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Showing Protein Eukaryotic translation initiation factor 5A-1-like (HMDBP10822)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP10822
Secondary Accession Numbers
  • 17102
Name Eukaryotic translation initiation factor 5A-1-like
Synonyms
  1. Eukaryotic initiation factor 5A isoform 1-like
  2. eIF-5A-1-like
  3. eIF-5A1-like
Gene Name EIF5AL1
Protein Type Unknown
Biological Properties
General Function Involved in RNA binding
Specific Function mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
nucleic acid binding
translation factor activity, nucleic acid binding
translation elongation factor activity
ribonucleoprotein binding
ribosome binding
rna binding
Process
metabolic process
macromolecule metabolic process
posttranscriptional regulation of gene expression
regulation of translation
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
regulation of gene expression
macromolecule modification
protein modification process
peptidyl-amino acid modification
peptidyl-lysine modification
peptidyl-lysine modification to hypusine
regulation of translational termination
positive regulation of translational termination
regulation of translational elongation
positive regulation of translational elongation
translational frameshifting
Cellular Location
  1. Nucleus
  2. Nucleus
  3. Cytoplasm
  4. Peripheral membrane protein
  5. Endoplasmic reticulum membrane
  6. Cytoplasmic side
  7. nuclear pore complex
Gene Properties
Chromosome Location Chromosome:1
Locus 10q22.3
SNPs EIF5AL1
Gene Sequence 
>465 bp
ATGGCAGATGATTTGGACTTCGAGACAGGAGATGCAGGGGCCTCAGCCACCTTCCCAATG
CAGTGCTCAGCATTACGTAAGAATGGCTTTGTGGTGCTCAAAGGCTGGCCATGTAAGATC
GTGGAGATGTCTGCTTCGAAGACTGGCAAGCACGGCCACGCCAAGGTCCATCTGGTTGGT
ATTGACATCTTTACTGGGAAGAAATATGAAGATATCTGCCCGTCAACTCATAATATGGAT
GTCCCCAACATCAAAAGGAATGACTTCCAGCTGATTGGCATCCAGGATGGGTACCTATCA
CTGCTCCAGGACAGCGGGGAGGTACCAGAGGACCTTCGTCTCCCTGAGGGAGACCTTGGC
AAGGAGATTGAGCAGAAGTACGACTGTGGAGAAGAGATCCTGATCACGGTGCTGTCTGCC
ATGACAGAGGAGGCAGCTGTTGCAATCAAGGCCATGGCAAAATAA
Protein Properties
Number of Residues 154
Molecular Weight 16773.0
Theoretical pI 4.61
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Eukaryotic translation initiation factor 5A-1-like
MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVG
IDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLG
KEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK
GenBank ID Protein 153791632
UniProtKB/Swiss-Prot ID Q6IS14
UniProtKB/Swiss-Prot Entry Name IF5AL_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001099692.1
GeneCard ID EIF5AL1
GenAtlas ID EIF5AL1
HGNC ID HGNC:17419
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]