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P23588

- IF4B_HUMAN

UniProt

P23588 - IF4B_HUMAN

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Protein
Eukaryotic translation initiation factor 4B
Gene
EIF4B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. translation initiation factor activity Source: ProtInc

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. insulin receptor signaling pathway Source: Reactome
  5. mRNA metabolic process Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  7. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  8. regulation of translational initiation Source: ProtInc
  9. translation Source: Reactome
  10. translational initiation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_6772. S6K1 signalling.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4B
Short name:
eIF-4B
Gene namesi
Name:EIF4B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:3285. EIF4B.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27713.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 611611Eukaryotic translation initiation factor 4B
PRO_0000081616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931Phosphoserine2 Publications
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine2 Publications
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei365 – 3651N6-acetyllysine By similarity
Modified residuei406 – 4061Phosphoserine3 Publications
Modified residuei412 – 4121Phosphothreonine1 Publication
Modified residuei418 – 4181Phosphoserine1 Publication
Modified residuei422 – 4221Phosphoserine; by RPS6KA1 and RPS6KB13 Publications
Modified residuei425 – 4251Phosphoserine1 Publication
Modified residuei445 – 4451Phosphoserine3 Publications
Modified residuei459 – 4591Phosphoserine1 Publication
Modified residuei498 – 4981Phosphoserine2 Publications
Modified residuei504 – 5041Phosphoserine2 Publications
Modified residuei586 – 5861N6-acetyllysine1 Publication
Modified residuei597 – 5971Phosphoserine4 Publications

Post-translational modificationi

Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23588.
PaxDbiP23588.
PRIDEiP23588.

PTM databases

PhosphoSiteiP23588.

Miscellaneous databases

PMAP-CutDBP23588.

Expressioni

Gene expression databases

ArrayExpressiP23588.
BgeeiP23588.
CleanExiHS_EIF4B.
GenevestigatoriP23588.

Organism-specific databases

HPAiCAB019440.
HPA046164.

Interactioni

Subunit structurei

Self-associates and interacts with EIF3 p170 subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
PLK1P533503EBI-970310,EBI-476768

Protein-protein interaction databases

BioGridi108291. 57 interactions.
IntActiP23588. 21 interactions.
MINTiMINT-210187.
STRINGi9606.ENSP00000262056.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 943
Beta strandi96 – 1027
Helixi109 – 1157
Turni116 – 1183
Beta strandi121 – 1255
Turni130 – 1334
Beta strandi140 – 1467
Helixi147 – 1548
Helixi155 – 1573
Beta strandi167 – 1704

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI8NMR-A88-178[»]
2J76NMR-E77-176[»]
ProteinModelPortaliP23588.
SMRiP23588. Positions 96-176.

Miscellaneous databases

EvolutionaryTraceiP23588.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 17378RRM
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi164 – 331168Arg-rich
Add
BLAST
Compositional biasi169 – 325157Asp-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238591.
HOGENOMiHOG000006553.
HOVERGENiHBG006129.
InParanoidiP23588.
KOiK03258.
OrthoDBiEOG7MKW86.
PhylomeDBiP23588.
TreeFamiTF101525.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23588-1 [UniParc]FASTAAdd to Basket

« Hide

MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVSKPVSW ADETDDLEGD    50
VSTTWHSNDD DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL 100
GNLPYDVTEE SIKEFFRGLN ISAVRLPREP SNPERLKGFG YAEFEDLDSL 150
LSALSLNEES LGNRRIRVDV ADQAQDKDRD DRSFGRDRNR DSDKTDTDWR 200
ARPATDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG YRDGPRRDMD 250
RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED 300
RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPKLNLKPRS TPKEDDSSAS 350
TSQSTRAASI FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLERRP 400
RERHPSWRSE ETQERERSRT GSESSQTGTS TTSSRNARRR ESEKSLENET 450
LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK ENAWVKRSSN PPARSQSSDT 500
EQQSPTSGGG KVAPAQPSEE GPGRKDENKV DGMNAPKGQT GNSSRGPGDG 550
GNRDHWKESD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG 600
EDENEGEDYA E 611
Length:611
Mass (Da):69,151
Last modified:September 2, 2008 - v2
Checksum:i31CEFEA865FB10D2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031P → R Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064710

