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MGI:Epb4.1

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Contents

Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Epb4.1 ( synonyms: 4.1R, D4Ertd442e, Elp-1, Elp1 )
Protein Name(s) erythrocyte protein band 4.1,
External Links
MGI MGI:95401

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0003779

actin binding

MGI:MGI:2135711
PMID:11274145[1]

ISS: Inferred from Sequence or Structural Similarity

F

From MGI

GO:0005198

structural molecule activity

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR008379

F

From MGI

GO:0005516

calmodulin binding

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0112

F

From MGI

GO:0005545

1-phosphatidylinositol binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P11171

F

From MGI

GO:0005634

nucleus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:C9JTS2

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0963

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR000798

C

From MGI

GO:0005794

Golgi apparatus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:C9JTS2

C

From MGI

GO:0005856

cytoskeleton

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0206

C

From MGI

GO:0005856

cytoskeleton

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR008379
InterPro:IPR000299
InterPro:IPR007477

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:C9JTS2

C

From MGI

GO:0008092

cytoskeletal protein binding

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR000798
InterPro:IPR007477

F

From MGI

GO:0008360

regulation of cell shape

MGI:MGI:2135711
PMID:11274145[1]

ISS: Inferred from Sequence or Structural Similarity

P

From MGI

GO:0015629

actin cytoskeleton

MGI:MGI:2135711
PMID:11274145[1]

ISS: Inferred from Sequence or Structural Similarity

C

From MGI

GO:0016020

membrane

MGI:MGI:3806792
PMID:18723693[2]

IDA: Inferred from Direct Assay

C

From MGI

GO:0019898

extrinsic to membrane

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR000798

C

From MGI

GO:0030036

actin cytoskeleton organization

MGI:MGI:2135711
PMID:11274145[1]

ISS: Inferred from Sequence or Structural Similarity

P

From MGI

GO:0030507

spectrin binding

MGI:MGI:2135711
PMID:11274145[1]

ISS: Inferred from Sequence or Structural Similarity

F

From MGI

GO:0030863

cortical cytoskeleton

MGI:MGI:3806792
PMID:18723693[2]

IDA: Inferred from Direct Assay

C

From MGI

GO:0030863

cortical cytoskeleton

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P11171

C

From MGI

GO:0030866

cortical actin cytoskeleton organization

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR007477

P

From MGI

GO:0032092

positive regulation of protein binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P11171

P

From MGI

GO:0032092

positive regulation of protein binding

MGI:MGI:4838723
PMID:20585040[3]

IGI: Inferred from Genetic Interaction

MGI:MGI:98385
MGI:MGI:98387

P

From MGI

GO:0043231

intracellular membrane-bounded organelle

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:C9JTS2

C

From MGI

GO:0043234

protein complex

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P11171

C

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 1.2 1.3 1.4 Kontrogianni-Konstantopoulos A et al. (2001) The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation. J Biol Chem 276: 20679-87 PubMed GONUTS page
  2. 2.0 2.1 Robledo RF et al. (2008) Targeted deletion of alpha-adducin results in absent beta- and gamma-adducin, compensated hemolytic anemia, and lethal hydrocephalus in mice. Blood 112: 4298-307 PubMed GONUTS page
  3. Korsgren C & Lux SE (2010) The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding. Blood 116: 2600-7 PubMed GONUTS page
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