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Q96F44

- TRI11_HUMAN

UniProt

Q96F44 - TRI11_HUMAN

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Protein

E3 ubiquitin-protein ligase TRIM11

Gene

TRIM11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri87 – 12842B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. innate immune response Source: UniProt
  3. negative regulation of neurogenesis Source: Ensembl
  4. negative regulation of transcription, DNA-templated Source: Ensembl
  5. negative regulation of viral entry into host cell Source: UniProt
  6. negative regulation of viral release from host cell Source: UniProt
  7. negative regulation of viral transcription Source: UniProt
  8. positive regulation of viral entry into host cell Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Antiviral defense, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRIM11
Synonyms:RNF92
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16281. TRIM11.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProt
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468E3 ubiquitin-protein ligase TRIM11PRO_0000056215Add
BLAST

Proteomic databases

MaxQBiQ96F44.
PaxDbiQ96F44.
PRIDEiQ96F44.

PTM databases

PhosphoSiteiQ96F44.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ96F44.
CleanExiHS_TRIM11.
ExpressionAtlasiQ96F44. baseline and differential.
GenevestigatoriQ96F44.

Organism-specific databases

HPAiHPA028541.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MED15Q96RN55EBI-851809,EBI-394506

Protein-protein interaction databases

BioGridi123523. 24 interactions.
IntActiQ96F44. 7 interactions.
MINTiMINT-2880011.
STRINGi9606.ENSP00000284551.

Structurei

3D structure databases

ProteinModelPortaliQ96F44.
SMRiQ96F44. Positions 9-56, 287-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini268 – 461194B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili129 – 20880Sequence AnalysisAdd
BLAST

Domaini

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.By similarity
The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins.By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri87 – 12842B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG303941.
GeneTreeiENSGT00760000118893.
HOVERGENiHBG001357.
InParanoidiQ96F44.
KOiK10650.
OMAiGDRTSWA.
OrthoDBiEOG7MKW64.
PhylomeDBiQ96F44.
TreeFamiTF338674.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96F44-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP
60 70 80 90 100
YACPECRELS PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA
110 120 130 140 150
AFCGDELRLL CAACERSGEH WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM
160 170 180 190 200
QDALLFQAQA DETCVLWQKM VESQRQNVLG EFERLRRLLA EEEQQLLQRL
210 220 230 240 250
EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA LGLLQDIKDA
260 270 280 290 300
LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL
310 320 330 340 350
ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD
360 370 380 390 400
RTSWALGVCR ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP
410 420 430 440 450
PRRVGIFLDY EAGHLSFYSA TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT
460
PMTICRPKGG SGDTLAPQ
Length:468
Mass (Da):52,774
Last modified:December 6, 2002 - v2
Checksum:i8DE4BDF79F221739
GO
Isoform 2 (identifier: Q96F44-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:385
Mass (Da):42,974
Checksum:i13A971DE70ECD27E
GO
Isoform 3 (identifier: Q96F44-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:467
Mass (Da):52,646
Checksum:iCEE334A7ADC3147E
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341G → D in BAG53535. (PubMed:14702039)Curated
Sequence conflicti260 – 2601Q → R in BAG37129. (PubMed:14702039)Curated
Sequence conflicti289 – 2891V → M in BAG53535. (PubMed:14702039)Curated
Sequence conflicti319 – 3191P → S in BAG53535. (PubMed:14702039)Curated
Sequence conflicti395 – 3984APLR → GSIP in AAG53498. (PubMed:11331580)Curated
Sequence conflicti467 – 4671P → A in AAG53498. (PubMed:11331580)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 1691Missing in isoform 3. 1 PublicationVSP_039628
Alternative sequencei288 – 38598DVTLD…VFLGS → RCGGPRWGDDSRRGPAKDLG SQPRVLCPATASSKLTVSWW WVVGKTSSAHTSDISCVGIF TPNNSSTSGNELGIQGFHSA LNRIASADTTGVSTDPTD in isoform 2. 1 PublicationVSP_012057Add
BLAST
Alternative sequencei386 – 46883Missing in isoform 2. 1 PublicationVSP_012058Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31048.1. [Q96F44-1]
RefSeqiNP_660215.1. NM_145214.2. [Q96F44-1]
UniGeneiHs.13543.

Genome annotation databases

EnsembliENST00000284551; ENSP00000284551; ENSG00000154370. [Q96F44-1]
ENST00000366699; ENSP00000355660; ENSG00000154370. [Q96F44-2]
GeneIDi81559.
KEGGihsa:81559.
UCSCiuc001hss.3. human. [Q96F44-1]
uc001hst.1. human. [Q96F44-2]
uc010pvx.2. human. [Q96F44-3]

Polymorphism databases

DMDMi26400672.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31048.1. [Q96F44-1 ]
RefSeqi NP_660215.1. NM_145214.2. [Q96F44-1 ]
UniGenei Hs.13543.

3D structure databases

ProteinModelPortali Q96F44.
SMRi Q96F44. Positions 9-56, 287-455.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123523. 24 interactions.
IntActi Q96F44. 7 interactions.
MINTi MINT-2880011.
STRINGi 9606.ENSP00000284551.

PTM databases

PhosphoSitei Q96F44.

Polymorphism databases

DMDMi 26400672.

Proteomic databases

MaxQBi Q96F44.
PaxDbi Q96F44.
PRIDEi Q96F44.

Protocols and materials databases

DNASUi 81559.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284551 ; ENSP00000284551 ; ENSG00000154370 . [Q96F44-1 ]
ENST00000366699 ; ENSP00000355660 ; ENSG00000154370 . [Q96F44-2 ]
GeneIDi 81559.
KEGGi hsa:81559.
UCSCi uc001hss.3. human. [Q96F44-1 ]
uc001hst.1. human. [Q96F44-2 ]
uc010pvx.2. human. [Q96F44-3 ]

Organism-specific databases

CTDi 81559.
GeneCardsi GC01M228581.
HGNCi HGNC:16281. TRIM11.
HPAi HPA028541.
MIMi 607868. gene.
neXtProti NX_Q96F44.
PharmGKBi PA38112.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303941.
GeneTreei ENSGT00760000118893.
HOVERGENi HBG001357.
InParanoidi Q96F44.
KOi K10650.
OMAi GDRTSWA.
OrthoDBi EOG7MKW64.
PhylomeDBi Q96F44.
TreeFami TF338674.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikii TRIM11.
GenomeRNAii 81559.
NextBioi 71834.
PROi Q96F44.
SOURCEi Search...

Gene expression databases

Bgeei Q96F44.
CleanExi HS_TRIM11.
ExpressionAtlasi Q96F44. baseline and differential.
Genevestigatori Q96F44.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view ]
PRINTSi PR01407. BUTYPHLNCDUF.
SMARTi SM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiTRI11_HUMAN
AccessioniPrimary (citable) accession number: Q96F44
Secondary accession number(s): A6NKE2
, B2RB82, B3KUS3, B4DX88, Q5VSU1, Q8NCA6, Q9C022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3