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Q9UPN9

- TRI33_HUMAN

UniProt

Q9UPN9 - TRI33_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM33

Gene

TRIM33

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor By similarity. Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).By similarity4 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei964 – 9652Breakpoint for translocation to form TRIM33-RET oncogene

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri125 – 15430RING-typePROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri212 – 25948B box-type 1PROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri271 – 31242B box-type 2PROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri887 – 93448PHD-typePROSITE-ProRule annotationsAdd
    BLAST

    GO - Molecular functioni

    1. co-SMAD binding Source: BHF-UCL
    2. DNA binding Source: UniProtKB-KW
    3. ligase activity Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. R-SMAD binding Source: BHF-UCL
    6. ubiquitin-protein transferase activity Source: Reactome
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. negative regulation of BMP signaling pathway Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    5. protein ubiquitination Source: UniProtKB
    6. regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    7. transcription, DNA-templated Source: Reactome
    8. transcription initiation from RNA polymerase II promoter Source: Reactome
    9. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    SignaLinkiQ9UPN9.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase TRIM33 (EC:6.3.2.-)
    Alternative name(s):
    Ectodermin homolog
    RET-fused gene 7 protein
    Short name:
    Protein Rfg7
    Transcription intermediary factor 1-gamma
    Short name:
    TIF1-gamma
    Tripartite motif-containing protein 33
    Gene namesi
    Name:TRIM33
    Synonyms:KIAA1113, RFG7, TIF1G
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:16290. TRIM33.

    Subcellular locationi

    Nucleus 3 Publications
    Note: In discrete nuclear dots resembling nuclear bodies.By similarity

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Thyroid papillary carcinoma (TPC) [MIM:188550]: A common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells.
    Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TRIM33 is found in thyroid papillary carcinomas. Translocation t(1;10)(p13;q11) with RET. The translocation generates the TRIM33/RET (PTC7) oncogene.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. 1 Publication
    Mutagenesisi128 – 1281C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. 1 Publication

    Organism-specific databases

    MIMi188550. phenotype.
    Orphaneti146. Papillary or follicular thyroid carcinoma.
    PharmGKBiPA38118.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11271127E3 ubiquitin-protein ligase TRIM33PRO_0000056395Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei763 – 7631N6-acetyllysine1 Publication
    Modified residuei769 – 7691N6-acetyllysine1 Publication
    Modified residuei793 – 7931N6-acetyllysineBy similarity
    Modified residuei862 – 8621Phosphoserine3 Publications
    Modified residuei951 – 9511N6-acetyllysineBy similarity
    Modified residuei953 – 9531N6-acetyllysine1 Publication
    Modified residuei1102 – 11021Phosphothreonine3 Publications
    Modified residuei1105 – 11051Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylated with SUMO1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UPN9.
    PaxDbiQ9UPN9.
    PRIDEiQ9UPN9.

    PTM databases

    PhosphoSiteiQ9UPN9.

    Miscellaneous databases

    PMAP-CutDBQ9UPN9.

    Expressioni

    Tissue specificityi

    Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors.

    Gene expression databases

    ArrayExpressiQ9UPN9.
    BgeeiQ9UPN9.
    CleanExiHS_TRIM33.
    GenevestigatoriQ9UPN9.

    Organism-specific databases

    HPAiHPA004345.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer with TRIM24 and TRIM28 family members. Interacts with SMAD4 in unstimulated cells. Found in a complex with SMAD2 and SMAD3 upon addition of TGF-beta. Interacts with SMAD2 and SMAD3. Interacts with SMAD4 under basal and induced conditions and, upon TGF-beta signaling, with activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon TGF-beta signaling.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMAD2Q157966EBI-2214398,EBI-1040141
    SMAD4Q134856EBI-2214398,EBI-347263

    Protein-protein interaction databases

    BioGridi119625. 48 interactions.
    DIPiDIP-54262N.
    IntActiQ9UPN9. 40 interactions.
    MINTiMINT-2822547.
    STRINGi9606.ENSP00000351250.

