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Q9UPN9

- TRI33_HUMAN

UniProt

Q9UPN9 - TRI33_HUMAN

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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

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 annotationAdd
BLAST
Zinc fingeri212 – 25948B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri271 – 31242B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri887 – 93448PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. co-SMAD binding Source: BHF-UCL
  2. DNA binding Source: UniProtKB-KW
  3. ligase activity Source: UniProtKB-KW
  4. R-SMAD binding Source: BHF-UCL
  5. ubiquitin-protein transferase activity Source: Reactome
  6. 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
Complete GO annotation...

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
ProteomesiUP000005640: Chromosome 1

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
Complete GO annotation...

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

BgeeiQ9UPN9.
CleanExiHS_TRIM33.
ExpressionAtlasiQ9UPN9. baseline and differential.
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. 57 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 – 8903Combined sources
Turni891 – 8933Combined sources
Beta strandi897 – 9015Combined sources
Beta strandi903 – 9064Combined sources
Turni911 – 9133Combined sources
Beta strandi914 – 9163Combined sources
Beta strandi918 – 9203Combined sources
Turni929 – 9313Combined sources
Beta strandi934 – 9363Combined sources
Helixi944 – 9474Combined sources
Helixi960 – 97415Combined sources
Helixi980 – 9823Combined sources
Helixi993 – 9964Combined sources
Helixi1003 – 10108Combined sources
Beta strandi1011 – 10133Combined sources
Helixi1021 – 104525Combined sources
Helixi1061 – 108020Combined sources
Beta strandi1081 – 10833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 217-263, 270-314, 883-1087.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini974 – 104673BromoPROSITE-ProRule annotationAdd
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 annotation
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00530000062982.
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]

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

        10         20         30         40         50
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG
60 70 80 90 100
GRAGAEGGAA GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA
110 120 130 140 150
PASAPAPGPS AGPPPGPPAS LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC
160 170 180 190 200
LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR CPVCRQECRQ IDLVDNYFVK
210 220 230 240 250
DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT CIEAHQRVKF
260 270 280 290 300
TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ
310 320 330 340 350
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE
360 370 380 390 400
VNETNKRVEQ EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN
410 420 430 440 450
DITGLSRQVK HVMNFTNWAI ASGSSTALLY SKRLITFQLR HILKARCDPV
460 470 480 490 500
PAANGAIRFH CDPTFWAKNV VNLGNLVIES KPAPGYTPNV VVGQVPPGTN
510 520 530 540 550
HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP APVPTTTTTT
560 570 580 590 600
QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP
610 620 630 640 650
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM
660 670 680 690 700
ANANRGPTSP SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL
710 720 730 740 750
SRYISGSHLP PQPTSTMNPS PGPSALSPGS SGLSNSHTPV RPPSTSSTGS
760 770 780 790 800
RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG TEDEICSFSG GVKQEKTEDG
810 820 830 840 850
RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI EPADMNESCK
860 870 880 890 900
QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL
910 920 930 940 950
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK
960 970 980 990 1000
KGKTAQGLSP VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP
1010 1020 1030 1040 1050
MDLSTVKKKL QKKHSQHYQI PDDFVADVRL IFKNCERFNE MMKVVQVYAD
1060 1070 1080 1090 1100
TQEINLKADS EVAQAGKAVA LYFEDKLTEI YSDRTFAPLP EFEQEEDDGE
1110 1120
VTEDSDEDFI QPRRKRLKSD ERPVHIK
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. Curated
The sequence BAA83065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI13548.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI21895.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

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

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 217-263, 270-314, 883-1087.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119625. 57 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.
GeneTreei ENSGT00530000062982.
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

Bgeei Q9UPN9.
CleanExi HS_TRIM33.
ExpressionAtlasi Q9UPN9. baseline and differential.
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

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  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: November 26, 2014
This is version 152 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