Full text data of EIF2D
EIF2D
(HCA56, LGTN)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 2D; eIF2d (Hepatocellular carcinoma-associated antigen 56; Ligatin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 2D; eIF2d (Hepatocellular carcinoma-associated antigen 56; Ligatin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P41214
ID EIF2D_HUMAN Reviewed; 584 AA.
AC P41214; Q5SY40; Q8IXV3; Q96DG3; Q96TG7; Q9NR27; Q9NSN0; Q9NV18;
read moreAC Q9NZ21;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MASS SPECTROMETRY, FUNCTION,
RP 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.,
RA Dunaevsky J.E., 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;
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-
RT associated 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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;
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.,
RA Walther T.C., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Translation initiation factor that is able to deliver
CC tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC finds its position in the P-site of 40S ribosomes, the situation
CC that takes place during initiation complex formation on some
CC specific RNAs. Its activity in tRNA binding with 40S subunits does
CC not require the presence of the aminoacyl moiety. Possesses the
CC unique ability to deliver non-Met (elongator) tRNAs into the P-
CC site of the 40S subunit. In addition to its role in initiation,
CC can promote release of deacylated tRNA and mRNA from recycled 40S
CC subunits following ABCE1-mediated dissociation of post-termination
CC ribosomal complexes into subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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
CC early differentiated states.
CC -!- SIMILARITY: Belongs to the eIF2D family.
CC -!- SIMILARITY: Contains 1 PUA domain.
CC -!- SIMILARITY: Contains 1 SUI1 domain.
CC -!- CAUTION: Was previously erroneously called ligatin, a trafficking
CC receptor for phosphoglycoproteins, while ligatin is actually a
CC distinct 10 kDa filamentous membrane protein encoded by a still
CC unidentified gene (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; CAI13533.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI13534.1; -; 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 PIR; A60697; A60697.
DR PIR; T47178; T47178.
DR RefSeq; NP_001188407.1; NM_001201478.1.
DR RefSeq; NP_008824.2; NM_006893.2.
DR UniGene; Hs.497581; -.
DR ProteinModelPortal; P41214; -.
DR SMR; P41214; 1-177.
DR IntAct; P41214; 1.
DR MINT; MINT-3015310; -.
DR PhosphoSite; P41214; -.
DR DMDM; 158957575; -.
DR PaxDb; P41214; -.
DR PRIDE; P41214; -.
DR DNASU; 1939; -.
DR Ensembl; ENST00000271764; ENSP00000271764; ENSG00000143486.
DR Ensembl; ENST00000367114; ENSP00000356081; ENSG00000143486.
DR Ensembl; ENST00000580424; ENSP00000464465; ENSG00000265823.
DR Ensembl; ENST00000585127; ENSP00000463712; ENSG00000265823.
DR GeneID; 1939; -.
DR KEGG; hsa:1939; -.
DR UCSC; uc001heh.2; human.
DR CTD; 1939; -.
DR GeneCards; GC01M206745; -.
DR HGNC; HGNC:6583; EIF2D.
DR HPA; HPA028220; -.
DR MIM; 613709; gene.
DR neXtProt; NX_P41214; -.
DR PharmGKB; PA30355; -.
DR eggNOG; COG2016; -.
DR HOVERGEN; HBG006268; -.
DR InParanoid; P41214; -.
DR KO; K15027; -.
DR OMA; TVMKLPW; -.
DR PhylomeDB; P41214; -.
DR ChiTaRS; EIF2D; human.
DR GeneWiki; LGTN; -.
DR GenomeRNAi; 1939; -.
DR NextBio; 7857; -.
DR PRO; PR:P41214; -.
DR ArrayExpress; P41214; -.
DR Bgee; P41214; -.
DR Genevestigator; P41214; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.30.780.10; -; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_domain.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR001950; TIF_SUI1.
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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1 584 Eukaryotic translation initiation factor
FT 2D.
FT /FTId=PRO_0000130611.
FT DOMAIN 93 173 PUA.
FT DOMAIN 491 564 SUI1.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 237 237 Phosphoserine.
FT VAR_SEQ 177 300 Missing (in isoform 2).
FT /FTId=VSP_006300.
