EPB41L2

Protein-coding gene in the species Homo sapiens
EPB41L2
Identifiers
AliasesEPB41L2, 4.1-G, 4.1G, erythrocyte membrane protein band 4.1 like 2
External IDsOMIM: 603237; MGI: 103009; HomoloGene: 37478; GeneCards: EPB41L2; OMA:EPB41L2 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for EPB41L2
Genomic location for EPB41L2
Band6q23.1-q23.2Start130,839,347 bp[1]
End131,063,322 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for EPB41L2
Genomic location for EPB41L2
Band10 A4|10 12.26 cMStart25,359,798 bp[2]
End25,523,519 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • epithelium of colon

  • sural nerve

  • tendon of biceps brachii

  • corpus callosum

  • dorsal motor nucleus of vagus nerve

  • inferior olivary nucleus

  • internal globus pallidus

  • trigeminal ganglion

  • right lung
Top expressed in
  • neural layer of retina

  • tail of embryo

  • genital tubercle

  • lens

  • optic nerve

  • sciatic nerve

  • epithelium of lens

  • zygote

  • retinal pigment epithelium

  • spermatid
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • structural molecule activity
  • PH domain binding
  • actin binding
  • spectrin binding
  • cytoskeletal protein binding
  • structural constituent of cytoskeleton
  • protein binding
Cellular component
  • extracellular exosome
  • cell junction
  • spectrin
  • nucleus
  • membrane
  • focal adhesion
  • nucleoplasm
  • cytoplasm
  • COP9 signalosome
  • cytoskeleton
  • cytosol
  • plasma membrane
  • cell cortex region
  • cell cortex
Biological process
  • cortical actin cytoskeleton organization
  • actomyosin structure organization
  • positive regulation of protein localization to cell cortex
  • cell cycle
  • cell division
  • transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2037

13822

Ensembl

ENSG00000079819

ENSMUSG00000019978

UniProt

O43491

O70318

RefSeq (mRNA)
NM_001135554
NM_001135555
NM_001199388
NM_001199389
NM_001252660

NM_001431
NM_001350299
NM_001350301
NM_001350302
NM_001350303
NM_001350304
NM_001350305
NM_001350306
NM_001350307
NM_001350308
NM_001350309
NM_001350310
NM_001350311
NM_001350312
NM_001350313
NM_001350314
NM_001350315
NM_001350320

NM_001199265
NM_013511
NM_001358751
NM_001358753
NM_001358754

NM_001358755

RefSeq (protein)
NP_001129026
NP_001129027
NP_001186317
NP_001239589
NP_001422

NP_001337228
NP_001337230
NP_001337231
NP_001337232
NP_001337233
NP_001337234
NP_001337235
NP_001337236
NP_001337237
NP_001337238
NP_001337239
NP_001337240
NP_001337241
NP_001337242
NP_001337243
NP_001337244
NP_001337249

NP_001186194
NP_038539
NP_001345680
NP_001345682
NP_001345683

NP_001345684
NP_001391726
NP_001391727
NP_001391728
NP_001391730
NP_001391731
NP_001391732
NP_001391734
NP_001391735
NP_001391736
NP_001391737
NP_001391738
NP_001391739
NP_001391740
NP_001391741
NP_001391742
NP_001391744
NP_001391745
NP_001391747
NP_001391748
NP_001391757
NP_001391758
NP_001391759
NP_001391760
NP_001391761
NP_001391762
NP_001391763
NP_001391764
NP_001391766
NP_001391767
NP_001391768
NP_001391769
NP_001391770
NP_001391771
NP_001391772
NP_001391773
NP_001391774
NP_001391775
NP_001391776
NP_001391777
NP_001391778
NP_001391779
NP_001391780
NP_001391781
NP_001391782
NP_001391783
NP_001391784

Location (UCSC)Chr 6: 130.84 – 131.06 MbChr 10: 25.36 – 25.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Band 4.1-like protein 2 is a protein that in humans is encoded by the EPB41L2 gene.[5][6][7]

Interactions

EPB41L2 has been shown to interact with FKBP2[8] and GRIA1.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000079819 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019978 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Parra M, Gascard P, Walensky LD, Snyder SH, Mohandas N, Conboy JG (April 1998). "Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family". Genomics. 49 (2): 298–306. doi:10.1006/geno.1998.5265. PMID 9598318.
  6. ^ Peters LL, Weier HU, Walensky LD, Snyder SH, Parra M, Mohandas N, Conboy JG (December 1998). "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.
  7. ^ "Entrez Gene: EPB41L2 erythrocyte membrane protein band 4.1-like 2".
  8. ^ Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (April 1998). "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1". The Journal of Cell Biology. 141 (1): 143–53. doi:10.1083/jcb.141.1.143. PMC 2132710. PMID 9531554.
  9. ^ Shen L, Liang F, Walensky LD, Huganir RL (November 2000). "Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association". The Journal of Neuroscience. 20 (21): 7932–40. doi:10.1523/jneurosci.20-21-07932.2000. PMC 6772741. PMID 11050113.

Further reading

  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (April 1998). "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1". The Journal of Cell Biology. 141 (1): 143–53. doi:10.1083/jcb.141.1.143. PMC 2132710. PMID 9531554.
  • Shen L, Liang F, Walensky LD, Huganir RL (November 2000). "Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association". The Journal of Neuroscience. 20 (21): 7932–40. doi:10.1523/jneurosci.20-21-07932.2000. PMC 6772741. PMID 11050113.
  • Kontrogianni-Konstantopoulos A, Frye CS, Benz EJ, Huang SC (June 2001). "The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation". The Journal of Biological Chemistry. 276 (23): 20679–87. doi:10.1074/jbc.M010581200. PMID 11274145.
  • Gimm JA, An X, Nunomura W, Mohandas N (June 2002). "Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins". Biochemistry. 41 (23): 7275–82. doi:10.1021/bi0256330. PMID 12044158.
  • 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". Molecular Pharmacology. 62 (3): 507–13. doi:10.1124/mol.62.3.507. PMID 12181426. S2CID 19901660.
  • Delhommeau F, Vasseur-Godbillon C, Leclerc P, Schischmanoff PO, Croisille L, Rince P, Morinière M, Benz EJ, Tchernia G, Tamagnini G, Ribeiro L, Delaunay J, Baklouti F (October 2002). "A splicing alteration of 4.1R pre-mRNA generates 2 protein isoforms with distinct assembly to spindle poles in mitotic cells". Blood. 100 (7): 2629–36. doi:10.1182/blood.V100.7.2629. PMID 12239178.
  • Lu D, Yan H, Othman T, Turner CP, Woolf T, Rivkees SA (January 2004). "Cytoskeletal protein 4.1G binds to the third intracellular loop of the A1 adenosine receptor and inhibits receptor action". The Biochemical Journal. 377 (Pt 1): 51–9. doi:10.1042/BJ20030952. PMC 1223836. PMID 12974671.
  • Ralston KJ, Hird SL, Zhang X, Scott JL, Jin B, Thorne RF, Berndt MC, Boyd AW, Burns GF (August 2004). "The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large". The Journal of Biological Chemistry. 279 (32): 33816–28. doi:10.1074/jbc.M401040200. PMID 15138281.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.


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