SIAH2_HUMAN
ID SIAH2_HUMAN Reviewed; 324 AA.
AC O43255; O43270;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=E3 ubiquitin-protein ligase SIAH2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase SIAH2 {ECO:0000305};
DE AltName: Full=Seven in absentia homolog 2;
DE Short=Siah-2;
DE Short=hSiah2;
GN Name=SIAH2;
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 TISSUE SPECIFICITY.
RX PubMed=9403064; DOI=10.1006/geno.1997.4997;
RA Hu G., Chung Y.-L., Glover T., Valentine V., Look A.T., Fearon E.R.;
RT "Characterization of human homologs of the Drosophila seven in absentia
RT (sina) gene.";
RL Genomics 46:103-111(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VAV1.
RX PubMed=10207103; DOI=10.1128/mcb.19.5.3798;
RA Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S.,
RA Varin-Blank N.;
RT "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling
RT pathways.";
RL Mol. Cell. Biol. 19:3798-3807(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP FUNCTION IN DEGRADATION OF DCC, AND INTERACTION WITH UBE2I AND DCC.
RX PubMed=9334332; DOI=10.1101/gad.11.20.2701;
RA Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.;
RT "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-
RT proteasome pathway.";
RL Genes Dev. 11:2701-2714(1997).
RN [5]
RP FUNCTION IN DEGRADATION OF POU2AF1.
RX PubMed=11483518; DOI=10.1093/emboj/20.15.4153;
RA Boehm J., He Y., Greiner A., Staudt L., Wirth T.;
RT "Regulation of BOB.1/OBF.1 stability by SIAH.";
RL EMBO J. 20:4153-4162(2001).
RN [6]
RP INTERACTION WITH CACYBP.
RX PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8;
RA Matsuzawa S., Reed J.C.;
RT "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
RT degradation linked to p53 responses.";
RL Mol. Cell 7:915-926(2001).
RN [7]
RP FUNCTION IN DEGRADATION OF TRAF2.
RX PubMed=12411493; DOI=10.1093/emboj/cdf576;
RA Habelhah H., Frew I.J., Laine A., Janes P.W., Relaix F., Sassoon D.,
RA Bowtell D.D.L., Ronai Z.;
RT "Stress-induced decrease in TRAF2 stability is mediated by Siah2.";
RL EMBO J. 21:5756-5765(2002).
RN [8]
RP INTERACTION WITH PEG10.
RX PubMed=12810624;
RA Okabe H., Satoh S., Furukawa Y., Kato T., Hasegawa S., Nakajima Y.,
RA Yamaoka Y., Nakamura Y.;
RT "Involvement of PEG10 in human hepatocellular carcinogenesis through
RT interaction with SIAH1.";
RL Cancer Res. 63:3043-3048(2003).
RN [9]
RP INTERACTION WITH EGLN2.
RX PubMed=16509823; DOI=10.1042/bj20051996;
RA Tian Y.M., Mole D.R., Ratcliffe P.J., Gleadle J.M.;
RT "Characterization of different isoforms of the HIF prolyl hydroxylase PHD1
RT generated by alternative initiation.";
RL Biochem. J. 397:179-186(2006).
RN [10]
RP FUNCTION, INTERACTION WITH SNCAIP, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=19224863; DOI=10.1074/jbc.m805990200;
RA Szargel R., Rott R., Eyal A., Haskin J., Shani V., Balan L., Wolosker H.,
RA Engelender S.;
RT "Synphilin-1A inhibits seven in absentia homolog (SIAH) and modulates
RT alpha-synuclein monoubiquitylation and inclusion formation.";
RL J. Biol. Chem. 284:11706-11716(2009).
