Reviewed, UniProtKB/Swiss-Prot P14373 (TRI27_HUMAN)

Names and origin

Protein names

Recommended name:
    Zinc finger protein RFP
Alternative name(s):
    Ret finger protein
    Tripartite motif-containing protein 27
    RING finger protein 76

Gene names

Name:	TRIM27
Synonyms:	RFP, RNF76

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA By similarity.
Subunit structure	Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4 and EID1. Ref.8 Ref.9 Ref.10 Ref.13 Ref.15
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Nuclear or cytoplasmic depending on the cell type By similarity. Colocalized with PML and EIF3S6 in nuclear bodies.
Tissue specificity	Expressed in testis namely within the seminiferous tubules. Ref.11
Domain	The coiled-coil region mediates interaction with EPC1 and CHD4. The B box and coiled-coil domains mediate interaction with PML. The B box and the distal coiled-coil domains mediate homomultimerisation. The B30.2 domain mediates interaction with EIF3S6.
Involvement in disease	A chromosomal aberration involving TRIM27 is a cause of thyroid papillary carcinoma (PACT) [MIM:188550]. Translocation t(6;10)(p21.3;q11.2) with RET. The translocation generates RFP/RET and delta RFP/RET oncogenes.
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 1 B box-type zinc finger. Contains 1 B30.2/SPRY domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: ProtInc negative regulation of gene expression, epigenetic Ref.10 Inferred from direct assay. Source: MGI negative regulation of transcription from RNA polymerase II promoter Ref.10 Inferred from direct assay. Source: MGI protein trimerization Inferred from direct assay. Source: UniProtKB spermatogenesis Ref.1 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB integral to plasma membrane Traceable author statement. Source: ProtInc membrane fraction Traceable author statement. Source: ProtInc nuclear membrane Ref.10 Inferred from direct assay. Source: MGI nucleoplasm Ref.10 Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.8 Ref.9 Ref.15 Inferred from physical interaction. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF3E	P60228	4	EBI-719493,EBI-347740

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: P14373-1)

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: P14373-2)

