ID   HECD1_HUMAN             Reviewed;        2610 AA.
AC   Q9ULT8; D3DS86; Q6P445; Q86VJ1; Q96F34; Q9UFZ7;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 4.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=E3 ubiquitin-protein ligase HECTD1 {ECO:0000305};
DE            EC=2.3.2.26 {ECO:0000269|PubMed:33711283};
DE   AltName: Full=E3 ligase for inhibin receptor;
DE            Short=EULIR {ECO:0000303|Ref.1};
DE   AltName: Full=HECT domain-containing protein 1;
GN   Name=HECTD1 {ECO:0000303|PubMed:33711283,
GN   ECO:0000312|HGNC:HGNC:20157}; Synonyms=KIAA1131;
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], AND VARIANT LEU-2027.
RA   Zhang H.;
RT   "EULIR is an E3 ubiquitin ligase for inhibin receptor.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-2610.
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1652-2610.
RC   TISSUE=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2091-2610.
RC   TISSUE=Muscle, and Urinary bladder;
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   INTERACTION WITH IGSF1.
RX   PubMed=12421765; DOI=10.1101/gr.406902;
RA   Nakayama M., Kikuno R., Ohara O.;
RT   "Protein-protein interactions between large proteins: two-hybrid screening
RT   using a functionally classified library composed of long cDNAs.";
RL   Genome Res. 12:1773-1784(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1760 AND SER-1772, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2318, 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   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-2579.
RX   PubMed=33711283; DOI=10.1016/j.stem.2021.02.008;
RA   Lv K., Gong C., Antony C., Han X., Ren J.G., Donaghy R., Cheng Y.,
RA   Pellegrino S., Warren A.J., Paralkar V.R., Tong W.;
RT   "HectD1 controls hematopoietic stem cell regeneration by coordinating
RT   ribosome assembly and protein synthesis.";
RL   Cell Stem Cell 28:1275-1290(2021).
RN   [16]
RP   STRUCTURE BY NMR OF 1266-1338.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of MIB-HERC2 domain in HECT domain containing protein
RT   1.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates
CC       (PubMed:33711283). Mediates 'Lys-63'-linked polyubiquitination of
CC       HSP90AA1 which leads to its intracellular localization and reduced
CC       secretion (By similarity). Negatively regulating HSP90AA1 secretion in
CC       cranial mesenchyme cells may impair their emigration and may be
CC       essential for the correct development of the cranial neural folds and
CC       neural tube closure (By similarity). Catalyzes ubiquitination and
CC       degradation of ZNF622, an assembly factor for the ribosomal 60S
CC       subunit, in hematopoietic cells, thereby promoting hematopoietic stem
CC       cell renewal (PubMed:33711283). {ECO:0000250|UniProtKB:Q69ZR2,
CC       ECO:0000269|PubMed:33711283}.
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=2.3.2.26; Evidence={ECO:0000269|PubMed:33711283};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:33711283}.
CC   -!- SUBUNIT: Interacts with IGSF1 (PubMed:12421765).
CC       {ECO:0000269|PubMed:12421765}.
CC   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
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DR   EMBL; AY254380; AAP13073.1; -; mRNA.
DR   EMBL; AL121808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW65950.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW65952.1; -; Genomic_DNA.
DR   EMBL; AB032957; BAA86445.2; -; mRNA.
DR   EMBL; AL110222; CAB53681.1; -; mRNA.
DR   EMBL; BC011658; AAH11658.2; -; mRNA.
DR   EMBL; BC063686; AAH63686.1; -; mRNA.
DR   CCDS; CCDS41939.1; -.
DR   PIR; T14761; T14761.
DR   RefSeq; NP_056197.3; NM_015382.3.
DR   RefSeq; XP_005267559.2; XM_005267502.2.
DR   PDB; 2DK3; NMR; -; A=1266-1338.
DR   PDB; 2LC3; NMR; -; A=1879-1966.
