(data stored in ACNUC6288 zone)

SWISSPROT: EI2BD_MOUSE

ID   EI2BD_MOUSE             Reviewed;         524 AA.
AC   Q61749; Q3TYW7; Q61748; Q8VC35;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   08-MAY-2019, entry version 132.
DE   RecName: Full=Translation initiation factor eIF-2B subunit delta;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit delta;
GN   Name=Eif2b4; Synonyms=Eif2b, Eif2bd, Jgr1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=CBA/J; TISSUE=Spleen;
RX   PubMed=7982969;
RA   Henderson R.A., Krissansen G.W., Yong R.Y., Leung E., Watson J.D.,
RA   Dholakia J.N.;
RT   "The delta-subunit of murine guanine nucleotide exchange factor eIF-
RT   2B. Characterization of cDNAs predicts isoforms differing at the
RT   amino-terminal end.";
RL   J. Biol. Chem. 269:30517-30523(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Salivary gland;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor
CC       2-bound GDP for GTP.
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma,
CC       delta and epsilon.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61749-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61749-2; Sequence=VSP_001434;
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family. {ECO:0000305}.
DR   EMBL; M98036; AAA68047.1; -; mRNA.
DR   EMBL; M98035; AAA68046.1; -; mRNA.
DR   EMBL; AK158282; BAE34444.1; -; mRNA.
DR   EMBL; CH466524; EDL37345.1; -; Genomic_DNA.
DR   EMBL; BC021884; AAH21884.1; -; mRNA.
DR   CCDS; CCDS19176.1; -. [Q61749-1]
DR   CCDS; CCDS51457.1; -. [Q61749-2]
DR   PIR; A55146; A55146.
DR   RefSeq; NP_001120827.1; NM_001127355.1. [Q61749-2]
DR   RefSeq; NP_001120828.1; NM_001127356.1. [Q61749-2]
DR   RefSeq; NP_034252.2; NM_010122.2. [Q61749-1]
DR   SMR; Q61749; -.
DR   STRING; 10090.ENSMUSP00000110250; -.
DR   iPTMnet; Q61749; -.
DR   PhosphoSitePlus; Q61749; -.
DR   EPD; Q61749; -.
DR   jPOST; Q61749; -.
DR   PaxDb; Q61749; -.
DR   PRIDE; Q61749; -.
DR   Ensembl; ENSMUST00000077693; ENSMUSP00000076875; ENSMUSG00000029145. [Q61749-1]
DR   Ensembl; ENSMUST00000114603; ENSMUSP00000110250; ENSMUSG00000029145. [Q61749-2]
DR   Ensembl; ENSMUST00000166769; ENSMUSP00000130880; ENSMUSG00000029145. [Q61749-2]
DR   GeneID; 13667; -.
DR   KEGG; mmu:13667; -.
DR   UCSC; uc008wxk.2; mouse. [Q61749-2]
DR   UCSC; uc008wxl.2; mouse. [Q61749-1]
DR   CTD; 8890; -.
DR   MGI; MGI:95300; Eif2b4.
DR   eggNOG; KOG1467; Eukaryota.
DR   eggNOG; COG1184; LUCA.
DR   GeneTree; ENSGT00550000075009; -.
DR   HOGENOM; HOG000176924; -.
DR   InParanoid; Q61749; -.
DR   KO; K03680; -.
DR   OMA; LNYDITP; -.
DR   OrthoDB; 797227at2759; -.
DR   TreeFam; TF101508; -.
DR   Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR   ChiTaRS; Eif2b4; mouse.
DR   PRO; PR:Q61749; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029145; Expressed in 291 organ(s), highest expression level in primary oocyte.
DR   ExpressionAtlas; Q61749; baseline and differential.
DR   Genevisible; Q61749; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:MGI.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; ISO:MGI.
DR   GO; GO:0009408; P:response to heat; ISO:MGI.
DR   GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q61749.
DR   SWISS-2DPAGE; Q61749.
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q9UI10}.
FT   CHAIN         2    524       Translation initiation factor eIF-2B
FT                                subunit delta.
FT                                /FTId=PRO_0000156068.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q9UI10}.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UI10}.
FT   MOD_RES      86     86       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UI10}.
FT   VAR_SEQ       1     10       MAAVAVAVRE -> MPTQQPAAPTSLPKSSRSLSGSLCALF
FT                                SDA (in isoform 2).
FT                                {ECO:0000303|PubMed:7982969}.
FT                                /FTId=VSP_001434.
FT   CONFLICT    302    302       R -> K (in Ref. 1; AAA68046/AAA68047).
FT                                {ECO:0000305}.
SQ   SEQUENCE   524 AA;  57624 MW;  86CDB70C63285A02 CRC64;
     MAAVAVAVRE ESRSEMKTEL SPRPGAAGRE LTQEEKLQLR KEKKQQKKKR KEEKGADQEI
     GSAVSAAQRQ DPIRELPGPG SQLGGTAGEK LPAGRSKAEL RAERRAKQEA ERALKQARKG
     EQGGVPPQAC PSTAGETTSG VKRVPEHTPA DDPTLLRRLL RKPDRQQVPT RKDYGSKVSL
     FSHLPQYSRQ SSLTQYMSIP SSVIHPAMVR LGLQYSQGLI SGSNARCIAL LHALQQVIQD
     YTTPPSEELS RDLVNKLKPY ISFLTQCRPM SASMCNAIKF LTKEVTGMSS SKREEEAKSE
     LREALDRYVQ EKIVLAAQAI SRFASTKISD GDVILVYGCS SLVSRILQEA RVEGRRFRVV
     VVDSRPRLEG RHMLHSLVRA GVPTSYLLIP AASYVLPEVS KVLLGAHALL ANGSVMSRVG
     TAQLALVARA HNVPVLVCCE TYKFCERVQT DAFVSNELDD PDDLQCKRGD QVALANWQSH
     PSLRLLNLVY DVTPPELVDL VITELGMIPC SSVPVVLRVK SSDQ
//

If you have problems or comments...

PBIL Back to PBIL home page