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Q9NYJ7

- DLL3_HUMAN

UniProt

Q9NYJ7 - DLL3_HUMAN

Protein

Delta-like protein 3

Gene

DLL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm By similarity.By similarity

    GO - Molecular functioni

    1. Notch binding Source: UniProtKB

    GO - Biological processi

    1. compartment pattern specification Source: Ensembl
    2. negative regulation of neurogenesis Source: Ensembl
    3. Notch signaling pathway Source: UniProtKB-KW
    4. paraxial mesoderm development Source: Ensembl
    5. skeletal system development Source: UniProtKB
    6. somitogenesis Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Notch signaling pathway

    Enzyme and pathway databases

    SignaLinkiQ9NYJ7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-like protein 3
    Alternative name(s):
    Drosophila Delta homolog 3
    Short name:
    Delta3
    Gene namesi
    Name:DLL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2909. DLL3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Spondylocostal dysostosis 1, autosomal recessive (SCDO1) [MIM:277300]: A condition of variable severity associated with vertebral and rib segmentation defects. The main skeletal malformations include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and other rib malformations. Deformity of the chest and spine (severe scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the malformation and leads to a dwarf-like appearance. As the thorax is small, infants frequently have respiratory insufficiency and repeated respiratory infections resulting in life-threatening complications in the first year of life.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti385 – 3851G → D in SCDO1. 1 Publication
    VAR_009952

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi277300. phenotype.
    Orphaneti2311. Autosomal recessive spondylocostal dysostosis.
    PharmGKBiPA27365.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 618592Delta-like protein 3PRO_0000007509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi220 ↔ 231PROSITE-ProRule annotation
    Disulfide bondi224 ↔ 237PROSITE-ProRule annotation
    Disulfide bondi239 ↔ 248PROSITE-ProRule annotation
    Disulfide bondi278 ↔ 289PROSITE-ProRule annotation
    Disulfide bondi283 ↔ 298PROSITE-ProRule annotation
    Disulfide bondi300 ↔ 309PROSITE-ProRule annotation
    Disulfide bondi316 ↔ 327PROSITE-ProRule annotation
    Disulfide bondi321 ↔ 339PROSITE-ProRule annotation
    Disulfide bondi341 ↔ 350PROSITE-ProRule annotation
    Disulfide bondi357 ↔ 368PROSITE-ProRule annotation
    Disulfide bondi362 ↔ 377PROSITE-ProRule annotation
    Disulfide bondi379 ↔ 388PROSITE-ProRule annotation
    Disulfide bondi395 ↔ 406PROSITE-ProRule annotation
    Disulfide bondi400 ↔ 415PROSITE-ProRule annotation
    Disulfide bondi417 ↔ 426PROSITE-ProRule annotation
    Disulfide bondi433 ↔ 444PROSITE-ProRule annotation
    Disulfide bondi438 ↔ 453PROSITE-ProRule annotation
    Disulfide bondi455 ↔ 464PROSITE-ProRule annotation

    Post-translational modificationi

    Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation.By similarity

    Keywords - PTMi

    Disulfide bond, Ubl conjugation

    Proteomic databases

    PaxDbiQ9NYJ7.
    PRIDEiQ9NYJ7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NYJ7.
    BgeeiQ9NYJ7.
    CleanExiHS_DLL3.
    GenevestigatoriQ9NYJ7.

    Organism-specific databases

    HPAiHPA056533.

    Interactioni

    Subunit structurei

    Can bind and activate Notch-1 or another Notch receptor.By similarity

    Protein-protein interaction databases

    BioGridi115922. 1 interaction.
    STRINGi9606.ENSP00000205143.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYJ7.
    SMRiQ9NYJ7. Positions 27-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 492466ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini514 – 618105CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei493 – 51321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini176 – 21540DSLAdd
    BLAST
    Domaini216 – 24934EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 31037EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini312 – 35140EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini353 – 38937EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini391 – 42737EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini429 – 46537EGF-like 6PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The DSL domain is required for binding to the Notch receptor.

