EPB41L1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Band 4.1-like protein 1''' is a [[protein]] that in humans is encoded by the ''EPB41L1'' [[gene]].<ref name="pmid9570967">{{cite journal | vauthors = Kim AC, Van Huffel C, Lutchman M, Chishti AH | title = Radiation hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human chromosome 20q11.2-q12 | journal = Genomics | volume = 49 | issue = 1 | pages = 165–6 | date = June 1998 | pmid = 9570967 | pmc =  | doi = 10.1006/geno.1998.5212 }}</ref><ref name="pmid9828140">{{cite journal | vauthors = Peters LL, Weier HU, Walensky LD, Snyder SH, Parra M, Mohandas N, Conboy JG | title = Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and human | journal = Genomics | volume = 54 | issue = 2 | pages = 348–50 | date = January 1999 | pmid = 9828140 | pmc = | doi = 10.1006/geno.1998.5537 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPB41L1 erythrocyte membrane protein band 4.1-like 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2036| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Erythrocyte membrane protein band 4.1-like 1
| HGNCid = 3378
| Symbol = EPB41L1
| AltSymbols =; 4.1N; DKFZp686H17242; KIAA0338; MGC11072
| OMIM = 602879
| ECnumber = 
| Homologene = 8126
| MGIid = 
| GeneAtlas_image1 = PBB_GE_EPB41L1_212336_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPB41L1_212339_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0008092 |text = cytoskeletal protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0030866 |text = cortical actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2036
    | Hs_Ensembl = ENSG00000088367
    | Hs_RefseqProtein = NP_036288
    | Hs_RefseqmRNA = NM_012156
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 34142840
    | Hs_GenLoc_end = 34284135
    | Hs_Uniprot = Q9H4G0
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Erythrocyte membrane protein band 4.1-like 1''', also known as '''EPB41L1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPB41L1 erythrocyte membrane protein band 4.1-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2036| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined.<ref name="entrez">{{cite web | title = Entrez Gene: EPB41L1 erythrocyte membrane protein band 4.1-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2036| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
EPB41L1 has been shown to [[Protein-protein interaction|interact]] with:
* [[CENTG1]],<ref name = pmid11136977>{{cite journal | vauthors = Ye K, Hurt KJ, Wu FY, Fang M, Luo HR, Hong JJ, Blackshaw S, Ferris CD, Snyder SH | title = Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N | journal = Cell | volume = 103 | issue = 6 | pages = 919–30 | date = December 2000 | pmid = 11136977 | doi =  10.1016/S0092-8674(00)00195-1}}</ref>
* [[Dopamine receptor D2]],<ref name = pmid12181426>{{cite journal | vauthors = Binda AV, Kabbani N, Lin R, Levenson R | title = D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N | journal = Mol. Pharmacol. | volume = 62 | issue = 3 | pages = 507–13 | date = September 2002 | pmid = 12181426 | doi =  10.1124/mol.62.3.507}}</ref>
* [[Dopamine receptor D3]],<ref name = pmid12181426/>
* [[ITPR1]],<ref name = pmid12676536>{{cite journal | vauthors = Maximov A, Tang TS, Bezprozvanny I | title = Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons | journal = Mol. Cell. Neurosci. | volume = 22 | issue = 2 | pages = 271–83 | date = February 2003 | pmid = 12676536 | doi =  10.1016/s1044-7431(02)00027-1}}</ref>  and
* [[Nuclear mitotic apparatus protein 1]].<ref name = pmid10594058>{{cite journal | vauthors = Ye K, Compton DA, Lai MM, Walensky LD, Snyder SH | title = Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor | journal = J. Neurosci. | volume = 19 | issue = 24 | pages = 10747–56 | date = December 1999 | pmid = 10594058 | doi =  }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P | title = New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. | journal = Front. Biosci. | volume = 11 | issue =  | pages = 1646–66 | year = 2006 | pmid = 16368544 | doi = 10.2741/1911 }}
| citations =
* {{cite journal | vauthors = Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. | journal = DNA Res. | volume = 4 | issue = 2 | pages = 141–50 | year = 1997 | pmid = 9205841 | doi = 10.1093/dnares/4.2.141 }}
*{{cite journal | author=Calinisan V, Gravem D, Chen RP, ''et al.'' |title=New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. |journal=Front. Biosci. |volume=11 |issue=  |pages= 1646-66 |year= 2006 |pmid= 16368544 |doi= }}
* {{cite journal | vauthors = Walensky LD, Blackshaw S, Liao D, Watkins CC, Weier HU, Parra M, Huganir RL, Conboy JG, Mohandas N, Snyder SH | title = A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1. | journal = J. Neurosci. | volume = 19 | issue = 15 | pages = 6457–67 | year = 1999 | pmid = 10414974 | doi =  }}
*{{cite journal | author=Nagase T, Ishikawa K, Nakajima D, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 2 |pages= 141-50 |year= 1997 |pmid= 9205841 |doi=  }}
* {{cite journal | vauthors = Ye K, Compton DA, Lai MM, Walensky LD, Snyder SH | title = Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. | journal = J. Neurosci. | volume = 19 | issue = 24 | pages = 10747–56 | year = 2000 | pmid = 10594058 | doi =  }}
*{{cite journal  | author=Kim AC, Van Huffel C, Lutchman M, Chishti AH |title=Radiation hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human chromosome 20q11.2-q12. |journal=Genomics |volume=49 |issue= 1 |pages= 165-6 |year= 1998 |pmid= 9570967 |doi= 10.1006/geno.1998.5212 }}
