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Protein

Zinc finger protein RFP

Gene

TRIM27

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853). 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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 12732B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • metal ion binding Source: ProtInc
  • nucleic acid binding Source: ProtInc
  • transmembrane receptor protein tyrosine kinase activity Source: ProtInc
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • cell proliferation Source: ProtInc
  • innate immune response Source: UniProtKB
  • interferon-gamma secretion Source: UniProtKB
  • negative regulation of adaptive immune response Source: UniProtKB
  • negative regulation of calcium ion import Source: UniProtKB
  • negative regulation of gene expression, epigenetic Source: MGI
  • negative regulation of interleukin-2 secretion Source: UniProtKB
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of tumor necrosis factor production Source: UniProtKB
  • negative regulation of viral release from host cell Source: Ensembl
  • negative regulation of viral transcription Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive regulation of actin nucleation Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein trimerization Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • spermatogenesis Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Transport, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SIGNORiP14373.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein RFP (EC:6.3.2.-)
Alternative name(s):
RING finger protein 76
Ret finger protein
Tripartite motif-containing protein 27
Gene namesi
Name:TRIM27
Synonyms:RFP, RNF76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9975. TRIM27.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GOC
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: ProtInc
  • nuclear membrane Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TRIM27/RFP is found in papillary thyroid carcinomas (PTCs). Translocation t(6;10)(p21.3;q11.2) with RET. The translocation generates TRIM27/RET and delta TRIM27/RET oncogenes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei315 – 3162Breakpoint for translocation to form the TRIM27/RET oncogene

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MalaCardsiTRIM27.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA162406956.

Polymorphism and mutation databases

BioMutaiTRIM27.
DMDMi132517.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Zinc finger protein RFPPRO_0000056240Add
BLAST

Proteomic databases

EPDiP14373.
MaxQBiP14373.
PaxDbiP14373.
PRIDEiP14373.

PTM databases

iPTMnetiP14373.
PhosphoSiteiP14373.

Expressioni

Tissue specificityi

Expressed in testis namely within the seminiferous tubules.1 Publication

Gene expression databases

BgeeiP14373.
CleanExiHS_TRIM27.
ExpressionAtlasiP14373. baseline and differential.
GenevisibleiP14373. HS.

Organism-specific databases

HPAiHPA048684.
HPA053408.

