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Protein

Delta-like protein 1

Gene

DLL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:11006133). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (By similarity). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation (PubMed:11581320). Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T cells and marginal zone (MZ) B cells (By similarity). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (PubMed:11581320). Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation througth regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis (By similarity).By similarity2 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • Notch binding Source: UniProtKB
  • Tat protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-HSA-1980148. Signaling by NOTCH3.
R-HSA-1980150. Signaling by NOTCH4.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2660826. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiO00548.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-like protein 1
Alternative name(s):
Drosophila Delta homolog 1
Short name:
Delta1
Short name:
H-Delta-1
Gene namesi
Name:DLL1
ORF Names:UNQ146/PRO172
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:2908. DLL1.

Subcellular locationi

  • Apical cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cell junctionadherens junction By similarity
  • Membrane raft By similarity

  • Note: Distributed around adherens junction in the apical endfeet through interactions with MAGI1.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 545528ExtracellularSequence analysisAdd
BLAST
Transmembranei546 – 56823HelicalSequence analysisAdd
BLAST
Topological domaini569 – 723155CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • cytoplasmic vesicle Source: Ensembl
  • extracellular region Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • membrane raft Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

MalaCardsiDLL1.
Orphaneti93925. Alobar holoprosencephaly.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBiPA27364.

Polymorphism and mutation databases

BioMutaiDLL1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 723706Delta-like protein 1PRO_0000007506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi179 ↔ 188By similarity
Disulfide bondi192 ↔ 204By similarity
Disulfide bondi212 ↔ 221By similarity
Disulfide bondi226 ↔ 237By similarity
Disulfide bondi230 ↔ 243By similarity
Disulfide bondi245 ↔ 254By similarity
Disulfide bondi257 ↔ 268By similarity
Disulfide bondi263 ↔ 274By similarity
Disulfide bondi276 ↔ 285By similarity
Disulfide bondi292 ↔ 304By similarity
Disulfide bondi298 ↔ 314By similarity
Disulfide bondi316 ↔ 325By similarity
Disulfide bondi332 ↔ 343By similarity
Disulfide bondi337 ↔ 352By similarity
Disulfide bondi354 ↔ 363By similarity
Disulfide bondi370 ↔ 381By similarity
Disulfide bondi375 ↔ 391By similarity
Disulfide bondi393 ↔ 402By similarity
Disulfide bondi409 ↔ 420By similarity
Disulfide bondi414 ↔ 429By similarity
Disulfide bondi431 ↔ 440By similarity
Disulfide bondi447 ↔ 458By similarity
Disulfide bondi452 ↔ 467By similarity
Disulfide bondi469 ↔ 478By similarity
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi485 ↔ 496By similarity
Disulfide bondi490 ↔ 505By similarity
Disulfide bondi507 ↔ 516By similarity
Cross-linki613 – 613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei694 – 6941Phosphoserine; by PKBBy similarity
Modified residuei697 – 6971PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation (By similarity). Ubiquitinated; promotes recycling back to the plasma membrane and confers a strong affinity for NOTCH1. Multi-ubiquitination of LYS-613 by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as activation of Notch signaling. Ubiquitinated by NEURL1B (By similarity).By similarity
Phosphorylated in a membrane association-dependent manner. Phosphorylation at Ser-697 requires the presence of Ser-694, whereas phosphorylation at Ser-694 occurs independently of the other site. Phosphorylation is required for full ligand activity in vitro and affects surface presentation, ectodomain shedding, and endocytosis.By similarity
O-fucosylated. Can be elongated to a disaccharide by MFNG.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO00548.
PRIDEiO00548.

PTM databases

iPTMnetiO00548.
PhosphoSiteiO00548.

Expressioni

Tissue specificityi

Expressed in heart and pancreas, with lower expression in brain and muscle and almost no expression in placenta, lung, liver and kidney.

