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Q9Y2J2

- E41L3_HUMAN

UniProt

Q9Y2J2 - E41L3_HUMAN

Protein

Band 4.1-like protein 3

Gene

EPB41L3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (05 Dec 2001)
      Previous versions | rss
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    Functioni

    Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural constituent of cytoskeleton Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cortical actin cytoskeleton organization Source: InterPro
    3. cortical cytoskeleton organization Source: BHF-UCL
    4. cytoskeletal anchoring at plasma membrane Source: BHF-UCL
    5. myelin maintenance Source: BHF-UCL
    6. neuron projection morphogenesis Source: BHF-UCL
    7. paranodal junction assembly Source: BHF-UCL
    8. protein localization to juxtaparanode region of axon Source: BHF-UCL
    9. protein localization to paranode region of axon Source: BHF-UCL
    10. protein localization to plasma membrane Source: BHF-UCL
    11. regulation of cell shape Source: BHF-UCL

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Gene namesi
    Name:EPB41L3
    Synonyms:DAL1, KIAA0987
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:3380. EPB41L3.

    Subcellular locationi

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

    GO - Cellular componenti

    1. axolemma Source: Ensembl
    2. cell-cell junction Source: HGNC
    3. cytoplasm Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. extrinsic component of membrane Source: InterPro
    6. juxtaparanode region of axon Source: BHF-UCL
    7. paranode region of axon Source: BHF-UCL
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA27813.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10871087Band 4.1-like protein 3PRO_0000219399Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 10871086Band 4.1-like protein 3, N-terminally processedPRO_0000423194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in Band 4.1-like protein 3, N-terminally processed1 Publication
    Modified residuei88 – 881Phosphoserine1 Publication
    Modified residuei460 – 4601Phosphoserine1 Publication
    Modified residuei469 – 4691Phosphothreonine1 Publication
    Modified residuei962 – 9621Phosphoserine1 Publication
    Modified residuei1081 – 10811PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2J2.
    PaxDbiQ9Y2J2.
    PRIDEiQ9Y2J2.

    PTM databases

    PhosphoSiteiQ9Y2J2.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ9Y2J2.
    BgeeiQ9Y2J2.
    CleanExiHS_EPB41L3.
    GenevestigatoriQ9Y2J2.

    Organism-specific databases

    HPAiHPA028605.

    Interactioni

    Subunit structurei

    Interacts (via FERM domain) with CADM1. Interacts with PRMT3, PRMT5 and PRMT6.4 Publications

    Protein-protein interaction databases

    BioGridi116753. 26 interactions.
    DIPiDIP-17035N.
    IntActiQ9Y2J2. 82 interactions.
    MINTiMINT-1630957.
    STRINGi9606.ENSP00000341138.

