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UniProtKB/Swiss-Prot entry O43432


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IF4G3_HUMAN
Primary accession number O43432
Secondary accession numbers Q15597 Q5SWC3 Q8NEN1
Integrated into Swiss-Prot on June 7, 2004
Sequence was last modified on March 1, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 80)
Name and origin of the protein
Protein name Eukaryotic translation initiation factor 4 gamma 3
Synonyms eIF-4-gamma 3
eIF-4G 3
eIF4G 3
eIF-4-gamma II
eIF4GII
Gene name
Name: EIF4G3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH EIF4A; EIF4E AND EIF3.
PubMed=9418880 [NCBI, ExPASy, EBI, Israel, Japan]
Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.;
"A novel functional human eukaryotic translation initiation factor 4G.";
Mol. Cell. Biol. 18:334-342(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 887-1585 (ISOFORM 1).
TISSUE=Ovary;
Klaudiny J.J., von der Kammer H.H., Scheit K.K.;
"Characterization of secretory proteins of human ovarian follicle cells by cDNA cloning.";
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH PABPC1.
DOI=10.1093/emboj/17.24.7480; PubMed=9857202 [NCBI, ExPASy, EBI, Israel, Japan]
Imataka H., Gradi A., Sonenberg N.;
"A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation.";
EMBO J. 17:7480-7489(1998).
[7]
PHOSPHORYLATION AT SER-1156 BY CAMK1.
DOI=10.1074/jbc.M308781200; PubMed=14507913 [NCBI, ExPASy, EBI, Israel, Japan]
Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.;
"Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I.";
J. Biol. Chem. 278:48570-48579(2003).
[8]
CLEAVAGE BY RHINOVIRUS PROTEASE.
DOI=10.1128/JVI.77.8.5026-5029.2003; PubMed=12663812 [NCBI, ExPASy, EBI, Israel, Japan]
Gradi A., Svitkin Y.V., Sommergruber W., Imataka H., Morino S., Skern T., Sonenberg N.;
"Human rhin4ovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different.";
J. Virol. 77:5026-5029(2003).
[9]
CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS PROTEASE.
DOI=10.1128/JVI.78.7.3271-3278.2004; PubMed=15016848 [NCBI, ExPASy, EBI, Israel, Japan]
Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.;
"Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro.";
J. Virol. 78:3271-3278(2004).
[10]
REVIEW.
DOI=10.1146/annurev.biochem.68.1.913; PubMed=10872469 [NCBI, ExPASy, EBI, Israel, Japan]
Gingras A.-C., Raught B., Sonenberg N.;
"eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation.";
Annu. Rev. Biochem. 68:913-963(1999).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-495, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[18]
STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
DOI=10.1023/A:1025442322316; PubMed=12975586 [NCBI, ExPASy, EBI, Israel, Japan]
Miura T., Shiratori Y., Shimma N.;
"Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII.";
J. Biomol. NMR 27:279-280(2003).
[19]
X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 745-986, AND MUTAGENESIS OF ARG-756; ARG-759; LYS-764; ARG-814; LYS-820 AND 834-ARG-LYS-835.
DOI=10.1016/S1097-2765(01)00167-8; PubMed=11172724 [NCBI, ExPASy, EBI, Israel, Japan]
Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T., Burley S.K.;
"A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery.";
Mol. Cell 7:193-203(2001).
Comments
  • FUNCTION: Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1.
  • SUBUNIT: Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA (By similarity).
  • INTERACTION:
    P60842:EIF4A1; NbExp=1; IntAct=EBI-464766, EBI-73449;
    Q14240:EIF4A2; NbExp=1; IntAct=EBI-464766, EBI-73473;
    Q09161:NCBP1; NbExp=1; IntAct=EBI-464766, EBI-464743;
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO43432-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO43432-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_010487, VSP_010488, VSP_010489.
  • PTM: Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.
  • SIMILARITY: Belongs to the eIF4G family.
  • SIMILARITY: Contains 5 HEAT repeats.
  • SIMILARITY: Contains 1 MI domain.
  • SIMILARITY: Contains 1 MIF4G domain.
  • SIMILARITY: Contains 1 W2 domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF012072; AAC02903.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL358392; CAI12155.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL606477; CAI12155.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627311; CAI12155.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL606477; CAI12534.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL358392; CAI12534.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627311; CAI12534.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627311; CAI14553.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL358392; CAI14553.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL606477; CAI14553.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471134; EAW94956.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030578; AAH30578.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z34918; CAA84397.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00411710; -.
IPI00646377; -.
PIR S49172; S49172.
RefSeq NP_003751.2; -.
UniGene Hs.467084
3D structure databases
PDB