* {{cite journal | vauthors = Shen L, Liang F, Walensky LD, Huganir RL | title = Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association. | journal = J. Neurosci. | volume = 20 | issue = 21 | pages = 7932–40 | year = 2001 | pmid = 11050113 | doi =  }}
*{{cite journal  | author=Peters LL, Weier HU, Walensky LD, ''et al.'' |title=Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and human. |journal=Genomics |volume=54 |issue= 2 |pages= 348-50 |year= 1999 |pmid= 9828140 |doi= 10.1006/geno.1998.5537 }}
* {{cite journal | vauthors = Ye K, Hurt KJ, Wu FY, Fang M, Luo HR, Hong JJ, Blackshaw S, Ferris CD, Snyder SH | title = Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N. | journal = Cell | volume = 103 | issue = 6 | pages = 919–30 | year = 2001 | pmid = 11136977 | doi = 10.1016/S0092-8674(00)00195-1 }}
*{{cite journal | author=Walensky LD, Blackshaw S, Liao D, ''et al.'' |title=A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1. |journal=J. Neurosci. |volume=19 |issue= 15 |pages= 6457-67 |year= 1999 |pmid= 10414974 |doi=  }}
* {{cite journal | vauthors = Binda AV, Kabbani N, Lin R, Levenson R | title = D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N. | journal = Mol. Pharmacol. | volume = 62 | issue = 3 | pages = 507–13 | year = 2002 | pmid = 12181426 | doi = 10.1124/mol.62.3.507 }}
*{{cite journal | author=Ye K, Compton DA, Lai MM, ''et al.'' |title=Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. |journal=J. Neurosci. |volume=19 |issue= 24 |pages= 10747-56 |year= 2000 |pmid= 10594058 |doi=  }}
* {{cite journal | vauthors = Zhang S, Mizutani A, Hisatsune C, Higo T, Bannai H, Nakayama T, Hattori M, Mikoshiba K | title = Protein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cells. | journal = J. Biol. Chem. | volume = 278 | issue = 6 | pages = 4048–56 | year = 2003 | pmid = 12444087 | pmc = 2366074 | doi = 10.1074/jbc.M209960200 }}
*{{cite journal | author=Shen L, Liang F, Walensky LD, Huganir RL |title=Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association. |journal=J. Neurosci. |volume=20 |issue= 21 |pages= 7932-40 |year= 2001 |pmid= 11050113 |doi=  }}
* {{cite journal | vauthors = Coleman SK, Cai C, Mottershead DG, Haapalahti JP, Keinänen K | title = Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein. | journal = J. Neurosci. | volume = 23 | issue = 3 | pages = 798–806 | year = 2003 | pmid = 12574408 | doi =  }}
*{{cite journal | author=Ye K, Hurt KJ, Wu FY, ''et al.'' |title=Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N. |journal=Cell |volume=103 |issue= 6 |pages= 919-30 |year= 2001 |pmid= 11136977 |doi=  }}
* {{cite journal | vauthors = Maximov A, Tang TS, Bezprozvanny I | title = Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons. | journal = Mol. Cell. Neurosci. | volume = 22 | issue = 2 | pages = 271–83 | year = 2003 | pmid = 12676536 | doi = 10.1016/S1044-7431(02)00027-1 }}
*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
* {{cite journal | vauthors = Nagaraja GM, Kandpal RP | title = Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins. | journal = Biochem. Biophys. Res. Commun. | volume = 313 | issue = 3 | pages = 654–65 | year = 2004 | pmid = 14697242 | doi = 10.1016/j.bbrc.2003.12.001 }}
*{{cite journal | author=Binda AV, Kabbani N, Lin R, Levenson R |title=D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N. |journal=Mol. Pharmacol. |volume=62 |issue= 3 |pages= 507-13 |year= 2002 |pmid= 12181426 |doi= }}
* {{cite journal | vauthors = Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP | title = Phosphoproteomic analysis of the developing mouse brain. | journal = Mol. Cell. Proteomics | volume = 3 | issue = 11 | pages = 1093–101 | year = 2005 | pmid = 15345747 | doi = 10.1074/mcp.M400085-MCP200 }}
*{{cite journal | author=Zhang S, Mizutani A, Hisatsune C, ''et al.'' |title=Protein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cells. |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 4048-56 |year= 2003 |pmid= 12444087 |doi= 10.1074/jbc.M209960200 }}
* {{cite journal | vauthors = Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP | title = A probability-based approach for high-throughput protein phosphorylation analysis and site localization. | journal = Nat. Biotechnol. | volume = 24 | issue = 10 | pages = 1285–92 | year = 2006 | pmid = 16964243 | doi = 10.1038/nbt1240 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Coleman SK, Cai C, Mottershead DG, ''et al.'' |title=Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein. |journal=J. Neurosci. |volume=23 |issue= 3 |pages= 798-806 |year= 2003 |pmid= 12574408 |doi=  }}
*{{cite journal | author=Maximov A, Tang TS, Bezprozvanny I |title=Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons. |journal=Mol. Cell. Neurosci. |volume=22 |issue= 2 |pages= 271-83 |year= 2003 |pmid= 12676536 |doi= }}
*{{cite journal | author=Nagaraja GM, Kandpal RP |title=Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins. |journal=Biochem. Biophys. Res. Commun. |volume=313 |issue= 3 |pages= 654-65 |year= 2004 |pmid= 14697242 |doi= }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Ballif BA, Villén J, Beausoleil SA, ''et al.'' |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell Proteomics |volume=3 |issue= 11 |pages= 1093-101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
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Latest revision as of 02:07, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Band 4.1-like protein 1 is a protein that in humans is encoded by the EPB41L1 gene.[1][2][3]

