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Protein

Delta and Notch-like epidermal growth factor-related receptor

Gene

Dner

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates neuron-glia interaction during astrocytogenesis. May promote differentiation of Bergmann glia during cerebellar development by activating DELTEX-dependent NOTCH1 signaling.2 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • Notch binding Source: MGI

GO - Biological processi

  • central nervous system development Source: Ensembl
  • glial cell differentiation Source: MGI
  • Notch receptor processing Source: MGI
  • Notch signaling pathway Source: Reactome
  • skeletal muscle fiber development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta and Notch-like epidermal growth factor-related receptor
Alternative name(s):
Brain EGF repeat-containing transmembrane protein
Gene namesi
Name:Dner
Synonyms:Bet, Bret
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2152889. Dner.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 640615ExtracellularSequence analysisAdd
BLAST
Transmembranei641 – 66121HelicalSequence analysisAdd
BLAST
Topological domaini662 – 73776CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • dendrite Source: MGI
  • early endosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show no obvious abnormality and no apparent survival disadvantage. However, they have delayed cerebellar histogenesis and exhibit motor discoordination at adult stages.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi677 – 6771Y → A: Fails to be restricted to the somatodendritic compartment. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 737712Delta and Notch-like epidermal growth factor-related receptorPRO_0000253558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 59PROSITE-ProRule annotation
Disulfide bondi53 ↔ 80PROSITE-ProRule annotation
Disulfide bondi82 ↔ 91PROSITE-ProRule annotation
Disulfide bondi98 ↔ 108PROSITE-ProRule annotation
Disulfide bondi103 ↔ 121PROSITE-ProRule annotation
Disulfide bondi123 ↔ 132PROSITE-ProRule annotation
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence analysis
Disulfide bondi319 ↔ 336PROSITE-ProRule annotation
Disulfide bondi338 ↔ 347PROSITE-ProRule annotation
Disulfide bondi353 ↔ 364PROSITE-ProRule annotation
Disulfide bondi358 ↔ 378PROSITE-ProRule annotation
Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
Disulfide bondi396 ↔ 407PROSITE-ProRule annotation
Disulfide bondi401 ↔ 416PROSITE-ProRule annotation
Disulfide bondi418 ↔ 427PROSITE-ProRule annotation
Disulfide bondi434 ↔ 445PROSITE-ProRule annotation
Disulfide bondi439 ↔ 454PROSITE-ProRule annotation
Disulfide bondi456 ↔ 465PROSITE-ProRule annotation
Disulfide bondi472 ↔ 482PROSITE-ProRule annotation
Disulfide bondi477 ↔ 491PROSITE-ProRule annotation
Disulfide bondi493 ↔ 502PROSITE-ProRule annotation
Disulfide bondi509 ↔ 520PROSITE-ProRule annotation
Disulfide bondi514 ↔ 529PROSITE-ProRule annotation
Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
Disulfide bondi547 ↔ 558PROSITE-ProRule annotation
Disulfide bondi552 ↔ 567PROSITE-ProRule annotation
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi569 ↔ 578PROSITE-ProRule annotation
Disulfide bondi585 ↔ 596PROSITE-ProRule annotation
Disulfide bondi590 ↔ 605PROSITE-ProRule annotation
Disulfide bondi607 ↔ 616PROSITE-ProRule annotation
Modified residuei685 – 6851PhosphoserineCombined sources
Modified residuei711 – 7111PhosphotyrosineCombined sources
Modified residuei714 – 7141PhosphothreonineCombined sources
Modified residuei721 – 7211PhosphotyrosineCombined sources
Modified residuei722 – 7221PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8JZM4.
PaxDbiQ8JZM4.
PRIDEiQ8JZM4.

PTM databases

iPTMnetiQ8JZM4.
PhosphoSiteiQ8JZM4.

Expressioni

Tissue specificityi

Specifically expressed in brain neurons (at protein level).2 Publications

Developmental stagei

Expression in the central nervous system starts at E11, peaks during postnatal development and declines in the adult brain. At P7 and P20, present in several types of post-mitotic neurons, including cortical and hippocampal pyramidal neurons, cerebellar granule cells and Purkinje cells. Absent from mitotic neuroblasts in the ventricular zones.2 Publications

Gene expression databases

BgeeiQ8JZM4.
CleanExiMM_DNER.
ExpressionAtlasiQ8JZM4. baseline and differential.
GenevisibleiQ8JZM4. MM.