RN [11]
RP FUNCTION, INTERACTION WITH DYRK2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-16; THR-26; SER-28; SER-68 AND THR-119, MUTAGENESIS OF SER-16; THR-26;
RP SER-28; SER-68 AND THR-119, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22878263; DOI=10.1093/jmcb/mjs047;
RA Perez M., Garcia-Limones C., Zapico I., Marina A., Schmitz M.L., Munoz E.,
RA Calzado M.A.;
RT "Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic
RT signaling pathways.";
RL J. Mol. Cell Biol. 4:316-330(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP FUNCTION, AND INTERACTION WITH NR1D1 AND NR1D2.
RX PubMed=26392558; DOI=10.1073/pnas.1501204112;
RA DeBruyne J.P., Baggs J.E., Sato T.K., Hogenesch J.B.;
RT "Ubiquitin ligase Siah2 regulates RevErbalpha degradation and the mammalian
RT circadian clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:12420-12425(2015).
RN [14]
RP FUNCTION, AND INTERACTION WITH AXIN1.
RX PubMed=28546513; DOI=10.1101/gad.300053.117;
RA Ji L., Jiang B., Jiang X., Charlat O., Chen A., Mickanin C., Bauer A.,
RA Xu W., Yan X., Cong F.;
RT "The SIAH E3 ubiquitin ligases promote Wnt/beta-catenin signaling through
RT mediating Wnt-induced Axin degradation.";
RL Genes Dev. 31:904-915(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins (PubMed:9334332,
CC PubMed:11483518, PubMed:19224863). E3 ubiquitin ligases accept
CC ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates (PubMed:9334332, PubMed:11483518, PubMed:19224863). Mediates
CC E3 ubiquitin ligase activity either through direct binding to
CC substrates or by functioning as the essential RING domain subunit of
CC larger E3 complexes (PubMed:9334332, PubMed:11483518, PubMed:19224863).
CC Triggers the ubiquitin-mediated degradation of many substrates,
CC including proteins involved in transcription regulation (GPS2, POU2AF1,
CC PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein
CC (BAG1), and a protein involved in synaptic vesicle function in neurons
CC (SYP) (PubMed:9334332, PubMed:11483518, PubMed:19224863). Mediates
CC ubiquitination and proteasomal degradation of DYRK2 in response to
CC hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor
CC suppression, cell cycle, transcription and signaling processes
CC (PubMed:9334332, PubMed:11483518, PubMed:19224863, PubMed:22878263).
CC Has some overlapping function with SIAH1 (PubMed:9334332,
CC PubMed:11483518, PubMed:19224863). Triggers the ubiquitin-mediated
CC degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493).
CC Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates
CC cellular clock function via ubiquitination of the circadian
CC transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal
CC degradation (PubMed:26392558). Plays an important role in mediating the
CC rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their
CC circadian profile of protein abundance (PubMed:26392558). Mediates
CC ubiquitination and degradation of EGLN2 and EGLN3 in response to the
CC unfolded protein response (UPR), leading to their degradation and
CC subsequent stabilization of ATF4 (By similarity). Also part of the Wnt
CC signaling pathway in which it mediates the Wnt-induced ubiquitin-
CC mediated proteasomal degradation of AXIN1.
CC {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:11483518,
CC ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863,
CC ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558,
CC ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}.
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 -!- ACTIVITY REGULATION: Inhibited by interaction with SNCAIP (isoform 2,
CC but not isoform 1). May be inhibited by interaction with PEG10.
CC {ECO:0000269|PubMed:19224863}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with UBE2E2. Interacts with PEG3 (By
CC similarity). Interacts with VAV1, without mediating its ubiquitin-
CC mediated degradation. Interacts with CACYBP/SIP. Probable component of
CC some large E3 complex possibly composed of UBE2D1, SIAH2, CACYBP/SIP,
CC SKP1, APC and TBL1X. Interacts with PEG10, which may inhibit its
CC activity. Interacts with EGLN2 and SNCAIP. Interacts with DYRK2.
