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Protein

Band 4.1-like protein 2

Gene

Epb41l2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • actin binding Source: MGI
  • PH domain binding Source: MGI
  • spectrin binding Source: MGI
  • structural molecule activity Source: InterPro

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • cortical actin cytoskeleton organization Source: InterPro
  • regulation of cell shape Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Band 4.1-like protein 2
Alternative name(s):
Generally expressed protein 4.1
Short name:
4.1G
Gene namesi
Name:Epb41l2
Synonyms:Epb4.1l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:103009. Epb41l2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 988987Band 4.1-like protein 2PRO_0000219398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei7 – 71PhosphoserineBy similarity
Modified residuei38 – 381PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineBy similarity
Modified residuei395 – 3951PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineBy similarity
Modified residuei543 – 5431PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei582 – 5821PhosphoserineCombined sources
Modified residuei606 – 6061PhosphotyrosineCombined sources
Modified residuei610 – 6101PhosphoserineCombined sources
Modified residuei630 – 6301PhosphoserineCombined sources
Modified residuei698 – 6981PhosphoserineCombined sources
Modified residuei745 – 7451PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO70318.
MaxQBiO70318.
PaxDbiO70318.
PeptideAtlasiO70318.
PRIDEiO70318.

PTM databases

iPTMnetiO70318.
PhosphoSiteiO70318.
SwissPalmiO70318.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

CleanExiMM_EPB4.1L2.
GenevisibleiO70318. MM.

Interactioni

Subunit structurei

The CTD domain interacts with FKBP2. Interacts with FCGR1A (By similarity). Interacts with TRPC4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Mpp6Q9JLB03EBI-643339,EBI-771456

GO - Molecular functioni

  • actin binding Source: MGI
  • PH domain binding Source: MGI
  • spectrin binding Source: MGI

Protein-protein interaction databases

BioGridi199460. 3 interactions.
IntActiO70318. 5 interactions.
MINTiMINT-4093830.
STRINGi10090.ENSMUSP00000055122.

Structurei

3D structure databases

ProteinModelPortaliO70318.
SMRiO70318. Positions 214-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini211 – 492282FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 651157HydrophilicAdd
BLAST
Regioni652 – 837186Spectrin--actin-bindingAdd
BLAST
Regioni838 – 988151C-terminal (CTD)Add
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3527. Eukaryota.
ENOG410Y7NQ. LUCA.
GeneTreeiENSGT00760000118823.
HOGENOMiHOG000228841.
HOVERGENiHBG007777.
InParanoidiO70318.
KOiK06107.
OMAiQAEVGKD.
OrthoDBiEOG7Z69BP.
TreeFamiTF351626.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
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_dom-like.
IPR007477. SAB_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF05902. 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]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP
60 70 80 90 100
PVERQSTPRL RKRGKDPSEN RGISRFIPPW LKKQRSYNLV VAKDGGDKKE
110 120 130 140 150
PTQADVEDQI LGKEESLPEE ESRAKGDAEE MAQRKHLEVQ VEVREAKPAL
160 170 180 190 200
KSSVETQPAE EVRKDKEETI QDTQEEKLEG GAAKRETKEV QTSELKAEVA
210 220 230 240 250
SQKATKKTKT VLAKVTLLDG TEYSCDLEKR AKGQVLFDRV CEHLNLLEKD
260 270 280 290 300
YFGLLFQDHP EQKNWLDPAK EIKRQLKNLP WLFTFNVKFY PPDPSQLTED
310 320 330 340 350
ITRYFLCLQL RQDIASGRLP CSFVTHALLG SYTLQAEHGD YDPEEYDSID
360 370 380 390 400
LGDFQFAPAH TKELEEKVSE LHKTHRGLSP AQADSQFLEN AKRLSMYGVD
410 420 430 440 450
LHHAKDSEGV DIKLGVCANG LLIYKDRLRI NRFAWPKILK ISYKRSNFYI
460 470 480 490 500
KVRPAELEQF ESTIGFKLPN HRAAKRLWKV CVEHHTFYRL VSPEQPPKTK
510 520 530 540 550
FLTLGSKFRY SGRTQAQTRE ASTLIDRPAP QFERASSKRV SRSLDGAPIG
560 570 580 590 600
VVDQSPPGEG SVPGPGVISY TTIQDGRRDS KSPTKATPLP AEGKKNTLRV
610 620 630 640 650
DGDNIYVRHS NLMLEDLDKA QEAILKHQAS ISELKRNFMA STPEPRPSEW
660 670 680 690 700
EKRRVTPLPF QPQASSHETL NVVEEKKRAE VGKDESVITE EMNGKEMSPG
710 720 730 740 750
HGPGETRKVE PVAHKDSTSL SSESSSSSSE SEEDVGEYQP HHRVTEGTIR
760 770 780 790 800
EEQEECDEEL EEEPGQGAKV VEREAAVPDA VPDRQAGASV LPVETEAQEH
810 820 830 840 850
VVAQKLPGEK GAHGGTAEQD PREEAEEDPH RVNGEVPHLD LDGLPEIICC
860 870 880 890 900
SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG
910 920 930 940 950
DSGVLLTAQT ITSESASTTT TTHITKTVKG GISETRIEKR IVITGDAALD
960 970 980
HDQALAQAIR EAREQHPDMS VTRVVVHKET ELAEEGEE
Length:988
Mass (Da):109,940
Last modified:October 3, 2012 - v2
Checksum:iD3DA78BFA14E3FBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti660 – 6601F → L in AAC40083 (PubMed:9531554).Curated
Sequence conflicti680 – 6801E → G in AAC40083 (PubMed:9531554).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044312 mRNA. Translation: AAC40083.1.
AC153547 Genomic DNA. No translation available.
AC153550 Genomic DNA. No translation available.
AC156274 Genomic DNA. No translation available.
CH466540 Genomic DNA. Translation: EDL04798.1.
CCDSiCCDS23754.1.
RefSeqiNP_001186194.1. NM_001199265.1.
NP_038539.2. NM_013511.3.
UniGeneiMm.306026.

Genome annotation databases

EnsembliENSMUST00000053748; ENSMUSP00000055122; ENSMUSG00000019978.
ENSMUST00000092645; ENSMUSP00000090314; ENSMUSG00000019978.
GeneIDi13822.
KEGGimmu:13822.
UCSCiuc007erk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044312 mRNA. Translation: AAC40083.1.
AC153547 Genomic DNA. No translation available.
AC153550 Genomic DNA. No translation available.
AC156274 Genomic DNA. No translation available.
CH466540 Genomic DNA. Translation: EDL04798.1.
CCDSiCCDS23754.1.
RefSeqiNP_001186194.1. NM_001199265.1.
NP_038539.2. NM_013511.3.
UniGeneiMm.306026.

3D structure databases

ProteinModelPortaliO70318.
SMRiO70318. Positions 214-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199460. 3 interactions.
IntActiO70318. 5 interactions.
MINTiMINT-4093830.
STRINGi10090.ENSMUSP00000055122.

PTM databases

iPTMnetiO70318.
PhosphoSiteiO70318.
SwissPalmiO70318.

Proteomic databases

EPDiO70318.
MaxQBiO70318.
PaxDbiO70318.
PeptideAtlasiO70318.
PRIDEiO70318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053748; ENSMUSP00000055122; ENSMUSG00000019978.
ENSMUST00000092645; ENSMUSP00000090314; ENSMUSG00000019978.
GeneIDi13822.
KEGGimmu:13822.
UCSCiuc007erk.2. mouse.

Organism-specific databases

CTDi2037.
MGIiMGI:103009. Epb41l2.

Phylogenomic databases

eggNOGiKOG3527. Eukaryota.
ENOG410Y7NQ. LUCA.
GeneTreeiENSGT00760000118823.
HOGENOMiHOG000228841.
HOVERGENiHBG007777.
InParanoidiO70318.
KOiK06107.
OMAiQAEVGKD.
OrthoDBiEOG7Z69BP.
TreeFamiTF351626.

Miscellaneous databases

PROiO70318.
SOURCEiSearch...

Gene expression databases

CleanExiMM_EPB4.1L2.
GenevisibleiO70318. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
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_dom-like.
IPR007477. SAB_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF05902. 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]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1."
    Walensky L.D., Gascard P., Fields M.E., Blackshaw S., Conboy J.G., Mohandas N., Snyder S.H.
    J. Cell Biol. 141:143-153(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FKBP2.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-86; SER-201; SER-582 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND TYR-606, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-201; SER-395; SER-543; SER-555; SER-561; SER-582; SER-610; SER-630 AND THR-745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiE41L2_MOUSE
AccessioniPrimary (citable) accession number: O70318
Secondary accession number(s): G3X9B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 3, 2012
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.