UniProt Accession

 41_HUMAN; P11171; B1ALH8; B1ALH9; D3DPM9; D3DPN0; P11176; Q14245; Q5TB35; Q5VXN8; Q8IXV9; Q9Y578; Q9Y579 

Genbank Protein ID

 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 

Genbank Nucleotide ID

 AAA35795.1; AAA35793.1; AAA35794.1; AAA35797.1; AAD42222.1; CAI21967.1; CAI21967.1; CAI21966.1; CAI21966.1; CAI21968.1; CAI21969.1; CAI21969.1; CAI21970.1; CAI21970.1; CAH71636.1; CAH71636.1; CAH71637.1; CAH71637.1; CAH71638.1; CAH71638.1; CAH71639.1; CAH71639.1; EAX07663.1; EAX07665.1; EAX07667.1; EAX07668.1; AAH39079.1; AAD42223.1 

Protein Name

 Protein 4.1 

Protein Synonyms/Alias

 P4.1; 4.1R; Band 4.1; EPB4.1 

Gene Name

 EPB41 

Gene Synonyms/Alias

 E41P 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
88	RLFSSFLKRPKSQVS	ubiquitination	[1, 2]
231	CVVEKHAKGQDLLKR	ubiquitination	[3]
361	KLAPNQTKELEEKVM	acetylation	[4]
361	KLAPNQTKELEEKVM	ubiquitination	[3]
366	QTKELEEKVMELHKS	acetylation	[4]
366	QTKELEEKVMELHKS	ubiquitination	[3]
372	EKVMELHKSYRSMTP	ubiquitination	[3]
506	KFLALGSKFRYSGRT	ubiquitination	[3]
808	TQITKTVKGGISETR	ubiquitination	[5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. 

Sequence Annotation

 DOMAIN 210 491 FERM.
 REGION 494 614 Hydrophilic.
 REGION 615 713 Spectrin--actin-binding.
 REGION 714 864 C-terminal (CTD).
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 60 60 Phosphothreonine; by CDK1.
 MOD_RES 84 84 Phosphoserine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 152 152 Phosphoserine.
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 191 191 Phosphoserine.
 MOD_RES 222 222 Phosphotyrosine (By similarity).
 MOD_RES 540 540 Phosphoserine (By similarity).
 MOD_RES 542 542 Phosphoserine (By similarity).
 MOD_RES 555 555 Phosphoserine.
 MOD_RES 660 660 Phosphotyrosine; by EGFR.
 MOD_RES 674 674 Phosphoserine (By similarity).
 MOD_RES 712 712 Phosphoserine; by CDK1.  

Keyword

 3D-structure; Actin-binding; Alternative splicing; Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Elliptocytosis; Glycoprotein; Hereditary hemolytic anemia; Nucleus; Phosphoprotein; Polymorphism; Pyropoikilocytosis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 864 AA 

Protein Sequence

Gene Ontology

 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0008091; C:spectrin; TAS:ProtInc.
 GO:0014731; C:spectrin-associated cytoskeleton; TAS:BHF-UCL.
 GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
 GO:0030507; F:spectrin binding; TAS:BHF-UCL.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
 GO:0008015; P:blood circulation; TAS:ProtInc.
 GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
 GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL. 

Interpro

 IPR008379; Band_4.1_C.
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 IPR021187; Band_41_protein.
 IPR000798; Ez/rad/moesin_like.
 IPR014847; FERM-adjacent.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR019747; FERM_CS.
 IPR000299; FERM_domain.
 IPR018979; FERM_N.
 IPR018980; FERM_PH-like_C.
 IPR011993; PH_like_dom.
 IPR007477; SAB_dom. 

Pfam

 PF05902; 4_1_CTD
 PF08736; FA
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N
 PF04382; SAB 

SMART

 SM00295; B41 

PROSITE

 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 

PRINTS

 PR00935; BAND41.
 PR00661; ERMFAMILY.