ID MKRN2_HUMAN Reviewed; 416 AA. AC Q9H000; A6NIA2; B3KRC5; B4DPR4; Q8N391; Q96BD4; Q9BUY2; Q9NRY1; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 2. DT 07-OCT-2020, entry version 179. DE RecName: Full=Probable E3 ubiquitin-protein ligase makorin-2; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 62; DE AltName: Full=RING-type E3 ubiquitin transferase makorin-2 {ECO:0000305}; GN Name=MKRN2; Synonyms=RNF62; ORFNames=HSPC070; 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), AND TISSUE RP SPECIFICITY. RX PubMed=11597136; DOI=10.1006/geno.2001.6627; RA Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.; RT "Phylogenetic conservation of the makorin-2 gene, encoding a multiple zinc- RT finger protein, antisense to the raf1 proto-oncogene."; RL Genomics 77:119-126(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-416 (ISOFORM 1/2). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of CC ubiquitin moieties onto substrate proteins. {ECO:0000250}. 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; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- INTERACTION: CC Q9H000; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2341005, EBI-8643161; CC Q9H000; O00303: EIF3F; NbExp=3; IntAct=EBI-2341005, EBI-711990; CC Q9H000; P42858: HTT; NbExp=3; IntAct=EBI-2341005, EBI-466029; CC Q9H000; P63244: RACK1; NbExp=3; IntAct=EBI-2341005, EBI-296739; CC Q9H000; P51668: UBE2D1; NbExp=6; IntAct=EBI-2341005, EBI-743540; CC Q9H000; Q9Y2X8: UBE2D4; NbExp=6; IntAct=EBI-2341005, EBI-745527; CC Q9H000; E9KL35; NbExp=3; IntAct=EBI-2341005, EBI-8456500; CC Q9H000; PRO_0000037311 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-2341005, EBI-25474079; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H000-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H000-2; Sequence=VSP_055275; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11597136}. CC -!- MISCELLANEOUS: Partially overlaps and is antisense to the RAF1 proto- CC oncogene. 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; AF302084; AAG30426.1; -; mRNA. DR EMBL; AF277170; AAG27595.1; -; Genomic_DNA. DR EMBL; AF277164; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF277165; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF277166; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF277167; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF277168; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF277169; AAG27595.1; JOINED; Genomic_DNA. DR EMBL; AF161555; AAF29042.2; -; mRNA. DR EMBL; AK091318; BAG52337.1; -; mRNA. DR EMBL; AK298463; BAG60676.1; -; mRNA. DR EMBL; AC018500; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64132.1; -; Genomic_DNA. DR EMBL; CH471055; EAW64133.1; -; Genomic_DNA. DR EMBL; BC001799; AAH01799.2; -; mRNA. DR EMBL; BC015715; AAH15715.1; -; mRNA. DR EMBL; AL834512; CAD39168.1; -; mRNA. DR CCDS; CCDS33702.1; -. [Q9H000-1] DR CCDS; CCDS63545.1; -. [Q9H000-2] DR RefSeq; NP_001258636.1; NM_001271707.1. [Q9H000-2] DR RefSeq; NP_054879.3; NM_014160.4. [Q9H000-1] DR SMR; Q9H000; -. DR BioGRID; 117142; 44. DR IntAct; Q9H000; 30. DR MINT; Q9H000; -. DR STRING; 9606.ENSP00000170447; -. DR iPTMnet; Q9H000; -. DR PhosphoSitePlus; Q9H000; -. DR BioMuta; MKRN2; -. DR DMDM; 45645205; -. DR EPD; Q9H000; -. DR jPOST; Q9H000; -. DR