DR   PDB; 3DKM; X-ray; 1.60 A; A=1271-1341.
DR   PDBsum; 2DK3; -.
DR   PDBsum; 2LC3; -.
DR   PDBsum; 3DKM; -.
DR   AlphaFoldDB; Q9ULT8; -.
DR   BMRB; Q9ULT8; -.
DR   SMR; Q9ULT8; -.
DR   BioGRID; 117359; 405.
DR   DIP; DIP-31669N; -.
DR   IntAct; Q9ULT8; 54.
DR   MINT; Q9ULT8; -.
DR   STRING; 9606.ENSP00000382269; -.
DR   GlyCosmos; Q9ULT8; 12 sites, 2 glycans.
DR   GlyGen; Q9ULT8; 21 sites, 2 O-linked glycans (21 sites).
DR   iPTMnet; Q9ULT8; -.
DR   PhosphoSitePlus; Q9ULT8; -.
DR   SwissPalm; Q9ULT8; -.
DR   BioMuta; HECTD1; -.
DR   DMDM; 313104227; -.
DR   EPD; Q9ULT8; -.
DR   jPOST; Q9ULT8; -.
DR   MassIVE; Q9ULT8; -.
DR   MaxQB; Q9ULT8; -.
DR   PaxDb; 9606-ENSP00000382269; -.
DR   PeptideAtlas; Q9ULT8; -.
DR   ProteomicsDB; 85108; -.
DR   Pumba; Q9ULT8; -.
DR   Antibodypedia; 5457; 144 antibodies from 25 providers.
DR   DNASU; 25831; -.
DR   Ensembl; ENST00000399332.6; ENSP00000382269.1; ENSG00000092148.14.
DR   Ensembl; ENST00000553700.5; ENSP00000450697.1; ENSG00000092148.14.
DR   GeneID; 25831; -.
DR   KEGG; hsa:25831; -.
DR   MANE-Select; ENST00000399332.6; ENSP00000382269.1; NM_015382.4; NP_056197.3.
DR   UCSC; uc001wrc.1; human.
DR   AGR; HGNC:20157; -.
DR   CTD; 25831; -.
DR   DisGeNET; 25831; -.
DR   GeneCards; HECTD1; -.
DR   HGNC; HGNC:20157; HECTD1.
DR   HPA; ENSG00000092148; Tissue enhanced (skeletal).
DR   MIM; 618649; gene.
DR   neXtProt; NX_Q9ULT8; -.
DR   OpenTargets; ENSG00000092148; -.
DR   PharmGKB; PA134989284; -.
DR   VEuPathDB; HostDB:ENSG00000092148; -.
DR   eggNOG; KOG4276; Eukaryota.
DR   GeneTree; ENSGT00940000156572; -.
DR   HOGENOM; CLU_000869_0_0_1; -.
DR   InParanoid; Q9ULT8; -.
DR   OMA; INHTLTM; -.
DR   OrthoDB; 1093891at2759; -.
DR   PhylomeDB; Q9ULT8; -.
DR   TreeFam; TF323674; -.
DR   PathwayCommons; Q9ULT8; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9ULT8; -.
DR   SIGNOR; Q9ULT8; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 25831; 305 hits in 1213 CRISPR screens.
DR   ChiTaRS; HECTD1; human.
DR   EvolutionaryTrace; Q9ULT8; -.
DR   GenomeRNAi; 25831; -.
DR   Pharos; Q9ULT8; Tbio.
DR   PRO; PR:Q9ULT8; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9ULT8; Protein.
DR   Bgee; ENSG00000092148; Expressed in tibialis anterior and 176 other cell types or tissues.
DR   ExpressionAtlas; Q9ULT8; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0035904; P:aorta development; ISS:BHF-UCL.
DR   GO; GO:0003170; P:heart valve development; ISS:BHF-UCL.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0003281; P:ventricular septum development; ISS:BHF-UCL.