Interactioni

Subunit structurei

Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4 and EID1. Interacts with MAGED4, MAGEF1 and MAGEL2. Interacts with herpes simplex virus protein ICP0.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K9323EBI-719493,EBI-10174671
A8KAD63EBI-719493,EBI-10174974
E5KN553EBI-719493,EBI-10176944
ABCF3Q9NUQ84EBI-719493,EBI-717672
AENQ8WTP83EBI-719493,EBI-8637627
AESQ081173EBI-719493,EBI-717810
AMOTL2Q9Y2J4-43EBI-719493,EBI-10187270
ARHGEF3Q9NR813EBI-719493,EBI-10312733
ARHGEF5Q127743EBI-719493,EBI-602199
ARMC7Q9H6L43EBI-719493,EBI-742909
ARPINQ7Z6K53EBI-719493,EBI-10258086
ATPAF2Q8N5M13EBI-719493,EBI-1166928
BABAM1Q9NWV83EBI-719493,EBI-745725
BAG1Q999333EBI-719493,EBI-1030678
BAG5Q9UL153EBI-719493,EBI-356517
BEX2Q9BXY83EBI-719493,EBI-745073
BMP7A8K5713EBI-719493,EBI-10174327
BYSLQ138953EBI-719493,EBI-358049
C14orf105Q17R993EBI-719493,EBI-10238351
C20orf195Q9BVV23EBI-719493,EBI-744935
CCDC102BA1A4H13EBI-719493,EBI-10171570
CCDC87Q9NVE43EBI-719493,EBI-749261
CCDC92Q53HC03EBI-719493,EBI-719994
CCDC94Q9BW853EBI-719493,EBI-10300345
CCHCR1Q8TD31-33EBI-719493,EBI-10175300
CDC20BQ86Y333EBI-719493,EBI-10260504
CDC23Q9UJX24EBI-719493,EBI-396137
CDK18Q070023EBI-719493,EBI-746238
CDKL3Q8IVW43EBI-719493,EBI-3919850
CHCHD3Q9NX633EBI-719493,EBI-743375
CKS1BP610243EBI-719493,EBI-456371
CLK2P497603EBI-719493,EBI-750020
CPNE2Q96FN43EBI-719493,EBI-7097057
CSRP2Q165273EBI-719493,EBI-2959737
CSRP2BPQ9H8E83EBI-719493,EBI-750907
DCXO436023EBI-719493,EBI-8646694
DDX6P261963EBI-719493,EBI-351257
DMRT3Q9NQL93EBI-719493,EBI-9679045
DTNBP1Q96EV83EBI-719493,EBI-465804
EHHADHQ084263EBI-719493,EBI-2339219
EIF3DO153713EBI-719493,EBI-353818
EIF3EP602287EBI-719493,EBI-347740
EIF4EP067303EBI-719493,EBI-73440
EIF4E2O605733EBI-719493,EBI-398610
FAM103A1Q9BTL33EBI-719493,EBI-744023
FAM110AQ9BQ893EBI-719493,EBI-1752811
FAM126BQ8IXS83EBI-719493,EBI-8787606
FAM193BQ96PV7-23EBI-719493,EBI-10292648
FAM214AQ32MH53EBI-719493,EBI-2866142
FAM214BQ7L5A33EBI-719493,EBI-745689
FAM64AQ9BSJ63EBI-719493,EBI-2568609
FAM83AQ86UY53EBI-719493,EBI-1384254
FANCMQ8IYD83EBI-719493,EBI-3957237
FARS2O953633EBI-719493,EBI-2513774
FBF1Q8TES7-63EBI-719493,EBI-10244131
