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Protein

Tripartite motif-containing protein 5

Gene

TRIM5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. 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).8 Publications

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 – 59RING-typePROSITE-ProRule annotationAdd BLAST45
Zinc fingeri90 – 132B box-typePROSITE-ProRule annotationAdd BLAST43

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • protein binding, bridging Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • signaling pattern recognition receptor activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of innate immune response Source: UniProtKB
  • autophagy Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of viral entry into host cell Source: UniProtKB
  • negative regulation of viral release from host cell Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein trimerization Source: UniProtKB
  • regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • regulation of protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

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

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-877300. Interferon gamma signaling.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16276. TRIM5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15C → A: Abolishes E3 ligase activity. 1 Publication1
Mutagenesisi332R → A, G, H, P, Q or S: Increases strongly cell restriction against HIV-1 and SIVmac infection. 1 Publication1
Mutagenesisi332R → D, E or L: Increases strongly cell restriction against HIV-1 infection. 1 Publication1
Mutagenesisi332R → K: No effect on HIV-1 and SIVmac infection. 1 Publication1

Organism-specific databases

DisGeNETi85363.
OpenTargetsiENSG00000132256.
PharmGKBiPA38109.

Polymorphism and mutation databases

BioMutaiTRIM5.
DMDMi38605459.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000562012 – 493Tripartite motif-containing protein 5Add BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei86PhosphoserineCombined sources1

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, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9C035.
MaxQBiQ9C035.
PaxDbiQ9C035.
PeptideAtlasiQ9C035.
PRIDEiQ9C035.

PTM databases

iPTMnetiQ9C035.
PhosphoSitePlusiQ9C035.

Expressioni

Gene expression databases

BgeeiENSG00000132256.
ExpressionAtlasiQ9C035. baseline and differential.
GenevisibleiQ9C035. HS.

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, MAP3K7/TAK1, TAB2 and TAB3 (PubMed:21512573, PubMed:22078707). Interacts with SQSTM1 (PubMed:20357094, PubMed:25127057). Interacts with TRIM6 and TRIM34 (PubMed:21680743, PubMed:17156811). Interacts with ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3C and BECN1 (PubMed:25127057).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-924214,EBI-924214
Q2Y0803EBI-924230,EBI-924086From a different organism.
SNAI1O958633EBI-924214,EBI-1045459
TRIM32Q130492EBI-924214,EBI-742790

GO - Molecular functioni

  • protein binding, bridging Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi124491. 53 interactors.
IntActiQ9C035. 21 interactors.
MINTiMINT-6631391.
STRINGi9606.ENSP00000369373.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni16 – 18Combined sources3
Beta strandi29 – 31Combined sources3
Helixi38 – 45Combined sources8
Turni46 – 50Combined sources5
Turni56 – 58Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi92 – 94Combined sources3
Turni96 – 98Combined sources3
Beta strandi104 – 106Combined sources3
Turni107 – 109Combined sources3
Beta strandi111 – 113Combined sources3
Helixi115 – 118Combined sources4
Turni121 – 125Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ECVNMR-A1-78[»]
2YRGNMR-A86-129[»]
ProteinModelPortaliQ9C035.
SMRiQ9C035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C035.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini281 – 493B30.2/SPRYPROSITE-ProRule annotationAdd BLAST213

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 198Required for interaction with GABARAP and for autophagyBy similarityAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili130 – 241Sequence analysisAdd BLAST112

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 (PubMed:22482711). The coiled coil domain is important for higher order multimerization by promoting the initial dimerization (By similarity).By similarity1 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)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 59RING-typePROSITE-ProRule annotationAdd BLAST45
Zinc fingeri90 – 132B box-typePROSITE-ProRule annotationAdd BLAST43

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITG7. Eukaryota.
ENOG410XWDC. LUCA.
GeneTreeiENSGT00760000118893.
HOVERGENiHBG001357.
InParanoidiQ9C035.
KOiK10648.
OMAiNENYQPK.
OrthoDBiEOG091G04O8.
PhylomeDBiQ9C035.
TreeFamiTF338674.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
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.
[Graphical view]
PANTHERiPTHR24103:SF396. PTHR24103:SF396. 1 hit.
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 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. AlignAdd to basket