1HU3; X-ray; 2.37 A; A=745-1003.[ExPASy / RCSB / EBI]
PDBsum 1HU3; -.
ModBase O43432.
Protein-protein interaction databases
IntAct O43432; 4.
PTM databases
PhosphoSite O43432; -.
Organism-specific databases
GeneCards GC01M021005; -.
H-InvDB HIX0023524; -.
HGNC HGNC:3298; EIF4G3.
GenAtlas EIF4G3.
MIM 603929; gene. [NCBI / EBI]
PharmGKB PA27724; -.
Gene expression databases
ArrayExpress O43432; -.
Bgee O43432; -.
CleanEx HS_EIF4G3; -.
GermOnline ENSG00000075151; Homo sapiens.
Ontologies
GO
GO:0016281; Cellular component: eukaryotic translation initiation factor 4F complex (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000339; Molecular function: RNA cap binding (traceable author statement from ProtInc).
GO:0003743; Molecular function: translation initiation factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006446; Biological process: regulation of translational initiation (traceable author statement from ProtInc).
GO:0016070; Biological process: RNA metabolic process (inferred from electronic annotation from InterPro).
GO:0006412; Biological process: translation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003307; eIF5C.
IPR003891; Initiation_fac_eIF4g_MI.
IPR016021; MIF4-like_typ_1/2/3.
IPR003890; MIF4G-like_typ-3.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.230; eIF5C; 1.
G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
Pfam PF02847; MA3; 1.
PF02854; MIF4G; 1.
PF02020; W2; 1.
Pfam graphical view of domain structure.
SMART SM00515; eIF5C; 1.
SM00544; MA3; 1.
SM00543; MIF4G; 1.
SMART graphical view of domain structure.
PROSITE PS50077; HEAT_REPEAT; FALSE_NEG.
PS51366; MI; 1.
PS51363; W2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O43432; -.
Genome annotation databases
Ensembl ENSG00000075151; Homo sapiens. [Contig view]
GeneID 8672; -.
KEGG hsa:8672; -.
Phylogenomic databases
HOVERGEN O43432; -.
OMA O43432; ISMRELI.
Other
NextBio 32529; -.
PMAP-CutDB O43432; -.
SOURCE EIF4G3; Homo sapiens.
ProtoNet O43432.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Coiled coil; Host-virus interaction; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; Repeat; RNA-binding; Translation regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1585  1585     Eukaryotic translation initiation factor 4 gamma 3. PRO_0000213329
REPEAT   745    783  39     HEAT 1. 
DOMAIN   755    983  229     MIF4G. 
REPEAT   784    831  48     HEAT 2. 
REPEAT   832    905  74     HEAT 3. 
REPEAT   906    944  39     HEAT 4. 
REPEAT   945    984  40     HEAT 5. 
DOMAIN   1221   1343  123     MI. 
DOMAIN   1416   1585  170     W2. 
REGION   134    162  29     PABPC1-binding. 
REGION   619    630  12     EIF4E-binding (By similarity). 
REGION   699   1019  321     eIF3/EIF4A-binding (By similarity). 
REGION   1433   1585  153     EIF4A-binding (By similarity). 
REGION   1571   1585  15     Necessary but not sufficient for MKNK1-binding (By similarity). 
COILED   447    475  29     Potential. 
COILED   994   1023  30     Potential. 
SITE   699    700  2     Cleavage; by enterovirus/rhinovirus protease 2A. 
SITE   700    701  2     Cleavage; by foot-and-mouth disease virus leader protease. 
MOD_RES   230    230        Phosphoserine. 
MOD_RES   232    232        Phosphoserine. 
MOD_RES   240    240        Phosphoserine (By similarity). 
MOD_RES   267    267        Phosphoserine (By similarity). 
MOD_RES   495    495        Phosphoserine. 
MOD_RES   1156   1156        Phosphoserine; by CaMK1. 
VAR_SEQ   11     11        F -> FAAGPRPPHHQF (in isoform 2). VSP_010487
VAR_SEQ   499    504        AQIAIT -> ETSNEC (in isoform 2). VSP_010488
VAR_SEQ   505   1585        Missing (in isoform 2). VSP_010489
VARIANT   378    378  1     Q -> R (in dbSNP:rs35731992 [NCBI]). VAR_048924 
VARIANT   496    496  1     P -> A (in dbSNP:rs35176330 [NCBI]). VAR_034009 
VARIANT   1185   1185  1     D -> E (in dbSNP:rs2230572 [NCBI]). VAR_048925 
MUTAGEN   756    756        R->D: Reduces binding to EIF4A; when associated with D-759 and D-764. 
MUTAGEN   759    759        R->D: Reduces binding to EIF4A; when associated with D-756 and D-764. 
MUTAGEN   764    764        K->D: Reduces binding to EIF4A; when associated with D-756 and D-759. 
MUTAGEN   814    814        R->D: Reduces binding to EIF4A; when associated with D-820. 
MUTAGEN   820    820        K->D: Reduces binding to EIF4A; when associated with D-814. 
MUTAGEN   834    835        RK->DD: Reduces binding to IRES. 
CONFLICT   159    159        M -> I (in Ref. 4; AAH30578). 
CONFLICT   333    333        D -> G (in Ref. 4; AAH30578). 
HELIX   746    762  17      
HELIX   770    777  8      
HELIX   785    801  17      
HELIX   803    805  3      
HELIX   806    816  11      
HELIX   833    848  16      
HELIX   885    900  16      
TURN   901    903  3      
HELIX   907    919  13      
HELIX   923    940  18      
TURN   943    945  3      
HELIX   946    961  16      
HELIX   967    981  15      
TURN   982    984  3      
Sequence information
Length: 1585 AA [This is the length of the unprocessed precursor] Molecular weight: 176652 Da [This is the MW of the unprocessed precursor] CRC64: EA483139373DCA5C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM VNHLPMPYPV 