    Structurei

    Secondary structure

    1
    1087
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi109 – 1157
    Beta strandi121 – 1277
    Helixi132 – 14211
    Helixi148 – 1503
    Beta strandi151 – 1566
    Beta strandi162 – 1643
    Helixi171 – 1744
    Beta strandi180 – 1889
    Helixi193 – 1953
    Helixi199 – 21416
    Helixi222 – 23716
    Turni242 – 2443
    Turni247 – 2526
    Beta strandi256 – 2583
    Helixi261 – 27313
    Turni274 – 2763
    Helixi279 – 29012
    Turni294 – 2974
    Beta strandi299 – 3046
    Beta strandi310 – 3156
    Beta strandi317 – 3248
    Beta strandi327 – 3337
    Helixi334 – 3363
    Beta strandi339 – 3435
    Beta strandi346 – 3516
    Turni354 – 3574
    Beta strandi361 – 3666
    Helixi370 – 38819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HE7X-ray2.00A108-390[»]
    3BINX-ray2.30A109-390[»]
    ProteinModelPortaliQ9Y2J2.
    SMRiQ9Y2J2. Positions 108-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2J2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini110 – 391282FERMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni394 – 513120HydrophilicAdd
    BLAST
    Regioni514 – 860347Spectrin--actin-bindingSequence AnalysisAdd
    BLAST
    Regioni861 – 1083223C-terminal (CTD)Add
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG242913.
    HOGENOMiHOG000228840.
    HOVERGENiHBG007777.
    InParanoidiQ9Y2J2.
    KOiK06107.
    OMAiSTDTAIT.
    OrthoDBiEOG7Z69BP.
    PhylomeDBiQ9Y2J2.
    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.
    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.
    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]
    PIRSFiPIRSF002304. Membrane_skeletal_4_1. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9Y2J2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA     50
    AAAHSTPVRR EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP 100
    LKIVKKPKSM QCKVILLDGS EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY 150
    FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW HFSFNVKFYP PDPAQLSEDI 200
    TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY DPDECGSDYI 250
    SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL 300
    HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK 350
    IRPGEFEQFE STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL 400
    TLGSKFRYSG RTQAQTRRAS ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT 450
    GQYATTKGIS QTNLITTVTP EKKAEEERDE EEDKRRKGEE VTPISAIRHE 500
    GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP GYEPSRAEHL 550
    PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL 600
    DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV 650
    PYALTLSFPL ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD 700
    GETTATESDQ EEDAELKAQE LEKTQDDLMK HQTNISELKR TFLETSTDTA 750
    VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV PEETKQSSGE KLMDGSEIFS 800
    LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT VHHLPLSTEK 850
    VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG 900
    AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST 950
    VKTETISFGS VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP 1000
    GVLMSAQTIT SETTSTTTTT HITKTVKGGI SETRIEKRIV ITGDADIDHD 1050
    QALAQAIKEA KEQHPDMSVT KVVVHKETEI TPEDGED 1087
    Length:1,087
    Mass (Da):120,678
    Last modified:December 5, 2001 - v2
    Checksum:i0A33CA4A43F12620
    GO
    Isoform 2 (identifier: Q9Y2J2-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:865
    Mass (Da):96,514
    Checksum:iC2070B01BF7F9422
    GO
    Isoform 3 (identifier: Q9Y2J2-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:612
    Mass (Da):69,521
    Checksum:i3881FB17E0DBAD00
    GO
    Isoform 4 (identifier: Q9Y2J2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-446: G → GASVNENHEIYMKDSMSAA
         503-689: Missing.
         1052-1052: A → E
         1053-1087: Missing.

    Show »
    Length:883
    Mass (Da):98,461
    Checksum:iE25FB2E14F6745D3
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121K → E in BAH12571. (PubMed:14702039)Curated
    Sequence conflicti32 – 321Missing in AAC79806. (PubMed:9892180)Curated
    Sequence conflicti498 – 4981R → Q in AAC79806. (PubMed:9892180)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti555 – 5551A → T.
    Corresponds to variant rs9966357 [ dbSNP | Ensembl ].
    VAR_048353
    Natural varianti575 – 5751Y → C.
    Corresponds to variant rs8082898 [ dbSNP | Ensembl ].
    VAR_048354
    Natural varianti859 – 8591E → Q.
    Corresponds to variant rs8096452 [ dbSNP | Ensembl ].
    VAR_048355

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei446 – 4461G → GASVNENHEIYMKDSMSAA in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_000482
    Alternative sequencei503 – 689187Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_000483Add
    BLAST
    Alternative sequencei708 – 71912Missing in isoform 2 and isoform 3. 2 PublicationsVSP_000484Add
    BLAST
    Alternative sequencei784 – 82441Missing in isoform 2 and isoform 3. 2 PublicationsVSP_000485Add
    BLAST
    Alternative sequencei835 – 1087253Missing in isoform 3. 1 PublicationVSP_000486Add
    BLAST
    Alternative sequencei1052 – 10521A → E in isoform 4. 1 PublicationVSP_054819
    Alternative sequencei1053 – 108735Missing in isoform 4. 1 PublicationVSP_054820Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069072 mRNA. Translation: AAC79806.1. Frameshift.
    AB023204 mRNA. Translation: BAA76831.1. Different initiation.
    AK297406 mRNA. Translation: BAH12571.1.
    AP001032 Genomic DNA. No translation available.
    AP005059 Genomic DNA. No translation available.
    AP005671 Genomic DNA. No translation available.
    BC006141 mRNA. Translation: AAH06141.1.
    CCDSiCCDS11838.1. [Q9Y2J2-1]
    CCDS62381.1. [Q9Y2J2-2]
    CCDS62382.1. [Q9Y2J2-4]
    RefSeqiNP_001268462.1. NM_001281533.1. [Q9Y2J2-4]
    NP_001268463.1. NM_001281534.1. [Q9Y2J2-2]
    NP_001268464.1. NM_001281535.1.
    NP_036439.2. NM_012307.3. [Q9Y2J2-1]
    UniGeneiHs.213394.