    Structurei

    Secondary structure

    1
    1127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi888 – 8903
    Turni891 – 8933
    Beta strandi897 – 9015
    Beta strandi903 – 9064
    Turni911 – 9133
    Beta strandi914 – 9163
    Beta strandi918 – 9203
    Turni929 – 9313
    Beta strandi934 – 9363
    Helixi944 – 9474
    Helixi960 – 97415
    Helixi980 – 9823
    Helixi993 – 9964
    Helixi1003 – 10108
    Beta strandi1011 – 10133
    Helixi1021 – 104525
    Helixi1061 – 108020
    Beta strandi1081 – 10833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U5MX-ray3.08A/B/C/D/E/F/G/H/I/J/K/L882-1087[»]
    3U5NX-ray1.95A/B882-1087[»]
    3U5OX-ray2.70A/B/C/D/E/F/G/H882-1087[»]
    3U5PX-ray2.80A/B/C/D/E/F/G/H882-1087[»]
    ProteinModelPortaliQ9UPN9.
    SMRiQ9UPN9. Positions 124-191, 270-314, 883-1087.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini974 – 104673BromoPROSITE-ProRule annotationsAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 147147Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repressionAdd
    BLAST
    Regioni299 – 401103Necessary for oligomerizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili299 – 401103Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 186Poly-Gly
    Compositional biasi44 – 496Poly-Glu
    Compositional biasi545 – 5506Poly-Thr

    Sequence similaritiesi

    Belongs to the TRIM/RBCC family.Curated
    Contains 2 B box-type zinc fingers.PROSITE-ProRule annotations
    Contains 1 bromo domain.PROSITE-ProRule annotations
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotations
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotations

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri125 – 15430RING-typePROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri212 – 25948B box-type 1PROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri271 – 31242B box-type 2PROSITE-ProRule annotationsAdd
    BLAST
    Zinc fingeri887 – 93448PHD-typePROSITE-ProRule annotationsAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOVERGENiHBG054599.
    InParanoidiQ9UPN9.
    KOiK08883.
    OMAiNNKDDDP.
    OrthoDBiEOG790FZZ.
    PhylomeDBiQ9UPN9.
    TreeFamiTF106455.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 2 hits.
    4.10.45.10. 1 hit.
    InterProiIPR003649. Bbox_C.
    IPR001487. Bromodomain.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR000315. Znf_B-box.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00643. zf-B_box. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 2 hits.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q9UPN9-1) [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

    MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG     50
    GRAGAEGGAA GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA 100
    PASAPAPGPS AGPPPGPPAS LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC 150
    LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR CPVCRQECRQ IDLVDNYFVK 200
    DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT CIEAHQRVKF 250
    TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ 300
    LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE 350
    VNETNKRVEQ EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN 400
    DITGLSRQVK HVMNFTNWAI ASGSSTALLY SKRLITFQLR HILKARCDPV 450
    PAANGAIRFH CDPTFWAKNV VNLGNLVIES KPAPGYTPNV VVGQVPPGTN 500
    HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP APVPTTTTTT 550
    QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP 600
    GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM 650
    ANANRGPTSP SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL 700
    SRYISGSHLP PQPTSTMNPS PGPSALSPGS SGLSNSHTPV RPPSTSSTGS 750
    RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG TEDEICSFSG GVKQEKTEDG 800
    RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI EPADMNESCK 850
    QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL 900
    CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK 950
    KGKTAQGLSP VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP 1000
    MDLSTVKKKL QKKHSQHYQI PDDFVADVRL IFKNCERFNE MMKVVQVYAD 1050
    TQEINLKADS EVAQAGKAVA LYFEDKLTEI YSDRTFAPLP EFEQEEDDGE 1100
    VTEDSDEDFI QPRRKRLKSD ERPVHIK 1127
    Length:1,127
    Mass (Da):122,533
    Last modified:November 30, 2010 - v3
    Checksum:i7A36013799E9933C
    GO
    Isoform Beta (identifier: Q9UPN9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1041-1057: Missing.

