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Identification
HMDB Protein ID HMDBP08322
Secondary Accession Numbers
  • 14034
Name Cdc42 effector protein 4
Synonyms
  1. Binder of Rho GTPases 4
Gene Name CDC42EP4
Protein Type Unknown
Biological Properties
General Function Involved in GTP-Rho binding
Specific Function Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Cytoplasm
  2. Endomembrane system
  3. Peripheral membrane protein
  4. cytoskeleton
Gene Properties
Chromosome Location Chromosome:1
Locus 17q24-q25
SNPs CDC42EP4
Gene Sequence
>1071 bp
ATGCCAATCCTCAAGCAACTGGTGTCCAGCTCGGTGCACTCCAAGCGCCGTTCCCGAGCG
GACCTCACGGCCGAGATGATCAGCGCCCCGCTGGGCGACTTCCGCCACACCATGCACGTT
GGCCGGGCCGGAGACGCCTTTGGGGACACCTCCTTCCTCAATAGCAAGGCTGGCGAGCCC
GACGGCGAGTCCTTGGACGAACAGCCCTCTTCTTCATCTTCCAAACGCAGTCTCCTGTCC
AGGAAGTTCCGGGGCAGCAAGCGGTCACAGTCGGTGACCAGGGGGGAGCGGGAGCAGCGT
GACATGCTGGGCTCCCTGCGGGACTCGGCCCTGTTTGTCAAGAATGCCATGTCCCTGCCC
CAGCTCAATGAGAAGGAGGCCGCGGAGAAGGGCACCAGTAAGCTGCCCAAGAGCCTGTCA
TCCAGCCCCGTGAAGAAGGCCAATGACGGGGAGGGCGGCGATGAGGAGGCGGGCACGGAG
GAGGCAGTGCCCCGTCGGAATGGGGCCGCGGGTCCACATTCCCCTGACCCCCTCCTCGAT
GAGCAGGCCTTTGGGGATCTGACAGATCTGCCTGTCGTGCCCAAGGCCACGTACGGGCTG
AAGCATGCGGAGTCCATCATGTCCTTCCACATCGACCTGGGGCCCTCCATGCTGGGTGAC
GTCCTCAGCATCATGGACAAGGAGGAGTGGGACCCCGAGGAGGGGGAGGGTGGTTACCAT
GGCGATGAGGGCGCCGCTGGCACCATCACCCAGGCTCCCCCGTACGCCGTGGCGGCCCCT
CCCCTGGCAAGGCAGGAAGGCAAGGCTGGCCCAGACTTGCCCTCCCTCCCCTCCCATGCT
CTGGAGGATGAGGGGTGGGCAGCAGCGGCCCCCAGCCCCGGCTCAGCCCGCAGCATGGGC
AGCCACACCACACGGGACAGCAGCTCCCTCTCCAGCTGCACCTCAGGCATCCTGGAGGAG
CGCAGCCCTGCCTTCCGGGGGCCGGACAGGGCCCGGGCTGCTGTCTCAAGACAGCCAGAC
AAGGAGTTCTCCTTCATGGATGAGGAGGAGGAGGATGAAATCCGTGTGTGA
Protein Properties
Number of Residues 356
Molecular Weight 37979.4
Theoretical pI 4.82
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Cdc42 effector protein 4
MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEP
DGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLP
QLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLD
EQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYH
GDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMG
SHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV
GenBank ID Protein 11036449
UniProtKB/Swiss-Prot ID Q9H3Q1
UniProtKB/Swiss-Prot Entry Name BORG4_HUMAN
PDB IDs Not Available
GenBank Gene ID AB042237
GeneCard ID CDC42EP4
GenAtlas ID CDC42EP4
HGNC ID HGNC:17147
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. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: 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. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]
  8. Hirsch DS, Pirone DM, Burbelo PD: A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes. J Biol Chem. 2001 Jan 12;276(2):875-83. [PubMed:11035016 ]
  9. Osada N, Kusuda J, Suzuki Y, Sugano S, Hashimoto K: Sequence analysis, gene expression, and chromosomal assignment of mouse Borg4 gene and its human orthologue. J Hum Genet. 2000;45(6):374-7. [PubMed:11185749 ]