Q9C035 (TRIM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tripartite motif-containing protein 5
EC=6.3.2.-

Alternative name(s):
RING finger protein 88

Gene names

Name:	TRIM5
Synonyms:	RNF88

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › P-body. Note: Closely associates with proteasomal subunits in cytoplasmic bodies By similarity. Co-localizes 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 process	Antiviral defense Host-virus interaction Immunity Innate immunity Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Traceable author statement Ref.21Ref.27. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of I-kappaB kinase/NF-kappaB cascade 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi 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_function	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
itself		2	EBI-924214,EBI-924214
	Q2Y080	3	EBI-924230,EBI-924086	From a different organism.
TRIM32	Q13049	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 493

493

Tripartite motif-containing protein 5

PRO_0000056201

Regions

Domain

281 – 493

213

B30.2/SPRY

Zinc finger

15 – 59

45

RING-type

Zinc finger

90 – 132

43

B box-type

Coiled coil

130 – 241

112

Potential

Natural variations

Alternative sequence

249 – 271

23

GVDGV…TFPKN → DGERDLEEARNFSKKSKESV SSS in isoform Epsilon.

VSP_009016

Alternative sequence

249 – 257

9

GVDGVIKRT → VKSGKKPEH in isoform Iota.

VSP_044095

Alternative sequence

258 – 493

236

Missing in isoform Iota.

VSP_044096

Alternative sequence

272 – 493

222

Missing in isoform Epsilon.

VSP_009017

Alternative sequence

299 – 347

49

VDVTV…NYCTG → GKEKSHYHKPPCGLSLLLSL SFRILCSLLGSCFKIYDSPS KTHITYPSL in isoform Gamma.

VSP_009012

Alternative sequence

299 – 326

28

VDVTV…SPKPQ → GWSAMARSRFTATSTSQIQA ILLPQPPK in isoform Delta.

VSP_009014

Alternative sequence

327 – 493

167

Missing in isoform Delta.

VSP_009015

Alternative sequence

348 – 493

146

Missing in isoform Gamma.

VSP_009013

Alternative sequence

390 – 400

11

NENYQPKYGYW → KRFMILLPRHT in isoform Beta.

VSP_009010

Alternative sequence

401 – 493

93

Missing in isoform Beta.

VSP_009011

Natural variant

31

1

G → S. Ref.9

VAR_060707

Natural variant

43

1

H → Y. Ref.3 Ref.9
Corresponds to variant rs3740996 [ dbSNP | Ensembl ].

VAR_017397

Natural variant

58

1

C → Y. Ref.9

VAR_060708

Natural variant

110

1

G → E. Ref.9

VAR_060709

Natural variant

112

1

V → F. Ref.9
Corresponds to variant rs11601507 [ dbSNP | Ensembl ].

VAR_030154

Natural variant

136

1

R → Q. Ref.1 Ref.4 Ref.6 Ref.9
Corresponds to variant rs10838525 [ dbSNP | Ensembl ].

VAR_017398

Natural variant

249

1

G → D. Ref.3 Ref.9
Corresponds to variant rs11038628 [ dbSNP | Ensembl ].

VAR_030155

Natural variant

419

1

H → Y. Ref.9
Corresponds to variant rs28381981 [ dbSNP | Ensembl ].

VAR_030156

Natural variant

467

1

C → S. Ref.9

VAR_060710

Natural variant

479

1

P → L. Ref.9
Corresponds to variant rs7104422 [ dbSNP | Ensembl ].

VAR_030157

Experimental info

Mutagenesis

15

1

C → A: Abolishes E3 ligase activity. Ref.4

Mutagenesis

332

1

R → A, G, H, P, Q or S: Increases strongly cell restriction against HIV-1 and SIVmac infection. Ref.13

Mutagenesis

332

1

R → D, E or L: Increases strongly cell restriction against HIV-1 infection. Ref.13

Mutagenesis

332

1

R → K: No effect on HIV-1 and SIVmac infection. Ref.13

Sequence conflict

76

1

I → L in BAB55218. Ref.2

Sequence conflict

130

1

L → P in BAB55218. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

493

Helix Strand Turn

Details...

