SELB_HUMAN
ID SELB_HUMAN Reviewed; 596 AA.
AC P57772; Q96HZ6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=Elongation factor sec;
DE AltName: Full=Eukaryotic elongation factor, selenocysteine-tRNA-specific;
GN Name=EEFSEC; Synonyms=SELB;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-596 (ISOFORM 1/2).
RX PubMed=10970870; DOI=10.1093/emboj/19.17.4796;
RA Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., Krol A.;
RT "Characterization of mSelB, a novel mammalian elongation factor for
RT selenoprotein translation.";
RL EMBO J. 19:4796-4805(2000).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP 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 [6]
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).
CC -!- FUNCTION: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P57772-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57772-2; Sequence=VSP_057185;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. SelB subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AL449214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007933; AAH07933.1; -; mRNA.
DR EMBL; AF268872; AAG13375.1; -; mRNA.
DR CCDS; CCDS33849.1; -. [P57772-1]
DR RefSeq; NP_068756.2; NM_021937.4. [P57772-1]
DR PDB; 5IZK; X-ray; 3.25 A; A/B=1-596.
DR PDB; 5IZL; X-ray; 2.72 A; A/B=1-596.
DR PDB; 5IZM; X-ray; 3.40 A; A/B=2-596.
DR PDBsum; 5IZK; -.
DR PDBsum; 5IZL; -.
DR PDBsum; 5IZM; -.
DR AlphaFoldDB; P57772; -.
DR SMR; P57772; -.
DR BioGRID; 121953; 50.
DR IntAct; P57772; 10.
DR MINT; P57772; -.
DR STRING; 9606.ENSP00000254730; -.
DR GlyGen; P57772; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P57772; -.
DR MetOSite; P57772; -.
DR PhosphoSitePlus; P57772; -.
DR SwissPalm; P57772; -.
DR BioMuta; EEFSEC; -.
DR DMDM; 259016384; -.
DR EPD; P57772; -.
DR jPOST; P57772; -.
DR MassIVE; P57772; -.
DR MaxQB; P57772; -.
DR PaxDb; P57772; -.
DR PeptideAtlas; P57772; -.
DR PRIDE; P57772; -.
DR ProteomicsDB; 57034; -. [P57772-1]
DR Antibodypedia; 46656; 113 antibodies from 20 providers.
DR DNASU; 60678; -.
DR Ensembl; ENST00000254730.11; ENSP00000254730.5; ENSG00000132394.11. [P57772-1]
DR Ensembl; ENST00000644579.2; ENSP00000494933.1; ENSG00000284869.2. [P57772-1]
DR GeneID; 60678; -.
DR KEGG; hsa:60678; -.
DR MANE-Select; ENST00000254730.11; ENSP00000254730.5; NM_021937.5; NP_068756.2.
DR UCSC; uc003eki.4; human. [P57772-1]
DR CTD; 60678; -.
DR DisGeNET; 60678; -.
DR GeneCards; EEFSEC; -.
DR HGNC; HGNC:24614; EEFSEC.
DR HPA; ENSG00000132394; Low tissue specificity.
DR MIM; 607695; gene.
DR neXtProt; NX_P57772; -.
DR OpenTargets; ENSG00000132394; -.
DR PharmGKB; PA142671916; -.
DR VEuPathDB; HostDB:ENSG00000132394; -.
DR eggNOG; KOG0461; Eukaryota.
DR GeneTree; ENSGT00940000158170; -.
DR HOGENOM; CLU_019148_0_0_1; -.
DR InParanoid; P57772; -.
DR OMA; LAFWGRI; -.
DR OrthoDB; 616182at2759; -.
DR PhylomeDB; P57772; -.
DR TreeFam; TF300432; -.
DR PathwayCommons; P57772; -.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR SignaLink; P57772; -.
DR BioGRID-ORCS; 60678; 263 hits in 1082 CRISPR screens.
DR ChiTaRS; EEFSEC; human.
DR GenomeRNAi; 60678; -.
DR Pharos; P57772; Tbio.
DR PRO; PR:P57772; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P57772; protein.
DR Bgee; ENSG00000132394; Expressed in apex of heart and 97 other tissues.
DR ExpressionAtlas; P57772; baseline and differential.
DR Genevisible; P57772; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IEA:Ensembl.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; GTP-binding; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..596
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091478"
FT DOMAIN 5..217
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 46..50
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 92..95
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 146..149
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 185..187
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 548..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..553
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 551..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 146..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHW4"
FT MOD_RES 556
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHW4"
FT VAR_SEQ 1..31
FT /note="MAGRRVNVNVGVLGHIDSGKTALARALSTTA -> MASC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057185"
FT VARIANT 435
FT /note="A -> V (in dbSNP:rs34326479)"
FT /id="VAR_055712"
FT CONFLICT 577
FT /note="L -> F (in Ref. 3; AAG13375)"
FT /evidence="ECO:0000305"
FT STRAND 5..19
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5IZK"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:5IZL"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:5IZM"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5IZM"
FT HELIX 156..170
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 239..251
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5IZL"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5IZK"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 309..317
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5IZM"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 410..422
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 444..454
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 468..481
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 483..492
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 500..503
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5IZL"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:5IZM"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 538..542
FT /evidence="ECO:0007829|PDB:5IZL"
FT STRAND 575..584
FT /evidence="ECO:0007829|PDB:5IZL"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:5IZL"
SQ SEQUENCE 596 AA; 65305 MW; C92C43E3F250F686 CRC64;
MAGRRVNVNV GVLGHIDSGK TALARALSTT ASTAAFDKQP QSRERGITLD LGFSCFSVPL
PARLRSSLPE FQAAPEAEPE PGEPLLQVTL VDCPGHASLI RTIIGGAQII DLMMLVIDVT
KGMQTQSAEC LVIGQIACQK LVVVLNKIDL LPEGKRQAAI DKMTKKMQKT LENTKFRGAP
IIPVAAKPGG PEAPETEAPQ GIPELIELLT SQISIPTRDP SGPFLMSVDH CFSIKGQGTV
MTGTILSGSI SLGDSVEIPA LKVVKKVKSM QMFHMPITSA MQGDRLGICV TQFDPKLLER
GLVCAPESLH TVHAALISVE KIPYFRGPLQ TKAKFHITVG HETVMGRLMF FSPAPDNFDQ
EPILDSFNFS QEYLFQEQYL SKDLTPAVTD NDEADKKAGQ ATEGHCPRQQ WALVEFEKPV
TCPRLCLVIG SRLDADIHTN TCRLAFHGIL LHGLEDRNYA DSFLPRLKVY KLKHKHGLVE
RAMDDYSVIG RSLFKKETNI QLFVGLKVHL STGELGIIDS AFGQSGKFKI HIPGGLSPES
KKILTPALKK RARAGRGEAT RQEESAERSE PSQHVVLSLT FKRYVFDTHK RMVQSP
