ID MKRN1_HUMAN Reviewed; 482 AA. AC Q9UHC7; A4D1T7; B3KXB4; Q256Y7; Q59G11; Q6GSF1; Q9H0G0; Q9UEZ7; Q9UHW2; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=E3 ubiquitin-protein ligase makorin-1; DE EC=2.3.2.27 {ECO:0000269|PubMed:19536131}; DE AltName: Full=RING finger protein 61; DE AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000305}; GN Name=MKRN1; Synonyms=RNF61; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT LEU-243, AND RP TISSUE SPECIFICITY. RX PubMed=10843807; DOI=10.1006/geno.2000.6199; RA Gray T.A., Hernandez L., Carey A.H., Schaldach M.A., Smithwick M.J., RA Rus K., Marshall Graves J.A., Stewart C.L., Nicholls R.D.; RT "The ancient source of a distinct gene family encoding proteins featuring RT RING and C(3)H zinc-finger motifs with abundant expression in developing RT brain and nervous system."; RL Genomics 66:76-86(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Miroci H., Mohr E.; RT "Role of trans-acting factors in the subcellular transport of vasopressin RT mRNA."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LEU-243. RC TISSUE=Brain, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-243. RC TISSUE=Brain, and Skin; 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-452 (ISOFORM 3). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP MUTAGENESIS OF HIS-307, UBIQUITINATION, AND INTERACTION WITH TERT. RX PubMed=15805468; DOI=10.1101/gad.1289405; RA Kim J.H., Park S.-M., Kang M.R., Oh S.-Y., Lee T.H., Muller M.T., RA Chung I.K.; RT "Ubiquitin ligase MKRN1 modulates telomere length homeostasis through a RT proteolysis of hTERT."; RL Genes Dev. 19:776-781(2005). RN [12] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16785614; DOI=10.1385/endo:29:2:363; RA Omwancha J., Zhou X.-F., Chen S.-Y., Baslan T., Fisher C.J., Zheng Z., RA Cai C., Shemshedini L.; RT "Makorin RING finger protein 1 (MKRN1) has negative and positive effects on RT RNA polymerase II-dependent transcription."; RL Endocrine 29:363-373(2006). RN [13] RP INDUCTION. RX PubMed=19604354; DOI=10.1186/1471-2407-9-232; RA Shimada H., Shiratori T., Yasuraoka M., Kagaya A., Kuboshima M., Nomura F., RA Takiguchi M., Ochiai T., Matsubara H., Hiwasa T.; RT "Identification of Makorin 1 as a novel SEREX antigen of esophageal RT squamous cell carcinoma."; RL BMC Cancer 9:232-232(2009). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH TP53 AND RP CDKN1A. RX PubMed=19536131; DOI=10.1038/emboj.2009.164; RA Lee E.-W., Lee M.-S., Camus S., Ghim J., Yang M.-R., Oh W., Ha N.-C., RA Lane D.P., Song J.; RT "Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell RT cycle arrest and apoptosis."; RL EMBO J. 28:2100-2113(2009). CC -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of CC ubiquitin moieties onto substrate proteins. These substrates include CC FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing CC p53/TP53 under normal conditions, but stimulates apoptosis by CC repressing CDKN1A under stress conditions. Acts as a negative regulator CC of telomerase. Has negative and positive effects on RNA polymerase II- CC dependent transcription. {ECO:0000269|PubMed:16785614, CC ECO:0000269|PubMed:19536131}. 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:19536131}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:19536131}. CC -!- SUBUNIT: Interacts with p53/TP53 and CDKN1A. Interacts with TERT, CC modulating telomere length homeostasis. {ECO:0000269|PubMed:15805468, CC ECO:0000269|PubMed:19536131}. CC -!