050 mRNA Translation: BAD93337.1
AB210051 mRNA Translation: BAD93338.1
AY843504 Genomic DNA Translation: AAV91975.1

3D structure databases

ProteinModelPortaliQ587N7
SMRiQ587N7
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ587N7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG001357

Enzyme and pathway databases

UniPathwayi
UPA00143

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR003879 Butyrophylin_SPRY
IPR013320 ConA-like_dom_sf
IPR003877 SPRY_dom
IPR032917 TRIM5
IPR027370 Znf-RING_LisH
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR24103:SF426 PTHR24103:SF426, 2 hits
PfamiView protein in Pfam
PF00622 SPRY, 1 hit
PF00643 zf-B_box, 1 hit
PF13445 zf-RING_UBOX, 1 hit
PRINTSiPR01407 BUTYPHLNCDUF
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit
SM00449 SPRY, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS50119 ZF_BBOX, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTRIM5_CHLAE
AccessioniPrimary (citable) accession number: Q587N7
Secondary accession number(s): Q587N8
, Q5D7J3, Q6BC81, Q6GX23, Q6GX24
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: May 10, 2005
Last modified: November 7, 2018
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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