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Protein

Down syndrome cell adhesion molecule homolog

Gene

Dscam

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

Functioni

Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:18216855, PubMed:19196994, PubMed:19945391). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). In spinal chord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38. Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).By similarity4 Publications

GO - Biological processi

  • camera-type eye photoreceptor cell differentiation Source: UniProtKB
  • dendrite morphogenesis Source: MGI
  • dendrite self-avoidance Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  • locomotory behavior Source: MGI
  • negative regulation of cell adhesion Source: UniProtKB
  • positive regulation of axon extension involved in axon guidance Source: UniProtKB
  • positive regulation of phosphorylation Source: UniProtKB
  • post-embryonic retina morphogenesis in camera-type eye Source: MGI
  • retina layer formation Source: UniProtKB
  • synapse assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-376172. DSCAM interactions.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Down syndrome cell adhesion molecule homolog
Gene namesi
Name:Dscam
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1196281. Dscam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 15941577ExtracellularSequence analysisAdd
BLAST
Transmembranei1595 – 161521HelicalSequence analysisAdd
BLAST
Topological domaini1616 – 2013398CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • growth cone Source: UniProtKB
  • integral component of plasma membrane Source: InterPro
  • plasma membrane Source: UniProtKB
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

The ganglion cell layer and developing inner plexiform layer in the retina are disorganised at postnatal day 4 (P4). This desorganisation persisted into adulthood in amacrine and ganglions cells. Amacrine and ganglion cell populations show fasciculated dendrites that self-crossed and their cell bodies are randomly distributed or pulled into clumps.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 20131996Down syndrome cell adhesion molecule homologPRO_0000392478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 102PROSITE-ProRule annotation
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi145 ↔ 197PROSITE-ProRule annotation
Disulfide bondi246 ↔ 293PROSITE-ProRule annotation
Disulfide bondi335 ↔ 385PROSITE-ProRule annotation
Disulfide bondi428 ↔ 484PROSITE-ProRule annotation
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi525 ↔ 575PROSITE-ProRule annotation
Disulfide bondi617 ↔ 669PROSITE-ProRule annotation
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi711 ↔ 766PROSITE-ProRule annotation
Disulfide bondi809 ↔ 865PROSITE-ProRule annotation
Glycosylationi1160 – 11601N-linked (GlcNAc...)Sequence analysis
Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1307 ↔ 1359PROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated at tyrosine residues. Phosphorylation is enhanced by netrin.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9ERC8.
PaxDbiQ9ERC8.
PRIDEiQ9ERC8.

PTM databases

iPTMnetiQ9ERC8.
PhosphoSiteiQ9ERC8.

Expressioni

Tissue specificityi

In the retina, expressed in dopaminergic and Nos1-positive amacrine cells and most retinal ganglion cells (at protein level). Expressed in the brain with highest levels in the cortex, olfactory bulb, hippocampus, thalamus, cerebellum and spinal cord. Expressed in the retinal ganglion layer (RGL).4 Publications

Developmental stagei

Expressed in embryo at 11 dpc. Expressed in the spinal cord, including the motor columns, motor axons, dorsal root ganglions, commissural axons and ventral funiculus at 11.5 dpc (at protein level). Expressed in the retinal ganglion layer (RGL) at 12.5, 14.5 and 17 dpc. Expressed in hindbrain (cerebellar plate neurons), midbrain and forebrain at 10 dpc. Expressed in follicles of vibrissae and nasal processes at 12 dpc. Expressed in eyes at 14 dpc. Expressed in spinal cord, heart, liver, forelimb and hindlimb, buds at 14 dpc onwards.3 Publications

Gene expression databases

BgeeiQ9ERC8.
GenevisibleiQ9ERC8. MM.

Interactioni

Subunit structurei

Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. The interaction with PAK1 is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via cytoplasmic domain) with PAK1. Interacts (via extracellular domain) with NTN1 (PubMed:18585357). Interacts with DCC; the interaction is abolished in response to NTN1 (PubMed:18585357).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DccP702114EBI-1798601,EBI-1798863
DccQ631554EBI-1798601,EBI-1798965From a different organism.
NTN1Q909227EBI-1798601,EBI-1798593From a different organism.

Protein-protein interaction databases

IntActiQ9ERC8. 4 interactions.
STRINGi10090.ENSMUSP00000056040.