DR   CDD; cd21062; BTHB_HectD1; 1.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 1.10.720.80; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR041200; FKBP3_BTHB.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR045322; HECTD1/TRIP12-like.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR037252; Mib_Herc2_sf.
DR   InterPro; IPR012919; SUN_dom.
DR   PANTHER; PTHR45670:SF19; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF18410; BTHB; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF06701; MIB_HERC2; 1.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51416; MIB_HERC2; 1.
DR   Genevisible; Q9ULT8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Phosphoprotein; Reference proteome; Repeat;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..2610
FT                   /note="E3 ubiquitin-protein ligase HECTD1"
FT                   /id="PRO_0000083945"
FT   REPEAT          395..424
FT                   /note="ANK 1"
FT   REPEAT          426..455
FT                   /note="ANK 2"
FT   REPEAT          459..491
FT                   /note="ANK 3"
FT   REPEAT          579..612
FT                   /note="ANK 4"
FT   DOMAIN          1266..1338
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT   DOMAIN          2151..2610
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          246..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1343..1406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1496..1515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1592..1611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1674..1757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1777..1797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2029..2103
FT                   /note="K-box"
FT   REGION          2297..2318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1345..1401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1675..1700
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1701..1721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1743..1757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2579
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69ZR2"
FT   MOD_RES         1384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69ZR2"
FT   MOD_RES         1488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q69ZR2"
FT   MOD_RES         1760
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1772
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         656
FT                   /note="Q -> H (in dbSNP:rs11620816)"
FT                   /id="VAR_059666"
FT   VARIANT         2027
FT                   /note="P -> L (in dbSNP:rs1315794)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_067707"
FT   MUTAGEN         2579
FT                   /note="C->G: Abolished E3 ubiquitin-protein ligase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:33711283"
FT   CONFLICT        561
FT                   /note="K -> Q (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        603
FT                   /note="L -> I (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611..613
FT                   /note="FLD -> YKH (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="K -> Q (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        894
FT                   /note="E -> K (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        927..944
FT                   /note="SMDLDMKQDCSQLVERIN -> VSIFRATKQKQNEVPKVILS (in Ref.
FT                   1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        951
FT                   /note="S -> T (in Ref. 1; AAP13073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1281
FT                   /note="I -> T (in Ref. 2; BAA86445)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1270..1272
FT                   /evidence="ECO:0007829|PDB:2DK3"
FT   STRAND          1279..1282
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   TURN            1289..1292
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   STRAND          1299..1301
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   STRAND          1309..1314
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   TURN            1315..1317
