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Q9C035 (TRIM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tripartite motif-containing protein 5

EC=6.3.2.-
Alternative name(s):
RING finger protein 88
Gene names
Name:TRIM5
Synonyms:RNF88
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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) and equine infectious anemia virus (EIAV). Ref.4 Ref.5 Ref.11 Ref.12 Ref.14 Ref.21 Ref.24 Ref.27

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.11 Ref.16 Ref.17 Ref.21 Ref.23

Subcellular location

CytoplasmP-body. Note: Closely associates with proteasomal subunits in cytoplasmic bodies By similarity. Colocalizes with SQSTM1 in cytoplasmic bodies. Ref.11 Ref.17

Domain

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 (Ref.26).

The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (Ref.26).

The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization (Ref.26).

Post-translational modification

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.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 1 B30.2/SPRY domain.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Traceable author statement Ref.21Ref.27. Source: UniProtKB

innate immune response

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of viral entry into host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of viral release from host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.21. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.21. Source: UniProtKB

protein trimerization

Inferred from direct assay PubMed 17156811. Source: UniProtKB

regulation of lipopolysaccharide-mediated signaling pathway

Inferred from mutant phenotype Ref.21. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasmic mRNA processing body

Inferred from direct assay Ref.17Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionsignaling pattern recognition receptor activity

Inferred from direct assay Ref.21. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.21. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-924214,EBI-924214
Q2Y0803EBI-924230,EBI-924086From a different organism.
TRIM32Q130492EBI-924214,EBI-742790

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q9C035-1)

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.
Isoform Beta (identifier: Q9C035-2)

The sequence of this isoform differs from the canonical sequence as follows:
     390-400: NENYQPKYGYW → KRFMILLPRHT
     401-493: Missing.
Note: Probable artifact.
Isoform Gamma (identifier: Q9C035-3)

The sequence of this isoform differs from the canonical sequence as follows:
     299-347: VDVTVAPNNI...TFVNFNYCTG → GKEKSHYHKP...SKTHITYPSL
     348-493: Missing.
Isoform Delta (identifier: Q9C035-4)

The sequence of this isoform differs from the canonical sequence as follows:
     299-326: VDVTVAPNNISCAVISEDKRQVSSPKPQ → GWSAMARSRFTATSTSQIQAILLPQPPK
     327-493: Missing.
Isoform Epsilon (identifier: Q9C035-5)

Also known as: Kappa;

The sequence of this isoform differs from the canonical sequence as follows:
     249-271: GVDGVIKRTENVTLKKPETFPKN → DGERDLEEARNFSKKSKESVSSS
     272-493: Missing.
Isoform Iota (identifier: Q9C035-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 493492Tripartite motif-containing protein 5
PRO_0000056201

Regions

Domain281 – 493213B30.2/SPRY
Zinc finger15 – 5945RING-type
Zinc finger90 – 13243B box-type
Coiled coil130 – 241112 Potential

Amino acid modifications

Modified residue21N-acetylalanine

Natural variations

Alternative sequence249 – 27123GVDGV…TFPKN → DGERDLEEARNFSKKSKESV SSS in isoform Epsilon.
VSP_009016
Alternative sequence249 – 2579GVDGVIKRT → VKSGKKPEH in isoform Iota.
VSP_044095
Alternative sequence258 – 493236Missing in isoform Iota.
VSP_044096
Alternative sequence272 – 493222Missing in isoform Epsilon.
VSP_009017
Alternative sequence299 – 34749VDVTV…NYCTG → GKEKSHYHKPPCGLSLLLSL SFRILCSLLGSCFKIYDSPS KTHITYPSL in isoform Gamma.
VSP_009012
Alternative sequence299 – 32628VDVTV…SPKPQ → GWSAMARSRFTATSTSQIQA ILLPQPPK in isoform Delta.
VSP_009014
Alternative sequence327 – 493167Missing in isoform Delta.
VSP_009015
Alternative sequence348 – 493146Missing in isoform Gamma.
VSP_009013
Alternative sequence390 – 40011NENYQPKYGYW → KRFMILLPRHT in isoform Beta.
VSP_009010
Alternative sequence401 – 49393Missing in isoform Beta.
VSP_009011
Natural variant311G → S. Ref.9
Corresponds to variant rs59896509 [ dbSNP | Ensembl ].
VAR_060707
Natural variant431H → Y. Ref.3 Ref.9
Corresponds to variant rs3740996 [ dbSNP | Ensembl ].
VAR_017397
Natural variant581C → Y. Ref.9
Corresponds to variant rs61432120 [ dbSNP | Ensembl ].
VAR_060708
Natural variant1101G → E. Ref.9
Corresponds to variant rs56348930 [ dbSNP | Ensembl ].
VAR_060709
Natural variant1121V → F. Ref.9
Corresponds to variant rs11601507 [ dbSNP | Ensembl ].
VAR_030154
Natural variant1361R → Q. Ref.1 Ref.4 Ref.6 Ref.9
Corresponds to variant rs10838525 [ dbSNP | Ensembl ].
VAR_017398
Natural variant2491G → D. Ref.3 Ref.9
Corresponds to variant rs11038628 [ dbSNP | Ensembl ].
VAR_030155
Natural variant4191H → Y. Ref.9
Corresponds to variant rs28381981 [ dbSNP | Ensembl ].
VAR_030156
Natural variant4671C → S. Ref.9
Corresponds to variant rs59218593 [ dbSNP | Ensembl ].
VAR_060710
Natural variant4791P → L. Ref.9
Corresponds to variant rs7104422 [ dbSNP | Ensembl ].
VAR_030157

