SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9C035

- TRIM5_HUMAN

UniProt

Q9C035 - TRIM5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tripartite motif-containing protein 5

Gene
TRIM5, RNF88
Organism
Homo sapiens (Human)
Status
Reviewed - 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) and equine infectious anemia virus (EIAV).8 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5945RING-typeAdd
BLAST
Zinc fingeri90 – 13243B box-typeAdd
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
Complete GO annotation...

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

GO - Cellular componenti

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

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.

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 TAB3.5 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.

Miscellaneous databases

EvolutionaryTraceiQ9C035.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini281 – 493213B30.2/SPRYAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili130 – 241112 Reviewed predictionAdd
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 (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.
Contains 1 B30.2/SPRY domain.

Zinc finger

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

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. VSP_009016Add
BLAST
Alternative sequencei249 – 2579GVDGVIKRT → VKSGKKPEH in isoform Iota. VSP_044095
Alternative sequencei258 – 493236Missing in isoform Iota. VSP_044096Add
BLAST
Alternative sequencei272 – 493222Missing in isoform Epsilon. VSP_009017Add
BLAST
Alternative sequencei299 – 34749VDVTV…NYCTG → GKEKSHYHKPPCGLSLLLSL SFRILCSLLGSCFKIYDSPS KTHITYPSL in isoform Gamma. VSP_009012Add
BLAST
Alternative sequencei299 – 32628VDVTV…SPKPQ → GWSAMARSRFTATSTSQIQA ILLPQPPK in isoform Delta. VSP_009014Add
BLAST
Alternative sequencei327 – 493167Missing in isoform Delta. VSP_009015Add
BLAST
Alternative sequencei348 – 493146Missing in isoform Gamma. VSP_009013Add
BLAST
Alternative sequencei390 – 40011NENYQPKYGYW → KRFMILLPRHT in isoform Beta. VSP_009010Add
BLAST
Alternative sequencei401 – 49393Missing in isoform Beta. VSP_009011Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761I → L in BAB55218. 1 Publication
Sequence conflicti130 – 1301L → P in BAB55218. 1 Publication

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]
ENST00000396855; ENSP00000380064; ENSG00000132256. [Q9C035-4]
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 ]
ENST00000396855 ; ENSP00000380064 ; ENSG00000132256 . [Q9C035-4 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 137 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

Similar proteinsi