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Protein

Down syndrome cell adhesion molecule

Gene

DSCAM

Organism
Homo sapiens (Human)
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:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. 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 (PubMed:18585357, PubMed:19196994). Enhances netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). 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

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Neurogenesis

Enzyme and pathway databases

ReactomeiR-HSA-376172. DSCAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Down syndrome cell adhesion molecule
Alternative name(s):
CHD2
Gene namesi
Name:DSCAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:3039. DSCAM.

Subcellular locationi

Isoform Long :
  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cell projectionaxon By similarity
  • Cell junctionsynapse By similarity

  • Note: Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 15951578ExtracellularSequence analysisAdd
BLAST
Transmembranei1596 – 161621HelicalSequence analysisAdd
BLAST
Topological domaini1617 – 2012396CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27491.

Polymorphism and mutation databases

BioMutaiDSCAM.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 20121995Down syndrome cell adhesion moleculePRO_0000014747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence analysis
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi525 ↔ 575PROSITE-ProRule annotation
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi617 ↔ 669PROSITE-ProRule annotation
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence analysis
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence analysis
Glycosylationi710 – 7101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi711 ↔ 766PROSITE-ProRule annotation
Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence analysis
Disulfide bondi809 ↔ 865PROSITE-ProRule annotation
Glycosylationi924 – 9241N-linked (GlcNAc...)Sequence analysis
Glycosylationi1142 – 11421N-linked (GlcNAc...)Sequence analysis
Glycosylationi1160 – 11601N-linked (GlcNAc...)Sequence analysis
Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence analysis
Glycosylationi1271 – 12711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1307 ↔ 1359PROSITE-ProRule annotation
Glycosylationi1341 – 13411N-linked (GlcNAc...)Sequence analysis
Glycosylationi1488 – 14881N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated at tyrosine residues. Phosphorylation is enhanced by netrin.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO60469.
PaxDbiO60469.
PeptideAtlasiO60469.
PRIDEiO60469.

PTM databases

iPTMnetiO60469.
PhosphoSiteiO60469.

Expressioni

Tissue specificityi

Primarily expressed in brain.

Gene expression databases

BgeeiO60469.
CleanExiHS_DSCAM.
ExpressionAtlasiO60469. baseline and differential.
GenevisibleiO60469. HS.

Organism-specific databases

HPAiHPA019324.

Interactioni

Subunit structurei

Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (PubMed:15169762). Interacts (via extracellular domain) with NTN1 (PubMed:19196994). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1. Interacts with RAC1; the interaction requires PAK1.By similarity2 Publications

Protein-protein interaction databases

BioGridi108160. 1 interaction.
STRINGi9606.ENSP00000383303.

Structurei

3D structure databases

ProteinModelPortaliO60469.
SMRiO60469. Positions 980-1089.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 12991Ig-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

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 (By similarity).By similarity

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.
HOVERGENiHBG051409.
InParanoidiO60469.
KOiK06767.
OMAiWTLDEDP.
OrthoDBiEOG7R830M.
PhylomeDBiO60469.
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. 5 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 8 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: O60469-1) [UniParc]FASTAAdd to basket

Also known as: CHD2-42

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
MWILALSLFQ SFANVFSEDL HSSLYFVNAS LQEVVFASTT 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
VEAYITVVSW EKDTVSLVSG SRFLITSTGA LYIKDVQNED GLYNYRCITR
210 220 230 240 250
HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ RVELPCKALG
260 270 280 290 300
HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENIRPSDSGS YVCEVSNRYG
310 320 330 340 350
TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGT EDQELSWYRN
360 370 380 390 400
GEILNPGKNV RITGINHENL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV
410 420 430 440 450
VLEDGTPKII SAFSEKVVSP AEPVSLMCNV KGTPLPTITW TLDDDPILKG
460 470 480 490 500
GSHRISQMIT SEGNVVSYLN ISSSQVRDGG VYRCTANNSA GVVLYQARIN
510 520 530 540 550
VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN SNLLPFNHRQ
560 570 580 590 600
VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ
610 620 630 640 650
PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPGS 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
QGQKKEMSCT 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 PSNELTITAD EAAPDGPPQE VHLEPISSQS
1010 1020 1030 1040 1050
IRVTWKAPKK HLQNGIIRGY QIGYREYSTG GNFQFNIISV DTSGDSEVYT
1060 1070 1080 1090 1100
LDNLNKFTQY GLVVQACNRA GTGPSSQEII TTTLEDVPSY PPENVQAIAT
1110 1120 1130 1140 1150
SPESISISWS TLSKEALNGI LQGFRVIYWA NLMDGELGEI KNITTTQPSL
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
AEDSGYYSCI 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 VQNEEGLTTN EGLKMLVTIS
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 PTPRAAGSVD KESDSYSVSP SQDTDRARSS
1810 1820 1830 1840 1850
MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG
1860 1870 1880 1890 1900
TNEYTDSLTS STPSESGICR FTASPPKPQD GGRVMNMAVP KAHRPGDLIH
1910 1920 1930 1940 1950
LPPYLRMDFL LNRGGPGTSR DLSLGQACLE PQKSRTLKRP TVLEPIPMEA
1960 1970 1980 1990 2000
ASSASSTREG QSWQPGAVAT LPQREGAELG QAAKMSSSQE SLLDSRGHLK
2010
GNNPYAKSYT LV
Length:2,012
Mass (Da):222,260
Last modified:December 1, 2000 - v2
Checksum:i0E33CFB781A08334
GO
Isoform Short (identifier: O60469-2) [UniParc]FASTAAdd to basket

Also known as: CHD2-52

The sequence of this isoform differs from the canonical sequence as follows:
     1562-1571: NFATLNYDGS → KEAARCKEFS
     1572-2012: Missing.