FBXW5Q969U63EBI-719493,EBI-741068
FHL3Q96C983EBI-719493,EBI-10229248
FLJ38668C0H5X23EBI-719493,EBI-10176227
FOXB1Q998533EBI-719493,EBI-3916225
FOXC2Q999583EBI-719493,EBI-3956892
GATAD2BQ8WXI93EBI-719493,EBI-923440
GEMP550403EBI-719493,EBI-744104
GFAPP141363EBI-719493,EBI-744302
GFM2Q969S93EBI-719493,EBI-2371750
GLYCTKQ8IVS83EBI-719493,EBI-748515
GNPDA2Q8TDQ73EBI-719493,EBI-10275006
GPANK1O958723EBI-719493,EBI-751540
GRB2P629933EBI-719493,EBI-401755
HAUS1Q96CS23EBI-719493,EBI-2514791
ILKQ134183EBI-719493,EBI-747644
INPP5JQ157353EBI-719493,EBI-10236940
IQUBQ8NA543EBI-719493,EBI-10220600
JOSD1Q150404EBI-719493,EBI-2510602
KANSL1I3L4J33EBI-719493,EBI-10178305
KAT5Q929933EBI-719493,EBI-399080
KCTD9Q7L2733EBI-719493,EBI-4397613
KIAA1683Q9H0B33EBI-719493,EBI-745878
KIFC3Q9BVG83EBI-719493,EBI-2125614
LASP1Q148473EBI-719493,EBI-742828
LENG1Q96BZ83EBI-719493,EBI-726510
LGALS14Q8TCE93EBI-719493,EBI-10274069
LINC00526Q96FQ73EBI-719493,EBI-10286106
LINGO1Q96FE53EBI-719493,EBI-719955
LMO1P258003EBI-719493,EBI-8639312
MAD2L2Q9UI953EBI-719493,EBI-77889
MAPKBP1O603363EBI-719493,EBI-947402
MAT2BQ9NZL93EBI-719493,EBI-10317491
MCM7P339933EBI-719493,EBI-355924
MEMO1Q9Y3163EBI-719493,EBI-1104564
MIA3Q5JRA6-23EBI-719493,EBI-10244342
MID2Q9UJV3-23EBI-719493,EBI-10172526
MOSP005403EBI-719493,EBI-1757866
MRPL40Q9NQ503EBI-719493,EBI-1053902
MTMR6Q9Y2173EBI-719493,EBI-766064
NCK2O436393EBI-719493,EBI-713635
NDEL1Q9GZM84EBI-719493,EBI-928842
NEBLO760413EBI-719493,EBI-2880203
NEDD9Q145114EBI-719493,EBI-2108053
NEIL2Q969S23EBI-719493,EBI-10281234
NEK6Q9HC983EBI-719493,EBI-740364
NELFEP186153EBI-719493,EBI-348444
NME7Q9Y5B83EBI-719493,EBI-744782
NOD2Q9HC2910EBI-719493,EBI-7445625
NOTCH2NLQ7Z3S93EBI-719493,EBI-945833
NR1D2Q6NSM03EBI-719493,EBI-10250949
NUDT21O438093EBI-719493,EBI-355720
OAS1P009733EBI-719493,EBI-3932815
PIK3C2BO007505EBI-719493,EBI-641107
PLEKHN1Q494U13EBI-719493,EBI-10241513
POLE2P562823EBI-719493,EBI-713847
POLR1CO151603EBI-719493,EBI-1055079
POLR3CQ9BUI43EBI-719493,EBI-5452779
PPLO604373EBI-719493,EBI-368321
PPP1R18Q6NYC84EBI-719493,EBI-2557469
PRAM1Q96QH23EBI-719493,EBI-2860740
PRKAA1Q131313EBI-719493,EBI-1181405
PRPF31F1T0A53EBI-719493,EBI-10177194
