HUMAN:41

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EPB41 (synonyms: E41P)
Protein Name(s)	Protein 4.1 P4.1 4.1R Band 4.1 EPB4.1
External Links
UniProt	P11171
EMBL	M14993 J03796 J03796 M61733 AF156225 AL138785 AL357500 AL138785 AL357500 AL138785 AL138785 AL357500 AL138785 AL357500 AL357500 AL138785 AL357500 AL138785 AL357500 AL138785 AL357500 AL138785 CH471059 CH471059 CH471059 CH471059 BC039079 AF156226
CCDS	CCDS330.1 CCDS331.1 CCDS332.1 CCDS53288.1 CCDS53289.1
PIR	A39810
RefSeq	NP_001159477.1 NP_001159478.1 NP_004428.1 NP_976217.1 XP_005245818.1 XP_005245821.1
UniGene	Hs.175437 Hs.708933 Hs.712722
PDB	1GG3 2RQ1 3QIJ
PDBsum	1GG3 2RQ1 3QIJ
DisProt	DP00678
ProteinModelPortal	P11171
SMR	P11171
BioGrid	108349
DIP	DIP-17032N
IntAct	P11171
MINT	MINT-1208648
TCDB	8.A.25.1.2
PhosphoSite	P11171
UniCarbKB	P11171
DMDM	90101808
MaxQB	P11171
PaxDb	P11171
PRIDE	P11171
DNASU	2035
Ensembl	ENST00000343067 ENST00000347529 ENST00000349460 ENST00000373797 ENST00000373798 ENST00000373800
GeneID	2035
KEGG	hsa:2035
UCSC	uc001brg.2 uc001brh.2 uc001bri.2 uc001brk.3 uc001brl.2 uc001brm.2 uc009vtm.2
CTD	2035
GeneCards	GC01P029213
HGNC	HGNC:3377
HPA	HPA028414
MIM	130500 266140 611804
neXtProt	NX_P11171
Orphanet	288
PharmGKB	PA27810
eggNOG	NOG242913
GeneTree	ENSGT00760000118823
HOVERGEN	HBG007777
InParanoid	P11171
KO	K06107
OMA	HREDPDF
OrthoDB	EOG7Z69BP
PhylomeDB	P11171
TreeFam	TF351626
ChiTaRS	EPB41
EvolutionaryTrace	P11171
GeneWiki	EPB41
GenomeRNAi	2035
NextBio	8259
PMAP-CutDB	B1ALH9
PRO	PR:P11171
Proteomes	UP000005640
Bgee	P11171
CleanEx	HS_EPB41
ExpressionAtlas	P11171
Genevestigator	P11171
GO	GO:0030863 GO:0019898 GO:0005634 GO:0005886 GO:0043234 GO:0008091 GO:0014731 GO:0005545 GO:0030507 GO:0005200 GO:0030036 GO:0008015 GO:0030866 GO:0032092
Gene3D	1.20.80.10 2.30.29.30
InterPro	IPR008379 IPR019749 IPR021187 IPR000798 IPR014847 IPR014352 IPR019748 IPR019747 IPR000299 IPR018979 IPR018980 IPR011993 IPR007477 IPR029071
Pfam	PF05902 PF08736 PF09380 PF00373 PF09379 PF04382
PIRSF	PIRSF002304
PRINTS	PR00935 PR00661
SMART	SM00295
SUPFAM	SSF47031 SSF54236
PROSITE	PS00660 PS00661 PS50057

