Q96F44 (TRI11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase TRIM11
EC=6.3.2.-

Alternative name(s):
Protein BIA1
RING finger protein 92
Tripartite motif-containing protein 11

Gene names

Name:	TRIM11
Synonyms:	RNF92

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	468 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Binds cytoplasmic tail of integrin alpha-1. Interacts with the HN peptide By similarity. Interacts with PHOX2B By similarity. Interacts with PAX6 By similarity. Interacts with MED15/ARC105; this interaction leads to MED15 ubiquitination and proteasomal degradation. Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.6 Ref.7.
Tissue specificity	Ubiquitous.
Domain	The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6 By similarity. They are also involved in MED15-binding. The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins By similarity.
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.
Sequence caution	The sequence AAH11629.1 differs from that shown. Reason: Erroneous initiation. The sequence BAG53535.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG63300.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Antiviral defense Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of neurogenesis Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96F44-1)

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 2 (identifier: Q96F44-2)

The sequence of this isoform differs from the canonical sequence as follows:
     288-385: DVTLDPDTAN...GFWILVFLGS → RCGGPRWGDD...TTGVSTDPTD
     386-468: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q96F44-3)

The sequence of this isoform differs from the canonical sequence as follows:
     169-169: Missing.

Note: May be due to competing acceptor splice site. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	E3 ubiquitin-protein ligase TRIM11		PRO_0000056215
Regions
	Domain	268 – 461	194	B30.2/SPRY
	Zinc finger	16 – 57	42	RING-type
	Zinc finger	87 – 128	42	B box-type
	Coiled coil	129 – 208	80	Potential
Natural variations
	Alternative sequence	169	1	Missing in isoform 3.		VSP_039628
	Alternative sequence	288 – 385	98	DVTLD…VFLGS → RCGGPRWGDDSRRGPAKDLG SQPRVLCPATASSKLTVSWW WVVGKTSSAHTSDISCVGIF TPNNSSTSGNELGIQGFHSA LNRIASADTTGVSTDPTD in isoform 2.		VSP_012057
	Alternative sequence	386 – 468	83	Missing in isoform 2.		VSP_012058
Experimental info
	Sequence conflict	234	1	G → D in BAG53535. Ref.2
	Sequence conflict	260	1	Q → R in BAG37129. Ref.2
	Sequence conflict	289	1	V → M in BAG53535. Ref.2
	Sequence conflict	319	1	P → S in BAG53535. Ref.2
	Sequence conflict	395 – 398	4	APLR → GSIP in AAG53498. Ref.5
	Sequence conflict	467	1	P → A in AAG53498. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: 8DE4BDF79F221739	FASTA	468	52,774
	10 20 30 40 50 60 MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 70 80 90 100 110 120 PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH 130 140 150 160 170 180 WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQKM VESQRQNVLG 190 200 210 220 230 240 EFERLRRLLA EEEQQLLQRL EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA 250 260 270 280 290 300 LGLLQDIKDA LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL 310 320 330 340 350 360 ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD RTSWALGVCR 370 380 390 400 410 420 ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP PRRVGIFLDY EAGHLSFYSA 430 440 450 460 TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT PMTICRPKGG SGDTLAPQ
	Isoform 2 [UniParc]. Checksum: 13A971DE70ECD27E	FASTA	385	42,974
	10 20 30 40 50 60 MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 70 80 90 100 110 120 PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH 130 140 150 160 170 180 WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQKM VESQRQNVLG 190 200 210 220 230 240 EFERLRRLLA EEEQQLLQRL EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA 250 260 270 280 290 300 LGLLQDIKDA LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGRCG GPRWGDDSRR 310 320 330 340 350 360 GPAKDLGSQP RVLCPATASS KLTVSWWWVV GKTSSAHTSD ISCVGIFTPN NSSTSGNELG 370 380 IQGFHSALNR IASADTTGVS TDPTD