CC Interacts with NR1D1 and NR1D2 (PubMed:26392558). Interacts with DCC
CC (PubMed:9334332). Interacts with AXIN1 (PubMed:28546513).
CC {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:10207103,
CC ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:12810624,
CC ECO:0000269|PubMed:16509823, ECO:0000269|PubMed:19224863,
CC ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558,
CC ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}.
CC -!- INTERACTION:
CC O43255; O95835: LATS1; NbExp=2; IntAct=EBI-948141, EBI-444209;
CC O43255; Q9NRM7: LATS2; NbExp=6; IntAct=EBI-948141, EBI-3506895;
CC O43255; P35372: OPRM1; NbExp=3; IntAct=EBI-948141, EBI-2624570;
CC O43255; Q7Z6J0: SH3RF1; NbExp=3; IntAct=EBI-948141, EBI-311339;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19224863,
CC ECO:0000269|PubMed:22878263}. Nucleus {ECO:0000269|PubMed:22878263}.
CC Note=Predominantly cytoplasmic. Partially nuclear.
CC {ECO:0000269|PubMed:22878263}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level.
CC {ECO:0000269|PubMed:9403064}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC homodimerization and the interaction with substrate proteins. It is
CC related to the TRAF family. {ECO:0000250|UniProtKB:P61092}.
CC -!- PTM: Phosphorylated at Ser-28 by MAPK14, which mediates the degradation
CC by the proteasome of EGLN3 (By similarity). Phosphorylated at Ser-28 by
CC DYRK2; this increases the ubiquitin ligase activity and promotes
CC degradation of EGLN3. {ECO:0000250|UniProtKB:Q06986,
CC ECO:0000269|PubMed:22878263}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SIAH2ID46199ch3q25.html";
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DR EMBL; U76248; AAC51908.1; -; mRNA.
DR EMBL; Y15268; CAA75557.1; -; mRNA.
DR EMBL; BC013082; AAH13082.1; -; mRNA.
DR CCDS; CCDS3152.1; -.
DR RefSeq; NP_005058.3; NM_005067.5.
DR PDB; 5H9M; X-ray; 1.76 A; A/B=131-321.
DR PDBsum; 5H9M; -.
DR AlphaFoldDB; O43255; -.
DR SMR; O43255; -.
DR BioGRID; 112373; 85.
DR CORUM; O43255; -.
DR DIP; DIP-41874N; -.
DR IntAct; O43255; 25.
DR MINT; O43255; -.
DR STRING; 9606.ENSP00000322457; -.
DR TCDB; 8.A.133.1.2; the siah1 e3 ubiquitin-protein ligase (siah1) family.
DR iPTMnet; O43255; -.
DR PhosphoSitePlus; O43255; -.
DR BioMuta; SIAH2; -.
DR MassIVE; O43255; -.
DR MaxQB; O43255; -.
DR PaxDb; O43255; -.
DR PeptideAtlas; O43255; -.
DR PRIDE; O43255; -.
DR ProteomicsDB; 48838; -.
DR Antibodypedia; 33601; 245 antibodies from 29 providers.
DR DNASU; 6478; -.
DR Ensembl; ENST00000312960.4; ENSP00000322457.3; ENSG00000181788.4.
DR GeneID; 6478; -.
DR KEGG; hsa:6478; -.
DR MANE-Select; ENST00000312960.4; ENSP00000322457.3; NM_005067.7; NP_005058.3.
DR UCSC; uc003eyi.4; human.
DR CTD; 6478; -.
DR DisGeNET; 6478; -.
DR GeneCards; SIAH2; -.
DR HGNC; HGNC:10858; SIAH2.
DR HPA; ENSG00000181788; Low tissue specificity.
DR MIM; 602213; gene.
DR neXtProt; NX_O43255; -.
DR OpenTargets; ENSG00000181788; -.
DR PharmGKB; PA35760; -.
DR VEuPathDB; HostDB:ENSG00000181788; -.