    Show »
    Length:1,110
    Mass (Da):120,541
    Checksum:i1D415E1C620703A8
    GO

    Sequence cautioni

    The sequence AAD17259.1 differs from that shown. Reason: Frameshift at position 1114.
    The sequence BAA83065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI13548.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI21895.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671V → A.
    Corresponds to variant rs6691166 [ dbSNP | Ensembl ].
    VAR_029494
    Natural varianti580 – 5801M → I in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042376
    Natural varianti696 – 6961L → S.1 Publication
    Corresponds to variant rs56151583 [ dbSNP | Ensembl ].
    VAR_042377
    Natural varianti811 – 8111E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042378
    Natural varianti840 – 8401I → T.4 Publications
    Corresponds to variant rs6537825 [ dbSNP | Ensembl ].
    VAR_024616
    Natural varianti885 – 8851P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042379
    Natural varianti961 – 9611V → M.1 Publication
    Corresponds to variant rs55688622 [ dbSNP | Ensembl ].
    VAR_042380
    Natural varianti1090 – 10901P → T.1 Publication
    Corresponds to variant rs55784699 [ dbSNP | Ensembl ].
    VAR_042381

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1041 – 105717Missing in isoform Beta. 2 PublicationsVSP_005774Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891V → E in CAB55313. (PubMed:10439047)Curated
    Sequence conflicti451 – 4533PAA → LLH in CAB55313. (PubMed:10439047)Curated
    Sequence conflicti909 – 9091F → S in CAB55313. (PubMed:10439047)Curated
    Sequence conflicti1037 – 10371R → T in AAD17259. (PubMed:10022127)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119043 mRNA. Translation: AAD17259.1. Frameshift.
    AF220136 mRNA. Translation: AAG53509.1.
    AF220137 mRNA. Translation: AAG53510.1.
    AB029036 mRNA. Translation: BAA83065.1. Different initiation.
    AL390241, AL035410 Genomic DNA. Translation: CAI13548.1. Sequence problems.
    AL390241, AL035410 Genomic DNA. Translation: CAI13550.1.
    AL390241, AL035410 Genomic DNA. Translation: CAI13551.1.
    AL035410, AL390241 Genomic DNA. Translation: CAI21895.1. Sequence problems.
    AL035410, AL390241 Genomic DNA. Translation: CAI21896.1.
    AL035410, AL390241 Genomic DNA. Translation: CAI21897.1.
    AJ132948 mRNA. Translation: CAB55313.1.
    CCDSiCCDS872.1. [Q9UPN9-1]
    CCDS873.1. [Q9UPN9-2]
    RefSeqiNP_056990.3. NM_015906.3. [Q9UPN9-1]
    NP_148980.2. NM_033020.2. [Q9UPN9-2]
    UniGeneiHs.26837.

    Genome annotation databases

    EnsembliENST00000358465; ENSP00000351250; ENSG00000197323. [Q9UPN9-1]
    ENST00000369543; ENSP00000358556; ENSG00000197323. [Q9UPN9-2]
    GeneIDi51592.
    KEGGihsa:51592.
    UCSCiuc001eew.3. human. [Q9UPN9-1]
    uc001eex.3. human. [Q9UPN9-2]

    Polymorphism databases

    DMDMi313104270.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119043 mRNA. Translation: AAD17259.1 . Frameshift.
    AF220136 mRNA. Translation: AAG53509.1 .
    AF220137 mRNA. Translation: AAG53510.1 .
    AB029036 mRNA. Translation: BAA83065.1 . Different initiation.
    AL390241 , AL035410 Genomic DNA. Translation: CAI13548.1 . Sequence problems.
    AL390241 , AL035410 Genomic DNA. Translation: CAI13550.1 .
    AL390241 , AL035410 Genomic DNA. Translation: CAI13551.1 .
    AL035410 , AL390241 Genomic DNA. Translation: CAI21895.1 . Sequence problems.
    AL035410 , AL390241 Genomic DNA. Translation: CAI21896.1 .
    AL035410 , AL390241 Genomic DNA. Translation: CAI21897.1 .
    AJ132948 mRNA. Translation: CAB55313.1 .
    CCDSi CCDS872.1. [Q9UPN9-1 ]
    CCDS873.1. [Q9UPN9-2 ]
    RefSeqi NP_056990.3. NM_015906.3. [Q9UPN9-1 ]
    NP_148980.2. NM_033020.2. [Q9UPN9-2 ]
    UniGenei Hs.26837.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U5M X-ray 3.08 A/B/C/D/E/F/G/H/I/J/K/L 882-1087 [» ]
    3U5N X-ray 1.95 A/B 882-1087 [» ]
    3U5O X-ray 2.70 A/B/C/D/E/F/G/H 882-1087 [» ]
    3U5P X-ray 2.80 A/B/C/D/E/F/G/H 882-1087 [» ]
    ProteinModelPortali Q9UPN9.
    SMRi Q9UPN9. Positions 124-191, 270-314, 883-1087.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119625. 48 interactions.
    DIPi DIP-54262N.
    IntActi Q9UPN9. 40 interactions.
    MINTi MINT-2822547.
    STRINGi 9606.ENSP00000351250.