Gene expression databases

BgeeiO00548.
CleanExiHS_DLL1.
ExpressionAtlasiO00548. baseline and differential.
GenevisibleiO00548. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with TJP1. Interacts with MAGI1 (via PDZ domain); forms a complex with CTNNB1 and CDH2 and promotes recruitment to the adherens junction and stabilization on the cell surface. Interacts with PSEN1; undergoes a presenilin-dependent gamma-secretase cleavage that releases a Dll1-intracellular form. Interacts with MFAP5. Interacts with MIB1. Interacts with NEURL1B; leads to ubiquitination. Interacts with NEURL1 (By similarity). Interacts with SYNJ2BP; enhances DLL1 protein stability, and promotes Notch signaling in endothelial cells (PubMed:24025447). Interacts with MAGI1, MAGI2, MAGI3 and MPDZ (PubMed:15509766). Interacts (via ubiquitin) with EPN1 (via IUM domain); binding with NOTCH1 attached to neighboring cell, promotes ligand ubiquitination and EPN1 interaction, leading to NECD transendocytosis and Notch signaling (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi118391. 5 interactions.
STRINGi9606.ENSP00000355718.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 308Combined sources
Beta strandi57 – 6610Combined sources
Beta strandi78 – 836Combined sources
Beta strandi88 – 914Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi118 – 12811Combined sources
Beta strandi143 – 15210Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi169 – 17911Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi287 – 2893Combined sources
Helixi292 – 2954Combined sources
Beta strandi303 – 3064Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 3154Combined sources
Turni322 – 3254Combined sources
Turni331 – 3344Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi389 – 3924Combined sources
Beta strandi399 – 4024Combined sources
Helixi408 – 4114Combined sources
Beta strandi419 – 4224Combined sources
Beta strandi427 – 4304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XBMX-ray3.20A/B21-545[»]
ProteinModelPortaliO00548.
SMRiO00548. Positions 22-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 22145DSLPROSITE-ProRule annotationAdd
BLAST
Domaini226 – 25429EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 28529EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini292 – 32534EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini332 – 36332EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini370 – 40233EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini409 – 44032EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini447 – 47832EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini485 – 51632EGF-like 8PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni720 – 7234Interaction with MAGI1By similarity

Sequence similaritiesi

Contains 1 DSL domain.PROSITE-ProRule annotation
Contains 8 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IR7B. Eukaryota.
ENOG410XUNS. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000267024.
HOVERGENiHBG007139.
InParanoidiO00548.
KOiK06051.
OMAiGFYGRIC.
OrthoDBiEOG7GQXZ5.
PhylomeDBiO00548.
TreeFamiTF351835.

Family and domain databases

InterProiIPR001774. DSL.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR011651. Notch_ligand_N.
[Graphical view]
PfamiPF01414. DSL. 1 hit.
PF00008. EGF. 5 hits.
PF07657. MNNL. 1 hit.
[Graphical view]
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS51051. DSL. 1 hit.
PS00022. EGF_1. 8 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 7 hits.
PS01187. EGF_CA. 1 hit.
[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. AlignAdd to basket

Isoform 1 (identifier: O00548-1) [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
MGSRCALALA VLSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGAG
60 70 80 90 100
PPPCACRTFF RVCLKHYQAS VSPEPPCTYG SAVTPVLGVD SFSLPDGGGA
110 120 130 140 150
DSAFSNPIRF PFGFTWPGTF SLIIEALHTD SPDDLATENP ERLISRLATQ
160 170 180 190 200
RHLTVGEEWS QDLHSSGRTD LKYSYRFVCD EHYYGEGCSV FCRPRDDAFG
210 220 230 240 250
HFTCGERGEK VCNPGWKGPY CTEPICLPGC DEQHGFCDKP GECKCRVGWQ
260 270 280 290 300
GRYCDECIRY PGCLHGTCQQ PWQCNCQEGW GGLFCNQDLN YCTHHKPCKN
310 320 330 340 350
GATCTNTGQG SYTCSCRPGY TGATCELGID ECDPSPCKNG GSCTDLENSY
360 370 380 390 400
SCTCPPGFYG KICELSAMTC ADGPCFNGGR CSDSPDGGYS CRCPVGYSGF
410 420 430 440 450
NCEKKIDYCS SSPCSNGAKC VDLGDAYLCR CQAGFSGRHC DDNVDDCASS
460 470 480 490 500
PCANGGTCRD GVNDFSCTCP PGYTGRNCSA PVSRCEHAPC HNGATCHERG
510 520 530 540 550
HRYVCECARG YGGPNCQFLL PELPPGPAVV DLTEKLEGQG GPFPWVAVCA
560 570 580 590 600
GVILVLMLLL GCAAVVVCVR LRLQKHRPPA DPCRGETETM NNLANCQREK
610 620 630 640 650
DISVSIIGAT QIKNTNKKAD FHGDHSADKN GFKARYPAVD YNLVQDLKGD
660 670 680 690 700
DTAVRDAHSK RDTKCQPQGS SGEEKGTPTT LRGGEASERK RPDSGCSTSK
710 720
DTKYQSVYVI SEEKDECVIA TEV
Length:723
Mass (Da):78,056
Last modified:October 31, 2006 - v2
Checksum:i094B8F235DFD899D
GO
Isoform 2 (identifier: O00548-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     224-247: PICLPGCDEQHGFCDKPGECKCRV → RESLGRHRWLTRPRTRTTRRDGAS
     248-723: Missing.