FT VARIANT 210 210 T -> I (in dbSNP:rs35252702).
FT /FTId=VAR_052507.
FT CONFLICT 11 11 N -> D (in Ref. 3; BAA91942).
FT CONFLICT 66 66 S -> N (in Ref. 2; AAF34185/AAF74205).
FT CONFLICT 210 210 T -> N (in Ref. 2; AAF34185).
FT CONFLICT 304 308 GRQLD -> DDNWT (in Ref. 8; AAD41909).
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
//
ID EIF2D_HUMAN Reviewed; 584 AA.
AC P41214; Q5SY40; Q8IXV3; Q96DG3; Q96TG7; Q9NR27; Q9NSN0; Q9NV18;
read moreAC Q9NZ21;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MASS SPECTROMETRY, FUNCTION,
RP 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.,
RA Dunaevsky J.E., 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;
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-
RT associated 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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;
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.,
RA Walther T.C., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Translation initiation factor that is able to deliver
CC tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC finds its position in the P-site of 40S ribosomes, the situation
CC that takes place during initiation complex formation on some
CC specific RNAs. Its activity in tRNA binding with 40S subunits does
CC not require the presence of the aminoacyl moiety. Possesses the
CC unique ability to deliver non-Met (elongator) tRNAs into the P-
CC site of the 40S subunit. In addition to its role in initiation,
CC can promote release of deacylated tRNA and mRNA from recycled 40S
CC subunits following ABCE1-mediated dissociation of post-termination
CC ribosomal complexes into subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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
CC early differentiated states.
CC -!- SIMILARITY: Belongs to the eIF2D family.
CC -!- SIMILARITY: Contains 1 PUA domain.
CC -!- SIMILARITY: Contains 1 SUI1 domain.
CC -!- CAUTION: Was previously erroneously called ligatin, a trafficking
CC receptor for phosphoglycoproteins, while ligatin is actually a
CC distinct 10 kDa filamentous membrane protein encoded by a still
CC unidentified gene (PubMed:20566627).
CC -----------------------------------------------------------------------
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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; CAI13533.1; -; Genomic_DNA.
DR EMBL; AL591846; CAI13534.1; -; 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 PIR; A60697; A60697.
DR PIR; T47178; T47178.
DR RefSeq; NP_001188407.1; NM_001201478.1.
DR RefSeq; NP_008824.2; NM_006893.2.
DR UniGene; Hs.497581; -.
DR ProteinModelPortal; P41214; -.
DR SMR; P41214; 1-177.
DR IntAct; P41214; 1.
DR MINT; MINT-3015310; -.
DR PhosphoSite; P41214; -.
DR DMDM; 158957575; -.
DR PaxDb; P41214; -.
DR PRIDE; P41214; -.
DR DNASU; 1939; -.
DR Ensembl; ENST00000271764; ENSP00000271764; ENSG00000143486.
DR Ensembl; ENST00000367114; ENSP00000356081; ENSG00000143486.
DR Ensembl; ENST00000580424; ENSP00000464465; ENSG00000265823.
DR Ensembl; ENST00000585127; ENSP00000463712; ENSG00000265823.
DR GeneID; 1939; -.
DR KEGG; hsa:1939; -.
DR UCSC; uc001heh.2; human.
DR CTD; 1939; -.
DR GeneCards; GC01M206745; -.
DR HGNC; HGNC:6583; EIF2D.
DR HPA; HPA028220; -.
DR MIM; 613709; gene.
DR neXtProt; NX_P41214; -.
DR PharmGKB; PA30355; -.
DR eggNOG; COG2016; -.
DR HOVERGEN; HBG006268; -.
DR InParanoid; P41214; -.
DR KO; K15027; -.
DR OMA; TVMKLPW; -.
DR PhylomeDB; P41214; -.
DR ChiTaRS; EIF2D; human.
DR GeneWiki; LGTN; -.
DR GenomeRNAi; 1939; -.
DR NextBio; 7857; -.
DR PRO; PR:P41214; -.
DR ArrayExpress; P41214; -.
DR Bgee; P41214; -.
DR Genevestigator; P41214; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.30.780.10; -; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_domain.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR001950; TIF_SUI1.
