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Q9Y2J2 (E41L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Band 4.1-like protein 3
Alternative name(s):
4.1B
Differentially expressed in adenocarcinoma of the lung protein 1
Short name=DAL-1

Cleaved into the following chain:

  1. Band 4.1-like protein 3, N-terminally processed
Gene names
Name:EPB41L3
Synonyms:DAL1, KIAA0987
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5. Ref.1 Ref.5 Ref.6 Ref.7

Subunit structure

Interacts (via FERM domain) with CADM1. Interacts with PRMT3, PRMT5 and PRMT6. Ref.4 Ref.5 Ref.6 Ref.13

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Note: Detected in the cytoplasm of actively dividing cells. Ref.1

Tissue specificity

Expressed at high levels in brain, with lower levels in kidney, intestine, and testis. Detected in lung. Ref.1

Sequence similarities

Contains 1 FERM domain.

Sequence caution

The sequence AAC79806.1 differs from that shown. Reason: Frameshift at positions 29 and 59.

The sequence BAA76831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

cortical cytoskeleton organization

Traceable author statement PubMed 21966409. Source: BHF-UCL

cytoskeletal anchoring at plasma membrane

Traceable author statement PubMed 21966409. Source: BHF-UCL

myelin maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

paranodal junction assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to juxtaparanode region of axon

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to paranode region of axon

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cell shape

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentaxolemma

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay Ref.4. Source: HGNC

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of membrane

Inferred from electronic annotation. Source: InterPro

juxtaparanode region of axon

Inferred from sequence or structural similarity. Source: BHF-UCL

paranode region of axon

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionstructural constituent of cytoskeleton

Traceable author statement PubMed 21966409. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform A (identifier: Q9Y2J2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9Y2J2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     446-446: G → GASVNENHEIYMKDSMSAA
     503-689: Missing.
     708-719: Missing.
     784-824: Missing.
Isoform C (identifier: Q9Y2J2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     446-446: G → GASVNENHEIYMKDSMSAA
     503-689: Missing.
     708-719: Missing.
     784-824: Missing.
     835-1087: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10871087Band 4.1-like protein 3
PRO_0000219399
Initiator methionine11Removed; alternate Ref.9
Chain2 – 10871086Band 4.1-like protein 3, N-terminally processed
PRO_0000423194

Regions

Domain110 – 391282FERM
Region394 – 513120Hydrophilic
Region514 – 860347Spectrin--actin-binding Potential
Region861 – 1083223C-terminal (CTD)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue21N-acetylthreonine; in Band 4.1-like protein 3, N-terminally processed Ref.9
Modified residue881Phosphoserine Ref.12
Modified residue4601Phosphoserine Ref.12
Modified residue4691Phosphothreonine Ref.12
Modified residue9621Phosphoserine Ref.8
Modified residue10811Phosphothreonine By similarity

Natural variations

Alternative sequence4461G → GASVNENHEIYMKDSMSAA in isoform B and isoform C.
VSP_000482
Alternative sequence503 – 689187Missing in isoform B and isoform C.
VSP_000483
Alternative sequence708 – 71912Missing in isoform B and isoform C.
VSP_000484
Alternative sequence784 – 82441Missing in isoform B and isoform C.
VSP_000485
Alternative sequence835 – 1087253Missing in isoform C.
VSP_000486
Natural variant5551A → T.
Corresponds to variant rs9966357 [ dbSNP | Ensembl ].
VAR_048353
Natural variant5751Y → C.
Corresponds to variant rs8082898 [ dbSNP | Ensembl ].
VAR_048354
Natural variant8591E → Q.
Corresponds to variant rs8096452 [ dbSNP | Ensembl ].
VAR_048355

Experimental info

Sequence conflict321Missing in AAC79806. Ref.1
Sequence conflict4981R → Q in AAC79806. Ref.1

Secondary structure

...................................................... 1087
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 0A33CA4A43F12620

FASTA1,087120,678
        10         20         30         40         50         60 
MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR 

        70         80         90        100        110        120 
EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS 

       130        140        150        160        170        180 
EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW 

       190        200        210        220        230        240 
HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY 

       250        260        270        280        290        300 
DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL 

       310        320        330        340        350        360 
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE 

       370        380        390        400        410        420 
STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS 

       430        440        450        460        470        480 
ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE 

       490        500        510        520        530        540 
EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP 

       550        560        570        580        590        600 
GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL 

       610        620        630        640        650        660 
DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL 

       670        680        690        700        710        720 
ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE 

       730        740        750        760        770        780 
LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV 

       790        800        810        820        830        840 
PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT 

       850        860        870        880        890        900 
VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG 

       910        920        930        940        950        960 
AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS 

       970        980        990       1000       1010       1020 
VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT 

      1030       1040       1050       1060       1070       1080 
HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI 


TPEDGED 

« Hide

Isoform B [UniParc].

