EIF2D_HUMAN
ID EIF2D_HUMAN Reviewed; 584 AA.
AC P41214; Q5SY40; Q8IXV3; Q96DG3; Q96TG7; Q9NR27; Q9NSN0; Q9NV18; Q9NZ21;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Eukaryotic translation initiation factor 2D;
DE Short=eIF2d;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 56;
DE AltName: Full=Ligatin;
GN Name=EIF2D; Synonyms=HCA56, LGTN;
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] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20566627; DOI=10.1074/jbc.m110.119693;
RA Dmitriev S.E., Terenin I.M., Andreev D.E., Ivanov P.A., Dunaevsky J.E.,
RA Merrick W.C., Shatsky I.N.;
RT "GTP-independent tRNA delivery to the ribosomal P-site by a novel
RT eukaryotic translation factor.";
RL J. Biol. Chem. 285:26779-26787(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-associated
RT antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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=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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Lymph, and Testis;
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 196-584 (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 234-308.
RX PubMed=2482295; DOI=10.1242/jcs.93.2.227;
RA Jakoi E.R., Brown A.L., Ho Y.S., Snyderman R.;
RT "Molecular cloning of the cDNA for ligatin.";
RL J. Cell Sci. 93:227-232(1989).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS 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 [11]
RP FUNCTION.
RX PubMed=20713520; DOI=10.1101/gad.1957510;
RA Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U.,
RA Pestova T.V.;
RT "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation
RT and ribosomal recycling.";
RL Genes Dev. 24:1787-1801(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-361, 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).
CC -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC the P-site of 40S ribosomes, the situation that takes place during
CC initiation complex formation on some specific RNAs. Its activity in
CC tRNA binding with 40S subunits does not require the presence of the
CC aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC its role in initiation, can promote release of deacylated tRNA and mRNA
CC from recycled 40S subunits following ABCE1-mediated dissociation of
CC post-termination ribosomal complexes into subunits.
CC {ECO:0000269|PubMed:20566627, ECO:0000269|PubMed:20713520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20566627}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41214-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41214-2; Sequence=VSP_006300;
CC -!- DEVELOPMENTAL STAGE: Found during embryonic development and in early
CC differentiated states.
CC -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
CC -!- CAUTION: Was previously erroneously called ligatin, a trafficking
CC receptor for phosphoglycoproteins, while ligatin is actually a distinct
CC 10 kDa filamentous membrane protein encoded by a still unidentified
CC gene. {ECO:0000305|PubMed:20566627}.
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DR EMBL; AF220417; AAF34185.2; -; mRNA.
DR EMBL; AF262403; AAF74205.1; -; mRNA.
DR EMBL; AK001852; BAA91942.1; -; mRNA.
DR EMBL; AL591846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93536.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93540.1; -; Genomic_DNA.
DR EMBL; BC001585; AAH01585.1; -; mRNA.
DR EMBL; BC039134; AAH39134.2; -; mRNA.
DR EMBL; BC058905; AAH58905.1; -; mRNA.
DR EMBL; AL162001; CAB82330.1; -; mRNA.
DR EMBL; AF159586; AAD41909.1; -; mRNA.
DR CCDS; CCDS1465.1; -. [P41214-1]
DR CCDS; CCDS55680.1; -. [P41214-2]
DR PIR; A60697; A60697.
DR PIR; T47178; T47178.
DR RefSeq; NP_001188407.1; NM_001201478.1. [P41214-2]
DR RefSeq; NP_008824.2; NM_006893.2. [P41214-1]
DR PDB; 5OA3; EM; 4.30 A; 0=1-584.
DR PDB; 5OA9; X-ray; 1.80 A; A=380-584.
DR PDB; 5W2F; X-ray; 1.40 A; A=380-584.
DR PDBsum; 5OA3; -.
DR PDBsum; 5OA9; -.
DR PDBsum; 5W2F; -.
DR AlphaFoldDB; P41214; -.
DR SMR; P41214; -.
DR BioGRID; 108259; 36.
DR IntAct; P41214; 5.
DR MINT; P41214; -.
DR STRING; 9606.ENSP00000271764; -.
DR iPTMnet; P41214; -.
DR MetOSite; P41214; -.
DR PhosphoSitePlus; P41214; -.
DR BioMuta; EIF2D; -.
DR DMDM; 158957575; -.
DR EPD; P41214; -.
DR jPOST; P41214; -.
DR MassIVE; P41214; -.
DR MaxQB; P41214; -.
DR PaxDb; P41214; -.