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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1 584 Eukaryotic translation initiation factor
FT 2D.
FT /FTId=PRO_0000130611.
FT DOMAIN 93 173 PUA.
FT DOMAIN 491 564 SUI1.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 237 237 Phosphoserine.
FT VAR_SEQ 177 300 Missing (in isoform 2).
FT /FTId=VSP_006300.
FT VARIANT 210 210 T -> I (in dbSNP:rs35252702).
FT /FTId=VAR_052507.
FT CONFLICT 11 11 N -> D (in Ref. 3; BAA91942).
FT CONFLICT 66 66 S -> N (in Ref. 2; AAF34185/AAF74205).
FT CONFLICT 210 210 T -> N (in Ref. 2; AAF34185).
FT CONFLICT 304 308 GRQLD -> DDNWT (in Ref. 8; AAD41909).
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
//
MIM
613709
*RECORD*
*FIELD* NO
613709
*FIELD* TI
*613709 EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; EIF2D
;;HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN 56; HCA56;;
read moreLIGATIN, FORMERLY; LGTN, FORMERLY
*FIELD* TX
DESCRIPTION
EIF2D is a translation initiation factor that delivers tRNA to the P
site of the 40S ribosome in a GTP-independent manner. Previously, EIF2D
was erroneously called ligatin (LGTN; 151625) in the literature (see
NOMENCLATURE) (Dmitriev et al., 2010).
CLONING
Using mass spectrometry, Dmitriev et al. (2010) identified EIF2D as a
factor purified from HeLa cells that promoted GTP-independent binding of
the initiator tRNA, or met-tRNA-i(met) (see 180621), to the P site of
the 40S ribosome. By RT-PCR of HEK293T cell total RNA, Dmitriev et al.
(2010) isolated the EIF2D cDNA. The deduced 584-amino acid EIF2D protein
has a calculated molecular mass of 65 kD. It contains an N-terminal PUA
domain, which is found in proteins involved in RNA metabolism, and a
C-terminal SUI1 domain, which is found in EIF1 and plays a role in
initiator codon recognition. EIF2D purified from HeLa cells had an
apparent molecular mass of 70 to 72 kD. Transfected EIF2D colocalized
with endogenous EIF3 (see 602039) in the cytoplasm of HeLa cells. EIF2D
orthologs are present in all eukaryotic genomes.
GENE FUNCTION
Dmitriev et al. (2010) showed that recombinant human EIF2D promoted
binding of met-tRNA-i(met) to the P site of the 40S ribosome in a
GTP-independent manner. EIF2D could not deliver met-tRNA-i(met) to the
40S ribosome in the absence of the AUG codon. The aminoacyl moiety of
met-tRNA-i(met) was dispensable for EIF2D-promoted formation of its
complex with the 40S ribosome. In addition, EIF2D was not strictly
specific for the initiator tRNA and AUG codon and could deliver some
elongator tRNAs (e.g., tRNA(phe)) to the P site of the 40S ribosome when
it was programmed with the corresponding codon. EIF2D stabilized the
complex of 40S ribosomes with leaderless mRNA, and it strongly promoted
formation of complexes of 40S ribosomes with RNAs containing
single-stranded A-rich 5-prime UTRs.
MAPPING
Gross (2011) mapped the EIF2D gene to chromosome 1q32.1 based on an
alignment of the EIF2D sequence (GenBank GENBANK AF220417) with the
genomic sequence (GRCh37).
Using FISH, Malnar-Dragojevic et al. (1997) mapped the mouse Eif2d gene,
which they called ligatin (see NOMENCLATURE), to chromosome 1F. This
region is syntenic with human chromosome 1q31-q32.
NOMENCLATURE
Dmitriev et al. (2010) noted that a partial human EIF2D sequence
containing a frameshift had previously been characterized as a cDNA for
ligatin (LGTN; 151625) by Jakoi et al. (1989). Dmitriev et al. (2010)
presented several lines of evidence showing that EIF2D is unrelated to
ligatin, a peripheral membrane protein that binds and localizes
phosphoglycoproteins at the cell surface. Dmitriev et al. (2010) pointed
out that the misidentification of EIF2D as ligatin resulted in several
reports, including those of Jakoi et al. (1995), Severt et al. (1999),
Dang et al. (2006), and Lee et al. (2007), in which expression and/or
regulation of EIF2D were erroneously attributed to ligatin.