Show »
Length:1,571
Mass (Da):173,804
Checksum:i4B065ABB67B01110
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1893 – 2012120HRPGD…SYTLV → IGQVTSYICLHTLEWTFC in AAC17966 (PubMed:9426258).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti232 – 2321D → E.
Corresponds to variant rs2297270 [ dbSNP | Ensembl ].
VAR_020080

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1562 – 157110NFATLNYDGS → KEAARCKEFS in isoform Short. CuratedVSP_002502
Alternative sequencei1572 – 2012441Missing in isoform Short. CuratedVSP_002503Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023450 mRNA. Translation: AAC17967.1.
AF023449 mRNA. Translation: AAC17966.1.
AF217525 mRNA. Translation: AAF27525.1.
AL163283 Genomic DNA. Translation: CAB90464.1.
AL163282 Genomic DNA. Translation: CAB90436.1.
AL163281 Genomic DNA. Translation: CAB90444.1.
CCDSiCCDS42929.1. [O60469-1]
RefSeqiNP_001258463.1. NM_001271534.1.
NP_001380.2. NM_001389.3. [O60469-1]
UniGeneiHs.397800.

Genome annotation databases

EnsembliENST00000400454; ENSP00000383303; ENSG00000171587. [O60469-1]
GeneIDi1826.
KEGGihsa:1826.
UCSCiuc002yyq.2. human. [O60469-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023450 mRNA. Translation: AAC17967.1.
AF023449 mRNA. Translation: AAC17966.1.
AF217525 mRNA. Translation: AAF27525.1.
AL163283 Genomic DNA. Translation: CAB90464.1.
AL163282 Genomic DNA. Translation: CAB90436.1.
AL163281 Genomic DNA. Translation: CAB90444.1.
CCDSiCCDS42929.1. [O60469-1]
RefSeqiNP_001258463.1. NM_001271534.1.
NP_001380.2. NM_001389.3. [O60469-1]
UniGeneiHs.397800.

3D structure databases

ProteinModelPortaliO60469.
SMRiO60469. Positions 980-1089.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108160. 1 interaction.
STRINGi9606.ENSP00000383303.

PTM databases

iPTMnetiO60469.
PhosphoSiteiO60469.

Polymorphism and mutation databases

BioMutaiDSCAM.

Proteomic databases

EPDiO60469.
PaxDbiO60469.
PeptideAtlasiO60469.
PRIDEiO60469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000400454; ENSP00000383303; ENSG00000171587. [O60469-1]
GeneIDi1826.
KEGGihsa:1826.
UCSCiuc002yyq.2. human. [O60469-1]

Organism-specific databases

CTDi1826.
GeneCardsiDSCAM.
HGNCiHGNC:3039. DSCAM.
HPAiHPA019324.
MIMi602523. gene.
neXtProtiNX_O60469.
PharmGKBiPA27491.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQJM. Eukaryota.
ENOG410XQX7. LUCA.
GeneTreeiENSGT00760000118840.
HOVERGENiHBG051409.
InParanoidiO60469.
KOiK06767.
OMAiWTLDEDP.
OrthoDBiEOG7R830M.
PhylomeDBiO60469.
TreeFamiTF316846.

Enzyme and pathway databases

ReactomeiR-HSA-376172. DSCAM interactions.

Miscellaneous databases

ChiTaRSiDSCAM. human.
GenomeRNAii1826.
PROiO60469.
SOURCEiSearch...

Gene expression databases

BgeeiO60469.
CleanExiHS_DSCAM.
ExpressionAtlasiO60469. baseline and differential.
GenevisibleiO60469. HS.

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. 5 hits.
[Graphical view]
SMARTiSM00060. FN3. 6 hits.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00406. IGv. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 10 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 6 hits.
PS50835. IG_LIKE. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DSCAM: a novel member of the immunoglobulin superfamily maps in a Down syndrome region and is involved in the development of the nervous system."
    Yamakawa K., Huot Y.-K., Haendelt M.A., Hubert R., Chen X.-N., Lyons G.E., Korenberg J.R.
    Hum. Mol. Genet. 7:227-237(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain.
  2. "Down syndrome cell adhesion molecule DSCAM mediates homophilic intercellular adhesion."
    Agarwala K.L., Nakamura S., Tsutsumi Y., Yamakawa K.
    Brain Res. Mol. Brain Res. 79:118-126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    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: FUNCTION, INTERACTION WITH PAK1 AND RAC1.
  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.
  6. "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, INTERACTION WITH NTN1, PHOSPHORYLATION.

Entry informationi

Entry nameiDSCAM_HUMAN
AccessioniPrimary (citable) accession number: O60469
Secondary accession number(s): O60468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 6, 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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.