Tag | Content |
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CPLM ID | CPLM-000939 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Down syndrome cell adhesion molecule |
Protein Synonyms/Alias | CHD2 |
Gene Name | DSCAM |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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1641 | LAEMLMSKNTRTSDT | ubiquitination | [1] |
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Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | 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. 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. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38. |
Sequence Annotation | DOMAIN 39 129 Ig-like C2-type 1. DOMAIN 125 216 Ig-like C2-type 2. DOMAIN 225 305 Ig-like C2-type 3. DOMAIN 313 401 Ig-like C2-type 4. DOMAIN 407 500 Ig-like C2-type 5. DOMAIN 504 592 Ig-like C2-type 6. DOMAIN 596 685 Ig-like C2-type 7. DOMAIN 690 783 Ig-like C2-type 8. DOMAIN 787 883 Ig-like C2-type 9. DOMAIN 885 978 Fibronectin type-III 1. DOMAIN 984 1082 Fibronectin type-III 2. DOMAIN 1088 1183 Fibronectin type-III 3. DOMAIN 1189 1279 Fibronectin type-III 4. DOMAIN 1285 1377 Ig-like C2-type 10. DOMAIN 1376 1470 Fibronectin type-III 5. DOMAIN 1476 1566 Fibronectin type-III 6. CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). CARBOHYD 470 470 N-linked (GlcNAc...) (Potential). CARBOHYD 487 487 N-linked (GlcNAc...) (Potential). CARBOHYD 512 512 N-linked (GlcNAc...) (Potential). CARBOHYD 556 556 N-linked (GlcNAc...) (Potential). CARBOHYD 658 658 N-linked (GlcNAc...) (Potential). CARBOHYD 666 666 N-linked (GlcNAc...) (Potential). CARBOHYD 710 710 N-linked (GlcNAc...) (Potential). CARBOHYD 748 748 N-linked (GlcNAc...) (Potential). CARBOHYD 795 795 N-linked (GlcNAc...) (Potential). CARBOHYD 924 924 N-linked (GlcNAc...) (Potential). CARBOHYD 1142 1142 N-linked (GlcNAc...) (Potential). CARBOHYD 1160 1160 N-linked (GlcNAc...) (Potential). CARBOHYD 1250 1250 N-linked (GlcNAc...) (Potential). CARBOHYD 1271 1271 N-linked (GlcNAc...) (Potential). CARBOHYD 1341 1341 N-linked (GlcNAc...) (Potential). CARBOHYD 1488 1488 N-linked (GlcNAc...) (Potential). DISULFID 46 102 By similarity. DISULFID 145 197 By similarity. DISULFID 246 293 By similarity. DISULFID 335 385 By similarity. DISULFID 428 484 By similarity. DISULFID 525 575 By similarity. DISULFID 617 669 By similarity. DISULFID 711 766 By similarity. DISULFID 809 865 By similarity. DISULFID 1307 1359 By similarity. |
Keyword | Alternative splicing; Cell adhesion; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2012 AA |
Protein Sequence | MWILALSLFQ SFANVFSEDL HSSLYFVNAS LQEVVFASTT GTLVPCPAAG IPPVTLRWYL 60 ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY YCTAENPSGK IRSQDVHIKA 120 VLREPYTVRV EDQKTMRGNV AVFKCIIPSS VEAYITVVSW EKDTVSLVSG SRFLITSTGA 180 LYIKDVQNED GLYNYRCITR HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ 240 RVELPCKALG HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENIRPSDSGS YVCEVSNRYG 300 TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGT EDQELSWYRN GEILNPGKNV 360 RITGINHENL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV VLEDGTPKII SAFSEKVVSP 420 AEPVSLMCNV KGTPLPTITW TLDDDPILKG GSHRISQMIT SEGNVVSYLN ISSSQVRDGG 480 VYRCTANNSA GVVLYQARIN VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN 540 SNLLPFNHRQ VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ 600 PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPGS LGVTIDNIDF TSSLRISNLS 660 LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD GIYGKAVILN CSAEGYPVPT 720 IVWKFSKGAG VPQFQPIALN GRIQVLSNGS LLIKHVVEED SGYYLCKVSN DVGADVSKSM 780 YLTVKIPAMI TSYPNTTLAT QGQKKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK 840 EVGEEVISTL QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART 900 ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI HPSSTYSIRM 960 YAKNRIGKSE PSNELTITAD EAAPDGPPQE VHLEPISSQS IRVTWKAPKK HLQNGIIRGY 1020 QIGYREYSTG GNFQFNIISV DTSGDSEVYT LDNLNKFTQY GLVVQACNRA GTGPSSQEII 1080 TTTLEDVPSY PPENVQAIAT SPESISISWS TLSKEALNGI LQGFRVIYWA NLMDGELGEI 1140 KNITTTQPSL ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA 1200 SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN LSRNRQYSVW 1260 VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM KDIVLPCKAV GDPSPAVKWM 1320 KDSNGTPSLV TIDGRRSIFS NGSFIIRTVK AEDSGYYSCI ANNNWGSDEI ILNLQVQVPP 1380 DQPRLTVSKT TSSSITLSWL PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN 1440 LKCGTWYKFT LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN 1500 DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV CNSAGCAEKQ 1560 ANFATLNYDG STIPPLIKSV VQNEEGLTTN EGLKMLVTIS CILVGVLLLF VLLLVVRRRR 1620 REQRLKRLRD AKSLAEMLMS KNTRTSDTLS KQQQTLRMHI DIPRAQLLIE ERDTMETIDD 1680 RSTVLLTDAD FGEAAKQKSL TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP 1740 TARNRYASQW TLNRPHPTIS AHTLTTDWRL PTPRAAGSVD KESDSYSVSP SQDTDRARSS 1800 MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG TNEYTDSLTS 1860 STPSESGICR FTASPPKPQD GGRVMNMAVP KAHRPGDLIH LPPYLRMDFL LNRGGPGTSR 1920 DLSLGQACLE PQKSRTLKRP TVLEPIPMEA ASSASSTREG QSWQPGAVAT LPQREGAELG 1980 QAAKMSSSQE SLLDSRGHLK GNNPYAKSYT LV 2012 |
Gene Ontology | GO:0030424; C:axon; ISS:UniProtKB. GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. GO:0030426; C:growth cone; ISS:UniProtKB. GO:0005887; C:integral to plasma membrane; TAS:ProtInc. GO:0007155; P:cell adhesion; TAS:ProtInc. GO:0048813; P:dendrite morphogenesis; IEA:Compara. GO:0070593; P:dendrite self-avoidance; ISS:UniProtKB. GO:0007626; P:locomotory behavior; IEA:Compara. GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB. GO:0048842; P:positive regulation of axon extension involved in axon guidance; IDA:UniProtKB. GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB. GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IEA:Compara. |
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