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Reviewed, UniProtKB/Swiss-Prot Q9Y2J2 (E41L3_HUMAN)

Last modified November 25, 2008. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Gene names
Name: EPB41L3
Synonyms: DAL1, KIAA0987
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Critical growth regulator in the pathogenesis of meningiomas.

Subunit structure

Interacts with CADM1.

Subcellular location

Cytoplasm › cytoskeletonBy similarity.

Tissue specificity

Expressed at high levels in brain, with lower levels in kidney, intestine, and testis.

Sequence similarities

Contains 1 FERM domain.

Sequence caution

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

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Ontologies

Keywords

   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcortical actin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell-cell junction Ref.4

Inferred from direct assay. Source: HGNC

cytoplasm

Inferred from electronic annotation. Source: InterPro

cytoskeleton

Inferred from electronic annotation. Source: InterPro

extrinsic to membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionactin binding

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Alternative products

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

Notes: 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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10871087Band 4.1-like protein 3
PRO_0000219399

Regions

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

Amino acid modifications

Modified residue881Phosphoserine By similarity
Modified residue4431Phosphoserine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4621Phosphothreonine By similarity
Modified residue4691Phosphothreonine By similarity
Modified residue7031Phosphothreonine By similarity
Modified residue7041Phosphothreonine By similarity
Modified residue7081Phosphoserine By similarity
Modified residue7621Phosphoserine
Modified residue7841Phosphothreonine By similarity
Modified residue7871Phosphoserine By similarity
Modified residue7881Phosphoserine By similarity
Modified residue9621Phosphoserine
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

Experimental info

Sequence conflict321Missing Ref.2
Sequence conflict4981R → Q Ref.2

Secondary structure

1 ...................................................... 1087
Helix Strand Turn

Details...

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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

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Isoform B [UniParc].

Checksum: C2070B01BF7F9422
Show »

86596,514
Isoform C [UniParc].

Checksum: 3881FB17E0DBAD00
Show »

61269,521

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References

« Hide 'large scale' references
[1]"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: 10231032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Brain.
[2]"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: 9892180] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
Tissue: Lung.
[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: 15489334] [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: 12234973] [Abstract]
Cited for: INTERACTION WITH CADM1.
[5]"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 SER-962, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, MASS SPECTROMETRY.
Tissue: Platelet.

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Cross-references

Sequence databases

AB023204 mRNA. Translation: BAA76831.1. Different initiation.
AF069072 mRNA. Translation: AAC79806.1. Frameshift.
BC006141 mRNA. Translation: AAH06141.1.
RefSeqNP_036439.2.
UniGeneHs.213394

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2HE7X-ray2.00A108-390[»]
3BINX-ray2.30A109-390[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:17035N.