- INTERACTION: CC Q9UHC7; Q13895: BYSL; NbExp=3; IntAct=EBI-373524, EBI-358049; CC Q9UHC7; P38936: CDKN1A; NbExp=5; IntAct=EBI-373524, EBI-375077; CC Q9UHC7; Q9UER7: DAXX; NbExp=3; IntAct=EBI-373524, EBI-77321; CC Q9UHC7; Q3B820: FAM161A; NbExp=3; IntAct=EBI-373524, EBI-719941; CC Q9UHC7; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-373524, EBI-11980301; CC Q9UHC7; P41227: NAA10; NbExp=5; IntAct=EBI-373524, EBI-747693; CC Q9UHC7; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-373524, EBI-746259; CC Q9UHC7; P54725: RAD23A; NbExp=5; IntAct=EBI-373524, EBI-746453; CC Q9UHC7; P54727: RAD23B; NbExp=3; IntAct=EBI-373524, EBI-954531; CC Q9UHC7; O00560: SDCBP; NbExp=3; IntAct=EBI-373524, EBI-727004; CC Q9UHC7; P04637: TP53; NbExp=8; IntAct=EBI-373524, EBI-366083; CC Q9UHC7; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-373524, EBI-7353612; CC Q9UHC7; P51668: UBE2D1; NbExp=3; IntAct=EBI-373524, EBI-743540; CC Q9UHC7; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-373524, EBI-745527; CC Q9UHC7; Q5VVQ6: YOD1; NbExp=5; IntAct=EBI-373524, EBI-2510804; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UHC7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHC7-2; Sequence=VSP_040361; CC Name=3; CC IsoId=Q9UHC7-3; Sequence=VSP_040363, VSP_040364; CC Name=4; CC IsoId=Q9UHC7-4; Sequence=VSP_040362; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10843807, CC ECO:0000269|PubMed:16785614}. CC -!- INDUCTION: Frequently induced in esophageal squamous cell carcinoma CC (SCC) tissues. {ECO:0000269|PubMed:19604354}. CC -!- PTM: Auto-ubiquitinated; which leads to proteasomal degradation. CC {ECO:0000269|PubMed:15805468}. 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; AF192784; AAF17487.1; -; mRNA. DR EMBL; AF192793; AAF18979.1; -; Genomic_DNA. DR EMBL; AF192789; AAF18979.1; JOINED; Genomic_DNA. DR EMBL; AF192790; AAF18979.1; JOINED; Genomic_DNA. DR EMBL; AF192791; AAF18979.1; JOINED; Genomic_DNA. DR EMBL; AF192792; AAF18979.1; JOINED; Genomic_DNA. DR EMBL; AM236048; CAJ84705.1; -; mRNA. DR EMBL; AF117233; AAF17214.1; -; mRNA. DR EMBL; AL136812; CAB66746.1; -; mRNA. DR EMBL; AK127030; BAG54426.1; -; mRNA. DR EMBL; AK315552; BAG37929.1; -; mRNA. DR EMBL; AC069335; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236950; EAL24026.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83949.1; -; Genomic_DNA. DR EMBL; BC025955; AAH25955.1; -; mRNA. DR EMBL; BC037400; AAH37400.1; -; mRNA. DR EMBL; BC064838; AAH64838.1; -; mRNA. DR EMBL; AB209298; BAD92535.1; -; mRNA. DR CCDS; CCDS47725.1; -. [Q9UHC7-4] DR CCDS; CCDS5860.1; -. [Q9UHC7-1] DR RefSeq; NP_001138597.1; NM_001145125.1. [Q9UHC7-4] DR RefSeq; NP_038474.2; NM_013446.3. [Q9UHC7-1] DR RefSeq; XP_011514299.1; XM_011515997.2. [Q9UHC7-2] DR RefSeq; XP_011514300.1; XM_011515998.1. [Q9UHC7-2] DR AlphaFoldDB; Q9UHC7; -. DR BioGRID; 117141; 215. DR IntAct; Q9UHC7; 46. DR MINT; Q9UHC7; -. DR STRING; 9606.ENSP00000255977; -. DR iPTMnet; Q9UHC7; -. DR PhosphoSitePlus; Q9UHC7; -. DR BioMuta; MKRN1; -. DR DMDM; 67477468; -. DR EPD; Q9UHC7; -. DR jPOST; Q9UHC7; -. DR MassIVE; Q9UHC7; -. DR MaxQB; Q9UHC7; -. DR PaxDb; 9606-ENSP00000255977; -. DR PeptideAtlas; Q9UHC7; -. DR ProteomicsDB; 84313; -. [Q9UHC7-1] DR ProteomicsDB; 84314; -. [Q9UHC7-2] DR ProteomicsDB; 84315; -. [Q9UHC7-3] DR ProteomicsDB; 84316; -. [Q9UHC7-4] DR Pumba; Q9UHC7; -. DR Antibodypedia; 437; 403 antibodies from 30 providers. DR DNASU; 23608; -. DR Ensembl; ENST00000255977.7; ENSP00000255977.2; ENSG00000133606.11. [Q9UHC7-1] DR Ensembl; ENST00000443720.6; ENSP00000416369.2; ENSG00000133606.11. [Q9UHC7-4] DR Ensembl; ENST00000474576.5; ENSP00000417863.1; ENSG00000133606.11. [Q9UHC7-2] DR GeneID; 23608; -. DR KEGG; hsa:23608; -. DR MANE-Select; ENST00000255977.7; ENSP00000255977.2; NM_013446.4; NP_038474.2. DR UCSC; uc003vvt.2; human. [Q9UHC7-1] DR AGR; HGNC:7112; -. DR CTD; 23608; -. DR DisGeNET; 23608; -. DR GeneCards; MKRN1; -. DR HGNC; HGNC:7112; MKRN1. DR HPA; ENSG00000133606; Low tissue specificity. DR MIM; 607754; gene. DR neXtProt; NX_Q9UHC7; -. DR OpenTargets; ENSG00000133606; -. DR PharmGKB; PA30831; -. DR VEuPathDB; HostDB:ENSG00000133606; -. DR eggNOG; KOG1039; Eukaryota. DR GeneTree; ENSGT00950000183077; -. DR HOGENOM; CLU_040815_4_1_1; -. DR InParanoid; Q9UHC7; -. DR OMA; QQTNVEM; -. DR OrthoDB; 2906101at2759; -. DR PhylomeDB; Q9UHC7; -. DR TreeFam; TF315108; -. DR