UB2E3_HUMAN
ID UB2E3_HUMAN Reviewed; 207 AA.
AC Q969T4; B2RAD6; D3DPG3; Q5U0R7; Q7Z4W4;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 E3;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme E3;
DE AltName: Full=UbcH9;
DE AltName: Full=Ubiquitin carrier protein E3;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-23 kDa;
DE AltName: Full=Ubiquitin-protein ligase E3;
GN Name=UBE2E3; Synonyms=UBCE4, UBCH9;
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 [MRNA], TISSUE SPECIFICITY, FUNCTION, AND MUTAGENESIS
RP OF CYS-145.
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=10343118; DOI=10.1159/000015229;
RA Ito K., Kato S., Matsuda Y., Kimura M., Okano Y.;
RT "cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias
RT UbcH9), encoding an N-terminally extended human ubiquitin-conjugating
RT enzyme.";
RL Cytogenet. Cell Genet. 84:99-104(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Umbilical cord blood;
RA Shen Y., Ye M., Fu G., Zhou J., Zhang Q., Huang Q., Xu S., He K., Chen S.,
RA Mao M., Chen Z.;
RT "Human UbcM2 gene, complete cds.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-201.
RA Xin Y.R., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Mus musculus ubiquitin-
RT conjugating enzyme UbcM2.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and PNS;
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15545318; DOI=10.1083/jcb.200406001;
RA Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.;
RT "Ubiquitin charging of human class III ubiquitin-conjugating enzymes
RT triggers their nuclear import.";
RL J. Cell Biol. 167:649-659(2004).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP 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: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and
CC 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates
CC in the regulation of transepithelial sodium transport in renal cells.
CC May be involved in cell growth arrest. {ECO:0000269|PubMed:10343118,
CC ECO:0000269|PubMed:20061386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: The ubiquitin-loaded form interacts specifically with
CC importin-11 (IPO11), leading to its import into the nucleus. Interacts
CC with NEDD4L. {ECO:0000250|UniProtKB:P52483}.
CC -!- INTERACTION:
CC Q969T4; Q96B67: ARRDC3; NbExp=7; IntAct=EBI-348496, EBI-2875665;
CC Q969T4; P54253: ATXN1; NbExp=7; IntAct=EBI-348496, EBI-930964;
CC Q969T4; Q96EP1-2: CHFR; NbExp=3; IntAct=EBI-348496, EBI-12344389;
CC Q969T4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-348496, EBI-724310;
CC Q969T4; P04792: HSPB1; NbExp=3; IntAct=EBI-348496, EBI-352682;
CC Q969T4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-348496, EBI-10975473;
CC Q969T4; O15344: MID1; NbExp=8; IntAct=EBI-348496, EBI-2340316;
CC Q969T4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-348496, EBI-10172526;
CC Q969T4; Q96FW1: OTUB1; NbExp=8; IntAct=EBI-348496, EBI-1058491;
CC Q969T4; Q9NXJ5-2: PGPEP1; NbExp=5; IntAct=EBI-348496, EBI-12813581;
CC Q969T4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-348496, EBI-79165;
CC Q969T4; P60891: PRPS1; NbExp=3; IntAct=EBI-348496, EBI-749195;
CC Q969T4; Q9Y3C5: RNF11; NbExp=4; IntAct=EBI-348496, EBI-396669;
CC Q969T4; Q9Y4L5: RNF115; NbExp=4; IntAct=EBI-348496, EBI-2129242;
CC Q969T4; Q96GF1: RNF185; NbExp=8; IntAct=EBI-348496, EBI-2340249;
CC Q969T4; Q99496: RNF2; NbExp=6; IntAct=EBI-348496, EBI-722416;
CC Q969T4; Q96BH1: RNF25; NbExp=3; IntAct=EBI-348496, EBI-2129220;
CC Q969T4; Q99942: RNF5; NbExp=11; IntAct=EBI-348496, EBI-348482;
CC Q969T4; Q9HCM9: TRIM39; NbExp=5; IntAct=EBI-348496, EBI-739510;
CC Q969T4; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-348496, EBI-11523450;
CC Q969T4; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-348496, EBI-9867283;
CC Q969T4; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-348496, EBI-6929619;
CC Q969T4; P02766: TTR; NbExp=3; IntAct=EBI-348496, EBI-711909;
CC Q969T4; Q969T9: WBP2; NbExp=3; IntAct=EBI-348496, EBI-727055;
CC Q969T4; O76024: WFS1; NbExp=3; IntAct=EBI-348496, EBI-720609;
CC Q969T4; O00308: WWP2; NbExp=3; IntAct=EBI-348496, EBI-743923;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15545318}. Cytoplasm
CC {ECO:0000269|PubMed:15545318}. Note=Shuttles between the nucleus and
CC cytoplasm in a IPO11-dependent manner.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Highly
CC expressed in skeletal muscle. {ECO:0000269|PubMed:10343118}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AB017644; BAA76544.1; -; mRNA.