Interactioni

Subunit structurei

Interacts with AP1G1. Interacts with NOTCH1.2 Publications

GO - Molecular functioni

  • Notch binding Source: MGI

Protein-protein interaction databases

BioGridi230612. 1 interaction.
STRINGi10090.ENSMUSP00000042927.

Structurei

3D structure databases

ProteinModelPortaliQ8JZM4.
SMRiQ8JZM4. Positions 48-142, 310-624.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 9249EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 13340EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini309 – 34840EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini349 – 39042EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini392 – 42837EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini430 – 46637EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini468 – 50336EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini505 – 54137EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini543 – 57937EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini581 – 61737EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 13390Interaction with NOTCH1Add
BLAST
Regioni677 – 6804Interaction with AP1G1 and somatodendritic targeting

Sequence similaritiesi

Contains 10 EGF-like domains.PROSITE-ProRule annotation
Contains 1 follistatin-like domain.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IR71. Eukaryota.
ENOG410ZUAK. LUCA.
GeneTreeiENSGT00840000129708.
HOGENOMiHOG000112241.
HOVERGENiHBG060866.
InParanoidiQ8JZM4.
OMAiWDQVEVI.
OrthoDBiEOG7MPRD8.
PhylomeDBiQ8JZM4.
TreeFamiTF351322.

Family and domain databases

InterProiIPR001881. 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_.
[Graphical view]
PfamiPF00008. EGF. 6 hits.
PF12661. hEGF. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS00022. EGF_1. 10 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 10 hits.
PS01187. EGF_CA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8JZM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPRRAQAPG APLLPVLALL PLLLGAGPQS GCLASPVSAA PLPAPGPCAS
60 70 80 90 100
QPCRNGGVCT PRSVTDQEHP AADAEPRYSC TCPAGVSGTY CQFVADPCAS
110 120 130 140 150
NPCHHGNCSS SSSSSSDSYL CICNDGYEGL NCEQPLPSIP TSGWTESTAP
160 170 180 190 200
RQLQPVPATQ EPDIILPRSQ ATVTLPTWQP KTGQKVVEMK WDQVEVVPDV
210 220 230 240 250
ACGNASSNNS AGGRLVSFEV PQNTSVKIRQ DANSLLILLW KVTATGFQQC
260 270 280 290 300
SLIDGRSVTP LQAPGGLVLL EEMLALGPNH FIGFVNDSVA KSIVALRLTL
310 320 330 340 350
VVKASNCVPG DSHSNDLECS GKGKCATKPS EATFSCTCQD QYIGTFCEEF
360 370 380 390 400
DACQRKPCQN EASCIDANEK QDGSNFTCLC LPGYTGELCQ SKIDYCVLDP
410 420 430 440 450
CRNGATCVSS LSGFTCQCLE GYFGSACEEK VDPCMSSPCQ NNGTCYVDGV
460 470 480 490 500
HFTCSCSPGF TGPTCAQLVD FCALSPCAHG MCRSVGTSYK CLCDPGYHGL
510 520 530 540 550
YCEEEYNECL SAPCLNAATC RDLINGYECV CLAEYKGTHC ELYKDPCANI
560 570 580 590 600
SCLNGGTCDS EGLNGTCICA PGFTGEECDI DINECDSNPC HHAGTCLDQP
610 620 630 640 650
NGYTCHCPHG WVGANCEIHL QWKSGHMAES LTNMPRHSLY IIIGALCVAF
660 670 680 690 700
ILMLIILIVG ICRISRIEYQ GSSRPAYEEF YNCRSIDSEF SNAIASIRHA
710 720 730
RFGKKSRPAM YDVTPIAYED YSPDDKPLVT LIKTKDL
Length:737
Mass (Da):78,747
Last modified:October 1, 2002 - v1
Checksum:i8C85694EB7420756
GO

Sequence cautioni

The sequence BAE31470.1 differs from that shown. Reason: Frameshift at position 631. Curated
The sequence BAE31828.1 differs from that shown. Reason: Frameshift at position 631. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti424 – 4241G → A in BAB72175 (PubMed:11997712).Curated
Sequence conflicti509 – 5102CL → SV in AAM14419 (PubMed:11950833).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032924 mRNA. Translation: AAK50342.1.
AF370126 mRNA. Translation: AAM14419.1.
AB067650 mRNA. Translation: BAB72175.1.
AK044597 mRNA. Translation: BAC31995.1.
AK152755 mRNA. Translation: BAE31470.1. Frameshift.
AK153235 mRNA. Translation: BAE31828.1. Frameshift.
BC022636 mRNA. Translation: AAH22636.1.
BC034634 mRNA. Translation: AAH34634.1.
CCDSiCCDS15105.1.
RefSeqiNP_690879.1. NM_152915.1.
UniGeneiMm.292560.

