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Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

Eif3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.1 Publication

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. translation initiation factor activity Source: MGI

GO - Biological processi

  1. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  2. regulation of translational initiation Source: MGI
  3. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit BUniRule annotation
Short name:
eIF3bUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9UniRule annotation
eIF-3-etaUniRule annotation
eIF3 p116
Gene namesi
Name:Eif3b
Synonyms:Eif3s9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:106478. Eif3b.

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  5. eukaryotic translation initiation factor 3 complex, eIF3m Source: MGI
  6. extracellular vesicular exosome Source: MGI
  7. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Embryonic death.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Eukaryotic translation initiation factor 3 subunit BPRO_0000223479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotation
Modified residuei31 – 311Phosphothreonine1 Publication
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei74 – 741Phosphothreonine2 Publications
Modified residuei75 – 751Phosphoserine3 Publications
Modified residuei79 – 791Phosphoserine4 Publications
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei120 – 1201Phosphoserine5 Publications
Modified residuei123 – 1231Phosphoserine4 Publications
Modified residuei141 – 1411PhosphoserineUniRule annotation
Modified residuei143 – 1431PhosphoserineUniRule annotation
Modified residuei153 – 1531PhosphoserineUniRule annotation
Modified residuei198 – 1981N6-acetyllysineBy similarity
Modified residuei228 – 2281PhosphoserineUniRule annotation
Modified residuei277 – 2771N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8JZQ9.
PaxDbiQ8JZQ9.
PRIDEiQ8JZQ9.

PTM databases

PhosphoSiteiQ8JZQ9.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8JZQ9.
GenevestigatoriQ8JZQ9.

Interactioni

Subunit structurei

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may also interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4g1Q6NZJ62EBI-4286513,EBI-8175606

Protein-protein interaction databases

BioGridi205699. 3 interactions.
IntActiQ8JZQ9. 11 interactions.
MINTiMINT-1899500.
STRINGi10090.ENSMUSP00000075175.

Structurei

3D structure databases

ProteinModelPortaliQ8JZQ9.
SMRiQ8JZQ9. Positions 159-263, 290-699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini174 – 25784RRMUniRule annotationAdd
BLAST
Repeati321 – 35939WD 1Add
BLAST
Repeati361 – 40646WD 2Add
BLAST
Repeati410 – 44839WD 3Add
BLAST
Repeati549 – 59042WD 4Add
BLAST
Repeati638 – 68346WD 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 402290Sufficient for interaction with EIF3EUniRule annotationAdd
BLAST
Regioni159 – 263105Sufficient for interaction with EIF3JUniRule annotationAdd
BLAST

Domaini

The RRM domain mediates interaction with EIF3J.UniRule annotation

Sequence similaritiesi

Belongs to the eIF-3 subunit B family.UniRule annotation
Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
Contains 5 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG5354.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiQ8JZQ9.
KOiK03253.
OMAiGRDQYAT.
OrthoDBiEOG7KM5S6.
PhylomeDBiQ8JZQ9.
TreeFamiTF101521.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 1 hit.
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8JZQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE
60 70 80 90 100
DAEAGPEPEV RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE
110 120 130 140 150
AVGEQARGHP SAGAEEEGGS DGSAAEAEPR ALENGEADEP SFSDPEDFVD
160 170 180 190 200
DVSEEELLGD VLKDRPQEAD GIDSVIVVDN VPQVGPDRLE KLKNVIHKIF
210 220 230 240 250
SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD GYKLDKQHTF
260 270 280 290 300
RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE
310 320 330 340 350
SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG
360 370 380 390 400
GDKFKQIQRF SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT
410 420 430 440 450
GHKKRGFHCE SSAHWPIFKW SHDGKFFARM TLDTLSIYET PSMGLLDKKS
460 470 480 490 500
LKISGIKDFS WSPGGNIIAF WVPEDKDIPA RVTLMQLPTR QEIRVRNLFN
510 520 530 540 550
VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE KQVPVDVVEM
560 570 580 590 600
KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA
610 620 630 640 650
NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP
660 670 680 690 700
TGRYVVTSVS WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL
710 720 730 740 750
LSQDQIKQIK KDLKKYSKIF EQKDRLSQSK ASKELVERRR TMMEDFRQYR
760 770 780 790 800
KMAQELYMKQ KNERLELRGG VDTDELDSNV DDWEEETIEF FVTEEVIPLG

SQE
Length:803
Mass (Da):91,370
Last modified:October 1, 2002 - v1
Checksum:iD770AC70BFE9832F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033722 mRNA. Translation: BAC28445.1.
AK167618 mRNA. Translation: BAE39671.1.
AK170938 mRNA. Translation: BAE42128.1.
BC007175 mRNA. Translation: AAH07175.1.
BC031704 mRNA. Translation: AAH31704.1.
CCDSiCCDS19819.1.
PIRiJC7862.
RefSeqiNP_598677.1. NM_133916.2.
UniGeneiMm.21671.

Genome annotation databases

EnsembliENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneIDi27979.
KEGGimmu:27979.
UCSCiuc009ahr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033722 mRNA. Translation: BAC28445.1.
AK167618 mRNA. Translation: BAE39671.1.
AK170938 mRNA. Translation: BAE42128.1.
BC007175 mRNA. Translation: AAH07175.1.
BC031704 mRNA. Translation: AAH31704.1.
CCDSiCCDS19819.1.
PIRiJC7862.
RefSeqiNP_598677.1. NM_133916.2.
UniGeneiMm.21671.

3D structure databases

ProteinModelPortaliQ8JZQ9.
SMRiQ8JZQ9. Positions 159-263, 290-699.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205699. 3 interactions.
IntActiQ8JZQ9. 11 interactions.
MINTiMINT-1899500.
STRINGi10090.ENSMUSP00000075175.

PTM databases

PhosphoSiteiQ8JZQ9.

Proteomic databases

MaxQBiQ8JZQ9.
PaxDbiQ8JZQ9.
PRIDEiQ8JZQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneIDi27979.
KEGGimmu:27979.
UCSCiuc009ahr.1. mouse.

Organism-specific databases

CTDi8662.
MGIiMGI:106478. Eif3b.

Phylogenomic databases

eggNOGiCOG5354.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiQ8JZQ9.
KOiK03253.
OMAiGRDQYAT.
OrthoDBiEOG7KM5S6.
PhylomeDBiQ8JZQ9.
TreeFamiTF101521.

Enzyme and pathway databases

ReactomeiREACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiEif3b. mouse.
NextBioi306472.
PROiQ8JZQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZQ9.
GenevestigatoriQ8JZQ9.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 1 hit.
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    Tissue: Embryonic stem cell.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cecum and Placenta.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
    Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
    EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND RPS6.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Reconstitution reveals the functional core of mammalian eIF3."
    Masutani M., Sonenberg N., Yokoyama S., Imataka H.
    EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75; SER-79; SER-90; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEIF3B_MOUSE
AccessioniPrimary (citable) accession number: Q8JZQ9
Secondary accession number(s): Q922K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2002
Last modified: April 1, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.