*FIELD* RF
1. Dang, C.; Gottschling, M.; Manning, K.; O'Currain, E.; Schneider,
S.; Sterry, W.; Stockfleth, E.; Nindl, I.: Identification of dysregulated
genes in cutaneous squamous cell carcinoma. Oncol. Rep. 16: 513-519,
2006.
2. Dmitriev, S. E.; Terenin, I. M.; Andreev, D. E.; Ivanov, P. A.;
Dunaevsky, J. E.; Merrick, W. C.; Shatsky, I. N.: GTP-independent
tRNA delivery to the ribosomal P-site by a novel eukaryotic translation
factor. J. Biol. Chem. 285: 26779-26787, 2010.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 1/24/2011.
4. Jakoi, E. R.; Brown, A. L.; Ho, Y.-S.; Snyderman, R.: Molecular
cloning of the cDNA for ligatin. J. Cell Sci. 93: 227-232, 1989.
5. Jakoi, E. R.; Panchision, D. M.; Gerwin, C. M.; DeLorenzo, R. J.
: Post-transcriptional regulation of gene expression in hippocampal
neurons by glutamate receptor activation. Brain Res. 693: 124-132,
1995.
6. Lee, M.; Kistler, C.; Hartmann, T. B.; Li, F.; Dummer, R.; Dippel,
E.; Booken, N.; Klemke, C. D.; Schadendorf, D.; Eichmuller, S. B.
: Immunoscreening of a cutaneous T-cell lymphoma library for plasma
membrane proteins. Cancer Immun. Immunother. 56: 783-795, 2007.
7. Malnar-Dragojevic, D.; Trachtulec, Z.; Vincek, V.: Assignment
of the mouse ligatin gene (Lgtn) to chromosome 1F by fluorescence
in situ hybridization. Genomics 40: 192-193, 1997.
8. Severt, W. L.; Biber, T. U.; Wu, X.; Hecht, N. B.; DeLorenzo, R.
J.; Jakoi, E. R.: The suppression of testis-brain RNA binding protein
and kinesin heavy chain disrupts mRNA sorting in dendrites. J. Cell
Sci. 112: 3691-3702, 1999.
*FIELD* CD
Matthew B. Gross: 1/21/2011
*FIELD* ED
mgross: 01/25/2011
mgross: 1/24/2011
*RECORD*
*FIELD* NO
613709
*FIELD* TI
*613709 EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; EIF2D
;;HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN 56; HCA56;;
read moreLIGATIN, FORMERLY; LGTN, FORMERLY
*FIELD* TX
DESCRIPTION
EIF2D is a translation initiation factor that delivers tRNA to the P
site of the 40S ribosome in a GTP-independent manner. Previously, EIF2D
was erroneously called ligatin (LGTN; 151625) in the literature (see
NOMENCLATURE) (Dmitriev et al., 2010).
CLONING
Using mass spectrometry, Dmitriev et al. (2010) identified EIF2D as a
factor purified from HeLa cells that promoted GTP-independent binding of
the initiator tRNA, or met-tRNA-i(met) (see 180621), to the P site of
the 40S ribosome. By RT-PCR of HEK293T cell total RNA, Dmitriev et al.
(2010) isolated the EIF2D cDNA. The deduced 584-amino acid EIF2D protein
has a calculated molecular mass of 65 kD. It contains an N-terminal PUA
domain, which is found in proteins involved in RNA metabolism, and a
C-terminal SUI1 domain, which is found in EIF1 and plays a role in
initiator codon recognition. EIF2D purified from HeLa cells had an
apparent molecular mass of 70 to 72 kD. Transfected EIF2D colocalized
with endogenous EIF3 (see 602039) in the cytoplasm of HeLa cells. EIF2D
orthologs are present in all eukaryotic genomes.