Function

Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined.[3]

Interactions

EPB41L1 has been shown to interact with:

References

  1. ↑ Kim AC, Van Huffel C, Lutchman M, Chishti AH (June 1998). "Radiation hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human chromosome 20q11.2-q12". Genomics. 49 (1): 165–6. doi:10.1006/geno.1998.5212. PMID 9570967.
  2. ↑ Peters LL, Weier HU, Walensky LD, Snyder SH, Parra M, Mohandas N, Conboy JG (January 1999). "Four paralogous protein 4.1 genes map to distinct chromosomes in mouse and human". Genomics. 54 (2): 348–50. doi:10.1006/geno.1998.5537. PMID 9828140.
  3. ↑ 3.0 3.1 "Entrez Gene: EPB41L1 erythrocyte membrane protein band 4.1-like 1".
  4. ↑ Ye K, Hurt KJ, Wu FY, Fang M, Luo HR, Hong JJ, Blackshaw S, Ferris CD, Snyder SH (December 2000). "Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N". Cell. 103 (6): 919–30. doi:10.1016/S0092-8674(00)00195-1. PMID 11136977.
  5. ↑ 5.0 5.1 Binda AV, Kabbani N, Lin R, Levenson R (September 2002). "D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N". Mol. Pharmacol. 62 (3): 507–13. doi:10.1124/mol.62.3.507. PMID 12181426.
  6. ↑ Maximov A, Tang TS, Bezprozvanny I (February 2003). "Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons". Mol. Cell. Neurosci. 22 (2): 271–83. doi:10.1016/s1044-7431(02)00027-1. PMID 12676536.
  7. ↑ Ye K, Compton DA, Lai MM, Walensky LD, Snyder SH (December 1999). "Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor". J. Neurosci. 19 (24): 10747–56. PMID 10594058.

Further reading

  • Calinisan V, Gravem D, Chen RP, Brittin S, Mohandas N, Lecomte MC, Gascard P (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium". Front. Biosci. 11: 1646–66. doi:10.2741/1911. PMID 16368544.
  • Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
  • Walensky LD, Blackshaw S, Liao D, Watkins CC, Weier HU, Parra M, Huganir RL, Conboy JG, Mohandas N, Snyder SH (1999). "A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1". J. Neurosci. 19 (15): 6457–67. PMID 10414974.
  • Ye K, Compton DA, Lai MM, Walensky LD, Snyder SH (2000). "Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor". J. Neurosci. 19 (24): 10747–56. PMID 10594058.
  • Shen L, Liang F, Walensky LD, Huganir RL (2001). "Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association". J. Neurosci. 20 (21): 7932–40. PMID 11050113.
  • Ye K, Hurt KJ, Wu FY, Fang M, Luo HR, Hong JJ, Blackshaw S, Ferris CD, Snyder SH (2001). "Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N". Cell. 103 (6): 919–30. doi:10.1016/S0092-8674(00)00195-1. PMID 11136977.
  • Binda AV, Kabbani N, Lin R, Levenson R (2002). "D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N". Mol. Pharmacol. 62 (3): 507–13. doi:10.1124/mol.62.3.507. PMID 12181426.
  • Zhang S, Mizutani A, Hisatsune C, Higo T, Bannai H, Nakayama T, Hattori M, Mikoshiba K (2003). "Protein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cells". J. Biol. Chem. 278 (6): 4048–56. doi:10.1074/jbc.M209960200. PMC 2366074. PMID 12444087.
  • Coleman SK, Cai C, Mottershead DG, Haapalahti JP, Keinänen K (2003). "Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein". J. Neurosci. 23 (3): 798–806. PMID 12574408.
  • Maximov A, Tang TS, Bezprozvanny I (2003). "Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons". Mol. Cell. Neurosci. 22 (2): 271–83. doi:10.1016/S1044-7431(02)00027-1. PMID 12676536.
  • Nagaraja GM, Kandpal RP (2004). "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins". Biochem. Biophys. Res. Commun. 313 (3): 654–65. doi:10.1016/j.bbrc.2003.12.001. PMID 14697242.
  • Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.


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