UBR2_MOUSE
ID UBR2_MOUSE Reviewed; 1755 AA.
AC Q6WKZ8; Q6DIB9; Q80U31; Q8BUL9; Q8CGW0; Q8K2I6; Q8R0V7; Q8R130;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase UBR2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:31268597};
DE AltName: Full=N-recognin-2;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR2;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-2;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-II;
GN Name=Ubr2; Synonyms=Kiaa0349;
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] (ISOFORM 2), INTERACTION WITH UBE2B, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14585983; DOI=10.1128/mcb.23.22.8255-8271.2003;
RA Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W., Sheng J.,
RA Xie Y., Varshavsky A.;
RT "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2
RT ubiquitin ligase of the N-end rule pathway.";
RL Mol. Cell. Biol. 23:8255-8271(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C3H/HeN;
RX PubMed=15548684; DOI=10.1158/0008-5472.can-04-2102;
RA Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W.,
RA Boyle W.J., Lacey D.L., Han H.Q.;
RT "Regulation of protein catabolism by muscle-specific and cytokine-inducible
RT ubiquitin ligase E3alpha-II during cancer cachexia.";
RL Cancer Res. 64:8193-8198(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Brain, Mammary gland, and Salivary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=16311597; DOI=10.1038/ng1681;
RA Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K., Durie P.R.,
RA Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A., Hamel B.C.J.,
RA Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W., Dumic M.,
RA Auslender R., Gil-da-Silva-Lopes V.L., Steinlicht S., Rauh M., Shalev S.A.,
RA Thiel C., Winterpacht A., Kwon Y.T., Varshavsky A., Reis A.;
RT "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes
RT pancreatic dysfunction, malformations and mental retardation (Johanson-
RT Blizzard syndrome).";
RL Nat. Genet. 37:1345-1350(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=16488448; DOI=10.1016/j.mrfmmm.2005.12.016;
RA Ouyang Y., Kwon Y.T., An J.Y., Eller D., Tsai S.-C., Diaz-Perez S.,
RA Troke J.J., Teitell M.A., Marahrens Y.;
RT "Loss of Ubr2, an E3 ubiquitin ligase, leads to chromosome fragility and
RT impaired homologous recombinational repair.";
RL Mutat. Res. 596:64-75(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=16606826; DOI=10.1073/pnas.0601700103;
RA An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.;
RT "Impaired neurogenesis and cardiovascular development in mice lacking the
RT E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2B AND HISTONE H2A.
RX PubMed=20080676; DOI=10.1073/pnas.0910267107;
RA An J.Y., Kim E.-A., Jiang Y., Zakrzewska A., Kim D.E., Lee M.J.,
RA Mook-Jung I., Zhang Y., Kwon Y.T.;
RT "UBR2 mediates transcriptional silencing during spermatogenesis via histone
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1912-1917(2010).
RN [11]
RP INTERACTION WITH TEX19.1 AND TEX19.2.
RX PubMed=21103378; DOI=10.1371/journal.pone.0014017;
RA Yang F., Cheng Y., An J.Y., Kwon Y.T., Eckardt S., Leu N.A.,
RA McLaughlin K.J., Wang P.J.;
RT "The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule
RT pathway, stabilizes Tex19.1 during spermatogenesis.";
RL PLoS ONE 5:E14017-E14017(2010).
RN [12]
RP FUNCTION, INTERACTION WITH L1RE1, AND TISSUE SPECIFICITY.
RX PubMed=28806172; DOI=10.7554/elife.26152;
RA MacLennan M., Garcia-Canadas M., Reichmann J., Khazina E., Wagner G.,
RA Playfoot C.J., Salvador-Palomeque C., Mann A.R., Peressini P., Sanchez L.,
RA Dobie K., Read D., Hung C.C., Eskeland R., Meehan R.R., Weichenrieder O.,
RA Garcia-Perez J.L., Adams I.R.;
RT "Mobilization of LINE-1 retrotransposons is restricted by Tex19.1 in mouse
RT embryonic stem cells.";
RL Elife 6:0-0(2017).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28708824; DOI=10.1371/journal.pgen.1006904;
RA Crichton J.H., Playfoot C.J., MacLennan M., Read D., Cooke H.J.,
RA Adams I.R.;
RT "Tex19.1 promotes Spo11-dependent meiotic recombination in mouse
RT spermatocytes.";
RL PLoS Genet. 13:E1006904-E1006904(2017).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH UBE2O.