GENE FUNCTION
Dmitriev et al. (2010) showed that recombinant human EIF2D promoted
binding of met-tRNA-i(met) to the P site of the 40S ribosome in a
GTP-independent manner. EIF2D could not deliver met-tRNA-i(met) to the
40S ribosome in the absence of the AUG codon. The aminoacyl moiety of
met-tRNA-i(met) was dispensable for EIF2D-promoted formation of its
complex with the 40S ribosome. In addition, EIF2D was not strictly
specific for the initiator tRNA and AUG codon and could deliver some
elongator tRNAs (e.g., tRNA(phe)) to the P site of the 40S ribosome when
it was programmed with the corresponding codon. EIF2D stabilized the
complex of 40S ribosomes with leaderless mRNA, and it strongly promoted
formation of complexes of 40S ribosomes with RNAs containing
single-stranded A-rich 5-prime UTRs.
MAPPING
Gross (2011) mapped the EIF2D gene to chromosome 1q32.1 based on an
alignment of the EIF2D sequence (GenBank GENBANK AF220417) with the
genomic sequence (GRCh37).
Using FISH, Malnar-Dragojevic et al. (1997) mapped the mouse Eif2d gene,
which they called ligatin (see NOMENCLATURE), to chromosome 1F. This
region is syntenic with human chromosome 1q31-q32.
NOMENCLATURE
Dmitriev et al. (2010) noted that a partial human EIF2D sequence
containing a frameshift had previously been characterized as a cDNA for
ligatin (LGTN; 151625) by Jakoi et al. (1989). Dmitriev et al. (2010)
presented several lines of evidence showing that EIF2D is unrelated to
ligatin, a peripheral membrane protein that binds and localizes
phosphoglycoproteins at the cell surface. Dmitriev et al. (2010) pointed
out that the misidentification of EIF2D as ligatin resulted in several
reports, including those of Jakoi et al. (1995), Severt et al. (1999),
Dang et al. (2006), and Lee et al. (2007), in which expression and/or
regulation of EIF2D were erroneously attributed to ligatin.
*FIELD* RF
1. Dang, C.; Gottschling, M.; Manning, K.; O'Currain, E.; Schneider,
S.; Sterry, W.; Stockfleth, E.; Nindl, I.: Identification of dysregulated
genes in cutaneous squamous cell carcinoma. Oncol. Rep. 16: 513-519,
2006.
2. Dmitriev, S. E.; Terenin, I. M.; Andreev, D. E.; Ivanov, P. A.;
Dunaevsky, J. E.; Merrick, W. C.; Shatsky, I. N.: GTP-independent
tRNA delivery to the ribosomal P-site by a novel eukaryotic translation
factor. J. Biol. Chem. 285: 26779-26787, 2010.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 1/24/2011.
4. Jakoi, E. R.; Brown, A. L.; Ho, Y.-S.; Snyderman, R.: Molecular
cloning of the cDNA for ligatin. J. Cell Sci. 93: 227-232, 1989.
5. Jakoi, E. R.; Panchision, D. M.; Gerwin, C. M.; DeLorenzo, R. J.
: Post-transcriptional regulation of gene expression in hippocampal
neurons by glutamate receptor activation. Brain Res. 693: 124-132,
1995.
6. Lee, M.; Kistler, C.; Hartmann, T. B.; Li, F.; Dummer, R.; Dippel,
E.; Booken, N.; Klemke, C. D.; Schadendorf, D.; Eichmuller, S. B.
: Immunoscreening of a cutaneous T-cell lymphoma library for plasma
membrane proteins. Cancer Immun. Immunother. 56: 783-795, 2007.
7. Malnar-Dragojevic, D.; Trachtulec, Z.; Vincek, V.: Assignment
of the mouse ligatin gene (Lgtn) to chromosome 1F by fluorescence
in situ hybridization. Genomics 40: 192-193, 1997.
8. Severt, W. L.; Biber, T. U.; Wu, X.; Hecht, N. B.; DeLorenzo, R.
J.; Jakoi, E. R.: The suppression of testis-brain RNA binding protein
and kinesin heavy chain disrupts mRNA sorting in dendrites. J. Cell
Sci. 112: 3691-3702, 1999.
*FIELD* CD
Matthew B. Gross: 1/21/2011
*FIELD* ED
mgross: 01/25/2011
mgross: 1/24/2011