Reviewed, UniProtKB/Swiss-Prot Q9C035 (TRIM5_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Isoform Alpha is a retrovirus restriction factor, which mediates species-specific, early block to retrovirus infection. Targets retroviral capsid soon after entry into the cell, and prevents reverse transcription of the virus RNA genome. Isoform Alpha trimers may make multiple contacts with the hexameric lattice of CA proteins which constitute the surface of retrovirion core, and somehow inactivate the virus. Restricts efficiently infection by N-MLV, but not HIV-1. May have E3 ubiquitin-protein ligase activity. Ref.9 Ref.11 Ref.14
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Isoform Alpha forms homotrimers, and may interact with retroviral CA protein. Isoform Delta interacts with BTBD1 and BTBD2. Ref.9 Ref.10 Ref.13
Subcellular location	Cytoplasm › P-body. Note: Cytoplasmic bodies. Ref.9
Domain	The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme By similarity.
Post-translational modification	Ubiquitinates itself in a RING finger- and UBE2D2-dependent manner (in vitro).
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 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	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic mRNA processing body Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Ref.1 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q2Y080	1	EBI-924230,EBI-924086	From a different organism.
gag	P03332	1	EBI-924230,EBI-935477	From a different organism.
UBE2D2	P62837	1	EBI-924243,EBI-347677

Alternative products

This entry describes 5 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)

The sequence of this isoform differs from the canonical sequence as follows:
     249-271: GVDGVIKRTENVTLKKPETFPKN → DGERDLEEARNFSKKSKESVSSS
     272-493: Missing.

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

Amino acid modifications

Modified residue

86

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

249 – 271

23

GVDGV…TFPKN → DGERDLEEARNFSKKSKESV SSS in isoform Epsilon.

VSP_009016

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

43

1

H → Y: dbSNP rs3740996. Ref.3

VAR_017397

Natural variant

112

1

V → F: dbSNP rs11601507.

VAR_030154

Natural variant

136

1

R → Q: dbSNP rs10838525.

VAR_017398

Natural variant

249

1

G → D: dbSNP rs11038628. Ref.3

VAR_030155

Natural variant

419

1

H → Y: dbSNP rs28381981.

VAR_030156

Natural variant

479

1

P → L: dbSNP rs7104422.

VAR_030157

Experimental info

Mutagenesis

332

1

R → A, G, H, P, Q or S: Increases strongly cell restriction against HIV-1 and SIVmac infection. Ref.12

Mutagenesis

332

1

R → D, E or L: Increases strongly cell restriction against HIV-1 infection. Ref.12

Mutagenesis

332

1

R → K: No effect on HIV-1 and SIVmac infection. Ref.12

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

Beta strand

128 – 130

3

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. 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. 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. 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. 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

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: 11331580] [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: 15249690] [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: 16401428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA), VARIANTS TYR-43 AND ASP-249.
[4]	"Ubiquitination of TRIM5alpha." Tanji K., Kamitani T. Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136. Tissue: Brain.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT GLN-136.
[6]	"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: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA). Tissue: Rhabdomyosarcoma.
[9]	"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: 12878161] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BTBD1 AND BTBD2.
[10]	"Retroviral restriction factor TRIM5alpha is a trimer." Mische C.C., Javanbakht H., Song B., Diaz-Griffero F., Stremlau M., Strack B., Si Z., Sodroski J. J. Virol. 79:14446-14450(2005) [PubMed: 16254380] [Abstract] Cited for: TRIMERIZATION (ISOFORM ALPHA).
[11]	"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: 16474118] [Abstract] Cited for: FUNCTION (ISOFORM ALPHA).
[12]	"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: 16809279] [Abstract] Cited for: MUTAGENESIS OF ARG-332.
[13]	"Characterization of TRIM5alpha trimerization and its contribution to human immunodeficiency virus capsid binding." Javanbakht H., Yuan W., Yeung D.F., Song B., Diaz-Griffero F., Li Y., Li X., Stremlau M., Sodroski J. Virology 353:234-246(2006) [PubMed: 16808955] [Abstract] Cited for: TRIMERIZATION (ISOFORM ALPHA).
[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: 16643975] [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: 16956947] [Abstract] Cited for: REVIEW.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, MASS SPECTROMETRY.
[17]	"Solution structure of the zinc finger, C3HC4 type (RING finger) domain and of the B-box domain of tripartite motif-containing protein 5." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-131.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AK027593 mRNA. Translation: BAB55218.1.
AC015691 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68775.1.
BC021258 mRNA. Translation: AAH21258.1.

IPI

IPI00394972.
IPI00394973.
IPI00394974.
IPI00394975.
IPI00873422.

RefSeq

NP_149023.1.
NP_149083.1.
NP_149084.1.

UniGene

Hs.370515

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9C035. 4 interactions.

PTM databases

PhosphoSite

Q9C035.

Proteomic databases

PRIDE

Q9C035.

Genome annotation databases

Ensembl

ENSG00000132256. Homo sapiens. [Contig view]

GeneID

85363.

KEGG

hsa:85363.

Organism-specific databases

GeneCards

GC11M005641.

HGNC

HGNC:16276. TRIM5.

HPA

CAB013497.

MIM

608487. gene.

PharmGKB

PA38109.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9C035.

OMA

Q9C035. VRAYWGK.

Gene expression databases

ArrayExpress

Q9C035.

Bgee

Q9C035.

GermOnline

ENSG00000132256. Homo sapiens.

Family and domain databases

InterPro

IPR001870. B302.
IPR003879. Butyrophylin.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

PRINTS

PR01407. BUTYPHLNCDUF.

SMART

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

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

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Other Resources

NextBio

75883.

SOURCE

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Entry information

Entry name

TRIM5_HUMAN

Accession

Primary (citable) accession number: Q9C035
Secondary accession number(s): A6NGQ1 , 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:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)