    Genome annotation databases

    EnsembliENST00000341928; ENSP00000343158; ENSG00000082397. [Q9Y2J2-1]
    ENST00000342933; ENSP00000341138; ENSG00000082397. [Q9Y2J2-1]
    ENST00000400111; ENSP00000382981; ENSG00000082397. [Q9Y2J2-2]
    ENST00000540638; ENSP00000442091; ENSG00000082397. [Q9Y2J2-2]
    ENST00000544123; ENSP00000441174; ENSG00000082397. [Q9Y2J2-4]
    GeneIDi23136.
    KEGGihsa:23136.
    UCSCiuc002kmt.1. human. [Q9Y2J2-1]
    uc002kmu.1. human. [Q9Y2J2-2]
    uc010dks.1. human. [Q9Y2J2-3]

    Polymorphism databases

    DMDMi17433099.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF069072 mRNA. Translation: AAC79806.1 . Frameshift.
    AB023204 mRNA. Translation: BAA76831.1 . Different initiation.
    AK297406 mRNA. Translation: BAH12571.1 .
    AP001032 Genomic DNA. No translation available.
    AP005059 Genomic DNA. No translation available.
    AP005671 Genomic DNA. No translation available.
    BC006141 mRNA. Translation: AAH06141.1 .
    CCDSi CCDS11838.1. [Q9Y2J2-1 ]
    CCDS62381.1. [Q9Y2J2-2 ]
    CCDS62382.1. [Q9Y2J2-4 ]
    RefSeqi NP_001268462.1. NM_001281533.1. [Q9Y2J2-4 ]
    NP_001268463.1. NM_001281534.1. [Q9Y2J2-2 ]
    NP_001268464.1. NM_001281535.1.
    NP_036439.2. NM_012307.3. [Q9Y2J2-1 ]
    UniGenei Hs.213394.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HE7 X-ray 2.00 A 108-390 [» ]
    3BIN X-ray 2.30 A 109-390 [» ]
    ProteinModelPortali Q9Y2J2.
    SMRi Q9Y2J2. Positions 108-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116753. 26 interactions.
    DIPi DIP-17035N.
    IntActi Q9Y2J2. 82 interactions.
    MINTi MINT-1630957.
    STRINGi 9606.ENSP00000341138.

    PTM databases

    PhosphoSitei Q9Y2J2.

    Polymorphism databases

    DMDMi 17433099.

    Proteomic databases

    MaxQBi Q9Y2J2.
    PaxDbi Q9Y2J2.
    PRIDEi Q9Y2J2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341928 ; ENSP00000343158 ; ENSG00000082397 . [Q9Y2J2-1 ]
    ENST00000342933 ; ENSP00000341138 ; ENSG00000082397 . [Q9Y2J2-1 ]
    ENST00000400111 ; ENSP00000382981 ; ENSG00000082397 . [Q9Y2J2-2 ]
    ENST00000540638 ; ENSP00000442091 ; ENSG00000082397 . [Q9Y2J2-2 ]
    ENST00000544123 ; ENSP00000441174 ; ENSG00000082397 . [Q9Y2J2-4 ]
    GeneIDi 23136.
    KEGGi hsa:23136.
    UCSCi uc002kmt.1. human. [Q9Y2J2-1 ]
    uc002kmu.1. human. [Q9Y2J2-2 ]
    uc010dks.1. human. [Q9Y2J2-3 ]

    Organism-specific databases

    CTDi 23136.
    GeneCardsi GC18M005382.
    HGNCi HGNC:3380. EPB41L3.
    HPAi HPA028605.
    MIMi 605331. gene.
    neXtProti NX_Q9Y2J2.
    PharmGKBi PA27813.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242913.
    HOGENOMi HOG000228840.
    HOVERGENi HBG007777.
    InParanoidi Q9Y2J2.
    KOi K06107.
    OMAi STDTAIT.
    OrthoDBi EOG7Z69BP.
    PhylomeDBi Q9Y2J2.
    TreeFami TF351626.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2J2.
    GeneWikii EPB41L3.
    GenomeRNAii 23136.
    NextBioi 35479474.
    PROi Q9Y2J2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2J2.
    Bgeei Q9Y2J2.
    CleanExi HS_EPB41L3.
    Genevestigatori Q9Y2J2.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami 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 ]
    PIRSFi PIRSF002304. Membrane_skeletal_4_1. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 3), 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 1).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2).
      Tissue: Lung.
    6. "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.
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "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].
    12. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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].
    15. "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.

    Entry informationi

    Entry nameiE41L3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2J2
    Secondary accession number(s): B7Z4I5
    , F5GX05, O95713, Q9BRP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: December 5, 2001
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3