Q9UPN9 (TRI33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRIM33
Synonyms:	KIAA1113, RFG7, TIF1G

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1127 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Traceable author statement. Source: Reactome zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD2	Q15796	6	EBI-2214398,EBI-1040141
SMAD4	Q13485	5	EBI-2214398,EBI-347263

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1127

1127

E3 ubiquitin-protein ligase TRIM33

PRO_0000056395

Regions

Domain

974 – 1046

73

Bromo

Zinc finger

125 – 154

30

RING-type

Zinc finger

212 – 259

48

B box-type 1

Zinc finger

271 – 312

42

B box-type 2

Zinc finger

887 – 934

48

PHD-type

Region

1 – 147

147

Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repression

Region

299 – 401

103

Necessary for oligomerization

Coiled coil

299 – 401

103

Potential

Compositional bias

13 – 18

6

Poly-Gly

Compositional bias

44 – 49

6

Poly-Glu

Compositional bias

545 – 550

6

Poly-Thr

Sites

Site

964 – 965

2

Breakpoint for translocation to form TRIM33-RET oncogene

Amino acid modifications

Modified residue

763

1

N6-acetyllysine Ref.11

Modified residue

769

1

N6-acetyllysine Ref.11

Modified residue

862

1

Phosphoserine Ref.9 Ref.12 Ref.14

Modified residue

953

1

N6-acetyllysine Ref.11

Modified residue

1102

1

Phosphothreonine Ref.9 Ref.12 Ref.14

Modified residue

1105

1

Phosphoserine Ref.9 Ref.12 Ref.14

Natural variations

Alternative sequence

1041 – 1057

17

Missing in isoform Beta.

VSP_005774

Natural variant

67

1

V → A.
Corresponds to variant rs6691166 [ dbSNP | Ensembl ].

VAR_029494

Natural variant

580

1

M → I in a glioblastoma multiforme sample; somatic mutation. Ref.15

VAR_042376

Natural variant

696

1

L → S. Ref.15
Corresponds to variant rs56151583 [ dbSNP | Ensembl ].

VAR_042377

Natural variant

811

1

E → K in a lung adenocarcinoma sample; somatic mutation. Ref.15

VAR_042378

Natural variant

840

1

I → T. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs6537825 [ dbSNP | Ensembl ].

VAR_024616

Natural variant

885

1

P → S in a glioblastoma multiforme sample; somatic mutation. Ref.15

VAR_042379

Natural variant

961

1

V → M. Ref.15
Corresponds to variant rs55688622 [ dbSNP | Ensembl ].

VAR_042380

Natural variant

1090

1

P → T. Ref.15
Corresponds to variant rs55784699 [ dbSNP | Ensembl ].

VAR_042381

Experimental info

Mutagenesis

125

1

C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128. Ref.7

Mutagenesis

128

1

C → A: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125. Ref.7

Sequence conflict

89

1

V → E in CAB55313. Ref.5

Sequence conflict

451 – 453

3

PAA → LLH in CAB55313. Ref.5

Sequence conflict

909

1

F → S in CAB55313. Ref.5

Sequence conflict

1037

1

R → T in AAD17259. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1127

Helix Strand Turn

Details...

Beta strand

888 – 890

3

Turn

891 – 893

3

Beta strand

897 – 901

5

Beta strand

903 – 906

4

Turn

911 – 913

3

Beta strand

914 – 916

3

Beta strand

918 – 920

3

Turn

929 – 931

3

Beta strand

934 – 936

3

Helix

944 – 947

4

Helix

960 – 974

15

Helix

980 – 982

3

Helix

993 – 996

4

Helix

1003 – 1010

8

Beta strand

1011 – 1013

3

Helix

1021 – 1045

25

Helix

1061 – 1080

20

Beta strand

1081 – 1083

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 7A36013799E9933C	FASTA	1,127	122,533
	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
	Isoform Beta [UniParc]. Checksum: 1D415E1C620703A8	FASTA	1,110	120,541
	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 ADSEVAQAGK AVALYFEDKL TEIYSDRTFA PLPEFEQEED 1090 1100 1110 DGEVTEDSDE DFIQPRRKRL KSDERPVHIK

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
+	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.

IPI

IPI00010252.
IPI00221114.

RefSeq

NP_056990.3. NM_015906.3.
NP_148980.2. NM_033020.2.

UniGene

Hs.26837.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9UPN9.

SMR

Q9UPN9. Positions 270-314, 883-1087.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-54262N.

IntAct

Q9UPN9. 38 interactions.

STRING

9606.ENSP00000351250.

PTM databases

PhosphoSite

Q9UPN9.

Polymorphism databases

DMDM

12643365.

Proteomic databases

PaxDb

Q9UPN9.

PRIDE

Q9UPN9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358465; ENSP00000351250; ENSG00000197323.
ENST00000369543; ENSP00000358556; ENSG00000197323.

GeneID

51592.

KEGG

hsa:51592.

UCSC

uc001eew.3. human.
uc001eex.3. human.

Organism-specific databases

CTD

51592.

GeneCards

GC01M114935.

H-InvDB

HIX0000910.

HGNC

HGNC:16290. TRIM33.

HPA

HPA004345.

MIM

188550. phenotype.
605769. gene.

neXtProt

NX_Q9UPN9.

Orphanet

146. Papillary or follicular thyroid carcinoma.

PharmGKB

PA38118.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOVERGEN

HBG054599.

InParanoid

Q9UPN9.

KO

K08883.

OMA

PIRSLMH.

OrthoDB

EOG4SN1N0.

PhylomeDB

Q9UPN9.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9UPN9.

Bgee

Q9UPN9.

CleanEx

HS_TRIM33.

Genevestigator

Q9UPN9.

GermOnline

ENSG00000197323. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.30.40.10. 2 hits.

InterPro

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]

Pfam

PF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF13639. zf-RING_2. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. False negative.
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]

ProtoNet

Search...

Other

ChiTaRS

TRIM33. human.

GenomeRNAi

51592.

NextBio

55433.

PMAP-CutDB

Q9UPN9.

SOURCE

Search...

Entry information

Entry name

TRI33_HUMAN

Accession

Primary (citable) accession number: Q9UPN9
Secondary accession number(s): O95855 , Q5TG72, Q5TG73, Q5TG74, Q9C017, Q9UJ79

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.