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0003779	actin binding	PMID:24434814^[1]	ECO:0000314			F		Figure 4 shows that the mutation S260 prevents the actin binding of the FRMD7, which encodes a member of the protein 4.1 family.	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P48193	C		Seeded From UniProt	complete
involved_in	GO:1904478	regulation of intestinal absorption	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P48193	P		Seeded From UniProt	complete
involved_in	GO:0051924	regulation of calcium ion transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P48193	P		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	PMID:6894932^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	results_in_morphogenesis_of:(UBERON:0000232)	Seeded From UniProt	complete
part_of	GO:0099738	cell cortex region	PMID:23870127^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904778	positive regulation of protein localization to cell cortex	PMID:23870127^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:6894932^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(UBERON:0000232)	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:20109190^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051219	phosphoprotein binding	PMID:20109190^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_input:(UniProtKB:Q14980)	Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:20109190^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_input:(UniProtKB:Q14980)	Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:20109190^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_input:(UniProtKB:Q14980)	Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	PMID:3693401^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:16060676^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030863	cortical cytoskeleton	PMID:16254212^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030036	actin cytoskeleton organization	PMID:8434260^[8]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005545	1-phosphatidylinositol binding	PMID:16669616^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0031032	actomyosin structure organization	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103006 PANTHER:PTN001150527 UniProtKB:Q9H329	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010434 PANTHER:PTN000589691 UniProtKB:O43491 UniProtKB:P11171	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904478	regulation of intestinal absorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	P		Seeded From UniProt	complete
involved_in	GO:0051924	regulation of calcium ion transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	P		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	P		Seeded From UniProt	complete
part_of	GO:0030863	cortical cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P48193 ensembl:ENSMUSP00000030739	C		Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2K161 ensembl:ENSRNOP00000071712	P		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2K161 ensembl:ENSRNOP00000071712	C		Seeded From UniProt	complete
part_of	GO:0009898	cytoplasmic side of plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2K161 ensembl:ENSRNOP00000071712	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2K161 ensembl:ENSRNOP00000071712	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A0G2K161 ensembl:ENSRNOP00000071712	F		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008379	F		Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008379	F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000299 InterPro:IPR007477 InterPro:IPR008379	C		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000798 InterPro:IPR007477	F		Seeded From UniProt	complete
involved_in	GO:0030866	cortical actin cytoskeleton organization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007477	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:9598318^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005200	structural constituent of cytoskeleton	PMID:6894932^[2]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030507	spectrin binding	PMID:3693401^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0014731	spectrin-associated cytoskeleton	PMID:3693401^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-6797568 Reactome:R-HSA-6797553	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0112	F		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0009	F		Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0138	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Zhang, X et al. (2014) Identification of three novel mutations in the FRMD7 gene for X-linked idiopathic congenital nystagmus. Sci Rep 4 3745 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Tchernia, G et al. (1981) Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. J. Clin. Invest. 68 454-60 PubMed GONUTS page
↑ ^3.0 ^3.1 Kiyomitsu, T & Cheeseman, IM (2013) Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase. Cell 154 391-402 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Treviño, MA et al. (2010) NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. BMC Biochem. 11 7 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Mische, SM et al. (1987) Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J. Cell Biol. 105 2837-45 PubMed GONUTS page
↑ An, X et al. (2005) Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate. Biochemistry 44 10681-8 PubMed GONUTS page
↑ Cioffi, DL et al. (2005) Activation of the endothelial store-operated ISOC Ca2+ channel requires interaction of protein 4.1 with TRPC4. Circ. Res. 97 1164-72 PubMed GONUTS page
↑ Conboy, JG (1993) Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. Semin. Hematol. 30 58-73 PubMed GONUTS page
↑ An, X et al. (2006) Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins. Biochemistry 45 5725-32 PubMed GONUTS page
↑ ^10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Parra, M et al. (1998) Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49 298-306 PubMed GONUTS page

[PMID:24434814-1] Zhang, X et al. (2014) Identification of three novel mutations in the FRMD7 gene for X-linked idiopathic congenital nystagmus. Sci Rep 4 3745 PubMed GONUTS page

[PMID:6894932-2] 2.0 ^2.1 ^2.2 Tchernia, G et al. (1981) Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. J. Clin. Invest. 68 454-60 PubMed GONUTS page

[PMID:23870127-3] 3.0 ^3.1 Kiyomitsu, T & Cheeseman, IM (2013) Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase. Cell 154 391-402 PubMed GONUTS page

[PMID:20109190-4] 4.0 ^4.1 ^4.2 ^4.3 Treviño, MA et al. (2010) NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. BMC Biochem. 11 7 PubMed GONUTS page

[PMID:3693401-5] 5.0 ^5.1 ^5.2 Mische, SM et al. (1987) Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J. Cell Biol. 105 2837-45 PubMed GONUTS page

[PMID:16060676-6] An, X et al. (2005) Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate. Biochemistry 44 10681-8 PubMed GONUTS page

[PMID:16254212-7] Cioffi, DL et al. (2005) Activation of the endothelial store-operated ISOC Ca2+ channel requires interaction of protein 4.1 with TRPC4. Circ. Res. 97 1164-72 PubMed GONUTS page

[PMID:8434260-8] Conboy, JG (1993) Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. Semin. Hematol. 30 58-73 PubMed GONUTS page

[PMID:16669616-9] An, X et al. (2006) Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins. Biochemistry 45 5725-32 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:9598318-11] Parra, M et al. (1998) Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49 298-306 PubMed GONUTS page

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HUMAN:41

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Notes

References

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