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641R → K in BAD96248. 1 Publication
Sequence conflicti246 – 2461R → C in AAH98437. 1 Publication
Sequence conflicti343 – 3431K → E in CAA39265. 1 Publication
Sequence conflicti391 – 3922LD → WN in CAA39265. 1 Publication
Sequence conflicti471 – 4711L → Q in AAH73154. 1 Publication
Sequence conflicti486 – 4861K → R in BAD96248. 1 Publication
Sequence conflicti611 – 6111E → D in CAG33239. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55733 Genomic DNA. Translation: CAA39265.1.
AB076839 mRNA. Translation: BAB82380.1.
CR456958 mRNA. Translation: CAG33239.1.
AK222528 mRNA. Translation: BAD96248.1.
CH471054 Genomic DNA. Translation: EAW96657.1.
BC073139 mRNA. Translation: AAH73139.1.
BC073154 mRNA. Translation: AAH73154.1.
BC098437 mRNA. Translation: AAH98437.1.
CCDSiCCDS41788.1.
PIRiS12566.
RefSeqiNP_001408.2. NM_001417.4.
UniGeneiHs.648394.
Hs.702041.

Genome annotation databases

EnsembliENST00000262056; ENSP00000262056; ENSG00000063046.
GeneIDi1975.
KEGGihsa:1975.
UCSCiuc001sbh.4. human.

Polymorphism databases

DMDMi205371761.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55733 Genomic DNA. Translation: CAA39265.1 .
AB076839 mRNA. Translation: BAB82380.1 .
CR456958 mRNA. Translation: CAG33239.1 .
AK222528 mRNA. Translation: BAD96248.1 .
CH471054 Genomic DNA. Translation: EAW96657.1 .
BC073139 mRNA. Translation: AAH73139.1 .
BC073154 mRNA. Translation: AAH73154.1 .
BC098437 mRNA. Translation: AAH98437.1 .
CCDSi CCDS41788.1.
PIRi S12566.
RefSeqi NP_001408.2. NM_001417.4.
UniGenei Hs.648394.
Hs.702041.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WI8 NMR - A 88-178 [» ]
2J76 NMR - E 77-176 [» ]
ProteinModelPortali P23588.
SMRi P23588. Positions 96-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108291. 57 interactions.
IntActi P23588. 21 interactions.
MINTi MINT-210187.
STRINGi 9606.ENSP00000262056.

PTM databases

PhosphoSitei P23588.

Polymorphism databases

DMDMi 205371761.

Proteomic databases

MaxQBi P23588.
PaxDbi P23588.
PRIDEi P23588.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262056 ; ENSP00000262056 ; ENSG00000063046 .
GeneIDi 1975.
KEGGi hsa:1975.
UCSCi uc001sbh.4. human.

Organism-specific databases

CTDi 1975.
GeneCardsi GC12P053400.
HGNCi HGNC:3285. EIF4B.
HPAi CAB019440.
HPA046164.
MIMi 603928. gene.
neXtProti NX_P23588.
PharmGKBi PA27713.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238591.
HOGENOMi HOG000006553.
HOVERGENi HBG006129.
InParanoidi P23588.
KOi K03258.
OrthoDBi EOG7MKW86.
PhylomeDBi P23588.
TreeFami TF101525.

Enzyme and pathway databases

Reactomei REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_6772. S6K1 signalling.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

EvolutionaryTracei P23588.
GeneWikii EIF4B.
GenomeRNAii 1975.
NextBioi 7995.
PMAP-CutDB P23588.
PROi P23588.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23588.
Bgeei P23588.
CleanExi HS_EIF4B.
Genevestigatori P23588.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of eukaryotic initiation factor 4B cDNA: sequence determination identifies a common RNA recognition motif."
    Milburn S.C., Hershey J.W.B., Davies M.V., Kelleher K., Kaufman R.J.
    EMBO J. 9:2783-2790(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Human eukaryotic initiation factor 4B."
    Yokoyama K.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix carcinoma.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Lung, Testis and Uterus.
  7. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-87; 118-135; 168-182; 189-225; 235-242; 340-372; 380-398; 473-486 AND 512-537, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence."
    Methot N., Pause A., Hershey J.W., Sonenberg N.
    Mol. Cell. Biol. 14:2307-2316(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3."
    Methot N., Song M.S., Sonenberg N.
    Mol. Cell. Biol. 16:5328-5334(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases."
    Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D., Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.
    EMBO J. 23:1761-1769(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-422.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity."
    Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.
    EMBO J. 25:2781-2791(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-422.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-219; SER-283; SER-459 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-192; SER-219; SER-406; SER-422; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; THR-412; SER-418; SER-425; SER-445; SER-498; SER-504 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Solution structure of the RNA binding domain of eukaryotic initiation factor 4B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 88-178.
  24. Cited for: VARIANT ARG-203.

Entry informationi

Entry nameiIF4B_HUMAN
AccessioniPrimary (citable) accession number: P23588
Secondary accession number(s): Q4G0E3
, Q53HQ2, Q6GPH5, Q6IB46, Q8WYK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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