Checksum: C2070B01BF7F9422
Show »

FASTA86596,514
Isoform C [UniParc].

Checksum: 3881FB17E0DBAD00
Show »

FASTA61269,521

References

« Hide 'large scale' references
[1]"A novel member of the NF2/ERM/4.1 superfamily with growth suppressing properties in lung cancer."
Tran Y.K., Boegler O., Gorse K.M., Wieland I., Green M.R., Newsham I.F.
Cancer Res. 59:35-43(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Lung.
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Lung.
[4]"Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer."
Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., Shibuya M., Murakami Y.
Cancer Res. 62:5129-5133(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CADM1.
[5]"DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo."
Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.
Oncogene 23:7761-7771(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRMT3; PRMT5 AND PRMT6.
[6]"The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner."
Jiang W., Roemer M.E., Newsham I.F.
Biochem. Biophys. Res. Commun. 329:522-530(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRMT5.
[7]"The tumor suppressor DAL-1/4.1B and protein methylation cooperate in inducing apoptosis in MCF-7 breast cancer cells."
Jiang W., Newsham I.F.
Mol. Cancer 5:4-4(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-460 AND THR-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)."
Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C., Obrink B., Hallberg B.M.
J. Biol. Chem. 286:4511-4516(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-390 IN COMPLEX WITH CADM1, INTERACTION WITH CADM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069072 mRNA. Translation: AAC79806.1. Frameshift.
AB023204 mRNA. Translation: BAA76831.1. Different initiation.
BC006141 mRNA. Translation: AAH06141.1.
RefSeqNP_001268462.1. NM_001281533.1.
NP_001268463.1. NM_001281534.1.
NP_001268464.1. NM_001281535.1.
NP_036439.2. NM_012307.3.
UniGeneHs.213394.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE7X-ray2.00A108-390[»]
3BINX-ray2.30A109-390[»]
ProteinModelPortalQ9Y2J2.
SMRQ9Y2J2. Positions 107-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116753. 25 interactions.
DIPDIP-17035N.
IntActQ9Y2J2. 82 interactions.
MINTMINT-1630957.
STRING9606.ENSP00000341138.

PTM databases

PhosphoSiteQ9Y2J2.

Polymorphism databases

DMDM17433099.

Proteomic databases

PaxDbQ9Y2J2.
PRIDEQ9Y2J2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341928; ENSP00000343158; ENSG00000082397. [Q9Y2J2-1]
ENST00000342933; ENSP00000341138; ENSG00000082397. [Q9Y2J2-1]
ENST00000400111; ENSP00000382981; ENSG00000082397. [Q9Y2J2-2]
ENST00000540638; ENSP00000442091; ENSG00000082397. [Q9Y2J2-2]
GeneID23136.
KEGGhsa:23136.
UCSCuc002kmt.1. human. [Q9Y2J2-1]
uc002kmu.1. human. [Q9Y2J2-2]
uc010dks.1. human. [Q9Y2J2-3]

Organism-specific databases

CTD23136.
GeneCardsGC18M005382.
HGNCHGNC:3380. EPB41L3.
HPAHPA028605.
MIM605331. gene.
neXtProtNX_Q9Y2J2.
PharmGKBPA27813.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242913.
HOGENOMHOG000228840.
HOVERGENHBG007777.
InParanoidQ9Y2J2.
KOK06107.
OMASTDTAIT.
OrthoDBEOG7Z69BP.
PhylomeDBQ9Y2J2.
TreeFamTF351626.

Gene expression databases

ArrayExpressQ9Y2J2.
BgeeQ9Y2J2.
CleanExHS_EPB41L3.
GenevestigatorQ9Y2J2.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR008379. 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.
[Graphical view]
PfamPF05902. 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]
PIRSFPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y2J2.
GeneWikiEPB41L3.
GenomeRNAi23136.
NextBio44399.
PROQ9Y2J2.
SOURCESearch...

Entry information

Entry nameE41L3_HUMAN
AccessionPrimary (citable) accession number: Q9Y2J2
Secondary accession number(s): O95713, Q9BRP5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM