Reviewed, UniProtKB/Swiss-Prot O43491 (E41L2_HUMAN)

Names and origin

Protein names

Recommended name:
    Band 4.1-like protein 2
Alternative name(s):
    Generally expressed protein 4.1
    4.1G

Gene names

Name:

EPB41L2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1005 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Subunit structure	The CTD domain interacts with FKBP2 By similarity. Interacts with FCGR1A.
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Tissue specificity	Widely expressed.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cortical actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular matrix Inferred from direct assay. Source: HPA extrinsic to membrane Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay. Source: HPA plasma membrane Ref.1 Inferred from direct assay. Source: HPA spectrin Ref.1 Traceable author statement. Source: ProtInc
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAQ	P27348	1	EBI-1052044,EBI-359854

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 1005	1004	Band 4.1-like protein 2		PRO_0000219397
Regions
	Domain	218 – 499	282	FERM
	Region	502 – 610	109	Hydrophilic
	Region	611 – 676	66	Spectrin--actin-binding
	Region	855 – 1005	151	Carboxyl-terminal (CTD)
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine Ref.5
	Modified residue	39	1	Phosphoserine Ref.6
	Modified residue	47	1	Phosphoserine Ref.10
	Modified residue	55	1	Phosphoserine Ref.11
	Modified residue	57	1	Phosphoserine Ref.11
	Modified residue	58	1	Phosphoserine Ref.9 Ref.11
	Modified residue	87	1	Phosphoserine Ref.9
	Modified residue	89	1	Phosphothreonine Ref.7
	Modified residue	499	1	Phosphoserine Ref.6
	Modified residue	550	1	Phosphoserine Ref.6 Ref.13
	Modified residue	598	1	Phosphoserine By similarity
	Modified residue	614	1	Phosphoserine Ref.11 Ref.13
	Modified residue	623	1	Phosphotyrosine Ref.8
	Modified residue	715	1	Phosphoserine Ref.13
	Modified residue	718	1	Phosphoserine Ref.13
	Modified residue	763	1	Phosphothreonine By similarity
	Modified residue	773	1	Phosphotyrosine Ref.9
Natural variations
	Natural variant	17	1	Q → H: dbSNP rs2297852.		VAR_020145

Sequences

	Sequence		Length	Mass (Da)
	O43491-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E86CB17488F6045F	FASTA	1,005	112,588
	10 20 30 40 50 60 MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP PAAESQSSLR 70 80 90 100 110 120 RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK EPTQAVVEEQ VLDKEEPLPE 130 140 150 160 170 180 EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV SKEEKPSVSK VEMQPTELVS KEREEKVKET 190 200 210 220 230 240 QEDKLEGGAA KRETKEVQTN ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG 250 260 270 280 290 300 QVLFDKVCEH LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD 310 320 330 340 350 360 PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP EEHGSIDLSE 370 380 390 400 410 420 FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR LSMYGVDLHH AKDSEGVDIK 430 440 450 460 470 480 LGVCANGLLI YKDRLRINRF AWPKILKISY KRSNFYIKVR PAELEQFEST IGFKLPNHRA 490 500 510 520 530 540 AKRLWKVCVE HHTFYRLVSP EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE 550 560 570 580 590 600 RTSSKRVSRS LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT 610 620 630 640 650 660 KAPHLQLIEG KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE LKRNFMESTP 670 680 690 700 710 720 EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP 730 740 750 760 770 780 GEIRKVEPVT QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE 790 800 810 820 830 840 PRPAAKVVER EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE 850 860 870 880 890 900 EAEEEPQKVN GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE 910 920 930 940 950 960 TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI 970 980 990 1000 TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family." Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N., Conboy J.G. Genomics 49:298-306(1998) [PubMed: 9598318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain and Heart.
[2]	Liu J., Zhou Y., Zhang B., Peng X., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W., Dozynkiewicz M., Norman J.C. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 161-171; 508-514 AND 875-886, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma and Pre-B cell.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-499 AND SER-550, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-623, MASS SPECTROMETRY.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-87 AND TYR-773, MASS SPECTROMETRY.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-57; SER-58 AND SER-614, MASS SPECTROMETRY.
[12]	"Protein 4.1G binds to a unique motif within the FcgammaRI cytoplasmic tail." Beekman J.M., Bakema J.E., van der Poel C.E., van der Linden J.A., van de Winkel J.G.J., Leusen J.H.W. Mol. Immunol. 45:2069-2075(2008) [PubMed: 18023480] [Abstract] Cited for: INTERACTION WITH FCGR1A.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-614; SER-715 AND SER-718, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF027299 mRNA. Translation: AAC16923.1. AY047584 mRNA. Translation: AAK95850.1. AL358943, AL590014 Genomic DNA. Translation: CAI20310.1. AL590014, AL358943 Genomic DNA. Translation: CAI40761.1. CH471051 Genomic DNA. Translation: EAW48062.1.
IPI	IPI00015973.
RefSeq	NP_001422.1.
UniGene	Hs.486470
3D structure databases
HSSP	HSSP built from PDB template 1GG3 based on UniProtKB P11171.
SMR	O43491. Positions 216-498.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:17034N.
IntAct	O43491. 3 interactions.
PTM databases
PhosphoSite	O43491.
Proteomic databases
PRIDE	O43491.
Genome annotation databases
Ensembl	ENSG00000079819. Homo sapiens. [Contig view]
GeneID	2037.
UCSC	uc003qch.1. human.
Organism-specific databases
GeneCards	GC06M131202.
H-InvDB	HIX0006217.
HGNC	HGNC:3379. EPB41L2.
HPA	HPA005730. HPA006642.
MIM	603237. gene.
PharmGKB	PA27812.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O43491.
HOVERGEN	O43491.
OMA	O43491. DATKEKP.
Gene expression databases
ArrayExpress	O43491.
Bgee	O43491.
CleanEx	HS_EPB41L2.
GermOnline	ENSG00000079819. Homo sapiens.
Family and domain databases
InterPro	IPR008379. Band_4.1_C. IPR019749. Band_41_domain. IPR019750. Band_41_sg. IPR000798. Ez/rad/moesin. 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_type. IPR007477. SAB. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF05902. 4_1_CTD. 1 hit. PF08736. FA. 1 hit. PF09380. FERM_C. 1 hit. PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. PF04382. SAB. 1 hit. [Graphical view]
PRINTS	PR00935. BAND41. PR00661. ERMFAMILY.
SMART	SM00295. B41. 1 hit. [Graphical view]
PROSITE	PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	8273.
SOURCE	Search...

Entry information

Entry name

E41L2_HUMAN

Accession

Primary (citable) accession number: O43491
Secondary accession number(s): Q5T4F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	June 1, 1998
Last modified:	July 7, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)