	Isoform 3 [UniParc]. Checksum: CEE334A7ADC3147E	FASTA	467	52,646
	10 20 30 40 50 60 MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 70 80 90 100 110 120 PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH 130 140 150 160 170 180 WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQMV ESQRQNVLGE 190 200 210 220 230 240 FERLRRLLAE EEQQLLQRLE EEELEVLPRL REGAAHLGQQ SAHLAELIAE LEGRCQLPAL 250 260 270 280 290 300 GLLQDIKDAL RRVQDVKLQP PEVVPMELRT VCRVPGLVET LRRFRGDVTL DPDTANPELI 310 320 330 340 350 360 LSEDRRSVQR GDLRQALPDS PERFDPGPCV LGQERFTSGR HYWEVEVGDR TSWALGVCRE 370 380 390 400 410 420 NVNRKEKGEL SAGNGFWILV FLGSYYNSSE RALAPLRDPP RRVGIFLDYE AGHLSFYSAT 430 440 450 460 DGSLLFIFPE IPFSGTLRPL FSPLSSSPTP MTICRPKGGS GDTLAPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Piecha D., Petersohn D., Eckes B., Krieg T. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"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] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-468 (ISOFORM 3). Tissue: Fetal brain, Teratocarcinoma and Testis.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 1). Tissue: Eye and Placenta.
[5]	"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] OF 395-468 (ISOFORM 1).
[6]	"TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system." Ishikawa H., Tachikawa H., Miura Y., Takahashi N. FEBS Lett. 580:4784-4792(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MED15, SUBCELLULAR LOCATION.
[7]	"TRIM E3 ligases interfere with early and late stages of the retroviral life cycle." Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W. PLoS Pathog. 4:E16-E16(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF327056 mRNA. Translation: AAM63957.1. AK074866 mRNA. Translation: BAC11254.1. AK314539 mRNA. Translation: BAG37129.1. AK097825 mRNA. Translation: BAG53535.1. Different initiation. AK301859 mRNA. Translation: BAG63300.1. Different initiation. AL670729 Genomic DNA. Translation: CAH71671.1. AL670729 Genomic DNA. Translation: CAH71672.1. BC011629 mRNA. Translation: AAH11629.1. Different initiation. BC069227 mRNA. Translation: AAH69227.1. AF220125 mRNA. Translation: AAG53498.1.
IPI	IPI00219527. IPI00385975. IPI00969554.
RefSeq	NP_660215.1. NM_145214.2.
UniGene	Hs.13543.
3D structure databases
ProteinModelPortal	Q96F44.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96F44. 5 interactions.
MINT	MINT-2880011.
STRING	9606.ENSP00000284551.
PTM databases
PhosphoSite	Q96F44.
Polymorphism databases
DMDM	26400672.
Proteomic databases
PaxDb	Q96F44.
PRIDE	Q96F44.
Protocols and materials databases
DNASU	81559.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000284551; ENSP00000284551; ENSG00000154370. ENST00000366699; ENSP00000355660; ENSG00000154370.
GeneID	81559.
KEGG	hsa:81559.
UCSC	uc001hss.3. human. uc001hst.1. human. uc010pvx.2. human.
Organism-specific databases
CTD	81559.
GeneCards	GC01M228581.
HGNC	HGNC:16281. TRIM11.
HPA	HPA028541.
MIM	607868. gene.
neXtProt	NX_Q96F44.
PharmGKB	PA38112.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG303941.
HOVERGEN	HBG001357.
InParanoid	Q96F44.
KO	K10650.
OMA	GDRTSWA.
OrthoDB	EOG42BX8J.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
Bgee	Q96F44.
CleanEx	HS_TRIM11.
Genevestigator	Q96F44.
GermOnline	ENSG00000154370. 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. IPR006574. PRY. IPR018355. SPla/RYanodine_receptor_subgr. IPR003877. SPRY_rcpt. IPR000315. Znf_B-box. IPR018957. Znf_C3HC4_RING-type. 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. PF00097. zf-C3HC4. 1 hit. [Graphical view]
PRINTS	PR01407. BUTYPHLNCDUF.
SMART	SM00336. BBOX. 1 hit. SM00589. PRY. 1 hit. SM00184. RING. 1 hit. SM00449. SPRY. 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
GenomeRNAi	81559.
NextBio	71834.
SOURCE	Search...

Entry information

Entry name

TRI11_HUMAN

Accession

Primary (citable) accession number: Q96F44
Secondary accession number(s): A6NKE2 , B2RB82, B3KUS3, B4DX88, Q5VSU1, Q8NCA6, Q9C022

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 6, 2002
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 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.