CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
1641LAEMLMSKNTRTSDTubiquitination[1]
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. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR013098; Ig_I-set.
 IPR003599; Ig_sub.
 IPR003598; Ig_sub2. 
Pfam
 PF00041; fn3
 PF07679; I-set 
SMART
 SM00060; FN3
 SM00409; IG
 SM00408; IGc2 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE 
PRINTS