        70         80         90        100        110        120 
PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFPNAYGT PFYPSQPVYQ 

       130        140        150        160        170        180 
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPTSTPTP 

       190        200        210        220        230        240 
PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS 

       250        260        270        280        290        300 
GEKKEQEGQT SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR 

       310        320        330        340        350        360 
CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV SSTNLINEIN 

       370        380        390        400        410        420 
GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE CIPAPITPST VPSFPPTPPT 

       430        440        450        460        470        480 
PPASPPHTPV IVPAAATTVS SPSAAITVQR VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ 

       490        500        510        520        530        540 
TEEILDSQNL NSRRSPVPAQ IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV 

       550        560        570        580        590        600 
LESEQDKMSQ GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS 

       610        620        630        640        650        660 
GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD VVLDKINQPK 

       670        680        690        700        710        720 
LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG SRRSQPGQRR EPRKIITVSV 

       730        740        750        760        770        780 
KEDVHLKKAE NAWKPSQKRD SQADDPENIK TQELFRKVRS ILNKLTPQMF NQLMKQVSGL 

       790        800        810        820        830        840 
TVDTEERLKG VIDLVFEKAI DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR 

       850        860        870        880        890        900 
CQKEFEKDKA DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF 

       910        920        930        940        950        960 
KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKIV 

       970        980        990       1000       1010       1020 
KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH KEAKIEEQEE QRKVQQLMTK 

      1030       1040       1050       1060       1070       1080 
EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS KFLKITKPTI DEKIQLVPKA QLGSWGKGSS 

      1090       1100       1110       1120       1130       1140 
GGAKASETDA LRSSASSLNR FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP 

      1150       1160       1170       1180       1190       1200 
LPSATARPNT FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE 

      1210       1220       1230       1240       1250       1260 
SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN AQGLLHVFVR 

      1270       1280       1290       1300       1310       1320 
VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS ETLELADDMA IDIPHIWLYL 

      1330       1340       1350       1360       1370       1380 
AELVTPMLKE GGISMRELTI EFSKPLLPVG RAGVLLSEIL HLLCKQMSHK KVGALWREAD 

      1390       1400       1410       1420       1430       1440 
LSWKDFLPEG EDVHNFLLEQ KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN 

      1450       1460       1470       1480       1490       1500 
DEQIFDWVEA NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL 

      1510       1520       1530       1540       1550       1560 
DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE SSKDPAEQNG 

      1570       1580 
KGVALKSVTA FFTWLREAEE ESEDN 

O43432 in FASTA format

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