Experimental info

Mutagenesis151C → A: Abolishes E3 ligase activity. Ref.4
Mutagenesis3321R → A, G, H, P, Q or S: Increases strongly cell restriction against HIV-1 and SIVmac infection. Ref.13
Mutagenesis3321R → D, E or L: Increases strongly cell restriction against HIV-1 infection. Ref.13
Mutagenesis3321R → K: No effect on HIV-1 and SIVmac infection. Ref.13
Sequence conflict761I → L in BAB55218. Ref.2
Sequence conflict1301L → P in BAB55218. Ref.2

Secondary structure

......................... 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8E61AAFD508AF6C0

FASTA49356,338
        10         20         30         40         50         60 
MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK GESSCPVCRI 

        70         80         90        100        110        120 
SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE KLLLFCQEDG KVICWLCERS 

       130        140        150        160        170        180 
QEHRGHHTFL TEEVAREYQV KLQAALEMLR QKQQEAEELE ADIREEKASW KTQIQYDKTN 

       190        200        210        220        230        240 
VLADFEQLRD ILDWEESNEL QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ 

       250        260        270        280        290        300 
GSVMELLQGV DGVIKRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD 

       310        320        330        340        350        360 
VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG SQSITSGKHY 

       370        380        390        400        410        420 
WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW VIGLEEGVKC SAFQDSSFHT 

       430        440        450        460        470        480 
PSVPFIVPLS VIICPDRVGV FLDYEACTVS FFNITNHGFL IYKFSHCSFS QPVFPYLNPR 

       490 
KCGVPMTLCS PSS 

« Hide

Isoform Beta [UniParc].

Checksum: E8AC7B014BF58488
Show »

FASTA40046,038
Isoform Gamma [UniParc].

Checksum: 07B838DB840C4F55
Show »

FASTA34740,108
Isoform Delta [UniParc].

Checksum: AB54B894549C8775
Show »

FASTA32637,685
Isoform Epsilon (Kappa) [UniParc].

Checksum: C988390B71D2B74F
Show »

FASTA27131,253
Isoform Iota [UniParc].

Checksum: 8769CFD2E659BEF5
Show »

FASTA25729,677

References

« Hide 'large scale' references
[1]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Trim5 TAKes on pattern recognition."
Tareen S.U., Emerman M.
Cell Host Microbe 9:349-350(2011) [PubMed] [Europe PMC] [Abstract]
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]"TRIM5 is an innate immune sensor for the retrovirus capsid lattice."
Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J., Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.
Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_149023.2. NM_033034.2.
NP_149083.2. NM_033092.2.
NP_149084.2. NM_033093.2.
XP_005253240.1. XM_005253183.1.
XP_005253241.1. XM_005253184.1.
XP_005253242.1. XM_005253185.1.
UniGeneHs.125300.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ECVNMR-A1-78[»]
2YRGNMR-A86-129[»]
ProteinModelPortalQ9C035.
SMRQ9C035. Positions 5-131, 255-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124491. 45 interactions.
IntActQ9C035. 18 interactions.
MINTMINT-6631391.

PTM databases

PhosphoSiteQ9C035.

Polymorphism databases

DMDM38605459.

Proteomic databases

PaxDbQ9C035.
PRIDEQ9C035.

Protocols and materials databases

DNASU85363.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380027; ENSP00000369366; ENSG00000132256. [Q9C035-4]
ENST00000380034; ENSP00000369373; ENSG00000132256. [Q9C035-1]
ENST00000396847; ENSP00000380058; ENSG00000132256. [Q9C035-3]
ENST00000396855; ENSP00000380064; ENSG00000132256. [Q9C035-4]
ENST00000433961; ENSP00000393052; ENSG00000132256. [Q9C035-5]
GeneID85363.
KEGGhsa:85363.
UCSCuc001mbm.2. human. [Q9C035-1]
uc001mbn.3. human. [Q9C035-4]
uc001mbp.3. human. [Q9C035-3]
uc021qcx.1. human. [Q9C035-6]

Organism-specific databases

CTD85363.
GeneCardsGC11M005641.
H-InvDBHIX0009393.
HGNCHGNC:16276. TRIM5.
HPACAB013497.
HPA023420.
HPA023422.
MIM608487. gene.
neXtProtNX_Q9C035.
PharmGKBPA38109.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253216.
HOVERGENHBG001357.
KOK10648.
OrthoDBEOG7RJPR6.
TreeFamTF338674.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9C035.
BgeeQ9C035.
GenevestigatorQ9C035.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. 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]
PfamPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM5. human.
EvolutionaryTraceQ9C035.
GeneWikiTRIM5alpha.
GenomeRNAi85363.
NextBio75883.
PROQ9C035.
SOURCESearch...

Entry information

Entry nameTRIM5_HUMAN
AccessionPrimary (citable) accession number: Q9C035
Secondary accession number(s): A6NGQ1 expand/collapse secondary AC list , 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 history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM