MKRN1_HUMAN
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 03-AUG-2022, entry version 188.
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}.
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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; 211.
DR IntAct; Q9UHC7; 47.
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; Q9UHC7; -.
DR PeptideAtlas; Q9UHC7; -.
DR PRIDE; Q9UHC7; -.
DR ProteomicsDB; 84313; -. [Q9UHC7-1]
DR ProteomicsDB; 84314; -. [Q9UHC7-2]
DR ProteomicsDB; 84315; -. [Q9UHC7-3]
DR ProteomicsDB; 84316; -. [Q9UHC7-4]
DR Antibodypedia; 437; 362 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 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; HNRECLE; -.
DR OrthoDB; 1388677at2759; -.
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 UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23608; 140 hits in 1085 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 212 other tissues.
DR ExpressionAtlas; Q9UHC7; baseline and differential.
DR Genevisible; Q9UHC7; HS.
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 Gene3D; 3.30.40.10; -; 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; PTHR11224; 1.
DR Pfam; PF15815; MKRN1_C; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF18044; zf-CCCH_4; 3.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; SSF90229; 3.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
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