FT                   /evidence="ECO:0007829|PDB:2DK3"
FT   STRAND          1319..1325
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   HELIX           1326..1328
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   STRAND          1332..1334
FT                   /evidence="ECO:0007829|PDB:3DKM"
FT   HELIX           1883..1886
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   HELIX           1896..1902
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   STRAND          1905..1908
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   HELIX           1910..1920
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   HELIX           1923..1928
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   HELIX           1935..1941
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   HELIX           1944..1957
FT                   /evidence="ECO:0007829|PDB:2LC3"
FT   TURN            1960..1962
FT                   /evidence="ECO:0007829|PDB:2LC3"
SQ   SEQUENCE   2610 AA;  289368 MW;  C02FB51A2AABF98B CRC64;
     MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI
     FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA
     EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ
     DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM
     AAAGGTVSGP SSACKPGRST TGAPSTTADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS
     ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
     RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA
     DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVAILQ
     SPGDWMCPVN KGDDKKKKDT NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI
     RKASLALIRK MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII
     RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE DAKELQQGKP
     YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG KLATMYSSGS PEGGSDSSES
     RSEFLEKLQR ARGQVKPSTS SQPILSAPGP TKLTVGNWSL TCLKEGEIAI HNSDGQQATI
     LKEDLPGFVF ESNRGTKHSF TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL
     YDDHFKAVES MPRGVVVTLR NIATQLESSW ELHTNRQCIE SENTWRDLMK TALENLIVLL
     KDENTISPYE MCSSGLVQAL LTVLNNSMDL DMKQDCSQLV ERINVFKTAF SENEDDESRP
     AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR FRLERAPGET ALIDRTGRML
     KMEPLATVES LEQYLLKMVA KQWYDFDRSS FVFVRKLREG QNFIFRHQHD FDENGIIYWI
     GTNAKTAYEW VNPAAYGLVV VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID
     LGLWVIPSAY TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL
     DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK AAKEAEANLR
     RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGSPQGEGT VTGELHNGWI DVTWDAGGSN
     SYRMGAEGKF DLKLAPGYDP DTVASPKPVS STVSGTTQSW SSLVKNNCPD KTSAAAGSSS
     RKGSSSSVCS VASSSDISLG STKTERRSEI VMEHSIVSGA DVHEPIVVLS SAENVPQTEV
     GSSSSASTST LTAETGSENA ERKLGPDSSV RTPGESSAIS MGIVSVSSPD VSSVSELTNK
     EAASQRPLSS SASNRLSVSS LLAAGAPMSS SASVPNLSSR ETSSLESFVR RVANIARTNA
     TNNMNLSRSS SDNNTNTLGR NVMSTATSPL MGAQSFPNLT TPGTTSTVTM STSSVTSSSN
     VATATTVLSV GQSLSNTLTT SLTSTSSESD TGQEAEYSLY DFLDSCRAST LLAELDDDED
     LPEPDEEDDE NEDDNQEDQE YEEVMILRRP SLQRRAGSRS DVTHHAVTSQ LPQVPAGAGS
     RPIGEQEEEE YETKGGRRRT WDDDYVLKRQ FSALVPAFDP RPGRTNVQQT TDLEIPPPGT
     PHSELLEEVE CTPSPRLALT LKVTGLGTTR EVELPLTNFR STIFYYVQKL LQLSCNGNVK
     SDKLRRIWEP TYTIMYREMK DSDKEKENGK MGCWSIEHVE QYLGTDELPK NDLITYLQKN
     ADAAFLRHWK LTGTNKSIRK NRNCSQLIAA YKDFCEHGTK SGLNQGAIST LQSSDILNLT
     KEQPQAKAGN GQNSCGVEDV LQLLRILYIV ASDPYSRISQ EDGDEQPQFT FPPDEFTSKK
     ITTKILQQIE EPLALASGAL PDWCEQLTSK CPFLIPFETR QLYFTCTAFG ASRAIVWLQN
     RREATVERTR TTSSVRRDDP GEFRVGRLKH ERVKVPRGES LMEWAENVMQ IHADRKSVLE
     VEFLGEEGTG LGPTLEFYAL VAAEFQRTDL GAWLCDDNFP DDESRHVDLG GGLKPPGYYV
     QRSCGLFTAP FPQDSDELER ITKLFHFLGI FLAKCIQDNR LVDLPISKPF FKLMCMGDIK
     SNMSKLIYES RGDRDLHCTE SQSEASTEEG HDSLSVGSFE EDSKSEFILD PPKPKPPAWF
     NGILTWEDFE LVNPHRARFL KEIKDLAIKR RQILSNKGLS EDEKNTKLQE LVLKNPSGSG
     PPLSIEDLGL NFQFCPSSRI YGFTAVDLKP SGEDEMITMD NAEEYVDLMF DFCMHTGIQK
     QMEAFRDGFN KVFPMEKLSS FSHEEVQMIL CGNQSPSWAA EDIINYTEPK LGYTRDSPGF
     LRFVRVLCGM SSDERKAFLQ FTTGCSTLPP GGLANLHPRL TVVRKVDATD ASYPSVNTCV
     HYLKLPEYSS EEIMRERLLA ATMEKGFHLN
//