RX PubMed=31268597; DOI=10.15252/embj.2019101996;
RA Xu H., Shi J., Gao H., Liu Y., Yang Z., Shao F., Dong N.;
RT "The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome
RT activation by anthrax lethal toxin.";
RL EMBO J. 38:e101996-e101996(2019).
RN [15]
RP FUNCTION, AND PATHWAY.
RX PubMed=30872531; DOI=10.1126/science.aau1208;
RA Chui A.J., Okondo M.C., Rao S.D., Gai K., Griswold A.R., Johnson D.C.,
RA Ball D.P., Taabazuing C.Y., Orth E.L., Vittimberga B.A., Bachovchin D.A.;
RT "N-terminal degradation activates the NLRP1B inflammasome.";
RL Science 364:82-85(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway (PubMed:14585983, PubMed:31268597, PubMed:30872531).
CC Recognizes and binds to proteins bearing specific N-terminal residues
CC that are destabilizing according to the N-end rule, leading to their
CC ubiquitination and subsequent degradation (PubMed:14585983,
CC PubMed:31268597, PubMed:30872531). Plays a critical role in chromatin
CC inactivation and chromosome-wide transcriptional silencing during
CC meiosis via ubiquitination of histone H2A (PubMed:14585983,
CC PubMed:20080676). Binds leucine and is a negative regulator of the
CC leucine-mTOR signaling pathway, thereby controlling cell growth (By
CC similarity). Required for spermatogenesis, promotes, with Tex19.1,
CC SPO11-dependent recombination foci to accumulate and drive robust
CC homologous chromosome synapsis (PubMed:28708824). Polyubiquitinates
CC LINE-1 retrotransposon encoded, LIRE1, which induces degradation,
CC inhibiting LINE-1 retrotransposon mobilization (PubMed:28806172).
CC Catalyzes ubiquitination and degradation of the N-terminal part of
CC Nlrp1b following Nlrp1b activation by pathogens and other damage-
CC associated signals: ubiquitination promotes degradation of the N-
CC terminal part and subsequent release of the cleaved C-terminal part of
CC Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by
CC host cell pyroptosis (PubMed:31268597, PubMed:30872531).
CC {ECO:0000250|UniProtKB:Q8IWV8, ECO:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:20080676, ECO:0000269|PubMed:28708824,
CC ECO:0000269|PubMed:28806172, ECO:0000269|PubMed:30872531,
CC ECO:0000269|PubMed:31268597}.
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:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:31268597};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:30872531}.
CC -!- SUBUNIT: Interacts with UBE2B; promotes the UBE2B-H2A interaction and
CC the ubiquitination of histone H2A by UBE2B and UBR2 (PubMed:14585983,
CC PubMed:20080676). Interacts with RECQL4 (By similarity). Interacts with
CC Tex19.1 and Tex19.2; does not lead to Tex19.1 degradation and
CC stabilizes it (PubMed:21103378). Interacts with L1RE1
CC (PubMed:28806172). Interacts with CASP8 (By similarity). Interacts with
CC ATXN3 (By similarity). Interacts with UBE2O (PubMed:31268597).
CC {ECO:0000250|UniProtKB:Q8IWV8, ECO:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:20080676, ECO:0000269|PubMed:21103378,
CC ECO:0000269|PubMed:28806172, ECO:0000269|PubMed:31268597}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:20080676}. Chromosome {ECO:0000269|PubMed:20080676}.
CC Note=Associated with chromatin during meiosis.
CC {ECO:0000269|PubMed:20080676}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6WKZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6WKZ8-2; Sequence=VSP_015173;
CC Name=3;
CC IsoId=Q6WKZ8-3; Sequence=VSP_015172, VSP_015173;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also expressed
CC in heart, kidney and testis. Expressed in acinar cells of the pancreas.
CC In testes, expressed primarily in spermatocytes. Expressed in
CC cerebellum (PubMed:28806172). {ECO:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:15548684, ECO:0000269|PubMed:16311597,
CC ECO:0000269|PubMed:28806172}.
CC -!- INDUCTION: In models of cancer cachexia, induced specifically at the
CC onset and during the progression of muscle wasting.
CC {ECO:0000269|PubMed:15548684}.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC {ECO:0000250|UniProtKB:Q8IWV8}.
CC -!- DOMAIN: The UBR-type zinc finger forms a pocket that mediates
CC recognition of type 1 N-degrons. It exhibits preference for Arginine in
CC first position, has poor affinity for histidine, and doesn't bind
CC acetylated peptides (By similarity). {ECO:0000250|UniProtKB:Q8IWV8}.