Structurei

3D structure databases

ProteinModelPortaliQ9ERC8.
SMRiQ9ERC8. Positions 980-1089.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 119100Ig-like C2-type 1Add
BLAST
Domaini125 – 21692Ig-like C2-type 2Add
BLAST
Domaini225 – 30581Ig-like C2-type 3Add
BLAST
Domaini313 – 40189Ig-like C2-type 4Add
BLAST
Domaini407 – 50094Ig-like C2-type 5Add
BLAST
Domaini504 – 59289Ig-like C2-type 6Add
BLAST
Domaini596 – 68590Ig-like C2-type 7Add
BLAST
Domaini690 – 78394Ig-like C2-type 8Add
BLAST
Domaini787 – 88397Ig-like C2-type 9Add
BLAST
Domaini885 – 98298Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini987 – 1086100Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1091 – 118797Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1191 – 128595Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1285 – 137793Ig-like C2-type 10Add
BLAST
Domaini1379 – 147395Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1474 – 1575102Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1617 – 16215Poly-Arg

Domaini

Ig-like C2-type domains 7 to 9 are sufficient for interaction with NTN1 and commissural axon outgrowth. The transmembrane domain is necessary for interaction with DCC.

Sequence similaritiesi

Contains 6 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IQJM. Eukaryota.
ENOG410XQX7. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000112277.
HOVERGENiHBG051409.
InParanoidiQ9ERC8.
KOiK06767.
OMAiMEPTPME.
OrthoDBiEOG7R830M.
PhylomeDBiQ9ERC8.
TreeFamiTF316846.

Family and domain databases

Gene3Di2.60.40.10. 16 hits.
InterProiIPR033027. DSCAM_ver.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PANTHERiPTHR10489:SF16. PTHR10489:SF16. 2 hits.
PfamiPF00041. fn3. 5 hits.
PF07679. I-set. 6 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ERC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWILALSLFQ SFANVFSEEP HSSLYFVNAS LQEVVFASTS GTLVPCPAAG
60 70 80 90 100
IPPVTLRWYL ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY
110 120 130 140 150
YCTAENPSGK IRSQDVHIKA VLREPYTVRV EDQKTMRGNV AVFKCIIPSS
160 170 180 190 200
VEAYVTVVSW EKDTVSLVSG SRFLITSTGA LYIKDVQNED GLYNYRCITR
210 220 230 240 250
HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ RVELPCKALG
260 270 280 290 300
HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENSRPSDSGS YVCEVSNRYG
310 320 330 340 350
TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGN EDQELSWYRN
360 370 380 390 400
GEILNPGKNV RITGLNHANL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV
410 420 430 440 450
VLEDGTPKII SAFSEKVVSP AEPVSLVCNV KGTPLPTVTW TLDDDPILKG
460 470 480 490 500
SGHRISQMIT SEGNVVSYLN ISSSQVRDGG VYRCTANNSA GVVLYQARIN
510 520 530 540 550
VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN ANLLPFNHRQ
560 570 580 590 600
VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ
610 620 630 640 650
PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPAS LGVTIDNIDF
660 670 680 690 700
TSSLRISNLS LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD
710 720 730 740 750
GIYGKAVILN CSAEGYPVPT IVWKFSKGAG VPQFQPIALN GRIQVLSNGS
760 770 780 790 800
LLIKHVVEED SGYYLCKVSN DVGADVSKSM YLTVKIPAMI TSYPNTTLAT
810 820 830 840 850
QGQRKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK EVGEEVISTL
860 870 880 890 900
QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART
910 920 930 940 950
ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI
960 970 980 990 1000
HPSSTYSIRM YAKNRIGKSE PSNEITITAD EAAPDGPPQE VHLEPTSSQS
1010 1020 1030 1040 1050
IRVTWKAPKK HLQNGIIRGY QIGYREYSTG GNFQFNIISI DTTGDSEVYT
1060 1070 1080 1090 1100
LDNLNKFTQY GLVVQACNRA GTGPSSQEII TTTLEDVPSY PPENVQAIAT
1110 1120 1130 1140 1150
SPESISISWS TLSKEALNGI LQGFRVIYWA NLIDGELGEI KNVTTTQPSL
1160 1170 1180 1190 1200
ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA
1210 1220 1230 1240 1250
SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN
1260 1270 1280 1290 1300
LSRNRQYSVW VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM
1310 1320 1330 1340 1350
KDIVLPCKAV GDPSPAVKWM KDSNGTPSLV TIDGRRSIFS NGSFIIRTVK
1360 1370 1380 1390 1400
AEDSGYYSCV ANNNWGSDEI ILNLQVQVPP DQPRLTVSKT TSSSITLSWL
1410 1420 1430 1440 1450
PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN LKCGTWYKFT
1460 1470 1480 1490 1500
LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN
1510 1520 1530 1540 1550
DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV
1560 1570 1580 1590 1600
CNSAGCAEKQ ANFATLNYDG STIPPLIKSV VQSEEGLTTN EGLKILVTIS
1610 1620 1630 1640 1650
CILVGVLLLF VLLLVVRRRR REQRLKRLRD AKSLAEMLMS KNTRTSDTLS
1660 1670 1680 1690 1700
KQQQTLRMHI DIPRAQLLIE ERDTMETIDD RSTVLLTDAD FGEAAKQKSL
1710 1720 1730 1740 1750
TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP TARNRYASQW
1760 1770 1780 1790 1800
TLNRPHPTIS AHTLTTDWRL PTPRATGSVD KESDSYSVSP SQDTDRARSS
1810 1820 1830 1840 1850
MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG
1860 1870 1880 1890 1900
TNEYTDSLTS STPSESGICR FTASPPKPQD GGRVVNMAVP KAHRPGDLIH
1910 1920 1930 1940 1950
LPPYLRMDFL LNRGAPGTSR DLSLGQACLE PQKSRTLKRP TVLEPTPMEA
1960 1970 1980 1990 2000
SSSTSSTREG QQSWQQGAVA TLPQREGAEL GQAAKMSSSQ ESLLDSRGHL
2010
KGNNPYAKSY TLV
Length:2,013
Mass (Da):222,268
Last modified:March 1, 2001 - v1
Checksum:i1F4AF07947BEBA77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005483 mRNA. Translation: AAF99440.1.
AF315558 mRNA. Translation: AAG28796.1.
CH466602 Genomic DNA. Translation: EDL03664.1.
CCDSiCCDS37415.1.
RefSeqiNP_112451.1. NM_031174.4.
UniGeneiMm.102437.
Mm.328737.

