MKRN2_HUMAN
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-AUG-2022, entry version 187.
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; 364.
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 PRIDE; 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 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; RYDHIRL; -.
DR OrthoDB; 1388677at2759; -.
DR PhylomeDB; Q9H000; -.
DR TreeFam; TF315108; -.
DR PathwayCommons; Q9H000; -.
DR SignaLink; Q9H000; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23609; 11 hits in 1112 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030274; F:LIM domain binding; 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: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:1901485; P:positive regulation of transcription factor catabolic process; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026293; Makorin_2.
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; PTHR11224; 1.
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; 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