DR EMBL; AF085362; AAD40197.1; -; mRNA.
DR EMBL; AF136176; AAP97266.1; -; mRNA.
DR EMBL; BT019345; AAV38152.1; -; mRNA.
DR EMBL; AK314145; BAG36833.1; -; mRNA.
DR EMBL; AC104076; AAY14882.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10989.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10990.1; -; Genomic_DNA.
DR EMBL; BC003554; AAH03554.1; -; mRNA.
DR EMBL; BC092407; AAH92407.1; -; mRNA.
DR CCDS; CCDS2282.1; -.
DR RefSeq; NP_001265483.1; NM_001278554.1.
DR RefSeq; NP_001265484.1; NM_001278555.1.
DR RefSeq; NP_006348.1; NM_006357.3.
DR RefSeq; NP_872619.1; NM_182678.2.
DR RefSeq; XP_005246301.1; XM_005246244.2.
DR AlphaFoldDB; Q969T4; -.
DR SMR; Q969T4; -.
DR BioGRID; 115740; 129.
DR IntAct; Q969T4; 88.
DR MINT; Q969T4; -.
DR STRING; 9606.ENSP00000386788; -.
DR MoonDB; Q969T4; Predicted.
DR iPTMnet; Q969T4; -.
DR PhosphoSitePlus; Q969T4; -.
DR SwissPalm; Q969T4; -.
DR BioMuta; UBE2E3; -.
DR DMDM; 47606197; -.
DR EPD; Q969T4; -.
DR jPOST; Q969T4; -.
DR MassIVE; Q969T4; -.
DR MaxQB; Q969T4; -.
DR PaxDb; Q969T4; -.
DR PeptideAtlas; Q969T4; -.
DR PRIDE; Q969T4; -.
DR ProteomicsDB; 75843; -.
DR TopDownProteomics; Q969T4; -.
DR Antibodypedia; 1150; 660 antibodies from 32 providers.
DR DNASU; 10477; -.
DR Ensembl; ENST00000392415.6; ENSP00000376215.2; ENSG00000170035.16.
DR Ensembl; ENST00000410062.9; ENSP00000386788.3; ENSG00000170035.16.
DR Ensembl; ENST00000602710.5; ENSP00000473623.1; ENSG00000170035.16.
DR Ensembl; ENST00000602959.5; ENSP00000473639.1; ENSG00000170035.16.
DR GeneID; 10477; -.
DR KEGG; hsa:10477; -.
DR MANE-Select; ENST00000410062.9; ENSP00000386788.3; NM_006357.4; NP_006348.1.
DR UCSC; uc002unr.3; human.
DR CTD; 10477; -.
DR DisGeNET; 10477; -.
DR GeneCards; UBE2E3; -.
DR HGNC; HGNC:12479; UBE2E3.
DR HPA; ENSG00000170035; Low tissue specificity.
DR MIM; 604151; gene.
DR neXtProt; NX_Q969T4; -.
DR OpenTargets; ENSG00000170035; -.
DR PharmGKB; PA37129; -.
DR VEuPathDB; HostDB:ENSG00000170035; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155392; -.
DR HOGENOM; CLU_030988_14_4_1; -.
DR InParanoid; Q969T4; -.
DR OMA; GDRAKHD; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; Q969T4; -.
DR TreeFam; TF101117; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; Q969T4; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q969T4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10477; 11 hits in 1051 CRISPR screens.
DR ChiTaRS; UBE2E3; human.
DR GeneWiki; UBE2E3; -.
DR GenomeRNAi; 10477; -.
DR Pharos; Q969T4; Tbio.
DR PRO; PR:Q969T4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q969T4; protein.
DR Bgee; ENSG00000170035; Expressed in ganglionic eminence and 100 other tissues.
DR ExpressionAtlas; Q969T4; baseline and differential.
DR Genevisible; Q969T4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Growth regulation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..207
FT /note="Ubiquitin-conjugating enzyme E2 E3"
FT /id="PRO_0000082474"
FT DOMAIN 61..207
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 201
FT /note="W -> R (in dbSNP:rs2368192)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023392"
FT MUTAGEN 145
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10343118"
FT CONFLICT 65
FT /note="R -> K (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Y -> C (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="P -> L (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="Y -> D (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> V (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="T -> M (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> V (in Ref. 3; AAP97266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22913 MW; 821CB1382478DC9F CRC64;
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS
TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY
PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV
GSIATQYLTN RAEHDRIARQ WTKRYAT
