RN214_MOUSE
ID RN214_MOUSE Reviewed; 668 AA.
AC Q8BFU3; Q3UWM9; Q6P3A7; Q80VI8; Q8BNZ6; Q8CC56; Q8CCP2; Q8CE92; Q8R5B9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=RING finger protein 214;
GN Name=Rnf214;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Diencephalon, Egg, Eye, Olfactory bulb, Skin, Spinal ganglion, and
RC Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Brain, Mammary gland, and 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-196 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BFU3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFU3-2; Sequence=VSP_023774, VSP_023775;
CC Name=3;
CC IsoId=Q8BFU3-3; Sequence=VSP_023773;
CC Name=4;
CC IsoId=Q8BFU3-4; Sequence=VSP_023776;
CC Name=5;
CC IsoId=Q8BFU3-5; Sequence=VSP_023774;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC28499.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC37365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE22885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK028768; BAC26109.1; -; mRNA.
DR EMBL; AK030208; BAC26843.1; -; mRNA.
DR EMBL; AK032376; BAC27844.1; -; mRNA.
DR EMBL; AK033867; BAC28499.1; ALT_SEQ; mRNA.
DR EMBL; AK051527; BAC34663.1; -; mRNA.
DR EMBL; AK078706; BAC37365.1; ALT_INIT; mRNA.
DR EMBL; AK136229; BAE22885.1; ALT_INIT; mRNA.
DR EMBL; BC023073; AAH23073.1; -; mRNA.
DR EMBL; BC049909; AAH49909.1; ALT_INIT; mRNA.
DR EMBL; BC064100; AAH64100.1; -; mRNA.
DR EMBL; BC094247; AAH94247.1; -; mRNA.
DR CCDS; CCDS23136.1; -. [Q8BFU3-1]
DR CCDS; CCDS80987.1; -. [Q8BFU3-5]
DR CCDS; CCDS80988.1; -. [Q8BFU3-2]
DR RefSeq; NP_001297768.1; NM_001310839.1. [Q8BFU3-5]
DR RefSeq; NP_001297769.1; NM_001310840.1. [Q8BFU3-2]
DR RefSeq; NP_848824.1; NM_178709.4. [Q8BFU3-1]
DR RefSeq; XP_011240801.1; XM_011242499.2.
DR RefSeq; XP_011240804.1; XM_011242502.2.
DR RefSeq; XP_011240805.1; XM_011242503.2. [Q8BFU3-2]
DR RefSeq; XP_017168820.1; XM_017313331.1.
DR AlphaFoldDB; Q8BFU3; -.
DR SMR; Q8BFU3; -.
DR BioGRID; 231638; 2.
DR IntAct; Q8BFU3; 1.
DR MINT; Q8BFU3; -.
DR STRING; 10090.ENSMUSP00000060941; -.
DR iPTMnet; Q8BFU3; -.
DR PhosphoSitePlus; Q8BFU3; -.
DR EPD; Q8BFU3; -.
DR jPOST; Q8BFU3; -.
DR MaxQB; Q8BFU3; -.
DR PaxDb; Q8BFU3; -.
DR PeptideAtlas; Q8BFU3; -.
DR PRIDE; Q8BFU3; -.
DR ProteomicsDB; 299845; -. [Q8BFU3-1]
DR ProteomicsDB; 299846; -. [Q8BFU3-2]
DR ProteomicsDB; 299847; -. [Q8BFU3-3]
DR ProteomicsDB; 299848; -. [Q8BFU3-4]
DR ProteomicsDB; 299849; -. [Q8BFU3-5]
DR Antibodypedia; 32345; 37 antibodies from 14 providers.
DR DNASU; 235315; -.
DR Ensembl; ENSMUST00000058720; ENSMUSP00000060941; ENSMUSG00000042790. [Q8BFU3-1]
DR Ensembl; ENSMUST00000160699; ENSMUSP00000123754; ENSMUSG00000042790. [Q8BFU3-1]
DR Ensembl; ENSMUST00000161187; ENSMUSP00000124296; ENSMUSG00000042790. [Q8BFU3-5]
DR Ensembl; ENSMUST00000161203; ENSMUSP00000123995; ENSMUSG00000042790. [Q8BFU3-2]
DR Ensembl; ENSMUST00000162369; ENSMUSP00000149889; ENSMUSG00000042790. [Q8BFU3-4]
DR GeneID; 235315; -.
