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 27-NOV-2024, entry version 200. 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}. 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; 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 EMDB; EMD-3770; -. DR SMR; P41214; -. DR BioGRID; 108259; 54. DR IntAct; P41214; 17. DR MINT; P41214; -. DR STRING; 9606.ENSP00000271764; -. DR iPTMnet; P41214; -. DR MetOSite; P41214; -. DR PhosphoSitePlus; P41214; -. DR BioMuta; EIF2D; -. DR DMDM; 158957575; -. DR jPOST; P41214; -. DR MassIVE; P41214; -. DR PaxDb; 9606-ENSP00000271764; -. DR PeptideAtlas; P41214; -. DR ProteomicsDB; 55417; -. [P41214-1] DR ProteomicsDB; 55418; -. [P41214-2] DR Pumba; P41214; -. DR Antibodypedia; 34586; 117 antibodies from 25 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 AGR; HGNC:6583; -. 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; 102595at2759; -. DR PhylomeDB; P41214; -. DR TreeFam; TF105830; -. DR PathwayCommons; P41214; -. DR SignaLink; P41214; -. DR BioGRID-ORCS; 1939; 19 hits in 1158 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 196 other cell types or tissues. DR ExpressionAtlas; P41214; baseline and differential. 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 CDD; cd11610; eIF2D_N; 1. DR CDD; cd21156; PUA_eIF2d-like; 1. DR DisProt; DP02704; -. DR FunFam; 3.10.400.20:FF:000002; Eukaryotic translation initiation factor 2D; 1. DR FunFam; 3.30.780.10:FF:000007; Putative eukaryotic translation initiation factor 2d; 1. DR Gene3D; 3.10.400.20; -; 1. DR Gene3D; 3.30.780.10; SUI1-like domain; 1. DR InterPro; IPR039757; EIF2D. DR InterPro; IPR048247; eIF2D_N. DR InterPro; IPR039759; eIF2D_SUI1. DR InterPro; IPR041366; Pre-PUA. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR048248; PUA_eIF2d-like. 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; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1. DR PANTHER; PTHR12217:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1. DR Pfam; PF17832; Pre-PUA; 1. DR Pfam; PF01253; SUI1; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF55159; eIF1-like; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR SUPFAM; SSF47592; SWIB/MDM2 domain; 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 Proteomics identification; 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 //