DR eggNOG; KOG3002; Eukaryota.
DR GeneTree; ENSGT00940000159812; -.
DR HOGENOM; CLU_028215_0_0_1; -.
DR InParanoid; O43255; -.
DR OMA; NKPCGKQ; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; O43255; -.
DR TreeFam; TF312976; -.
DR PathwayCommons; O43255; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O43255; -.
DR SIGNOR; O43255; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6478; 12 hits in 1124 CRISPR screens.
DR ChiTaRS; SIAH2; human.
DR GeneWiki; SIAH2; -.
DR GenomeRNAi; 6478; -.
DR Pharos; O43255; Tbio.
DR PRO; PR:O43255; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43255; protein.
DR Bgee; ENSG00000181788; Expressed in adrenal tissue and 184 other tissues.
DR ExpressionAtlas; O43255; baseline and differential.
DR Genevisible; O43255; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990000; P:amyloid fibril formation; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; PTHR45877; 1.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Biological rhythms; Cell cycle; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..324
FT /note="E3 ubiquitin-protein ligase SIAH2"
FT /id="PRO_0000056168"
FT ZN_FING 80..115
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 133..193
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..322
FT /note="SBD"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT COMPBIAS 14..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P61092"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:22878263"
FT MOD_RES 26
FT /note="Phosphothreonine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:22878263"
FT MOD_RES 28
FT /note="Phosphoserine; by DYRK2 and MAPK14"
FT /evidence="ECO:0000269|PubMed:22878263"
FT MOD_RES 68
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:22878263"
FT MOD_RES 119
FT /note="Phosphothreonine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:22878263"
FT MUTAGEN 16
FT /note="S->A: Strongly reduced phosphorylation by DYRK2;
FT when associated with A-26; A-28; A-68 and A-119."
FT /evidence="ECO:0000269|PubMed:22878263"
FT MUTAGEN 26
FT /note="T->A: Strongly reduced phosphorylation by DYRK2;
FT when associated with A-16; A-28; A-68 and A-119."
FT /evidence="ECO:0000269|PubMed:22878263"
FT MUTAGEN 28
FT /note="S->A: Strongly reduced phosphorylation by DYRK2;
FT when associated with A-16; A-26; A-68 and A-119."
FT /evidence="ECO:0000269|PubMed:22878263"
FT MUTAGEN 68
FT /note="S->A: Strongly reduced phosphorylation by DYRK2;
FT when associated with A-16; A-26; A-28 and A-119."
FT /evidence="ECO:0000269|PubMed:22878263"
FT MUTAGEN 119
FT /note="T->A: Strongly reduced phosphorylation by DYRK2;
FT when associated with A-16; A-26; A-28 and A-68."
FT /evidence="ECO:0000269|PubMed:22878263"
FT CONFLICT 200
FT /note="G -> E (in Ref. 1; AAC51908)"
FT /evidence="ECO:0000305"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5H9M"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 227..239
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5H9M"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:5H9M"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:5H9M"
SQ SEQUENCE 324 AA; 34615 MW; 2D5DD845666EC924 CRC64;
MSRPSSTGPS ANKPCSKQPP PQPQHTPSPA APPAAATISA AGPGSSAVPA AAAVISGPGG
GGGAGPVSPQ HHELTSLFEC PVCFDYVLPP ILQCQAGHLV CNQCRQKLSC CPTCRGALTP
SIRNLAMEKV ASAVLFPCKY ATTGCSLTLH HTEKPEHEDI CEYRPYSCPC PGASCKWQGS
LEAVMSHLMH AHKSITTLQG EDIVFLATDI NLPGAVDWVM MQSCFGHHFM LVLEKQEKYE
GHQQFFAIVL LIGTRKQAEN FAYRLELNGN RRRLTWEATP RSIHDGVAAA IMNSDCLVFD
TAIAHLFADN GNLGINVTIS TCCP
