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Q96F44

- TRI11_HUMAN

UniProt

Q96F44 - TRI11_HUMAN

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
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (06 Dec 2002)
      Previous versions | rss
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    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. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: Ensembl
    4. 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

    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-SubCell

    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.
    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. 14 interactions.
    IntActiQ96F44. 7 interactions.
    MINTiMINT-2880011.
    STRINGi9606.ENSP00000284551.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96F44.
    SMRiQ96F44. Positions 9-56, 289-455.
    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.
    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.
    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]
    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

    MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP    50
    YACPECRELS PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA 100
    AFCGDELRLL CAACERSGEH WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM 150
    QDALLFQAQA DETCVLWQKM VESQRQNVLG EFERLRRLLA EEEQQLLQRL 200
    EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA LGLLQDIKDA 250
    LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL 300
    ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD 350
    RTSWALGVCR ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP 400
    PRRVGIFLDY EAGHLSFYSA TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT 450
    PMTICRPKGG SGDTLAPQ 468
    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, 289-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123523. 14 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.
    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.
    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.
    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 ]
    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

    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 1, 2014
    This is version 131 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