    Sequence similaritiesi

    Contains 1 DSL domain.Curated
    Contains 6 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG244272.
    HOGENOMiHOG000267024.
    HOVERGENiHBG007139.
    InParanoidiQ9NYJ7.
    KOiK06051.
    OMAiDECRCLE.
    OrthoDBiEOG7P8P7B.
    PhylomeDBiQ9NYJ7.
    TreeFamiTF351835.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011651. Notch_ligand_N.
    [Graphical view]
    PfamiPF00008. EGF. 3 hits.
    PF12661. hEGF. 2 hits.
    PF07657. MNNL. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 6 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    PROSITEiPS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 6 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NYJ7-1) [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

    MVSPRMSGLL SQTVILALIF LPQTRPAGVF ELQIHSFGPG PGPGAPRSPC    50
    SARLPCRLFF RVCLKPGLSE EAAESPCALG AALSARGPVY TEQPGAPAPD 100
    LPLPDGLLQV PFRDAWPGTF SFIIETWREE LGDQIGGPAW SLLARVAGRR 150
    RLAAGGPWAR DIQRAGAWEL RFSYRARCEP PAVGTACTRL CRPRSAPSRC 200
    GPGLRPCAPL EDECEAPLVC RAGCSPEHGF CEQPGECRCL EGWTGPLCTV 250
    PVSTSSCLSP RGPSSATTGC LVPGPGPCDG NPCANGGSCS ETPRSFECTC 300
    PRGFYGLRCE VSGVTCADGP CFNGGLCVGG ADPDSAYICH CPPGFQGSNC 350
    EKRVDRCSLQ PCRNGGLCLD LGHALRCRCR AGFAGPRCEH DLDDCAGRAC 400
    ANGGTCVEGG GAHRCSCALG FGGRDCRERA DPCAARPCAH GGRCYAHFSG 450
    LVCACAPGYM GARCEFPVHP DGASALPAAP PGLRPGDPQR YLLPPALGLL 500
    VAAGVAGAAL LLVHVRRRGH SQDAGSRLLA GTPEPSVHAL PDALNNLRTQ 550
    EGSGDGPSSS VDWNRPEDVD PQGIYVISAP SIYAREVATP LFPPLHTGRA 600
    GQRQHLLFPY PSSILSVK 618
    Length:618
    Mass (Da):64,618
    Last modified:October 1, 2000 - v1
    Checksum:i58A9BC0A7DEAD1A0
    GO
    Isoform 2 (identifier: Q9NYJ7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         587-618: VATPLFPPLHTGRAGQRQHLLFPYPSSILSVK → A

    Note: No experimental confirmation available.

    Show »
    Length:587
    Mass (Da):61,178
    Checksum:i66503288EABBFECE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti318 – 3181D → N in BAC11535. (PubMed:16303743)Curated
    Sequence conflicti435 – 4351A → V in BAC11535. (PubMed:16303743)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151A → T.1 Publication
    VAR_046782
    Natural varianti142 – 1421L → Q.1 Publication
    Corresponds to variant rs55741253 [ dbSNP | Ensembl ].
    VAR_046783
    Natural varianti172 – 1721F → C.2 Publications
    Corresponds to variant rs8107127 [ dbSNP | Ensembl ].
    VAR_046784
    Natural varianti218 – 2181L → P.2 Publications
    Corresponds to variant rs1110627 [ dbSNP | Ensembl ].
    VAR_016776
    Natural varianti385 – 3851G → D in SCDO1. 1 Publication
    VAR_009952

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei587 – 61832VATPL…ILSVK → A in isoform 2. 1 PublicationVSP_045249Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241373
    , AF241367, AF241368, AF241369, AF241370, AF241371, AF241372 Genomic DNA. Translation: AAF62542.1.
    AK075302 mRNA. Translation: BAC11535.1.
    AC011500 Genomic DNA. No translation available.
    BC000218 mRNA. Translation: AAH00218.1.
    CCDSiCCDS12537.1. [Q9NYJ7-2]
    CCDS12538.1. [Q9NYJ7-1]
    RefSeqiNP_058637.1. NM_016941.3. [Q9NYJ7-1]
    NP_982353.1. NM_203486.2. [Q9NYJ7-2]
    UniGeneiHs.127792.