The sequence of this isoform differs from the canonical sequence as follows:
     354-358: FNLFP → SPSTT
     359-513: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 513	513	Zinc finger protein RFP		PRO_0000056240
Regions
	Domain	298 – 492	195	B30.2/SPRY
	Zinc finger	16 – 57	42	RING-type
	Zinc finger	96 – 127	32	B box-type
	Coiled coil	132 – 172	41	Potential
	Coiled coil	282 – 311	30	Potential
Sites
	Site	315 – 316	2	Breakpoint for translocation to form the RFP/RET oncogene
Natural variations
	Alternative sequence	354 – 358	5	FNLFP → SPSTT in isoform Beta.		VSP_010896
	Alternative sequence	359 – 513	155	Missing in isoform Beta.		VSP_010897
Experimental info
	Sequence conflict	446	1	E → K in AAH66924. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 6F963D9048D8A731	FASTA	513	58,490
	10 20 30 40 50 60 MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN VSCPQCRETF 70 80 90 100 110 120 PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEED QMPICVVCDR 130 140 150 160 170 180 SREHRGHSVL PLEEAVEGFK EQIQNQLDHL KRVKDLKKRR RAQGEQARAE LLSLTQMERE 190 200 210 220 230 240 KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ 250 260 270 280 290 300 QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS 310 320 330 340 350 360 DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERFNLFPCV 370 380 390 400 410 420 LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS APQNGFWAVS LWYGKEYWAL 430 440 450 460 470 480 TSPMTALPLR TPLQRVGIFL DYDAGEVSFY NVTERCHTFT FSHATFCGPV RPYFSLSYSG 490 500 510 GKSAAPLIIC PMSGIDGFSG HVGNHGHSME TSP
	Isoform Beta. Checksum: D722163761427340	FASTA	358	41,439
	10 20 30 40 50 60 MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN VSCPQCRETF 70 80 90 100 110 120 PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEED QMPICVVCDR 130 140 150 160 170 180 SREHRGHSVL PLEEAVEGFK EQIQNQLDHL KRVKDLKKRR RAQGEQARAE LLSLTQMERE 190 200 210 220 230 240 KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ 250 260 270 280 290 300 QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS 310 320 330 340 350 DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERSPSTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Developmentally regulated expression of a human 'finger'-containing gene encoded by the 5' half of the ret transforming gene." Takahashi M., Inaguma Y., Hiai H., Hirose F. Mol. Cell. Biol. 8:1853-1856(1988) [PubMed: 3380101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[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: 11331580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). Tissue: Testis and Uterus.
[5]	"ret transforming gene encodes a fusion protein homologous to tyrosine kinases." Takahashi M., Cooper G.M. Mol. Cell. Biol. 7:1378-1385(1987) [PubMed: 3037315] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH RET.
[6]	"RFP is a DNA binding protein associated with the nuclear matrix." Isomura T., Tamiya-Koizumi K., Suzuki M., Yoshida S., Taniguchi M., Matsuyama M., Ishigaki T., Sakuma S., Takahashi M. Nucleic Acids Res. 20:5305-5310(1992) [PubMed: 1437549] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution." Cao T., Borden K.L., Freemont P.S., Etkin L.D. J. Cell Sci. 110:1563-1571(1997) [PubMed: 9247190] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML." Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D. J. Cell Sci. 111:1319-1329(1998) [PubMed: 9570750] [Abstract] Cited for: INTERACTION WITH PML.
[9]	"Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies." Morris-Desbois C., Bochard V., Reynaud C., Jalinot P. J. Cell Sci. 112:3331-3342(1999) [PubMed: 10504338] [Abstract] Cited for: INTERACTION WITH EIF3S6.
[10]	"RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions." Shimono Y., Murakami H., Hasegawa Y., Takahashi M. J. Biol. Chem. 275:39411-39419(2000) [PubMed: 10976108] [Abstract] Cited for: INTERACTION WITH EPC1, FUNCTION.
[11]	"Differential expression of RET finger protein in testicular germ cell tumors." Tezel G., Nagasaka T., Shimono Y., Takahashi M. Pathol. Int. 52:623-627(2002) [PubMed: 12445133] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"The Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif." Dho S.H., Kwon K.S. J. Biol. Chem. 278:31902-31908(2003) [PubMed: 12807881] [Abstract] Cited for: FUNCTION.
[13]	"Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities." Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M. J. Biol. Chem. 278:51638-51645(2003) [PubMed: 14530259] [Abstract] Cited for: INTERACTION WITH CHD4.
[14]	"Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary thyroid carcinoma from externally irradiated patient." Saenko V., Rogounovitch T., Shimizu-Yoshida Y., Abrosimov A., Lushnikov E., Roumiantsev P., Matsumoto N., Nakashima M., Meirmanov S., Ohtsuru A., Namba H., Tsyb A., Yamashita S. Mutat. Res. 527:81-90(2003) [PubMed: 12787916] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH RET.
[15]	"Selective ablation of retinoblastoma protein function by the RET finger protein." Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M., Vivanco M.D., Sellers W.R., Mittnacht S. Mol. Cell 18:213-224(2005) [PubMed: 15837424] [Abstract] Cited for: INTERACTION WITH EID1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03407 mRNA. Translation: AAA36564.1. AF230393 mRNA. Translation: AAG50172.1. AF230394 mRNA. Translation: AAG50173.1. AL662859 Genomic DNA. Translation: CAI17553.1. AL662871 Genomic DNA. Translation: CAI18381.1. BX000360, BX537153 Genomic DNA. Translation: CAI18619.1. BX537153, BX000360 Genomic DNA. Translation: CAI18646.1. Z84474, Z84476 Genomic DNA. Translation: CAB06480.2. Z84476, Z84474 Genomic DNA. Translation: CAI19959.1. BC013580 mRNA. Translation: AAH13580.1. BC066924 mRNA. Translation: AAH66924.1.
IPI	IPI00412657. IPI00426252.
PIR	TVHURF. A28101.
RefSeq	NP_006501.1.
UniGene	Hs.440382
3D structure databases
HSSP	HSSP built from PDB template 1FRE based on UniProtKB Q92021.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14373. 9 interactions.
Proteomic databases
PRIDE	P14373.
Genome annotation databases
Ensembl	ENSG00000112448. Homo sapiens. [Contig view] ENSG00000204713. Homo sapiens. [Contig view] ENSG00000215641. Homo sapiens. [Contig view]
GeneID	5987.
KEGG	hsa:5987.
Organism-specific databases
GeneCards	GC06M028979.
H-InvDB	HIX0005677. HIX0057950. HIX0058125.
HGNC	HGNC:9975. TRIM27.
MIM	188550. phenotype. 602165. gene.
Orphanet	146. Thyroid carcinoma, papillary or follicular.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P14373.
HOVERGEN	P14373.
OMA	P14373. PLVICPM.
Gene expression databases
ArrayExpress	P14373.
Bgee	P14373.
CleanEx	HS_TRIM27.
GermOnline	ENSG00000204713. Homo sapiens.
Family and domain databases
InterPro	IPR001870. B302. IPR003879. Butyrophylin. IPR006574. PRY. IPR018355. SPla/RYanodine_receptor_sg. IPR003877. SPRY_rcpt. IPR000315. Znf_B-box. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00622. SPRY. 1 hit. PF00643. zf-B_box. 1 hit. PF00097. zf-C3HC4. 1 hit. [Graphical view]
PRINTS	PR01407. BUTYPHLNCDUF.
SMART	SM00336. BBOX. 1 hit. SM00589. PRY. 1 hit. SM00184. RING. 1 hit. SM00449. SPRY. 1 hit. [Graphical view]
PROSITE	PS50188. B302_SPRY. 1 hit. PS50119. ZF_BBOX. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23317.
SOURCE	Search...

Entry information

Entry name

TRI27_HUMAN

Accession

Primary (citable) accession number: P14373
Secondary accession number(s): Q5ST26 , Q6LA73, Q6NXR9, Q9BZY6, Q9UJL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)