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Q96F44 (TRI11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAntiviral defense
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from mutant phenotype Ref.7. Source: UniProt

negative regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

negative regulation of viral entry into host cell

Inferred from mutant phenotype Ref.7. Source: UniProt

negative regulation of viral release from host cell

Inferred from direct assay Ref.7. Source: UniProt

negative regulation of viral transcription

Inferred from direct assay Ref.7. Source: UniProt

positive regulation of viral entry into host cell

Inferred from mutant phenotype Ref.7. Source: UniProt

   Cellular_componentcytoplasm

Inferred from direct assay Ref.7. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MED15Q96RN55EBI-851809,EBI-394506

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468E3 ubiquitin-protein ligase TRIM11
PRO_0000056215

Regions

Domain268 – 461194B30.2/SPRY
Zinc finger16 – 5742RING-type
Zinc finger87 – 12842B box-type
Coiled coil129 – 20880 Potential

Natural variations

Alternative sequence1691Missing in isoform 3.
VSP_039628
Alternative sequence288 – 38598DVTLD…VFLGS → RCGGPRWGDDSRRGPAKDLG SQPRVLCPATASSKLTVSWW WVVGKTSSAHTSDISCVGIF TPNNSSTSGNELGIQGFHSA LNRIASADTTGVSTDPTD in isoform 2.
VSP_012057
Alternative sequence386 – 46883Missing in isoform 2.
VSP_012058

Experimental info

Sequence conflict2341G → D in BAG53535. Ref.2
Sequence conflict2601Q → R in BAG37129. Ref.2
Sequence conflict2891V → M in BAG53535. Ref.2
Sequence conflict3191P → S in BAG53535. Ref.2
Sequence conflict395 – 3984APLR → GSIP in AAG53498. Ref.5
Sequence conflict4671P → A in AAG53498. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 8DE4BDF79F221739

FASTA46852,774
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 13A971DE70ECD27E
Show »

FASTA38542,974
Isoform 3 [UniParc].

Checksum: CEE334A7ADC3147E
Show »

FASTA46752,646

References

« Hide '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. 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] (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. expand/collapse author list , 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.
CCDSCCDS31048.1. [Q96F44-1]
RefSeqNP_660215.1. NM_145214.2. [Q96F44-1]
UniGeneHs.13543.

3D structure databases

ProteinModelPortalQ96F44.
SMRQ96F44. Positions 9-56, 289-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123523. 14 interactions.
IntActQ96F44. 7 interactions.
MINTMINT-2880011.
STRING9606.ENSP00000284551.

PTM databases

PhosphoSiteQ96F44.

Polymorphism databases

DMDM26400672.

Proteomic databases

MaxQBQ96F44.
PaxDbQ96F44.
PRIDEQ96F44.

Protocols and materials databases

DNASU81559.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284551; ENSP00000284551; ENSG00000154370. [Q96F44-1]
ENST00000366699; ENSP00000355660; ENSG00000154370. [Q96F44-2]
GeneID81559.
KEGGhsa:81559.
UCSCuc001hss.3. human. [Q96F44-1]
uc001hst.1. human. [Q96F44-2]
uc010pvx.2. human. [Q96F44-3]

Organism-specific databases

CTD81559.
GeneCardsGC01M228581.
HGNCHGNC:16281. TRIM11.
HPAHPA028541.
MIM607868. gene.
neXtProtNX_Q96F44.
PharmGKBPA38112.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303941.
HOVERGENHBG001357.
InParanoidQ96F44.
KOK10650.
OMAGDRTSWA.
OrthoDBEOG7MKW64.
PhylomeDBQ96F44.
TreeFamTF338674.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeQ96F44.
CleanExHS_TRIM11.
GenevestigatorQ96F44.

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.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 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

GeneWikiTRIM11.
GenomeRNAi81559.
NextBio71834.
PROQ96F44.
SOURCESearch...

Entry information

Entry nameTRI11_HUMAN
AccessionPrimary (citable) accession number: Q96F44
Secondary accession number(s): A6NKE2 expand/collapse secondary AC list , B2RB82, B3KUS3, B4DX88, Q5VSU1, Q8NCA6, Q9C022
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: July 9, 2014
This is version 129 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM