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Q9UPN9 (TRI33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 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 names
Name:TRIM33
Synonyms:KIAA1113, RFG7, TIF1G
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1127 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to Ref.8, 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). Ref.1 Ref.7 Ref.8 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus. Note: In discrete nuclear dots resembling nuclear bodies By similarity. Ref.7 Ref.8 Ref.10

Tissue specificity

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.

Post-translational modification

Sumoylated with SUMO1 By similarity.

Involvement in disease

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.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 2 B box-type zinc fingers.

Contains 1 bromo domain.

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

negative regulation of BMP signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

negative regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

R-SMAD binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

co-SMAD binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.10PubMed 20603019PubMed 21597466. Source: IntAct

ubiquitin-protein transferase activity

Traceable author statement. Source: Reactome

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q9UPN9-1)

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 Beta (identifier: Q9UPN9-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11271127E3 ubiquitin-protein ligase TRIM33
PRO_0000056395

Regions

Domain974 – 104673Bromo
Zinc finger125 – 15430RING-type
Zinc finger212 – 25948B box-type 1
Zinc finger271 – 31242B box-type 2
Zinc finger887 – 93448PHD-type
Region1 – 147147Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repression
Region299 – 401103Necessary for oligomerization
Coiled coil299 – 401103 Potential
Compositional bias13 – 186Poly-Gly
Compositional bias44 – 496Poly-Glu
Compositional bias545 – 5506Poly-Thr

Sites

Site964 – 9652Breakpoint for translocation to form TRIM33-RET oncogene

Amino acid modifications

Modified residue7631N6-acetyllysine Ref.11
Modified residue7691N6-acetyllysine Ref.11
Modified residue7931N6-acetyllysine By similarity
Modified residue8621Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue9511N6-acetyllysine By similarity
Modified residue9531N6-acetyllysine Ref.11
Modified residue11021Phosphothreonine Ref.9 Ref.12 Ref.14
Modified residue11051Phosphoserine Ref.9 Ref.12 Ref.14

Natural variations

Alternative sequence1041 – 105717Missing in isoform Beta.
VSP_005774
Natural variant671V → A.
Corresponds to variant rs6691166 [ dbSNP | Ensembl ].
VAR_029494
Natural variant5801M → I in a glioblastoma multiforme sample; somatic mutation. Ref.15
VAR_042376
Natural variant6961L → S. Ref.15
Corresponds to variant rs56151583 [ dbSNP | Ensembl ].
VAR_042377
Natural variant8111E → K in a lung adenocarcinoma sample; somatic mutation. Ref.15
VAR_042378
Natural variant8401I → T. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs6537825 [ dbSNP | Ensembl ].
VAR_024616
Natural variant8851P → S in a glioblastoma multiforme sample; somatic mutation. Ref.15
VAR_042379
Natural variant9611V → M. Ref.15
Corresponds to variant rs55688622 [ dbSNP | Ensembl ].
VAR_042380
Natural variant10901P → T. Ref.15
Corresponds to variant rs55784699 [ dbSNP | Ensembl ].
VAR_042381

Experimental info

Mutagenesis1251C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. Ref.7
Mutagenesis1281C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. Ref.7
Sequence conflict891V → E in CAB55313. Ref.5
Sequence conflict451 – 4533PAA → LLH in CAB55313. Ref.5
Sequence conflict9091F → S in CAB55313. Ref.5
Sequence conflict10371R → T in AAD17259. Ref.1

Secondary structure

................................. 1127
Helix Strand Turn

Details...