PSMA1P257863EBI-719493,EBI-359352
PSMB1P206183EBI-719493,EBI-372273
PSMB3P497203EBI-719493,EBI-603340
PTPMT1Q8WUK03EBI-719493,EBI-7199479
PTPN23Q9H3S73EBI-719493,EBI-724478
PUS7LQ9H0K63EBI-719493,EBI-5464419
RAB7L1Q6FGU73EBI-719493,EBI-10249635
RBM23Q86U063EBI-719493,EBI-780319
RBM41Q96IZ53EBI-719493,EBI-740773
RCOR3Q9P2K33EBI-719493,EBI-743428
RHPN1Q8TCX53EBI-719493,EBI-746325
RIBC1Q8N4433EBI-719493,EBI-10265323
RNF213Q63HN8-63EBI-719493,EBI-10248548
SCNM1Q9BWG63EBI-719493,EBI-748391
SDCBPO005603EBI-719493,EBI-727004
SFRS2Q6NXQ03EBI-719493,EBI-10251550
SH2D4AQ9H7883EBI-719493,EBI-747035
SH2D4AQ9H788-23EBI-719493,EBI-10308083
SIAH1Q8IUQ43EBI-719493,EBI-747107
SLC15A3Q05CH43EBI-719493,EBI-10223741
SNRPAP090123EBI-719493,EBI-607085
SNRPB2P085793EBI-719493,EBI-1053651
SORBS3O605043EBI-719493,EBI-741237
SPATA2Q9UM823EBI-719493,EBI-744066
SPATC1LQ9H0A93EBI-719493,EBI-372911
STAMBPL1Q96FJ03EBI-719493,EBI-745021
STK16O757163EBI-719493,EBI-749295
STK25O005063EBI-719493,EBI-618295
TBC1D22BQ9NU193EBI-719493,EBI-8787464
TCEA2Q155603EBI-719493,EBI-710310
TCHPQ9BT923EBI-719493,EBI-740781
TEAD4D3DUQ63EBI-719493,EBI-10176734
TMSB4XQ0P5Q03EBI-719493,EBI-10226570
TPM3Q5VU623EBI-719493,EBI-10184033
TPRKBQ9Y3C43EBI-719493,EBI-750123
TRIM42A1L4B63EBI-719493,EBI-10172216
TSGA10IPQ3SY003EBI-719493,EBI-10241197
TSHZ3A1L0U73EBI-719493,EBI-10171826
TTLL10Q6ZVT03EBI-719493,EBI-7844656
TUFT1Q9NNX14EBI-719493,EBI-2557363
TXNDC9O145303EBI-719493,EBI-707554
USE1Q9NZ433EBI-719493,EBI-742842
USP2O756043EBI-719493,EBI-743272
UTP23Q9BRU93EBI-719493,EBI-5457544
VPS25Q9BRG13EBI-719493,EBI-741945
VPS28Q548N13EBI-719493,EBI-10243107
WDYHV1Q96HA83EBI-719493,EBI-741158
WT1-ASQ062503EBI-719493,EBI-10223946
XPAP230253EBI-719493,EBI-295222
ZC2HC1CQ53FD03EBI-719493,EBI-740767
ZFC3H1G3V1X13EBI-719493,EBI-6448783
ZFYVE21Q9BQ243EBI-719493,EBI-2849569
ZGPATQ8N5A53EBI-719493,EBI-3439227
ZGPATQ8N5A5-23EBI-719493,EBI-10183064
ZMYND19Q96E353EBI-719493,EBI-746595
ZNF250P15622-33EBI-719493,EBI-10177272
ZNF417Q8TAU34EBI-719493,EBI-740727
ZNF446Q96AF53EBI-719493,EBI-740232
ZNF572A1L4E93EBI-719493,EBI-10172590
ZNF572Q7Z3I73EBI-719493,EBI-10257016
ZNF581Q9P0T43EBI-719493,EBI-745520
ZNF79Q159373EBI-719493,EBI-10237274