Turn

16 – 18

3

Beta strand

29 – 31

3

Helix

38 – 45

8

Turn

46 – 50

5

Turn

56 – 58

3

Beta strand

64 – 66

3

Beta strand

92 – 94

3

Turn

96 – 98

3

Beta strand

104 – 106

3

Turn

107 – 109

3

Beta strand

111 – 113

3

Helix

115 – 118

4

Turn

121 – 125

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8E61AAFD508AF6C0	FASTA	493	56,338
	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
	Isoform Beta [UniParc]. Checksum: E8AC7B014BF58488	FASTA	400	46,038
	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 WEVDVSKKTA WILGVCAGFQ PDAMCNIEKK RFMILLPRHT
	Isoform Gamma [UniParc]. Checksum: 07B838DB840C4F55	FASTA	347	40,108
	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 LTDVRRYWGK 310 320 330 340 EKSHYHKPPC GLSLLLSLSF RILCSLLGSC FKIYDSPSKT HITYPSL
	Isoform Delta [UniParc]. Checksum: AB54B894549C8775	FASTA	326	37,685
	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 LTDVRRYWGW 310 320 SAMARSRFTA TSTSQIQAIL LPQPPK
	Isoform Epsilon (Kappa) [UniParc]. Checksum: C988390B71D2B74F	FASTA	271	31,253
	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 GSVMELLQDG ERDLEEARNF SKKSKESVSS S
	Isoform Iota [UniParc]. Checksum: 8769CFD2E659BEF5	FASTA	257	29,677
	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 GSVMELLQVK SGKKPEH

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[29]	"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

NIEHS-SNPs

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.

IPI

IPI00394972.
IPI00394973.
IPI00394974.
IPI00394975.
IPI00873422.

RefSeq

NP_149023.2. NM_033034.2.
NP_149083.2. NM_033092.2.
NP_149084.2. NM_033093.2.

UniGene

Hs.125300.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ECV	NMR	-	A	1-78	[»]
2YRG	NMR	-	A	86-129	[»]

ProteinModelPortal

Q9C035.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9C035. 18 interactions.

PTM databases

PhosphoSite

Q9C035.

Polymorphism databases

DMDM

38605459.

Proteomic databases

PaxDb

Q9C035.

PRIDE

Q9C035.

Protocols and materials databases

DNASU

85363.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380027; ENSP00000369366; ENSG00000132256.
ENST00000380034; ENSP00000369373; ENSG00000132256.
ENST00000396847; ENSP00000380058; ENSG00000132256.
ENST00000396855; ENSP00000380064; ENSG00000132256.
ENST00000433961; ENSP00000393052; ENSG00000132256.

GeneID

85363.

KEGG

hsa:85363.

UCSC

uc001mbm.2. human.
uc001mbn.3. human.
uc001mbp.3. human.

Organism-specific databases

CTD

85363.

GeneCards

GC11M005641.

H-InvDB

HIX0009393.

HGNC

HGNC:16276. TRIM5.

HPA

CAB013497.
HPA023420.
HPA023422.

MIM

608487. gene.

neXtProt

NX_Q9C035.

PharmGKB

PA38109.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253216.

HOVERGEN

HBG001357.

KO

K10648.

OMA

WILGVCA.

OrthoDB

EOG4229JJ.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9C035.

Bgee

Q9C035.

Genevestigator

Q9C035.

GermOnline

ENSG00000132256. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

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]

Pfam

PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]

PRINTS

PR01407. BUTYPHLNCDUF.

SMART

SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TRIM5. human.

EvolutionaryTrace

Q9C035.

GenomeRNAi

85363.

NextBio

75883.

SOURCE

Search...

Entry information

Entry name

TRIM5_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.