    Genome annotation databases

    EnsembliENST00000205143; ENSP00000205143; ENSG00000090932. [Q9NYJ7-1]
    ENST00000356433; ENSP00000348810; ENSG00000090932. [Q9NYJ7-2]
    GeneIDi10683.
    KEGGihsa:10683.
    UCSCiuc002olx.2. human. [Q9NYJ7-1]

    Polymorphism databases

    DMDMi12229810.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF241373
    , AF241367 , AF241368 , AF241369 , AF241370 , AF241371 , AF241372 Genomic DNA. Translation: AAF62542.1 .
    AK075302 mRNA. Translation: BAC11535.1 .
    AC011500 Genomic DNA. No translation available.
    BC000218 mRNA. Translation: AAH00218.1 .
    CCDSi CCDS12537.1. [Q9NYJ7-2 ]
    CCDS12538.1. [Q9NYJ7-1 ]
    RefSeqi NP_058637.1. NM_016941.3. [Q9NYJ7-1 ]
    NP_982353.1. NM_203486.2. [Q9NYJ7-2 ]
    UniGenei Hs.127792.

    3D structure databases

    ProteinModelPortali Q9NYJ7.
    SMRi Q9NYJ7. Positions 27-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115922. 1 interaction.
    STRINGi 9606.ENSP00000205143.

    Polymorphism databases

    DMDMi 12229810.

    Proteomic databases

    PaxDbi Q9NYJ7.
    PRIDEi Q9NYJ7.

    Protocols and materials databases

    DNASUi 10683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000205143 ; ENSP00000205143 ; ENSG00000090932 . [Q9NYJ7-1 ]
    ENST00000356433 ; ENSP00000348810 ; ENSG00000090932 . [Q9NYJ7-2 ]
    GeneIDi 10683.
    KEGGi hsa:10683.
    UCSCi uc002olx.2. human. [Q9NYJ7-1 ]

    Organism-specific databases

    CTDi 10683.
    GeneCardsi GC19P039989.
    GeneReviewsi DLL3.
    HGNCi HGNC:2909. DLL3.
    HPAi HPA056533.
    MIMi 277300. phenotype.
    602768. gene.
    neXtProti NX_Q9NYJ7.
    Orphaneti 2311. Autosomal recessive spondylocostal dysostosis.
    PharmGKBi PA27365.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244272.
    HOGENOMi HOG000267024.
    HOVERGENi HBG007139.
    InParanoidi Q9NYJ7.
    KOi K06051.
    OMAi DECRCLE.
    OrthoDBi EOG7P8P7B.
    PhylomeDBi Q9NYJ7.
    TreeFami TF351835.

    Enzyme and pathway databases

    SignaLinki Q9NYJ7.

    Miscellaneous databases

    GeneWikii DLL3.
    GenomeRNAii 10683.
    NextBioi 40615.
    PROi Q9NYJ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYJ7.
    Bgeei Q9NYJ7.
    CleanExi HS_DLL3.
    Genevestigatori Q9NYJ7.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011651. Notch_ligand_N.
    [Graphical view ]
    Pfami PF00008. EGF. 3 hits.
    PF12661. hEGF. 2 hits.
    PF07657. MNNL. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 6 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    PROSITEi PS00022. EGF_1. 6 hits.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in the human delta homologue, DLL3, cause axial skeletal defects in spondylocostal dysostosis."
      Bulman M.P., Kusumi K., Frayling T.M., McKeown C., Garrett C., Lander E.S., Krumlauf R., Hattersley A.T., Ellard S., Turnpenny P.D.
      Nat. Genet. 24:438-441(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT SCDO1 ASP-385.
    2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS CYS-172 AND PRO-218.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 1).
      Tissue: Brain.
    5. Cited for: VARIANTS THR-115; GLN-142; CYS-172 AND PRO-218.

    Entry informationi

    Entry nameiDLL3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYJ7
    Secondary accession number(s): E9PFG2, Q8NBS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3