Protein-protein interaction databases

BioGridi111919. 326 interactions.
IntActiP14373. 266 interactions.
MINTiMINT-1409274.
STRINGi9606.ENSP00000366404.

Structurei

3D structure databases

ProteinModelPortaliP14373.
SMRiP14373. Positions 2-56, 89-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini298 – 492195B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 17241Sequence analysisAdd
BLAST
Coiled coili282 – 31130Sequence analysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5742RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 12732B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITF0. Eukaryota.
ENOG410Z5PW. LUCA.
GeneTreeiENSGT00760000118893.
HOVERGENiHBG001357.
InParanoidiP14373.
KOiK12009.
OMAiFSGHVGS.
PhylomeDBiP14373.
TreeFamiTF350411.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 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. AlignAdd to basket

Isoform Alpha (identifier: P14373-1) [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
MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN
60 70 80 90 100
VSCPQCRETF PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR
110 120 130 140 150
EPLKLYCEED QMPICVVCDR SREHRGHSVL PLEEAVEGFK EQIQNQLDHL
160 170 180 190 200
KRVKDLKKRR RAQGEQARAE LLSLTQMERE KIVWEFEQLY HSLKEHEYRL
210 220 230 240 250
LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ QQPTRELLQD
260 270 280 290 300
IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS
310 320 330 340 350
DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN
360 370 380 390 400
PERFNLFPCV LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS
410 420 430 440 450
APQNGFWAVS LWYGKEYWAL TSPMTALPLR TPLQRVGIFL DYDAGEVSFY
460 470 480 490 500
NVTERCHTFT FSHATFCGPV RPYFSLSYSG GKSAAPLIIC PMSGIDGFSG
510
HVGNHGHSME TSP
Length:513
Mass (Da):58,490
Last modified:January 1, 1990 - v1
Checksum:i6F963D9048D8A731
GO
Isoform Beta (identifier: P14373-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:358
Mass (Da):41,439
Checksum:iD722163761427340
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4461E → K in AAH66924 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei354 – 3585FNLFP → SPSTT in isoform Beta. 1 PublicationVSP_010896
Alternative sequencei359 – 513155Missing in isoform Beta. 1 PublicationVSP_010897Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: CAI18618.1.
BX000360, BX537153 Genomic DNA. Translation: CAI18619.1.
BX537153, BX000360 Genomic DNA. Translation: CAI18645.1.
BX537153, BX000360 Genomic DNA. Translation: CAI18646.1.
AL662859 Genomic DNA. Translation: CAM24901.1.
AL662871 Genomic DNA. Translation: CAM25659.1.
BX005144, BX119924 Genomic DNA. Translation: CAM25871.1.
BX005144, BX119924 Genomic DNA. Translation: CAM25872.1.
BX119924, BX005144 Genomic DNA. Translation: CAM26230.1.
BX119924, BX005144 Genomic DNA. Translation: CAM26231.1.
CR759942 Genomic DNA. Translation: CAQ07942.1.
CR759942 Genomic DNA. Translation: CAQ07943.1.
Z84474, Z84476 Genomic DNA. Translation: CAB06480.2.
Z84476, Z84474 Genomic DNA. Translation: CAI19959.1.
CH471081 Genomic DNA. Translation: EAX03176.1.
CH471081 Genomic DNA. Translation: EAX03177.1.
BC013580 mRNA. Translation: AAH13580.1.
BC066924 mRNA. Translation: AAH66924.1.
CCDSiCCDS4654.1. [P14373-1]
PIRiA28101. TVHURF.
RefSeqiNP_006501.1. NM_006510.4. [P14373-1]
UniGeneiHs.440382.

Genome annotation databases

EnsembliENST00000377194; ENSP00000366399; ENSG00000204713. [P14373-2]
ENST00000377199; ENSP00000366404; ENSG00000204713. [P14373-1]
ENST00000400720; ENSP00000383555; ENSG00000215641. [P14373-1]
ENST00000412687; ENSP00000416281; ENSG00000234495. [P14373-2]
ENST00000417660; ENSP00000411026; ENSG00000215641. [P14373-2]
ENST00000427689; ENSP00000388622; ENSG00000237071. [P14373-2]
ENST00000431123; ENSP00000414793; ENSG00000229006. [P14373-1]
ENST00000435528; ENSP00000405229; ENSG00000237071. [P14373-1]
ENST00000437160; ENSP00000392787; ENSG00000234495. [P14373-1]
ENST00000452265; ENSP00000412445; ENSG00000229006. [P14373-2]
GeneIDi5987.
KEGGihsa:5987.
UCSCiuc003nlr.4. human. [P14373-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: CAI18618.1.
BX000360, BX537153 Genomic DNA. Translation: CAI18619.1.
BX537153, BX000360 Genomic DNA. Translation: CAI18645.1.
BX537153, BX000360 Genomic DNA. Translation: CAI18646.1.
AL662859 Genomic DNA. Translation: CAM24901.1.
AL662871 Genomic DNA. Translation: CAM25659.1.
BX005144, BX119924 Genomic DNA. Translation: CAM25871.1.
BX005144, BX119924 Genomic DNA. Translation: CAM25872.1.
BX119924, BX005144 Genomic DNA. Translation: CAM26230.1.
BX119924, BX005144 Genomic DNA. Translation: CAM26231.1.
CR759942 Genomic DNA. Translation: CAQ07942.1.
CR759942 Genomic DNA. Translation: CAQ07943.1.
Z84474, Z84476 Genomic DNA. Translation: CAB06480.2.
Z84476, Z84474 Genomic DNA. Translation: CAI19959.1.
CH471081 Genomic DNA. Translation: EAX03176.1.
CH471081 Genomic DNA. Translation: EAX03177.1.
BC013580 mRNA. Translation: AAH13580.1.
BC066924 mRNA. Translation: AAH66924.1.
CCDSiCCDS4654.1. [P14373-1]
PIRiA28101. TVHURF.
RefSeqiNP_006501.1. NM_006510.4. [P14373-1]
UniGeneiHs.440382.