Genome annotation databases

EnsembliENSMUST00000056102; ENSMUSP00000056040; ENSMUSG00000050272.
GeneIDi13508.
KEGGimmu:13508.
UCSCiuc008add.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005483 mRNA. Translation: AAF99440.1.
AF315558 mRNA. Translation: AAG28796.1.
CH466602 Genomic DNA. Translation: EDL03664.1.
CCDSiCCDS37415.1.
RefSeqiNP_112451.1. NM_031174.4.
UniGeneiMm.102437.
Mm.328737.

3D structure databases

ProteinModelPortaliQ9ERC8.
SMRiQ9ERC8. Positions 980-1089.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ERC8. 4 interactions.
STRINGi10090.ENSMUSP00000056040.

PTM databases

iPTMnetiQ9ERC8.
PhosphoSiteiQ9ERC8.

Proteomic databases

MaxQBiQ9ERC8.
PaxDbiQ9ERC8.
PRIDEiQ9ERC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056102; ENSMUSP00000056040; ENSMUSG00000050272.
GeneIDi13508.
KEGGimmu:13508.
UCSCiuc008add.2. mouse.

Organism-specific databases

CTDi1826.
MGIiMGI:1196281. Dscam.

Phylogenomic databases

eggNOGiENOG410IQJM. Eukaryota.
ENOG410XQX7. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000112277.
HOVERGENiHBG051409.
InParanoidiQ9ERC8.
KOiK06767.
OMAiMEPTPME.
OrthoDBiEOG7R830M.
PhylomeDBiQ9ERC8.
TreeFamiTF316846.

Enzyme and pathway databases

ReactomeiR-MMU-376172. DSCAM interactions.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

PROiQ9ERC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERC8.
GenevisibleiQ9ERC8. MM.

Family and domain databases

Gene3Di2.60.40.10. 16 hits.
InterProiIPR033027. DSCAM_ver.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PANTHERiPTHR10489:SF16. PTHR10489:SF16. 2 hits.
PfamiPF00041. fn3. 5 hits.
PF07679. I-set. 6 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DSCAM, a highly conserved gene in mammals, expressed in differentiating mouse brain."
    Agarwala K.L., Ganesh S., Amano K., Suzuki T., Yamakawa K.
    Biochem. Biophys. Res. Commun. 281:697-705(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: ICR.
  2. "Down syndrome cell adhesion molecule is conserved in mouse and highly expressed in the adult mouse brain."
    Barlow G.M., Micales B., Lyons G.E., Korenberg J.R.
    Cytogenet. Cell Genet. 94:155-162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The Down syndrome cell adhesion molecule (DSCAM) interacts with and activates Pak."
    Li W., Guan K.L.
    J. Biol. Chem. 279:32824-32831(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAK1.
  5. "DSCAM is a netrin receptor that collaborates with DCC in mediating turning responses to netrin-1."
    Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.
    Cell 133:1241-1254(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCC AND NTN1.
  6. "Neurite arborization and mosaic spacing in the mouse retina require DSCAM."
    Fuerst P.G., Koizumi A., Masland R.H., Burgess R.W.
    Nature 451:470-474(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  7. "DSCAM and DSCAML1 function in self-avoidance in multiple cell types in the developing mouse retina."
    Fuerst P.G., Bruce F., Tian M., Wei W., Elstrott J., Feller M.B., Erskine L., Singer J.H., Burgess R.W.
    Neuron 64:484-497(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "DSCAM functions as a netrin receptor in commissural axon pathfinding."
    Liu G., Li W., Wang L., Kar A., Guan K.L., Rao Y., Wu J.Y.
    Proc. Natl. Acad. Sci. U.S.A. 106:2951-2956(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDSCAM_MOUSE
AccessioniPrimary (citable) accession number: Q9ERC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 1, 2001
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.