MassIVE; Q9H000; -. DR MaxQB; Q9H000; -. DR PaxDb; Q9H000; -. DR PeptideAtlas; Q9H000; -. DR PRIDE; Q9H000; -. DR ProteomicsDB; 4805; -. DR ProteomicsDB; 80191; -. [Q9H000-1] DR Antibodypedia; 26240; 284 antibodies. DR DNASU; 23609; -. DR Ensembl; ENST00000170447; ENSP00000170447; ENSG00000075975. [Q9H000-1] DR Ensembl; ENST00000411987; ENSP00000396340; ENSG00000075975. [Q9H000-2] DR GeneID; 23609; -. DR KEGG; hsa:23609; -. DR UCSC; uc003bxd.5; human. [Q9H000-1] DR CTD; 23609; -. DR DisGeNET; 23609; -. DR EuPathDB; HostDB:ENSG00000075975.15; -. DR GeneCards; MKRN2; -. DR HGNC; HGNC:7113; MKRN2. DR HPA; ENSG00000075975; Low tissue specificity. DR MIM; 608426; gene. DR neXtProt; NX_Q9H000; -. DR OpenTargets; ENSG00000075975; -. DR PharmGKB; PA30832; -. DR eggNOG; KOG1039; Eukaryota. DR GeneTree; ENSGT00950000183077; -. DR HOGENOM; CLU_040815_0_1_1; -. DR InParanoid; Q9H000; -. DR KO; K15687; -. DR OMA; MAEEKTC; -. DR OrthoDB; 1388677at2759; -. DR PhylomeDB; Q9H000; -. DR TreeFam; TF315108; -. DR PathwayCommons; Q9H000; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 23609; 2 hits in 870 CRISPR screens. DR ChiTaRS; MKRN2; human. DR GenomeRNAi; 23609; -. DR Pharos; Q9H000; Tbio. DR PRO; PR:Q9H000; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H000; protein. DR Bgee; ENSG00000075975; Expressed in testis and 229 other tissues. DR ExpressionAtlas; Q9H000; baseline and differential. DR Genevisible; Q9H000; HS. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR026293; Makorin_2. 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:SF17; PTHR11224:SF17; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR Pfam; PF00642; zf-CCCH; 2. DR Pfam; PF18044; zf-CCCH_4; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00356; ZnF_C3H1; 4. DR SUPFAM; SSF90229; SSF90229; 2. 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; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..416 FT /note="Probable E3 ubiquitin-protein ligase makorin-2" FT /id="PRO_0000055955" FT ZN_FING 2..29 FT /note="C3H1-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 31..58 FT /note="C3H1-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 165..192 FT /note="C3H1-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 238..292 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 321..350 FT /note="C3H1-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 193..222 FT /note="Makorin-type Cys-His" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT VAR_SEQ 8..50 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055275" FT VARIANT 388 FT /note="R -> Q (in dbSNP:rs5746260)" FT /id="VAR_052085" FT CONFLICT 186 FT /note="V -> F (in Ref. 1; AAG30426/AAG27595)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="K -> E (in Ref. 2; AAF29042)" FT /evidence="ECO:0000305" SQ SEQUENCE 416 AA; 46940 MW; 1F1564E589EB6632 CRC64; MSTKQITCRY FMHGVCREGS QCLFSHDLAN SKPSTICKYY QKGYCAYGTR CRYDHTRPSA AAGGAVGTMA HSVPSPAFHS PHPPSEVTAS IVKTNSHEPG KREKRTLVLR DRNLSGMAER KTQPSMVSNP GSCSDPQPSP EMKPHSYLDA IRSGLDDVEA SSSYSNEQQL CPYAAAGECR FGDACVYLHG EVCEICRLQV LHPFDPEQRK AHEKICMLTF EHEMEKAFAF QASQDKVCSI CMEVILEKAS ASERRFGILS NCNHTYCLSC IRQWRCAKQF ENPIIKSCPE CRVISEFVIP SVYWVEDQNK KNELIEAFKQ GMGKKACKYF EQGKGTCPFG SKCLYRHAYP DGRLAEPEKP RKQLSSQGTV RFFNSVRLWD FIENRESRHV PNNEDVDMTE LGDLFMHLSG VESSEP //