RNF25_MOUSE
ID RNF25_MOUSE Reviewed; 456 AA.
AC Q9QZR0; Q3TAL8; Q9DCW7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 ubiquitin-protein ligase RNF25;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 25;
DE AltName: Full=RING finger protein AO7;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF25 {ECO:0000305};
GN Name=Rnf25;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-134; CYS-137;
RP CYS-152; HIS-157; CYS-158 AND CYS-160, INTERACTION WITH UBE2D2; UBE2E1 AND
RP UBE2E3, UBIQUITINATION, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell lymphoma;
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH NKD2.
RX PubMed=18757723; DOI=10.1073/pnas.0806298105;
RA Ding W., Li C., Hu T., Graves-Deal R., Fotia A.B., Weissman A.M.,
RA Coffey R.J.;
RT "EGF receptor-independent action of TGF-alpha protects Naked2 from AO7-
RT mediated ubiquitylation and proteasomal degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13433-13438(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of NKD2. Stimulates transcription
CC mediated by NF-kappa-B (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18757723}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBE2D2, and may also interact with UBE2E1 and
CC UBE2E3. Interacts with RELA (By similarity). Interacts with NKD2.
CC {ECO:0000250, ECO:0000269|PubMed:10500182,
CC ECO:0000269|PubMed:18757723}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10500182}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
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DR EMBL; AF171060; AAD48057.1; -; mRNA.
DR EMBL; AK002399; BAB22071.1; -; mRNA.
DR EMBL; AK171752; BAE42650.1; -; mRNA.
DR EMBL; BC022715; AAH22715.1; -; mRNA.
DR EMBL; BC048821; AAH48821.1; -; mRNA.
DR CCDS; CCDS15052.1; -.
DR RefSeq; NP_001292159.1; NM_001305230.1.
DR RefSeq; NP_067288.2; NM_021313.3.
DR AlphaFoldDB; Q9QZR0; -.
DR SMR; Q9QZR0; -.
DR BioGRID; 208313; 5.
DR STRING; 10090.ENSMUSP00000027357; -.
DR iPTMnet; Q9QZR0; -.
DR PhosphoSitePlus; Q9QZR0; -.
DR EPD; Q9QZR0; -.
DR MaxQB; Q9QZR0; -.
DR PaxDb; Q9QZR0; -.
DR PRIDE; Q9QZR0; -.
DR ProteomicsDB; 300457; -.
DR Antibodypedia; 34282; 156 antibodies from 28 providers.
DR DNASU; 57751; -.
DR Ensembl; ENSMUST00000027357; ENSMUSP00000027357; ENSMUSG00000026171.
DR GeneID; 57751; -.
DR KEGG; mmu:57751; -.
DR UCSC; uc007bms.3; mouse.
DR CTD; 64320; -.
DR MGI; MGI:1890215; Rnf25.
DR VEuPathDB; HostDB:ENSMUSG00000026171; -.
DR eggNOG; KOG4445; Eukaryota.
DR GeneTree; ENSGT00390000001557; -.
DR InParanoid; Q9QZR0; -.
DR OMA; HHRPWDC; -.
DR OrthoDB; 968943at2759; -.
DR PhylomeDB; Q9QZR0; -.
DR TreeFam; TF324097; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57751; 0 hits in 59 CRISPR screens.
DR PRO; PR:Q9QZR0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QZR0; protein.
DR Bgee; ENSMUSG00000026171; Expressed in retinal neural layer and 250 other tissues.
DR ExpressionAtlas; Q9QZR0; baseline and differential.
DR Genevisible; Q9QZR0; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039133; RNF25.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13198; PTHR13198; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..456
FT /note="E3 ubiquitin-protein ligase RNF25"
FT /id="PRO_0000056067"
FT DOMAIN 18..127
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT ZN_FING 134..199
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 269..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 134
FT /note="C->S: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT MUTAGEN 137
FT /note="C->S: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT MUTAGEN 152
FT /note="C->S: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT MUTAGEN 157
FT /note="H->C: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT MUTAGEN 158
FT /note="C->S: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT MUTAGEN 160
FT /note="C->S: No E2 binding. Loss of ubiquitination
FT activity."
FT /evidence="ECO:0000269|PubMed:10500182"
FT CONFLICT 182..183
FT /note="QH -> HD (in Ref. 1; AAD48057)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="E -> K (in Ref. 2; BAB22071)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="R -> G (in Ref. 2; BAB22071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 51227 MW; 75FA1351F8E9C4E3 CRC64;
MAASASTAAG EEDWVLPSEV EVLESIYLDE LQVMKGNGRS PWEIFITLHP ATAEVQDSQF
VCFTLVLRIP VQYPHEVPQI SIRNPRGLSD EQIHKISQAL GHVAKEGLGT AMLYELIEKG
KEILTDNNIP HGQCVICLYG FQEKEAFTKT PCYHYFHCHC LARYIQHMEQ ELTTQEQEQE
RQHVVTKQKA VGVQCPVCRE PLVYDLASLK AAPEPQQPME LYQPSAESLR QQEELKLLYQ
RQQEKGGIID LEAERNRYFI SLQQPPAALE PESAVDVSRE PQPPNALSAE QSTSLADQST
LPTSLPMTTQ YTYEKTSGAG PNQQRPGETQ KSVLDPPRHG RGSWRQYDRR HPKGGECCTP
KGTSEIHELP PPEKPLKETV DLKAEPRNKG LTGHPQEKGP GSWQGPSARR TRDCARWERS
KNRTPGSCYP HLPRGQGAYR SGTRREPLGL ESEEGS