DR KEGG; mmu:235315; -.
DR UCSC; uc009pgk.1; mouse. [Q8BFU3-1]
DR UCSC; uc009pgl.1; mouse. [Q8BFU3-5]
DR UCSC; uc009pgm.1; mouse. [Q8BFU3-2]
DR CTD; 257160; -.
DR MGI; MGI:2444451; Rnf214.
DR VEuPathDB; HostDB:ENSMUSG00000042790; -.
DR eggNOG; ENOG502QTPR; Eukaryota.
DR GeneTree; ENSGT00940000159470; -.
DR HOGENOM; CLU_019742_1_0_1; -.
DR InParanoid; Q8BFU3; -.
DR OMA; QEMTSEK; -.
DR OrthoDB; 497367at2759; -.
DR PhylomeDB; Q8BFU3; -.
DR TreeFam; TF333981; -.
DR BioGRID-ORCS; 235315; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rnf214; mouse.
DR PRO; PR:Q8BFU3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BFU3; protein.
DR Bgee; ENSMUSG00000042790; Expressed in retinal neural layer and 245 other tissues.
DR ExpressionAtlas; Q8BFU3; baseline and differential.
DR Genevisible; Q8BFU3; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT CHAIN 2..668
FT /note="RING finger protein 214"
FT /id="PRO_0000280547"
FT ZN_FING 623..665
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 220..379
FT /evidence="ECO:0000255"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND24"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023773"
FT VAR_SEQ 52..206
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023774"
FT VAR_SEQ 615
FT /note="Q -> QPLGRIRALHPAPLAQISPPMFLPSAQVSYPGRSSH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023775"
FT VAR_SEQ 616..668
FT /note="APPTCKLCLMCQKLVQPSELHPMACTHALHKECIKFWAQTNTNDTCPFCPTL
FT K -> VRGASGRELRPAERLRKKPTRRSGHEEIRARNICSAFLIIRSEFLLPSFLPSFL
FT PSFLPSFLPFFLSFLLVKFICVYVCVCVLCGSRKTTCGSPFSSTM (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023776"
FT CONFLICT 361
FT /note="E -> K (in Ref. 1; BAE22885)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="P -> H (in Ref. 1; BAC37365)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="Q -> H (in Ref. 1; BAC37365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 73625 MW; ECF534164BCCDE7E CRC64;
MAASEVAGLG AGTPSPSESS ALCASKSDES LPDGLSPKDS AQKQKNLSPP SVSSQMITKE
SNRNAHLEHP EQNPGSSVGD TSAAHEEVVG ENLVATALCL SGNGSQSDLK DLTNPAGEEG
DTSLRESLHP VTRSLKAGCH SKQLASGNCS EEKCPAASVL KEGSRDAGLD LLPVVPPANG
VEGVRVDQDD DQDSSSLKLS QNIAVQTDFK TADSEVNTDQ DIEKNLDKMM TERTLLKERY
QEVLDKQRQV ESQLQVQLKQ LQQRREEEMK NHQEILKAIQ DVTIKREETK KKIEKEKKEF
LQKEQDLKAE IEKLCEKGRR EVWEMELDRL KNQDGEINRN IMEETERAWK AEILSLESRK
ELLVLKLEEA EKEAELHLTY LKSTPPTLET VRSKQEWETR LNGVRIMKKN VRDQFNSHIQ
LVRNGAKLSS LPQIPTPTLP PPPSEADFML QVFQPSPSLT PRMPFSIGQV TMPMVMPSAD
PRSLSFPILN PALSQSSQPS PPLPGSHGRN SPGLGSLVSP HGPHMPPAAS IPPPPGLGGI
KASSETPRPQ PVDKLEKILE KLLTRFPQCN KAQMTNILQQ IKTARTTMAG LTMEELIQLV
AARLAEHERV ASSTQAPPTC KLCLMCQKLV QPSELHPMAC THALHKECIK FWAQTNTNDT
CPFCPTLK