Sequences

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

Last modified November 30, 2010. Version 3.
Checksum: 7A36013799E9933C

FASTA1,127122,533
        10         20         30         40         50         60 
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG GRAGAEGGAA 

        70         80         90        100        110        120 
GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA PASAPAPGPS AGPPPGPPAS 

       130        140        150        160        170        180 
LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR 

       190        200        210        220        230        240 
CPVCRQECRQ IDLVDNYFVK DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT 

       250        260        270        280        290        300 
CIEAHQRVKF TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ 

       310        320        330        340        350        360 
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE VNETNKRVEQ 

       370        380        390        400        410        420 
EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN DITGLSRQVK HVMNFTNWAI 

       430        440        450        460        470        480 
ASGSSTALLY SKRLITFQLR HILKARCDPV PAANGAIRFH CDPTFWAKNV VNLGNLVIES 

       490        500        510        520        530        540 
KPAPGYTPNV VVGQVPPGTN HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP 

       550        560        570        580        590        600 
APVPTTTTTT QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP 

       610        620        630        640        650        660 
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM ANANRGPTSP 

       670        680        690        700        710        720 
SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL SRYISGSHLP PQPTSTMNPS 

       730        740        750        760        770        780 
PGPSALSPGS SGLSNSHTPV RPPSTSSTGS RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG 

       790        800        810        820        830        840 
TEDEICSFSG GVKQEKTEDG RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI 

       850        860        870        880        890        900 
EPADMNESCK QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL 

       910        920        930        940        950        960 
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK KGKTAQGLSP 

       970        980        990       1000       1010       1020 
VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP MDLSTVKKKL QKKHSQHYQI 

      1030       1040       1050       1060       1070       1080 
PDDFVADVRL IFKNCERFNE MMKVVQVYAD TQEINLKADS EVAQAGKAVA LYFEDKLTEI 

      1090       1100       1110       1120 
YSDRTFAPLP EFEQEEDDGE VTEDSDEDFI QPRRKRLKSD ERPVHIK 

« Hide

Isoform Beta [UniParc].

Checksum: 1D415E1C620703A8
Show »

FASTA1,110120,541

References

« Hide 'large scale' references
[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]"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] (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. 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].
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [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.
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS872.1. [Q9UPN9-1]
CCDS873.1. [Q9UPN9-2]
RefSeqNP_056990.3. NM_015906.3. [Q9UPN9-1]
NP_148980.2. NM_033020.2. [Q9UPN9-2]
UniGeneHs.26837.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9UPN9.
SMRQ9UPN9. Positions 124-191, 270-314, 883-1087.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119625. 47 interactions.
DIPDIP-54262N.
IntActQ9UPN9. 40 interactions.
MINTMINT-2822547.
STRING9606.ENSP00000351250.

Chemistry

ChEMBLCHEMBL2176772.

PTM databases

PhosphoSiteQ9UPN9.

Polymorphism databases

DMDM313104270.

Proteomic databases

MaxQBQ9UPN9.
PaxDbQ9UPN9.
PRIDEQ9UPN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358465; ENSP00000351250; ENSG00000197323. [Q9UPN9-1]
ENST00000369543; ENSP00000358556; ENSG00000197323. [Q9UPN9-2]
GeneID51592.
KEGGhsa:51592.
UCSCuc001eew.3. human. [Q9UPN9-1]
uc001eex.3. human. [Q9UPN9-2]

Organism-specific databases

CTD51592.
GeneCardsGC01M114935.
H-InvDBHIX0000910.
HGNCHGNC:16290. TRIM33.
HPAHPA004345.
MIM188550. phenotype.
605769. gene.
neXtProtNX_Q9UPN9.
Orphanet146. Papillary or follicular thyroid carcinoma.
PharmGKBPA38118.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOVERGENHBG054599.
InParanoidQ9UPN9.
KOK08883.
OMANNKDDDP.
OrthoDBEOG790FZZ.
PhylomeDBQ9UPN9.
TreeFamTF106455.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkQ9UPN9.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UPN9.
BgeeQ9UPN9.
CleanExHS_TRIM33.
GenevestigatorQ9UPN9.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProIPR003649. 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]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50014. 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]
ProtoNetSearch...

Other

ChiTaRSTRIM33. human.
GeneWikiTRIM33.
GenomeRNAi51592.
NextBio55433.
PMAP-CutDBQ9UPN9.
PROQ9UPN9.
SOURCESearch...

Entry information

Entry nameTRI33_HUMAN
AccessionPrimary (citable) accession number: Q9UPN9
Secondary accession number(s): O95855 expand/collapse secondary AC list , Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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