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   03-MAY-2023, entry version 191.
DE   RecName: Full=E3 ubiquitin-protein ligase makorin-2 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9ERV1};
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).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=28008940; DOI=10.1038/srep39318;
RA   Qian X., Wang L., Zheng B., Shi Z.M., Ge X., Jiang C.F., Qian Y.C.,
RA   Li D.M., Li W., Liu X., Yin Y., Zheng J.T., Shen H., Wang M., Guo X.J.,
RA   He J., Lin M., Liu L.Z., Sha J.H., Jiang B.H.;
RT   "Deficiency of Mkrn2 causes abnormal spermiogenesis and spermiation, and
RT   impairs male fertility.";
RL   Sci. Rep. 6:39318-39318(2016).
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins (By similarity). Promotes
CC       the polyubiquitination and proteasome-dependent degradation of
CC       RELA/p65, thereby suppressing RELA-mediated NF-kappaB transactivation
CC       and negatively regulating inflammatory responses (By similarity). Plays
CC       a role in the regulation of spermiation and in male fertility (By
CC       similarity). {ECO:0000250|UniProtKB:Q9ERV1}.
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:Q9ERV1};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with PDLIM2 (via LIM zinc-binding domain) (By
CC       similarity). Interacts with RELA (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ERV1}.
CC   -!- INTERACTION:
CC       Q9H000; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2341005, EBI-8643161;
CC       Q9H000; Q01658: DR1; NbExp=3; IntAct=EBI-2341005, EBI-750300;
CC       Q9H000; O00303: EIF3F; NbExp=3; IntAct=EBI-2341005, EBI-711990;
CC       Q9H000; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2341005, EBI-1054873;
CC       Q9H000; P42858: HTT; NbExp=12; IntAct=EBI-2341005, EBI-466029;
CC       Q9H000; P63244: RACK1; NbExp=3; IntAct=EBI-2341005, EBI-296739;
CC       Q9H000; Q13148: TARDBP; NbExp=6; IntAct=EBI-2341005, EBI-372899;
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       Q9H000; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-2341005, EBI-25492388;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9ERV1}.
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: Expressed in sperm, with significantly reduced
CC       expression in sperm of patients with oligoasthenoteratozoospermia (at
CC       protein level) (PubMed:28008940). Widely expressed with expression in
CC       testis, ovary, small intestine, colon, peripheral blood leukocytes,
CC       fetal liver, bone marrow, thymus, lymph node and spleen
CC       (PubMed:11597136). {ECO:0000269|PubMed:11597136,
CC       ECO:0000269|PubMed:28008940}.
CC   -!- MISCELLANEOUS: Partially overlaps and is antisense to the RAF1 proto-
CC       oncogene.
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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   AlphaFoldDB; Q9H000; -.
DR   BioGRID; 117142; 378.
DR   IntAct; Q9H000; 35.
DR   MINT; Q9H000; -.
DR   STRING; 9606.ENSP00000170447; -.
DR   GlyGen; Q9H000; 1 site, 1 O-linked glycan (1 site).
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   ProteomicsDB; 4805; -.
DR   ProteomicsDB; 80191; -. [Q9H000-1]
DR   Antibodypedia; 26240; 307 antibodies from 28 providers.
DR   DNASU; 23609; -.
DR   Ensembl; ENST00000170447.12; ENSP00000170447.7; ENSG00000075975.17. [Q9H000-1]
DR   Ensembl; ENST00000411987.5; ENSP00000396340.1; ENSG00000075975.17. [Q9H000-2]
DR   Ensembl; ENST00000677816.1; ENSP00000502893.1; ENSG00000075975.17. [Q9H000-1]
DR   GeneID; 23609; -.
DR   KEGG; hsa:23609; -.
DR   MANE-Select; ENST00000170447.12; ENSP00000170447.7; NM_014160.5; NP_054879.3.
DR   UCSC; uc003bxd.5; human. [Q9H000-1]
DR   AGR; HGNC:7113; -.
DR   CTD; 23609; -.
DR   DisGeNET; 23609; -.
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   VEuPathDB; HostDB:ENSG00000075975; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   GeneTree; ENSGT00950000183077; -.
DR   HOGENOM; CLU_040815_0_1_1; -.
DR   InParanoid; Q9H000; -.
DR   OMA; MQGVCRE; -.
DR   OrthoDB; 2906101at2759; -.
DR   PhylomeDB; Q9H000; -.
DR   TreeFam; TF315108; -.
DR   PathwayCommons; Q9H000; -.
DR   SignaLink; Q9H000; -.
DR   SIGNOR; Q9H000; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 23609; 11 hits in 1190 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 secondary oocyte and 187 other tissues.
DR   ExpressionAtlas; Q9H000; baseline and differential.
DR   Genevisible; Q9H000; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   CDD; cd16731; RING-HC_MKRN2; 1.
DR   Gene3D; 2.30.30.1190; -; 1.
DR   Gene3D; 1.20.120.1350; Pneumovirus matrix protein 2 (M2), zinc-binding domain; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045072; MKRN-like.
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; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-2-RELATED; 1.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   Pfam; PF14608; zf-CCCH_2; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Differentiation; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Spermatogenesis; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..416
FT                   /note="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          113..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..222
FT                   /note="Makorin-type Cys-His"
FT   COMPBIAS        118..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|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
//