DR PeptideAtlas; P41214; -.
DR PRIDE; P41214; -.
DR ProteomicsDB; 55417; -. [P41214-1]
DR ProteomicsDB; 55418; -. [P41214-2]
DR Antibodypedia; 34586; 122 antibodies from 26 providers.
DR DNASU; 1939; -.
DR Ensembl; ENST00000271764.7; ENSP00000271764.2; ENSG00000143486.16. [P41214-1]
DR Ensembl; ENST00000367114.7; ENSP00000356081.3; ENSG00000143486.16. [P41214-2]
DR GeneID; 1939; -.
DR KEGG; hsa:1939; -.
DR MANE-Select; ENST00000271764.7; ENSP00000271764.2; NM_006893.3; NP_008824.2.
DR UCSC; uc001heh.4; human. [P41214-1]
DR CTD; 1939; -.
DR DisGeNET; 1939; -.
DR GeneCards; EIF2D; -.
DR HGNC; HGNC:6583; EIF2D.
DR HPA; ENSG00000143486; Low tissue specificity.
DR MIM; 613709; gene.
DR neXtProt; NX_P41214; -.
DR OpenTargets; ENSG00000143486; -.
DR PharmGKB; PA30355; -.
DR VEuPathDB; HostDB:ENSG00000143486; -.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR InParanoid; P41214; -.
DR OMA; MFLKPYR; -.
DR OrthoDB; 401807at2759; -.
DR PhylomeDB; P41214; -.
DR TreeFam; TF105830; -.
DR PathwayCommons; P41214; -.
DR SignaLink; P41214; -.
DR BioGRID-ORCS; 1939; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; EIF2D; human.
DR GeneWiki; LGTN; -.
DR GenomeRNAi; 1939; -.
DR Pharos; P41214; Tbio.
DR PRO; PR:P41214; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P41214; protein.
DR Bgee; ENSG00000143486; Expressed in left ovary and 194 other tissues.
DR ExpressionAtlas; P41214; baseline and differential.
DR Genevisible; P41214; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB.
DR CDD; cd11608; eIF2D_C; 1.
DR DisProt; DP02704; -.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR12217; PTHR12217; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01253; SUI1; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..584
FT /note="Eukaryotic translation initiation factor 2D"
FT /id="PRO_0000130611"
FT DOMAIN 93..173
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT DOMAIN 383..467
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT DOMAIN 491..564
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 223..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61211"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 177..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12097419"
FT /id="VSP_006300"
FT VARIANT 210
FT /note="T -> I (in dbSNP:rs35252702)"
FT /id="VAR_052507"
FT CONFLICT 11
FT /note="N -> D (in Ref. 3; BAA91942)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> N (in Ref. 2; AAF34185/AAF74205)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="T -> N (in Ref. 2; AAF34185)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..308
FT /note="GRQLD -> DDNWT (in Ref. 8; AAD41909)"
FT /evidence="ECO:0000305"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:5W2F"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 408..421
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5OA9"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:5OA9"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 491..499
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 517..528
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 553..561
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5W2F"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:5W2F"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:5W2F"
SQ SEQUENCE 584 AA; 64706 MW; C302B63268231154 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTTAF PTLGTDQVSE LVPGKEELNI VKLYAHKGDA
VTVYVSGGNP ILFELEKNLY PTVYTLWSYP DLLPTFTTWP LVLEKLVGGA DLMLPGLVMP
PAGLPQVQKG DLCAISLVGN RAPVAIGVAA MSTAEMLTSG LKGRGFSVLH TYQDHLWRSG
NKSSPPSIAP LALDSADLSE EKGSVQMDST LQGDMRHMTL EGEEENGEVH QAREDKSLSE
APEDTSTRGL NQDSTDSKTL QEQMDELLQQ CFLHALKCRV KKADLPLLTS TFLGSHMFSC
CPEGRQLDIK KSSYKKLSKF LQQMQQEQII QVKELSKGVE SIVAVDWKHP RITSFVIPEP
SPTSQTIQEG SREQPYHPPD IKPLYCVPAS MTLLFQESGH KKGSFLEGSE VRTIVINYAK
KNDLVDADNK NLVRLDPILC DCILEKNEQH TVMKLPWDSL LTRCLEKLQP AYQVTLPGQE
PIVKKGRICP IDITLAQRAS NKKVTVVRNL EAYGLDPYSV AAILQQRCQA STTVNPAPGA
KDSLQVQIQG NQVHHLGWLL LEEYQLPRKH IQGLEKALKP GKKK
