Q99PQ2 (TRI11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Tripartite motif-containing protein 11

Gene names

Name:

Trim11

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	467 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.6 Ref.8 Ref.9
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Binds cytoplasmic tail of integrin alpha-1 By similarity. Interacts with MED15/ARC105; this interaction leads to MED15 ubiquitination and proteasomal degradation By similarity. Interacts with the HN peptide. Interacts with PHOX2B. Interacts with PAX6. Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus. Note: In the nucleus, colocalizes with PAX6. Ref.8
Tissue specificity	Expressed in embryonic central nervous system (CNS), kidney, thymus and gut.
Induction	By PAX6. Ref.8
Domain	The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6. They are also involved in MED15-binding By similarity. Ref.8 The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins. Ref.8
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 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 mutant phenotype Ref.8. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB nucleus Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.8. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99PQ2-1)

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: Q99PQ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: Q → QLCIECCALEREASIAK

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	E3 ubiquitin-protein ligase TRIM11		PRO_0000056216
Regions
	Domain	267 – 460	194	B30.2/SPRY
	Zinc finger	16 – 57	42	RING-type
	Zinc finger	87 – 127	41	B box-type
	Coiled coil	128 – 207	80	Potential
Natural variations
	Alternative sequence	244	1	Q → QLCIECCALEREASIAK in isoform 2.		VSP_012059

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 82B7CF68807E9DA8	FASTA	467	52,580
	10 20 30 40 50 60 MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 70 80 90 100 110 120 AQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLT TFCGDDLSLL CPICERSEHW 130 140 150 160 170 180 THRVRPLQEA ADDLKGRLEK SLEHLRKQME DAMLFQAQAE ETCALWQKMV ESQRQNVLGE 190 200 210 220 230 240 FERLRRLLAE EEQQLLQKLE EEELEVLPRL REGAARLGQQ STQLAALISE LESRCQLPAL 250 260 270 280 290 300 GLLQDIKDAL CRVQDVKLQP PAVVPMELRT VCRVPGLVET LRRFRGDITL DPDTANPELV 310 320 330 340 350 360 LSEDRRSVQR GEQRQALPDN PERFDPGPCV LGQERITSGR HYWEVEVGDQ TSWALGVCKE 370 380 390 400 410 420 TANRKEKGEL SAGNGFWILV FLGSFYNSNE PAFSPLRDPP KRVGIFLDYE AGHLSFYSAT 430 440 450 460 DGSLLFIFPE TLFSGTLRPL FSPLSSSPTP MTICRLIGVS GDTLGPQ
	Isoform 2 [UniParc]. Checksum: 51BDFFCD514046FC	FASTA	483	54,314
	10 20 30 40 50 60 MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 70 80 90 100 110 120 AQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLT TFCGDDLSLL CPICERSEHW 130 140 150 160 170 180 THRVRPLQEA ADDLKGRLEK SLEHLRKQME DAMLFQAQAE ETCALWQKMV ESQRQNVLGE 190 200 210 220 230 240 FERLRRLLAE EEQQLLQKLE EEELEVLPRL REGAARLGQQ STQLAALISE LESRCQLPAL 250 260 270 280 290 300 GLLQLCIECC ALEREASIAK DIKDALCRVQ DVKLQPPAVV PMELRTVCRV PGLVETLRRF 310 320 330 340 350 360 RGDITLDPDT ANPELVLSED RRSVQRGEQR QALPDNPERF DPGPCVLGQE RITSGRHYWE 370 380 390 400 410 420 VEVGDQTSWA LGVCKETANR KEKGELSAGN GFWILVFLGS FYNSNEPAFS PLRDPPKRVG 430 440 450 460 470 480 IFLDYEAGHL SFYSATDGSL LFIFPETLFS GTLRPLFSPL SSSPTPMTIC RLIGVSGDTL GPQ

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] (ISOFORM 1).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Brain cortex and Dendritic cell.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 2).
[6]	"A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults." Niikura T., Hashimoto Y., Tajima H., Ishizaka M., Yamagishi Y., Kawasumi M., Nawa M., Terashita K., Aiso S., Nishimoto I. Eur. J. Neurosci. 17:1150-1158(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HUMANIN.
[7]	"Trim11 increases expression of dopamine beta-hydroxylase gene by interacting with Phox2b." Hong S.J., Chae H., Lardaro T., Hong S., Kim K.S. Biochem. Biophys. Res. Commun. 368:650-655(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PHOX2B.
[8]	"Trim11 modulates the function of neurogenic transcription factor Pax6 through ubiquitin-proteosome system." Tuoc T.C., Stoykova A. Genes Dev. 22:1972-1986(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAX6, DOMAIN B30.2, SUBCELLULAR LOCATION, INDUCTION.
[9]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF220124 mRNA. Translation: AAG53497.1. AK139477 mRNA. Translation: BAE24028.1. AK170656 mRNA. Translation: BAE41941.1. AL607108 Genomic DNA. Translation: CAM24055.1. AL662809 Genomic DNA. Translation: CAM24489.1. CH466628 Genomic DNA. Translation: EDL07693.1. BC020102 mRNA. Translation: AAH20102.1.
IPI	IPI00480525. IPI00626074.
RefSeq	NP_444398.1. NM_053168.1.
UniGene	Mm.248049. Mm.439976.
3D structure databases
ProteinModelPortal	Q99PQ2.
SMR	Q99PQ2. Positions 9-56, 288-456.
ModBase	Search...
PTM databases
PhosphoSite	Q99PQ2.
Proteomic databases
PaxDb	Q99PQ2.
PRIDE	Q99PQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000093061; ENSMUSP00000090749; ENSMUSG00000020455. ENSMUST00000108810; ENSMUSP00000104438; ENSMUSG00000020455.
GeneID	94091.
KEGG	mmu:338364. mmu:94091.
UCSC	uc007jcy.1. mouse. uc011xvj.1. mouse.
Organism-specific databases
CTD	201292. 81559.
MGI	MGI:2137355. Trim11.
Phylogenomic databases
eggNOG	NOG303941.
GeneTree	ENSGT00690000101646.
HOGENOM	HOG000234133.
HOVERGEN	HBG001357.
InParanoid	A2AB84.
KO	K10650. K12031.
OMA	GDRTSWA.
OrthoDB	EOG42BX8J.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q99PQ2.
Bgee	Q99PQ2.
CleanEx	MM_TRIM11.
Genevestigator	Q99PQ2.
GermOnline	ENSMUSG00000020455. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 4.10.45.10. 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
NextBio	352077.
SOURCE	Search...

Entry information

Entry name

TRI11_MOUSE

Accession

Primary (citable) accession number: Q99PQ2
Secondary accession number(s): A2A868 , A2AB84, Q3TCL5, Q8VDX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program