Show »
Length:247
Mass (Da):27,355
Checksum:iD93EB99469AE4871
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti498 – 4981E → Q in AAF05834 (PubMed:10688816).Curated
Sequence conflicti502 – 5021R → G in AAB61286 (PubMed:10079256).Curated
Sequence conflicti502 – 5021R → G in AAF05834 (PubMed:10688816).Curated
Sequence conflicti502 – 5021R → G in AAG09716 (PubMed:19906316).Curated
Sequence conflicti510 – 5101G → S in AAF05834 (PubMed:10688816).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti444 – 4441V → M.
Corresponds to variant rs16901311 [ dbSNP | Ensembl ].
VAR_048976

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei224 – 24724PICLP…CKCRV → RESLGRHRWLTRPRTRTTRR DGAS in isoform 2. 1 PublicationVSP_057186Add
BLAST
Alternative sequencei248 – 723476Missing in isoform 2. 1 PublicationVSP_057187Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003522 mRNA. Translation: AAB61286.1.
AF196571 mRNA. Translation: AAF05834.1.
EU927387 mRNA. Translation: ACH57449.1.
AF222310 Genomic DNA. Translation: AAG09716.1.
AY358892 mRNA. Translation: AAQ89251.1.
AK314234 mRNA. Translation: BAG36904.1.
AL078605 Genomic DNA. Translation: CAB89569.1.
CH471051 Genomic DNA. Translation: EAW47425.1.
CCDSiCCDS5313.1. [O00548-1]
RefSeqiNP_005609.3. NM_005618.3. [O00548-1]
XP_011534060.1. XM_011535758.1. [O00548-1]
XP_011544782.1. XM_011546480.1. [O00548-1]
UniGeneiHs.379912.

Genome annotation databases

EnsembliENST00000366756; ENSP00000355718; ENSG00000198719. [O00548-1]
ENST00000616526; ENSP00000480905; ENSG00000275555. [O00548-1]
GeneIDi28514.
KEGGihsa:28514.
UCSCiuc003qxm.3. human. [O00548-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003522 mRNA. Translation: AAB61286.1.
AF196571 mRNA. Translation: AAF05834.1.
EU927387 mRNA. Translation: ACH57449.1.
AF222310 Genomic DNA. Translation: AAG09716.1.
AY358892 mRNA. Translation: AAQ89251.1.
AK314234 mRNA. Translation: BAG36904.1.
AL078605 Genomic DNA. Translation: CAB89569.1.
CH471051 Genomic DNA. Translation: EAW47425.1.
CCDSiCCDS5313.1. [O00548-1]
RefSeqiNP_005609.3. NM_005618.3. [O00548-1]
XP_011534060.1. XM_011535758.1. [O00548-1]
XP_011544782.1. XM_011546480.1. [O00548-1]
UniGeneiHs.379912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XBMX-ray3.20A/B21-545[»]
ProteinModelPortaliO00548.
SMRiO00548. Positions 22-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118391. 5 interactions.
STRINGi9606.ENSP00000355718.