Genome annotation databases

EnsembliENSMUST00000049126; ENSMUSP00000042927; ENSMUSG00000036766.
GeneIDi227325.
KEGGimmu:227325.
UCSCiuc007bsw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032924 mRNA. Translation: AAK50342.1.
AF370126 mRNA. Translation: AAM14419.1.
AB067650 mRNA. Translation: BAB72175.1.
AK044597 mRNA. Translation: BAC31995.1.
AK152755 mRNA. Translation: BAE31470.1. Frameshift.
AK153235 mRNA. Translation: BAE31828.1. Frameshift.
BC022636 mRNA. Translation: AAH22636.1.
BC034634 mRNA. Translation: AAH34634.1.
CCDSiCCDS15105.1.
RefSeqiNP_690879.1. NM_152915.1.
UniGeneiMm.292560.

3D structure databases

ProteinModelPortaliQ8JZM4.
SMRiQ8JZM4. Positions 48-142, 310-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230612. 1 interaction.
STRINGi10090.ENSMUSP00000042927.

PTM databases

iPTMnetiQ8JZM4.
PhosphoSiteiQ8JZM4.

Proteomic databases

MaxQBiQ8JZM4.
PaxDbiQ8JZM4.
PRIDEiQ8JZM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049126; ENSMUSP00000042927; ENSMUSG00000036766.
GeneIDi227325.
KEGGimmu:227325.
UCSCiuc007bsw.1. mouse.

Organism-specific databases

CTDi92737.
MGIiMGI:2152889. Dner.

Phylogenomic databases

eggNOGiENOG410IR71. Eukaryota.
ENOG410ZUAK. LUCA.
GeneTreeiENSGT00840000129708.
HOGENOMiHOG000112241.
HOVERGENiHBG060866.
InParanoidiQ8JZM4.
OMAiWDQVEVI.
OrthoDBiEOG7MPRD8.
PhylomeDBiQ8JZM4.
TreeFamiTF351322.

Enzyme and pathway databases

ReactomeiR-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.

Miscellaneous databases

ChiTaRSiDner. mouse.
PROiQ8JZM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZM4.
CleanExiMM_DNER.
ExpressionAtlasiQ8JZM4. baseline and differential.
GenevisibleiQ8JZM4. MM.

Family and domain databases

InterProiIPR001881. 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_.
[Graphical view]
PfamiPF00008. EGF. 6 hits.
PF12661. hEGF. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS00022. EGF_1. 10 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 10 hits.
PS01187. EGF_CA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Delta/notch-like epidermal growth factor (EGF)-related receptor, a novel EGF-like repeat-containing protein targeted to dendrites of developing and adult central nervous system neurons."
    Eiraku M., Hirata Y., Takeshima H., Hirano T., Kengaku M.
    J. Biol. Chem. 277:25400-25407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-677, INTERACTION WITH AP1G1.
    Strain: ICR.
    Tissue: Brain.
  2. "BET, a novel neuronal transmembrane protein with multiple EGF-like motifs."
    Nishizumi H., Komiyama T., Miyabayashi T., Sakano S., Sakano H.
    NeuroReport 13:909-915(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Retina.
  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].
    Strain: FVB/N.
    Tissue: Colon and Eye.
  5. "DNER acts as a neuron-specific Notch ligand during Bergmann glial development."
    Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T., Kengaku M.
    Nat. Neurosci. 8:873-880(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOTCH1, FUNCTION.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-711 AND TYR-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; THR-714 AND SER-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiDNER_MOUSE
AccessioniPrimary (citable) accession number: Q8JZM4
Secondary accession number(s): Q3U697
, Q8R226, Q8R4T6, Q8VD97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.