EFHD2_HUMAN
ID EFHD2_HUMAN Reviewed; 240 AA.
AC Q96C19; Q5JYW9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=EFHD2; Synonyms=SWS1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, Testis, and Uterus;
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 PROTEIN SEQUENCE OF 2-12; 62-78; 103-118; 124-134; 139-159; 177-188 AND
RP 230-240, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 63-77; 79-87; 160-176 AND 207-218, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11788997;
RX DOI=10.1002/1615-9861(200201)2:1<105::aid-prot105>3.0.co;2-f;
RA Vuadens F., Gasparini D., Deon C., Sanchez J.-C., Hochstrasser D.F.,
RA Schneider P., Tissot J.-D.;
RT "Identification of specific proteins in different lymphocyte populations by
RT proteomic tools.";
RL Proteomics 2:105-111(2002).
RN [7]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15274114; DOI=10.1002/pmic.200300779;
RA Vuadens F., Rufer N., Kress A., Corthesy P., Schneider P., Tissot J.-D.;
RT "Identification of swiprosin 1 in human lymphocytes.";
RL Proteomics 4:2216-2220(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-76, AND
RP IDENTIFICATION BY 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 [12]
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 [13]
RP INTERACTION WITH CASP9, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19118655; DOI=10.1016/j.jprot.2008.11.016;
RA Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.;
RT "Comparative proteomics analysis of caspase-9-protein complexes in
RT untreated and cytochrome c/dATP stimulated lysates of NSCLC cells.";
RL J. Proteomics 72:575-585(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11; SER-74 AND SER-76, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-74 AND SER-76, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-76, AND
RP IDENTIFICATION BY 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May regulate B-cell receptor (BCR)-induced immature and
CC primary B-cell apoptosis. Plays a role as negative regulator of the
CC canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis
CC through the regulation of BCL2L1 abundance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CASP9; with inactive form.
CC {ECO:0000269|PubMed:19118655}.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000250}. Note=In a mouse
CC immature B-cell line WEHI-231. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found in lymphocytes; preferentially expressed in
CC CD8+ cells. {ECO:0000269|PubMed:11788997, ECO:0000269|PubMed:15274114}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL031283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471167; EAW51720.1; -; Genomic_DNA.
DR EMBL; BC007233; AAH07233.1; -; mRNA.
DR EMBL; BC014923; AAH14923.1; -; mRNA.
DR EMBL; BC023611; AAH23611.1; -; mRNA.
DR EMBL; BC068473; AAH68473.1; -; mRNA.
DR CCDS; CCDS155.1; -.
DR RefSeq; NP_077305.2; NM_024329.5.
DR PDB; 5H0P; X-ray; 1.86 A; A=70-184.
DR PDB; 5I2L; X-ray; 1.85 A; A=70-184.
DR PDB; 5I2O; X-ray; 1.95 A; A=70-184.
DR PDB; 5I2Q; X-ray; 1.94 A; A=70-184.
DR PDBsum; 5H0P; -.
DR PDBsum; 5I2L; -.
DR PDBsum; 5I2O; -.
DR PDBsum; 5I2Q; -.
DR AlphaFoldDB; Q96C19; -.
DR SMR; Q96C19; -.
DR BioGRID; 122597; 80.
DR IntAct; Q96C19; 26.
DR MINT; Q96C19; -.
DR STRING; 9606.ENSP00000365147; -.
DR GlyGen; Q96C19; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96C19; -.
DR MetOSite; Q96C19; -.
DR PhosphoSitePlus; Q96C19; -.
DR SwissPalm; Q96C19; -.
DR BioMuta; EFHD2; -.
DR DMDM; 20140139; -.
DR REPRODUCTION-2DPAGE; IPI00060181; -.
DR SWISS-2DPAGE; Q96C19; -.
DR EPD; Q96C19; -.
DR jPOST; Q96C19; -.
DR MassIVE; Q96C19; -.
DR MaxQB; Q96C19; -.
DR PaxDb; Q96C19; -.
DR PeptideAtlas; Q96C19; -.
DR PRIDE; Q96C19; -.
DR ProteomicsDB; 76150; -.
DR TopDownProteomics; Q96C19; -.
DR Antibodypedia; 28833; 176 antibodies from 34 providers.
DR DNASU; 79180; -.
DR Ensembl; ENST00000375980.9; ENSP00000365147.4; ENSG00000142634.13.
DR GeneID; 79180; -.
DR KEGG; hsa:79180; -.
DR MANE-Select; ENST00000375980.9; ENSP00000365147.4; NM_024329.6; NP_077305.2.
DR UCSC; uc001awh.2; human.
DR CTD; 79180; -.
DR DisGeNET; 79180; -.
DR GeneCards; EFHD2; -.
DR HGNC; HGNC:28670; EFHD2.
DR HPA; ENSG00000142634; Low tissue specificity.
DR MIM; 616450; gene.
DR neXtProt; NX_Q96C19; -.
DR OpenTargets; ENSG00000142634; -.
DR PharmGKB; PA134942316; -.
DR VEuPathDB; HostDB:ENSG00000142634; -.
DR eggNOG; KOG0041; Eukaryota.
DR GeneTree; ENSGT00390000012058; -.
DR HOGENOM; CLU_094429_0_0_1; -.
DR InParanoid; Q96C19; -.
DR OMA; SPREFML; -.
DR OrthoDB; 1511376at2759; -.
DR PhylomeDB; Q96C19; -.
DR TreeFam; TF320736; -.
DR PathwayCommons; Q96C19; -.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR SignaLink; Q96C19; -.
DR BioGRID-ORCS; 79180; 24 hits in 1079 CRISPR screens.
DR ChiTaRS; EFHD2; human.
DR GenomeRNAi; 79180; -.
DR Pharos; Q96C19; Tbio.
DR PRO; PR:Q96C19; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96C19; protein.
DR Bgee; ENSG00000142634; Expressed in granulocyte and 172 other tissues.
DR ExpressionAtlas; Q96C19; baseline and differential.
DR Genevisible; Q96C19; HS.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040365; EFHD1/2.
DR PANTHER; PTHR13025; PTHR13025; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..240
FT /note="EF-hand domain-containing protein D2"
FT /id="PRO_0000073645"
FT DOMAIN 92..127
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..163
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 13..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8Y0"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5I2L"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:5I2L"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:5I2L"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:5I2L"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:5I2L"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5I2L"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:5I2L"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:5I2L"
SQ SEQUENCE 240 AA; 26697 MW; 9FE3FEC3007A8FC2 CRC64;
MATDELATKL SRRLQMEGEG GGETPEQPGL NGAAAAAAGA PDEAAEALGS ADCELSAKLL
RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM
MEKLGAPQTH LGLKNMIKEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LCVLARLSEI
DVSSEGVKGA KSFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEMKQRKA AFKELQSTFK