PTM databases

iPTMnetiO00548.
PhosphoSiteiO00548.

Polymorphism and mutation databases

BioMutaiDLL1.

Proteomic databases

PaxDbiO00548.
PRIDEiO00548.

Protocols and materials databases

DNASUi28514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366756; ENSP00000355718; ENSG00000198719. [O00548-1]
ENST00000616526; ENSP00000480905; ENSG00000275555. [O00548-1]
GeneIDi28514.
KEGGihsa:28514.
UCSCiuc003qxm.3. human. [O00548-1]

Organism-specific databases

CTDi28514.
GeneCardsiDLL1.
HGNCiHGNC:2908. DLL1.
MalaCardsiDLL1.
MIMi606582. gene.
neXtProtiNX_O00548.
Orphaneti93925. Alobar holoprosencephaly.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBiPA27364.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR7B. Eukaryota.
ENOG410XUNS. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000267024.
HOVERGENiHBG007139.
InParanoidiO00548.
KOiK06051.
OMAiGFYGRIC.
OrthoDBiEOG7GQXZ5.
PhylomeDBiO00548.
TreeFamiTF351835.

Enzyme and pathway databases

ReactomeiR-HSA-1980148. Signaling by NOTCH3.
R-HSA-1980150. Signaling by NOTCH4.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2660826. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiO00548.

Miscellaneous databases

ChiTaRSiDLL1. human.
GeneWikiiDelta-like_1.
GenomeRNAii28514.
NextBioi35477994.
PROiO00548.
SOURCEiSearch...

Gene expression databases

BgeeiO00548.
CleanExiHS_DLL1.
ExpressionAtlasiO00548. baseline and differential.
GenevisibleiO00548. HS.

Family and domain databases

InterProiIPR001774. DSL.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR011651. Notch_ligand_N.
[Graphical view]
PfamiPF01414. DSL. 1 hit.
PF00008. EGF. 5 hits.
PF07657. MNNL. 1 hit.
[Graphical view]
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS51051. DSL. 1 hit.
PS00022. EGF_1. 8 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 7 hits.
PS01187. EGF_CA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A soluble form of human Delta-like-1 inhibits differentiation of hematopoietic progenitor cells."
    Han W., Ye Q., Moore M.A.S.
    Blood 95:1616-1625(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
    Wang P., Yu P., Gao P., Shi T., Ma D.
    BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Human Delta 1 gene sequence."
    Oda T., Chandrasekharappa S.C.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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 1).
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Physical interaction of Delta1, Jagged1, and Jagged2 with Notch1 and Notch3 receptors."
    Shimizu K., Chiba S., Saito T., Kumano K., Hirai H.
    Biochem. Biophys. Res. Commun. 276:385-389(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Differential effects of Notch ligands Delta-1 and Jagged-1 in human lymphoid differentiation."
    Jaleco A.C., Neves H., Hooijberg E., Gameiro P., Clode N., Haury M., Henrique D., Parreira L.
    J. Exp. Med. 194:991-1001(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Delta proteins and MAGI proteins: an interaction of Notch ligands with intracellular scaffolding molecules and its significance for zebrafish development."
    Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.
    Development 131:5659-5669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGI1; MAGI2; MAGI3 AND MPDZ.
  12. "Synaptojanin-2 binding protein stabilizes the Notch ligands DLL1 and DLL4 and inhibits sprouting angiogenesis."
    Adam M.G., Berger C., Feldner A., Yang W.J., Wuestehube-Lausch J., Herberich S.E., Pinder M., Gesierich S., Hammes H.P., Augustin H.G., Fischer A.
    Circ. Res. 113:1206-1218(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNJ2BP.

Entry informationi

Entry nameiDLL1_HUMAN
AccessioniPrimary (citable) accession number: O00548
Secondary accession number(s): B2RAK7
, B5M0B3, Q9NU41, Q9UJV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 31, 2006
Last modified: January 20, 2016
This is version 157 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 6
    Human chromosome 6: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.