Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

BioCyciZFISH:G66-33539-MONOMER.
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.
SIGNORiO00548.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Topological domaini18 – 545ExtracellularSequence analysisAdd BLAST528
Transmembranei546 – 568HelicalSequence analysisAdd BLAST23
Topological domaini569 – 723CytoplasmicSequence analysisAdd BLAST155

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

DisGeNETi28514.
MalaCardsiDLL1.
OpenTargetsiENSG00000198719.
ENSG00000275555.
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000750618 – 723Delta-like protein 1Add BLAST706

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi477N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi485 ↔ 496By similarity
Disulfide bondi490 ↔ 505By similarity
Disulfide bondi507 ↔ 516By similarity
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei694Phosphoserine; by PKBBy similarity1
Modified residuei697PhosphoserineBy similarity1

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

EPDiO00548.
PaxDbiO00548.
PeptideAtlasiO00548.
PRIDEiO00548.

PTM databases

iPTMnetiO00548.
PhosphoSitePlusiO00548.

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

BgeeiENSG00000198719.
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

GO - Molecular functioni

  • Notch binding Source: UniProtKB
  • Tat protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118391. 5 interactors.
STRINGi9606.ENSP00000355718.

Structurei

Secondary structure

1723
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 30Combined sources8
Beta strandi57 – 66Combined sources10
Beta strandi78 – 83Combined sources6
Beta strandi88 – 91Combined sources4
Beta strandi108 – 112Combined sources5
Beta strandi118 – 128Combined sources11
Beta strandi143 – 152Combined sources10
Beta strandi156 – 166Combined sources11
Beta strandi169 – 179Combined sources11
Beta strandi183 – 185Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi200 – 204Combined sources5
Beta strandi206 – 208Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi232 – 236Combined sources5
Beta strandi249 – 254Combined sources6
Beta strandi265 – 267Combined sources3
Beta strandi280 – 285Combined sources6
Beta strandi287 – 289Combined sources3
Helixi292 – 295Combined sources4
Beta strandi303 – 306Combined sources4
Beta strandi308 – 310Combined sources3
Beta strandi312 – 315Combined sources4
Turni322 – 325Combined sources4
Turni331 – 334Combined sources4
Beta strandi342 – 346Combined sources5
Beta strandi349 – 353Combined sources5
Beta strandi358 – 362Combined sources5
Beta strandi365 – 367Combined sources3
Beta strandi380 – 383Combined sources4
Beta strandi385 – 387Combined sources3
Beta strandi389 – 392Combined sources4
Beta strandi399 – 402Combined sources4
Helixi408 – 411Combined sources4
Beta strandi419 – 422Combined sources4
Beta strandi427 – 430Combined sources4

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini177 – 221DSLPROSITE-ProRule annotationAdd BLAST45
Domaini226 – 254EGF-like 1PROSITE-ProRule annotationAdd BLAST29
Domaini257 – 285EGF-like 2PROSITE-ProRule annotationAdd BLAST29
Domaini292 – 325EGF-like 3PROSITE-ProRule annotationAdd BLAST34
Domaini332 – 363EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST32
Domaini370 – 402EGF-like 5PROSITE-ProRule annotationAdd BLAST33
Domaini409 – 440EGF-like 6PROSITE-ProRule annotationAdd BLAST32
Domaini447 – 478EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST32
Domaini485 – 516EGF-like 8PROSITE-ProRule annotationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni720 – 723Interaction with MAGI1By similarity4

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.
OrthoDBiEOG091G07YQ.
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.
PF12661. hEGF. 1 hit.
PF07657. MNNL. 1 hit.
[Graphical view]
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 8 hits.
SM00179. EGF_CA. 6 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)DescriptionActionsGraphical viewLength
Sequence conflicti498E → Q in AAF05834 (PubMed:10688816).Curated1
Sequence conflicti502R → G in AAB61286 (PubMed:10079256).Curated1
Sequence conflicti502R → G in AAF05834 (PubMed:10688816).Curated1
Sequence conflicti502R → G in AAG09716 (PubMed:19906316).Curated1
Sequence conflicti510G → S in AAF05834 (PubMed:10688816).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048976444V → M.Corresponds to variant rs16901311dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_057186224 – 247PICLP…CKCRV → RESLGRHRWLTRPRTRTTRR DGAS in isoform 2. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_057187248 – 723Missing in isoform 2. 1 PublicationAdd BLAST476

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]
UniGeneiHs.379912.

Genome annotation databases

EnsembliENST00000366756; ENSP00000355718; ENSG00000198719. [O00548-1]
ENST00000616526; ENSP00000480905; ENSG00000275555. [O00548-1]
GeneIDi28514.
KEGGihsa:28514.
UCSCiuc003qxm.4. 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]
UniGeneiHs.379912.

3D structure databases

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

Protein-protein interaction databases

BioGridi118391. 5 interactors.
STRINGi9606.ENSP00000355718.

PTM databases

iPTMnetiO00548.
PhosphoSitePlusiO00548.

Polymorphism and mutation databases

BioMutaiDLL1.

Proteomic databases

EPDiO00548.
PaxDbiO00548.
PeptideAtlasiO00548.
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.4. human. [O00548-1]

Organism-specific databases

CTDi28514.
DisGeNETi28514.
GeneCardsiDLL1.
HGNCiHGNC:2908. DLL1.
MalaCardsiDLL1.
MIMi606582. gene.
neXtProtiNX_O00548.
OpenTargetsiENSG00000198719.
ENSG00000275555.
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.
OrthoDBiEOG091G07YQ.
PhylomeDBiO00548.
TreeFamiTF351835.

Enzyme and pathway databases

BioCyciZFISH:G66-33539-MONOMER.
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.
SIGNORiO00548.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000198719.
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.
PF12661. hEGF. 1 hit.
PF07657. MNNL. 1 hit.
[Graphical view]
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 8 hits.
SM00179. EGF_CA. 6 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...

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: November 2, 2016
This is version 164 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.