    Chemistry

    ChEMBLi CHEMBL2176772.

    PTM databases

    PhosphoSitei Q9UPN9.

    Polymorphism databases

    DMDMi 313104270.

    Proteomic databases

    MaxQBi Q9UPN9.
    PaxDbi Q9UPN9.
    PRIDEi Q9UPN9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358465 ; ENSP00000351250 ; ENSG00000197323 . [Q9UPN9-1 ]
    ENST00000369543 ; ENSP00000358556 ; ENSG00000197323 . [Q9UPN9-2 ]
    GeneIDi 51592.
    KEGGi hsa:51592.
    UCSCi uc001eew.3. human. [Q9UPN9-1 ]
    uc001eex.3. human. [Q9UPN9-2 ]

    Organism-specific databases

    CTDi 51592.
    GeneCardsi GC01M114935.
    H-InvDB HIX0000910.
    HGNCi HGNC:16290. TRIM33.
    HPAi HPA004345.
    MIMi 188550. phenotype.
    605769. gene.
    neXtProti NX_Q9UPN9.
    Orphaneti 146. Papillary or follicular thyroid carcinoma.
    PharmGKBi PA38118.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOVERGENi HBG054599.
    InParanoidi Q9UPN9.
    KOi K08883.
    OMAi NNKDDDP.
    OrthoDBi EOG790FZZ.
    PhylomeDBi Q9UPN9.
    TreeFami TF106455.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    SignaLinki Q9UPN9.

    Miscellaneous databases

    ChiTaRSi TRIM33. human.
    GeneWikii TRIM33.
    GenomeRNAii 51592.
    NextBioi 55433.
    PMAP-CutDB Q9UPN9.
    PROi Q9UPN9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UPN9.
    Bgeei Q9UPN9.
    CleanExi HS_TRIM33.
    Genevestigatori Q9UPN9.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 2 hits.
    4.10.45.10. 1 hit.
    InterProi IPR003649. Bbox_C.
    IPR001487. Bromodomain.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR000315. Znf_B-box.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00643. zf-B_box. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS50014. BROMODOMAIN_2. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TIF1gamma, a novel member of the transcriptional intermediary factor 1 family."
      Venturini L., You J., Stadler M., Galien R., Lallemand V., Koken M.H.M., Mattei M.-G., Ganser A., Chambon P., Losson R., De The H.
      Oncogene 18:1209-1217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBUNIT, VARIANT THR-840.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), VARIANT THR-840.
    3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT THR-840.
      Tissue: Brain.
    4. "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].
    5. "The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas."
      Klugbauer S., Rabes H.M.
      Oncogene 18:4388-4393(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-1127 (ISOFORMS ALPHA AND BETA), CHROMOSOMAL TRANSLOCATION WITH RET, VARIANT THR-840.
      Tissue: Thyroid.
    6. "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression."
      Peng H., Feldman I., Rauscher F.J. III
      J. Mol. Biol. 320:629-644(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    7. "Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase."
      Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M., Rugge M., Piccolo S.
      Cell 121:87-99(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION OF SMAD4, INTERACTION WITH SMAD4, MUTAGENESIS OF CYS-125 AND CYS-128, SUBCELLULAR LOCATION.
    8. "Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway."
      He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.
      Cell 125:929-941(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SMAD2 AND SMAD3, INTERACTION WITH SMAD2 AND SMAD3, SUBCELLULAR LOCATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination."
      Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L., Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L., Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.
      Cell 136:123-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMAD2 AND SMAD4.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769 AND LYS-953, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-580; SER-696; LYS-811; SER-885; MET-961 AND THR-1090.

    Entry informationi

    Entry nameiTRI33_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPN9
    Secondary accession number(s): O95855
    , Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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