RN181_MOUSE
ID RN181_MOUSE Reviewed; 165 AA.
AC Q9CY62; Q8CEU6; Q9D2T4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase RNF181 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9P0P0};
DE AltName: Full=RING finger protein 181;
GN Name=Rnf181 {ECO:0000312|MGI:MGI:1913760};
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, and DBA/2J;
RC TISSUE=Amnion, Head, Liver, Placenta, and 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] (ISOFORM 1).
RC STRAIN=FVB/N, and FVB/N-3; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Catalyzes
CC monoubiquitination of 26S proteasome subunit PSMC2/RPT1.
CC {ECO:0000250|UniProtKB:Q9P0P0}.
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; Evidence={ECO:0000250|UniProtKB:Q9P0P0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9P0P0}.
CC -!- SUBUNIT: Directly interacts with ITGA2B and, as a result, with integrin
CC ITGA2B/ITGB3. There is no evidence that integrin ITGA2B/ITGB3 is an
CC endogenous substrate for RNF181-directed ubiquitination.
CC {ECO:0000250|UniProtKB:Q9P0P0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CY62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CY62-2; Sequence=VSP_027006;
CC Name=3;
CC IsoId=Q9CY62-3; Sequence=VSP_027007;
CC -!- PTM: Auto-ubiquitinated as part of the enzymatic reaction.
CC {ECO:0000250|UniProtKB:Q9P0P0}.
CC -!- SIMILARITY: Belongs to the RNF181 family. {ECO:0000305}.
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DR EMBL; AK010854; BAB27224.1; -; mRNA.
DR EMBL; AK014094; BAC25424.1; -; mRNA.
DR EMBL; AK159788; BAE35371.1; -; mRNA.
DR EMBL; AK166904; BAE39106.1; -; mRNA.
DR EMBL; AK166995; BAE39174.1; -; mRNA.
DR EMBL; AK167396; BAE39485.1; -; mRNA.
DR EMBL; AK167633; BAE39684.1; -; mRNA.
DR EMBL; AK167935; BAE39939.1; -; mRNA.
DR EMBL; AK168670; BAE40520.1; -; mRNA.
DR EMBL; AK018849; BAB31462.1; -; mRNA.
DR EMBL; BC005559; AAH05559.1; -; mRNA.
DR EMBL; BC083119; AAH83119.1; -; mRNA.
DR CCDS; CCDS20240.1; -. [Q9CY62-1]
DR CCDS; CCDS85064.1; -. [Q9CY62-2]
DR CCDS; CCDS90058.1; -. [Q9CY62-3]
DR RefSeq; NP_001318096.1; NM_001331167.1. [Q9CY62-2]
DR RefSeq; NP_001318097.1; NM_001331168.1. [Q9CY62-3]
DR RefSeq; NP_001318098.1; NM_001331169.1. [Q9CY62-2]
DR RefSeq; NP_079883.3; NM_025607.4. [Q9CY62-1]
DR AlphaFoldDB; Q9CY62; -.
DR SMR; Q9CY62; -.
DR BioGRID; 211526; 27.
DR STRING; 10090.ENSMUSP00000066128; -.
DR iPTMnet; Q9CY62; -.
DR PhosphoSitePlus; Q9CY62; -.
DR EPD; Q9CY62; -.
DR MaxQB; Q9CY62; -.
DR PaxDb; Q9CY62; -.
DR PeptideAtlas; Q9CY62; -.
DR PRIDE; Q9CY62; -.
DR ProteomicsDB; 299841; -. [Q9CY62-1]
DR ProteomicsDB; 299842; -. [Q9CY62-2]
DR ProteomicsDB; 299843; -. [Q9CY62-3]
DR Antibodypedia; 31897; 102 antibodies from 23 providers.
DR Ensembl; ENSMUST00000069580; ENSMUSP00000066128; ENSMUSG00000055850. [Q9CY62-1]
DR Ensembl; ENSMUST00000069595; ENSMUSP00000070370; ENSMUSG00000055850. [Q9CY62-3]
DR Ensembl; ENSMUST00000154098; ENSMUSP00000138327; ENSMUSG00000055850. [Q9CY62-2]
DR GeneID; 66510; -.
DR KEGG; mmu:66510; -.
DR UCSC; uc009cii.1; mouse. [Q9CY62-1]
DR UCSC; uc009cij.1; mouse. [Q9CY62-3]
DR CTD; 51255; -.
DR MGI; MGI:1913760; Rnf181.
DR VEuPathDB; HostDB:ENSMUSG00000055850; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000165973; -.
DR HOGENOM; CLU_2173682_0_0_1; -.
DR InParanoid; Q9CY62; -.
DR OMA; EHLHGAM; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q9CY62; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66510; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf181; mouse.
DR PRO; PR:Q9CY62; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CY62; protein.
DR Bgee; ENSMUSG00000055850; Expressed in proximal tubule and 75 other tissues.
DR ExpressionAtlas; Q9CY62; baseline and differential.
DR Genevisible; Q9CY62; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..165
FT /note="E3 ubiquitin-protein ligase RNF181"
FT /id="PRO_0000295175"
FT ZN_FING 88..129
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0P0"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027006"
FT VAR_SEQ 17..85
FT /note="REARNNMLLELARRVRGAWSWAPGGRSLFNRMDFEDLGLVDWEHHLPPPAAK
FT AVVESLPRTVISSAKAD -> H (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027007"
SQ SEQUENCE 165 AA; 19101 MW; A53ADB27ECCDDCAE CRC64;
MASYFDEHDC EPLNPEREAR NNMLLELARR VRGAWSWAPG GRSLFNRMDF EDLGLVDWEH
HLPPPAAKAV VESLPRTVIS SAKADLKCPV CLLEFEAEET VIEMPCHHLF HSNCILPWLS
KTNSCPLCRH ELPTDDDSYE EHKKDKARRQ QQQHRLENLH GAMYT