CC -!- DISRUPTION PHENOTYPE: Male mice are viable but not fertile, due to
CC massive apoptosis of spermatocytes. They have a reduction of testis
CC weight of 68% and no detectable sperm in their epididymis. The
CC seminiferous tubules contain reduced numbers of post-meiotic round,
CC elongated spermatids and accumulation of pyknotic and zygotene-like
CC nuclei. Female mice show severe prenatal lethality, but the rare
CC surviving are fertile. Fibroblast cells display spontaneous chromosome
CC instability and fragility (PubMed:14585983, PubMed:16488448,
CC PubMed:28708824). UBR1 and UBR2 double knockout embryos die at
CC midgestation, with defects in neurogenesis and cardiovascular
CC development. These defects included reduced proliferation as well as
CC precocious migration and differentiation of neural progenitor cells
CC (PubMed:16606826). {ECO:0000269|PubMed:14585983,
CC ECO:0000269|PubMed:16488448, ECO:0000269|PubMed:16606826,
CC ECO:0000269|PubMed:28708824}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH31403.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65536.3; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY280958; AAQ17202.1; -; mRNA.
DR EMBL; AY061885; AAL32102.1; -; mRNA.
DR EMBL; AK122254; BAC65536.3; ALT_SEQ; Unassigned_DNA.
DR EMBL; BC025617; AAH25617.1; ALT_INIT; mRNA.
DR EMBL; BC026391; AAH26391.1; -; mRNA.
DR EMBL; BC031403; AAH31403.1; ALT_INIT; mRNA.
DR EMBL; BC075642; AAH75642.1; -; mRNA.
DR EMBL; AK083320; BAC38864.1; -; mRNA.
DR CCDS; CCDS28845.1; -. [Q6WKZ8-1]
DR CCDS; CCDS50127.1; -. [Q6WKZ8-2]
DR RefSeq; NP_001170845.1; NM_001177374.1. [Q6WKZ8-2]
DR RefSeq; NP_666190.2; NM_146078.3. [Q6WKZ8-1]
DR AlphaFoldDB; Q6WKZ8; -.
DR BMRB; Q6WKZ8; -.
DR SMR; Q6WKZ8; -.
DR BioGRID; 230327; 3.
DR ELM; Q6WKZ8; -.
DR STRING; 10090.ENSMUSP00000108961; -.
DR iPTMnet; Q6WKZ8; -.
DR PhosphoSitePlus; Q6WKZ8; -.
DR EPD; Q6WKZ8; -.
DR MaxQB; Q6WKZ8; -.
DR PaxDb; Q6WKZ8; -.
DR PeptideAtlas; Q6WKZ8; -.
DR PRIDE; Q6WKZ8; -.
DR ProteomicsDB; 300072; -. [Q6WKZ8-1]
DR ProteomicsDB; 300073; -. [Q6WKZ8-2]
DR ProteomicsDB; 300074; -. [Q6WKZ8-3]
DR Antibodypedia; 30162; 224 antibodies from 32 providers.
DR DNASU; 224826; -.
DR Ensembl; ENSMUST00000113335; ENSMUSP00000108961; ENSMUSG00000023977. [Q6WKZ8-2]
DR Ensembl; ENSMUST00000113337; ENSMUSP00000108963; ENSMUSG00000023977. [Q6WKZ8-1]
DR GeneID; 224826; -.
DR KEGG; mmu:224826; -.
DR UCSC; uc012aus.1; mouse. [Q6WKZ8-1]
DR UCSC; uc012auu.1; mouse. [Q6WKZ8-3]
DR CTD; 23304; -.
DR MGI; MGI:1861099; Ubr2.
DR VEuPathDB; HostDB:ENSMUSG00000023977; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; Q6WKZ8; -.
DR OMA; ILCQEDQ; -.
DR PhylomeDB; Q6WKZ8; -.
DR TreeFam; TF323875; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 224826; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ubr2; mouse.
DR PRO; PR:Q6WKZ8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6WKZ8; protein.
DR Bgee; ENSMUSG00000023977; Expressed in rostral migratory stream and 232 other tissues.
DR ExpressionAtlas; Q6WKZ8; baseline and differential.
DR Genevisible; Q6WKZ8; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IGI:MGI.
DR GO; GO:0070728; F:leucine binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0033522; P:histone H2A ubiquitination; IDA:UniProtKB.