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

        10         20         30         40         50
MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK
60 70 80 90 100
GESSCPVCRI SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE
110 120 130 140 150
KLLLFCQEDG KVICWLCERS QEHRGHHTFL TEEVAREYQV KLQAALEMLR
160 170 180 190 200
QKQQEAEELE ADIREEKASW KTQIQYDKTN VLADFEQLRD ILDWEESNEL
210 220 230 240 250
QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ GSVMELLQGV
260 270 280 290 300
DGVIKRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD
310 320 330 340 350
VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG
360 370 380 390 400
SQSITSGKHY WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW
410 420 430 440 450
VIGLEEGVKC SAFQDSSFHT PSVPFIVPLS VIICPDRVGV FLDYEACTVS
460 470 480 490
FFNITNHGFL IYKFSHCSFS QPVFPYLNPR KCGVPMTLCS PSS
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)DescriptionActionsGraphical viewLength
Sequence conflicti76I → L in BAB55218 (PubMed:15249690).Curated1
Sequence conflicti130L → P in BAB55218 (PubMed:15249690).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06070731G → S.1 PublicationCorresponds to variant rs59896509dbSNPEnsembl.1
Natural variantiVAR_01739743H → Y.2 PublicationsCorresponds to variant rs3740996dbSNPEnsembl.1
Natural variantiVAR_06070858C → Y.1 PublicationCorresponds to variant rs61432120dbSNPEnsembl.1
Natural variantiVAR_060709110G → E.1 PublicationCorresponds to variant rs56348930dbSNPEnsembl.1
Natural variantiVAR_030154112V → F.1 PublicationCorresponds to variant rs11601507dbSNPEnsembl.1
Natural variantiVAR_017398136R → Q.4 PublicationsCorresponds to variant rs10838525dbSNPEnsembl.1
Natural variantiVAR_030155249G → D.2 PublicationsCorresponds to variant rs11038628dbSNPEnsembl.1
Natural variantiVAR_030156419H → Y.1 PublicationCorresponds to variant rs28381981dbSNPEnsembl.1
Natural variantiVAR_060710467C → S.1 PublicationCorresponds to variant rs59218593dbSNPEnsembl.1
Natural variantiVAR_030157479P → L.1 PublicationCorresponds to variant rs7104422dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009016249 – 271GVDGV…TFPKN → DGERDLEEARNFSKKSKESV SSS in isoform Epsilon. 2 PublicationsAdd BLAST23
Alternative sequenceiVSP_044095249 – 257GVDGVIKRT → VKSGKKPEH in isoform Iota. Curated9
Alternative sequenceiVSP_044096258 – 493Missing in isoform Iota. CuratedAdd BLAST236
Alternative sequenceiVSP_009017272 – 493Missing in isoform Epsilon. 2 PublicationsAdd BLAST222
Alternative sequenceiVSP_009012299 – 347VDVTV…NYCTG → GKEKSHYHKPPCGLSLLLSL SFRILCSLLGSCFKIYDSPS KTHITYPSL in isoform Gamma. 2 PublicationsAdd BLAST49
Alternative sequenceiVSP_009014299 – 326VDVTV…SPKPQ → GWSAMARSRFTATSTSQIQA ILLPQPPK in isoform Delta. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_009015327 – 493Missing in isoform Delta. 1 PublicationAdd BLAST167
Alternative sequenceiVSP_009013348 – 493Missing in isoform Gamma. 2 PublicationsAdd BLAST146
Alternative sequenceiVSP_009010390 – 400NENYQPKYGYW → KRFMILLPRHT in isoform Beta. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_009011401 – 493Missing in isoform Beta. 1 PublicationAdd BLAST93

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005253183.2. [Q9C035-1]
XP_005253241.1. XM_005253184.2. [Q9C035-4]
XP_011518729.1. XM_011520427.1. [Q9C035-5]
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.3. human. [Q9C035-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005253183.2. [Q9C035-1]
XP_005253241.1. XM_005253184.2. [Q9C035-4]
XP_011518729.1. XM_011520427.1. [Q9C035-5]
UniGeneiHs.125300.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ECVNMR-A1-78[»]
2YRGNMR-A86-129[»]
ProteinModelPortaliQ9C035.
SMRiQ9C035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124491. 53 interactors.
IntActiQ9C035. 21 interactors.
MINTiMINT-6631391.
STRINGi9606.ENSP00000369373.

PTM databases

iPTMnetiQ9C035.
PhosphoSitePlusiQ9C035.

Polymorphism and mutation databases

BioMutaiTRIM5.
DMDMi38605459.

Proteomic databases

EPDiQ9C035.
MaxQBiQ9C035.
PaxDbiQ9C035.
PeptideAtlasiQ9C035.
PRIDEiQ9C035.

Protocols and materials databases

DNASUi85363.
Structural Biology KnowledgebaseSearch...

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.3. human. [Q9C035-1]

Organism-specific databases

CTDi85363.
DisGeNETi85363.
GeneCardsiTRIM5.
H-InvDBHIX0009393.
HGNCiHGNC:16276. TRIM5.
HPAiCAB013497.
HPA023420.
HPA023422.
MIMi608487. gene.
neXtProtiNX_Q9C035.
OpenTargetsiENSG00000132256.
PharmGKBiPA38109.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITG7. Eukaryota.
ENOG410XWDC. LUCA.
GeneTreeiENSGT00760000118893.
HOVERGENiHBG001357.
InParanoidiQ9C035.
KOiK10648.
OMAiNENYQPK.
OrthoDBiEOG091G04O8.
PhylomeDBiQ9C035.
TreeFamiTF338674.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiTRIM5. human.
EvolutionaryTraceiQ9C035.
GeneWikiiTRIM5alpha.
GenomeRNAii85363.
PROiQ9C035.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132256.
ExpressionAtlasiQ9C035. baseline and differential.
GenevisibleiQ9C035. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
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.
[Graphical view]
PANTHERiPTHR24103:SF396. PTHR24103:SF396. 1 hit.
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.