RN121_MOUSE
ID RN121_MOUSE Reviewed; 327 AA.
AC Q8R1Z9; Q3TXH5; Q8BP06; Q8BSB1; Q9D4X4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RING finger protein 121;
GN Name=Rnf121;
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 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, and Muellerian duct;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R1Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1Z9-2; Sequence=VSP_021683;
CC Name=3;
CC IsoId=Q8R1Z9-3; Sequence=VSP_021684;
CC -!- SIMILARITY: Belongs to the RNF121 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK016037; BAB30089.2; -; mRNA.
DR EMBL; AK034806; BAC28837.1; -; mRNA.
DR EMBL; AK078509; BAC37314.1; ALT_INIT; mRNA.
DR EMBL; AK159260; BAE34941.1; -; mRNA.
DR EMBL; AK169089; BAE40873.1; -; mRNA.
DR EMBL; AK168821; BAE40648.1; -; mRNA.
DR EMBL; BC022686; AAH22686.1; -; mRNA.
DR CCDS; CCDS21523.1; -. [Q8R1Z9-1]
DR RefSeq; NP_083487.2; NM_029211.2. [Q8R1Z9-1]
DR RefSeq; XP_006508338.1; XM_006508275.3. [Q8R1Z9-3]
DR AlphaFoldDB; Q8R1Z9; -.
DR BioGRID; 217307; 2.
DR STRING; 10090.ENSMUSP00000094396; -.
DR iPTMnet; Q8R1Z9; -.
DR PhosphoSitePlus; Q8R1Z9; -.
DR EPD; Q8R1Z9; -.
DR MaxQB; Q8R1Z9; -.
DR PaxDb; Q8R1Z9; -.
DR PeptideAtlas; Q8R1Z9; -.
DR PRIDE; Q8R1Z9; -.
DR ProteomicsDB; 300527; -. [Q8R1Z9-1]
DR ProteomicsDB; 300528; -. [Q8R1Z9-2]
DR ProteomicsDB; 300529; -. [Q8R1Z9-3]
DR Antibodypedia; 16872; 101 antibodies from 20 providers.
DR DNASU; 75212; -.
DR Ensembl; ENSMUST00000096639; ENSMUSP00000094396; ENSMUSG00000070426. [Q8R1Z9-1]
DR Ensembl; ENSMUST00000106953; ENSMUSP00000102566; ENSMUSG00000070426. [Q8R1Z9-2]
DR GeneID; 75212; -.
DR KEGG; mmu:75212; -.
DR UCSC; uc009iqg.1; mouse. [Q8R1Z9-1]
DR CTD; 55298; -.
DR MGI; MGI:1922462; Rnf121.
DR VEuPathDB; HostDB:ENSMUSG00000070426; -.
DR eggNOG; KOG1734; Eukaryota.
DR GeneTree; ENSGT00390000013075; -.
DR InParanoid; Q8R1Z9; -.
DR OMA; HQQHMDL; -.
DR OrthoDB; 1167893at2759; -.
DR PhylomeDB; Q8R1Z9; -.
DR TreeFam; TF314357; -.
DR BioGRID-ORCS; 75212; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf121; mouse.
DR PRO; PR:Q8R1Z9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R1Z9; protein.
DR Bgee; ENSMUSG00000070426; Expressed in embryonic brain and 236 other tissues.
DR ExpressionAtlas; Q8R1Z9; baseline and differential.
DR Genevisible; Q8R1Z9; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040176; RNF121/RNF175.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13407; PTHR13407; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H920"
FT CHAIN 2..327
FT /note="RING finger protein 121"
FT /id="PRO_0000261408"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 226..276
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H920"
FT VAR_SEQ 2..21
FT /note="AAVVEVEVGGGALAERELDE -> FCQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021683"
FT VAR_SEQ 2..21
FT /note="AAVVEVEVGGGALAERELDE -> RRVQADLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021684"
FT CONFLICT 56
FT /note="L -> I (in Ref. 1; BAC37314)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> G (in Ref. 1; BAB30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="H -> T (in Ref. 1; BAB30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="K -> N (in Ref. 1; BAB30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="Y -> C (in Ref. 1; BAB30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="T -> A (in Ref. 1; BAB30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="P -> H (in Ref. 1; BAE34941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37987 MW; 7A18948904669209 CRC64;
MAAVVEVEVG GGALAERELD EVDMSDLSPE EQWRVEHARM HAKHRGHEAM HAEMVLILIA
TLVVAQLLLV QWKQRHPRSY NMVTLFQMWV VPLYFTVKLH WWRFLVIWIF FSAVTAFVTF
RATRKPLVQT TPRLVYKWFL LIYKISYATG IVGYMAVMFT LFGLNLLFKI KPEDAMDFGI
SLLFYGLYYG VLERDFAEMC ADYMASTIGF YSESGMPTKH LSDSVCAVCG QQIFVDVNEE
GIIENTYRLS CNHVFHEFCI RGWCIVGKKQ TCPYCKEKVD LKRMFSNPWE RPHVMYGQLL
DWLRYLVAWQ PVIIGLVQGI SYILGLE