3D structure databases

ProteinModelPortaliP14373.
SMRiP14373. Positions 2-56, 89-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111919. 326 interactions.
IntActiP14373. 266 interactions.
MINTiMINT-1409274.
STRINGi9606.ENSP00000366404.

PTM databases

iPTMnetiP14373.
PhosphoSiteiP14373.

Polymorphism and mutation databases

BioMutaiTRIM27.
DMDMi132517.

Proteomic databases

EPDiP14373.
MaxQBiP14373.
PaxDbiP14373.
PRIDEiP14373.

Protocols and materials databases

DNASUi5987.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377194; ENSP00000366399; ENSG00000204713. [P14373-2]
ENST00000377199; ENSP00000366404; ENSG00000204713. [P14373-1]
ENST00000400720; ENSP00000383555; ENSG00000215641. [P14373-1]
ENST00000412687; ENSP00000416281; ENSG00000234495. [P14373-2]
ENST00000417660; ENSP00000411026; ENSG00000215641. [P14373-2]
ENST00000427689; ENSP00000388622; ENSG00000237071. [P14373-2]
ENST00000431123; ENSP00000414793; ENSG00000229006. [P14373-1]
ENST00000435528; ENSP00000405229; ENSG00000237071. [P14373-1]
ENST00000437160; ENSP00000392787; ENSG00000234495. [P14373-1]
ENST00000452265; ENSP00000412445; ENSG00000229006. [P14373-2]
GeneIDi5987.
KEGGihsa:5987.
UCSCiuc003nlr.4. human. [P14373-1]

Organism-specific databases

CTDi5987.
GeneCardsiTRIM27.
HGNCiHGNC:9975. TRIM27.
HPAiHPA048684.
HPA053408.
MalaCardsiTRIM27.
MIMi602165. gene.
neXtProtiNX_P14373.
Orphaneti146. Papillary or follicular thyroid carcinoma.
PharmGKBiPA162406956.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITF0. Eukaryota.
ENOG410Z5PW. LUCA.
GeneTreeiENSGT00760000118893.
HOVERGENiHBG001357.
InParanoidiP14373.
KOiK12009.
OMAiFSGHVGS.
PhylomeDBiP14373.
TreeFamiTF350411.

Enzyme and pathway databases

SIGNORiP14373.

Miscellaneous databases

ChiTaRSiTRIM27. human.
GeneWikiiTRIM27.
GenomeRNAii5987.
PROiP14373.
SOURCEiSearch...

Gene expression databases

BgeeiP14373.
CleanExiHS_TRIM27.
ExpressionAtlasiP14373. baseline and differential.
GenevisibleiP14373. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR020457. Znf_B-box_chordata.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01406. BBOXZNFINGER.
PR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  2. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Testis and Uterus.
  6. "ret transforming gene encodes a fusion protein homologous to tyrosine kinases."
    Takahashi M., Cooper G.M.
    Mol. Cell. Biol. 7:1378-1385(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH RET.
  7. Cited for: SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PML.
  10. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3S6.
  11. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPC1, FUNCTION.
  12. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD4.
  15. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH RET.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EID1.
  17. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  18. "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases."
    Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.
    Mol. Cell 39:963-974(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGED4; MAGEF1 AND MAGEL2.
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2beta."
    Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J., Salamon R.S., Backer J.M., Skolnik E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS UBIQUITIN LIGASE, INTERACTION WITH PIK3C2B.
  21. "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAGEL2, SUBCELLULAR LOCATION.
  22. "Identification of TRIM27 as a novel degradation target of Herpes Simplex Virus 1 ICP0."
    Conwell S.E., White A.E., Harper J.W., Knipe D.M.
    J. Virol. 89:220-229(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPES SIMPLEX VIRUS ICP0.

Entry informationi

Entry nameiTRI27_HUMAN
AccessioniPrimary (citable) accession number: P14373
Secondary accession number(s): A2BE15
, Q5RJA8, Q5ST26, Q6LA73, Q6NXR9, Q9BZY6, Q9UJL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 8, 2016
This is version 184 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.