DR GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.2670; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Coiled coil; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV8"
FT CHAIN 2..1755
FT /note="E3 ubiquitin-protein ligase UBR2"
FT /id="PRO_0000056141"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1108..1214
FT /note="RING-type; atypical"
FT REGION 1012..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1019..1054
FT /evidence="ECO:0000255"
FT COMPBIAS 1018..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV8"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015172"
FT VAR_SEQ 397..426
FT /note="RQLQRDFMEDDHERAVSVTALSVQFFTAPT -> ERLQRDYVTDDHDREFSV
FT ADLSVQIFTVPS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14585983,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015173"
FT CONFLICT 59
FT /note="Q -> L (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> Q (in Ref. 1; AAQ17202 and 3; BAC65536)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="S -> W (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> P (in Ref. 2; AAL32102)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..435
FT /note="RMLLTEE -> PNAPHRKK (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="L -> P (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="A -> S (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="S -> F (in Ref. 5; BAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1332
FT /note="C -> W (in Ref. 1; AAQ17202)"
FT /evidence="ECO:0000305"
FT CONFLICT 1619
FT /note="C -> S (in Ref. 4; AAH26391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1755 AA; 199155 MW; E6D413D674FBBFDA CRC64;
MASEMEPEVQ AIDRSLLECS AEEIAGRWLQ ATDLNREVYQ HLAHCVPKIY CRGPNPFPQK
EDTLAQHILL GPMEWYICAE DPALGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT
CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHKLSS SEVVEEEDPL
VHLSEDVIAR TYNIFAIMFR YAVDILTWEK ESELPEDLEV AEKSDTYYCM LFNDEVHTYE
QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC DQAKTVIVRN TSRQTKPLKV
QVMHSSVAAH QNFGLKALSW LGSVIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLNDS
KLWKGARSVY HQLFMSSLLM DLKYKKLFAL RFAKNYRQLQ RDFMEDDHER AVSVTALSVQ
FFTAPTLARM LLTEENLMTV IIKAFMDHLK HRDAQGRFQF ERYTALQAFK FRRVQSLILD
LKYVLISKPT EWSDELRQKF LQGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL
QMKLTHVISM VQDWCALDEK VLIEAYKKCL AVLTQCHGGF TDGEQPITLS ICGHSVETIR
YCVSQEKVSI HLPISRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA
QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL
YQLFSTPDYG KRFSSEVTHK DVVQQNNTLI EEMLYLIIML VGERFNPGVG QVAATDEIKR
EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIESVAHF KKPGLTGRGM YELKPECAKE
FNLYFYHFSR AEQSKAEEAQ RKLKRENKED TALPPPALPP FCPLFASLVN ILQCDVMLYI
MGTILQWAVE HHGSAWSESM LQRVLHLIGM ALQEEKHHLE NAVEGHVQTF TFTQKISKPG
DAPHNSPSIL AMLETLQNAP SLEAHKDMIR WLLKMFNAIK KIRECSSSSP VAEAEGTIME
ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DTSASATLDS
SPPVSDAALT ALGPAQTQVP EPRQFVTCIL CQEEQEVTVG SRAMVLAAFV QRSTVLSKDR
TKTIADPEKY DPLFMHPDLS CGTHTGSCGH VMHAHCWQRY FDSVQAKEQR RQQRLRLHTS
YDVENGEFLC PLCECLSNTV IPLLLPPRSI LSRRLNFSDQ PDLAQWTRAV TQQIKVVQML
RRKHNAADTS SSEDTEAMNI IPIPEGFRPD FYPRNPYSDS IKEMLTTFGT AAYKVGLKVH
PNEGDPRVPI LCWGTCAYTI QSIERILSDE EKPVFGPLPC RLDDCLRSLT RFAAAHWTVA
LLPVVQGHFC KLFASLVPSD SYEDLPCILD IDMFHLLVGL VLAFPALQCQ DFSGSSLATG
DLHIFHLVTM AHIVQILLTS CTEENGMDQE NPTGEEELAI LSLHKTLHQY TGSALKEAPS
GWHLWRSVRA AIMPFLKCSA LFFHYLNGVP APPDLQVSGT SHFEHLCNYL SLPTNLIHLF
QENSDIMNSL IESWCQNSEV KRYLNGERGA ISYPRGANKL IDLPEDYSSL INQASNFSCP
KSGGDKSRAP TLCLVCGSLL CSQSYCCQAE LEGEDVGACT AHTYSCGSGA GIFLRVRECQ
VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCQER FRKIQKLWQQ HSITEEIGHA
QEANQTLVGI DWQHL