PathwayCommons; Q9UHC7; -. DR Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol. DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9UHC7; -. DR SIGNOR; Q9UHC7; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 23608; 144 hits in 1165 CRISPR screens. DR ChiTaRS; MKRN1; human. DR GenomeRNAi; 23608; -. DR Pharos; Q9UHC7; Tbio. DR PRO; PR:Q9UHC7; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UHC7; Protein. DR Bgee; ENSG00000133606; Expressed in sperm and 214 other cell types or tissues. DR ExpressionAtlas; Q9UHC7; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase. DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR CDD; cd16730; RING-HC_MKRN1_3; 1. DR Gene3D; 2.30.30.1190; -; 1. DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR045072; MKRN-like. DR InterPro; IPR031644; MKRN1_C. DR InterPro; IPR041367; Znf-CCCH_4. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR000571; Znf_CCCH. DR InterPro; IPR036855; Znf_CCCH_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR11224:SF37; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-1; 1. DR PANTHER; PTHR11224; MAKORIN-RELATED; 1. DR Pfam; PF15815; MKRN1_C; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR Pfam; PF14608; zf-CCCH_2; 1. DR Pfam; PF18044; zf-CCCH_4; 3. DR SMART; SM00184; RING; 1. DR SMART; SM00356; ZnF_C3H1; 4. DR SUPFAM; SSF90229; CCCH zinc finger; 3. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50103; ZF_C3H1; 4. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9UHC7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Metal-binding; Reference proteome; Repeat; KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..482 FT /note="E3 ubiquitin-protein ligase makorin-1" FT /id="PRO_0000055952" FT ZN_FING 55..82 FT /note="C3H1-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 84..111 FT /note="C3H1-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 208..235 FT /note="C3H1-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 281..335 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 364..393 FT /note="C3H1-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 26..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 236..263 FT /note="Makorin-type Cys-His" FT VAR_SEQ 1..64 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_040361" FT VAR_SEQ 330..482 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10931946, ECO:0000303|Ref.2" FT /id="VSP_040362" FT VAR_SEQ 366..412 FT /note="SNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYR -> R FT YEHCSLFSSEEPNRAWVHFEKNGAALYTPTSFLPFFDFPGQFILSP (in isoform FT 3)" FT /evidence="ECO:0000303|Ref.10" FT /id="VSP_040363" FT VAR_SEQ 413..482 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.10" FT /id="VSP_040364" FT VARIANT 243 FT /note="V -> L (in dbSNP:rs2272095)" FT /evidence="ECO:0000269|PubMed:10843807, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_012161" FT VARIANT 439 FT /note="V -> A (in dbSNP:rs1062786)" FT /id="VAR_057214" FT MUTAGEN 307 FT /note="H->E: Loss of E3 ligase activity, but no effect on FT transcription regulation." FT /evidence="ECO:0000269|PubMed:15805468" FT CONFLICT 149 FT /note="A -> R (in Ref. 3; AAF17214)" FT /evidence="ECO:0000305" FT CONFLICT 197 FT /note="K -> E (in Ref. 5; BAG54426)" FT /evidence="ECO:0000305" FT CONFLICT 274..275 FT /note="QR -> S (in Ref. 3; AAF17214)" FT /evidence="ECO:0000305" FT CONFLICT 395..396 FT /note="GR -> AG (in Ref. 1; AAF17487)" FT /evidence="ECO:0000305" SQ SEQUENCE 482 AA; 53349 MW; AE8FAF010A5CDFC0 CRC64; MAEAATPGTT ATTSGAGAAA ATAAAASPTP IPTVTAPSLG AGGGGGGSDG SGGGWTKQVT CRYFMHGVCK EGDNCRYSHD LSDSPYSVVC KYFQRGYCIY GDRCRYEHSK PLKQEEATAT ELTTKSSLAA SSSLSSIVGP LVEMNTGEAE SRNSNFATVG AGSEDWVNAI EFVPGQPYCG RTAPSCTEAP LQGSVTKEES EKEQTAVETK KQLCPYAAVG ECRYGENCVY LHGDSCDMCG LQVLHPMDAA QRSQHIKSCI EAHEKDMELS FAVQRSKDMV CGICMEVVYE KANPSERRFG ILSNCNHTYC LKCIRKWRSA KQFESKIIKS CPECRITSNF VIPSEYWVEE KEEKQKLILK YKEAMSNKAC RYFDEGRGSC PFGGNCFYKH AYPDGRREEP QRQKVGTSSR YRAQRRNHFW ELIEERENSN PFDNDEEEVV TFELGEMLLM LLAAGGDDEL TDSEDEWDLF HDELEDFYDL DL //