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Q9Y2J2

- E41L3_HUMAN

UniProt

Q9Y2J2 - E41L3_HUMAN

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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

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. 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
Complete GO annotation...

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-KW
  4. cytoskeleton Source: UniProtKB-KW
  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
Complete GO annotation...

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

BgeeiQ9Y2J2.
CleanExiHS_EPB41L3.
ExpressionAtlasiQ9Y2J2. baseline and differential.
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. 27 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.
GeneTreeiENSGT00760000118823.
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

        10         20         30         40         50
MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA
60 70 80 90 100
AAAHSTPVRR EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP
110 120 130 140 150
LKIVKKPKSM QCKVILLDGS EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY
160 170 180 190 200
FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW HFSFNVKFYP PDPAQLSEDI
210 220 230 240 250
TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY DPDECGSDYI
260 270 280 290 300
SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL
310 320 330 340 350
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK
360 370 380 390 400
IRPGEFEQFE STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL
410 420 430 440 450
TLGSKFRYSG RTQAQTRRAS ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT
460 470 480 490 500
GQYATTKGIS QTNLITTVTP EKKAEEERDE EEDKRRKGEE VTPISAIRHE
510 520 530 540 550
GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP GYEPSRAEHL
560 570 580 590 600
PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL
610 620 630 640 650
DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV
660 670 680 690 700
PYALTLSFPL ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD
710 720 730 740 750
GETTATESDQ EEDAELKAQE LEKTQDDLMK HQTNISELKR TFLETSTDTA
760 770 780 790 800
VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV PEETKQSSGE KLMDGSEIFS
810 820 830 840 850
LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT VHHLPLSTEK
860 870 880 890 900
VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG
910 920 930 940 950
AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST
960 970 980 990 1000
VKTETISFGS VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP
1010 1020 1030 1040 1050
GVLMSAQTIT SETTSTTTTT HITKTVKGGI SETRIEKRIV ITGDADIDHD
1060 1070 1080
QALAQAIKEA KEQHPDMSVT KVVVHKETEI TPEDGED
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]
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. 27 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 ]
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.
GeneTreei ENSGT00760000118823.
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

Bgeei Q9Y2J2.
CleanExi HS_EPB41L3.
ExpressionAtlasi Q9Y2J2. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
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
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