DSCAM_HUMAN - dbPTM
DSCAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DSCAM_HUMAN
UniProt AC O60469
Protein Name Down syndrome cell adhesion molecule
Gene Name DSCAM
Organism Homo sapiens (Human).
Sequence Length 2012
Subcellular Localization Isoform Short: Secreted .
Isoform Long: Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Cell junction, synapse . Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons.
Protein 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. [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]
Protein Sequence MWILALSLFQSFANVFSEDLHSSLYFVNASLQEVVFASTTGTLVPCPAAGIPPVTLRWYLATGEEIYDVPGIRHVHPNGTLQIFPFPPSSFSTLIHDNTYYCTAENPSGKIRSQDVHIKAVLREPYTVRVEDQKTMRGNVAVFKCIIPSSVEAYITVVSWEKDTVSLVSGSRFLITSTGALYIKDVQNEDGLYNYRCITRHRYTGETRQSNSARLFVSDPANSAPSILDGFDHRKAMAGQRVELPCKALGHPEPDYRWLKDNMPLELSGRFQKTVTGLLIENIRPSDSGSYVCEVSNRYGTAKVIGRLYVKQPLKATISPRKVKSSVGSQVSLSCSVTGTEDQELSWYRNGEILNPGKNVRITGINHENLIMDHMVKSDGGAYQCFVRKDKLSAQDYVQVVLEDGTPKIISAFSEKVVSPAEPVSLMCNVKGTPLPTITWTLDDDPILKGGSHRISQMITSEGNVVSYLNISSSQVRDGGVYRCTANNSAGVVLYQARINVRGPASIRPMKNITAIAGRDTYIHCRVIGYPYYSIKWYKNSNLLPFNHRQVAFENNGTLKLSDVQKEVDEGEYTCNVLVQPQLSTSQSVHVTVKVPPFIQPFEFPRFSIGQRVFIPCVVVSGDLPITITWQKDGRPIPGSLGVTIDNIDFTSSLRISNLSLMHNGNYTCIARNEAAAVEHQSQLIVRVPPKFVVQPRDQDGIYGKAVILNCSAEGYPVPTIVWKFSKGAGVPQFQPIALNGRIQVLSNGSLLIKHVVEEDSGYYLCKVSNDVGADVSKSMYLTVKIPAMITSYPNTTLATQGQKKEMSCTAHGEKPIIVRWEKEDRIINPEMARYLVSTKEVGEEVISTLQILPTVREDSGFFSCHAINSYGEDRGIIQLTVQEPPDPPEIEIKDVKARTITLRWTMGFDGNSPITGYDIECKNKSDSWDSAQRTKDVSPQLNSATIIDIHPSSTYSIRMYAKNRIGKSEPSNELTITADEAAPDGPPQEVHLEPISSQSIRVTWKAPKKHLQNGIIRGYQIGYREYSTGGNFQFNIISVDTSGDSEVYTLDNLNKFTQYGLVVQACNRAGTGPSSQEIITTTLEDVPSYPPENVQAIATSPESISISWSTLSKEALNGILQGFRVIYWANLMDGELGEIKNITTTQPSLELDGLEKYTNYSIQVLAFTRAGDGVRSEQIFTRTKEDVPGPPAGVKAAAASASMVFVSWLPPLKLNGIIRKYTVFCSHPYPTVISEFEASPDSFSYRIPNLSRNRQYSVWVVAVTSAGRGNSSEIITVEPLAKAPARILTFSGTVTTPWMKDIVLPCKAVGDPSPAVKWMKDSNGTPSLVTIDGRRSIFSNGSFIIRTVKAEDSGYYSCIANNNWGSDEIILNLQVQVPPDQPRLTVSKTTSSSITLSWLPGDNGGSSIRGYILQYSEDNSEQWGSFPISPSERSYRLENLKCGTWYKFTLTAQNGVGPGRISEIIEAKTLGKEPQFSKEQELFASINTTRVRLNLIGWNDGGCPITSFTLEYRPFGTTVWTTAQRTSLSKSYILYDLQEATWYELQMRVCNSAGCAEKQANFATLNYDGSTIPPLIKSVVQNEEGLTTNEGLKMLVTISCILVGVLLLFVLLLVVRRRRREQRLKRLRDAKSLAEMLMSKNTRTSDTLSKQQQTLRMHIDIPRAQLLIEERDTMETIDDRSTVLLTDADFGEAAKQKSLTVTHTVHYQSVSQATGPLVDVSDARPGTNPTTRRNAKAGPTARNRYASQWTLNRPHPTISAHTLTTDWRLPTPRAAGSVDKESDSYSVSPSQDTDRARSSMVSTESASSTYEELARAYEHAKMEEQLRHAKFTITECFISDTSSEQLTAGTNEYTDSLTSSTPSESGICRFTASPPKPQDGGRVMNMAVPKAHRPGDLIHLPPYLRMDFLLNRGGPGTSRDLSLGQACLEPQKSRTLKRPTVLEPIPMEAASSASSTREGQSWQPGAVATLPQREGAELGQAAKMSSSQESLLDSRGHLKGNNPYAKSYTLV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
28N-linked_GlycosylationHSSLYFVNASLQEVV
HHHHHEEECCCEEEE
17.57UniProtKB CARBOHYD
78N-linked_GlycosylationGIRHVHPNGTLQIFP
CCCEECCCCCEEEEE
41.00UniProtKB CARBOHYD
113PhosphorylationNPSGKIRSQDVHIKA
CCCCCCCCCCEEEEE
33.92-
119UbiquitinationRSQDVHIKAVLREPY
CCCCEEEEEEECCCE
19.98-
135PhosphorylationVRVEDQKTMRGNVAV
EEECCCCCCCCCEEE
13.38-
176PhosphorylationSGSRFLITSTGALYI
ECCEEEEECCCCEEE
23.5329083192
177PhosphorylationGSRFLITSTGALYIK
CCEEEEECCCCEEEE
20.1829083192
178PhosphorylationSRFLITSTGALYIKD
CEEEEECCCCEEEEE
20.1629083192
182PhosphorylationITSTGALYIKDVQNE
EECCCCEEEEECCCC
12.8529083192
274PhosphorylationLSGRFQKTVTGLLIE
ECHHHHHHEEEEEEE
16.7124043423
276PhosphorylationGRFQKTVTGLLIENI
HHHHHHEEEEEEECC
27.6124043423
414PhosphorylationPKIISAFSEKVVSPA
CCEEEECCCCCCCCC
35.9024719451
452PhosphorylationDPILKGGSHRISQMI
CCCCCCCCEEEEEEE
20.4723403867
456PhosphorylationKGGSHRISQMITSEG
CCCCEEEEEEEECCC
17.4123403867
460PhosphorylationHRISQMITSEGNVVS
EEEEEEEECCCCEEE
18.5123403867
461PhosphorylationRISQMITSEGNVVSY
EEEEEEECCCCEEEE
32.3623403867
467PhosphorylationTSEGNVVSYLNISSS
ECCCCEEEEEEECCC
21.4423403867
470N-linked_GlycosylationGNVVSYLNISSSQVR
CCEEEEEEECCCCEE
24.70UniProtKB CARBOHYD
485PhosphorylationDGGVYRCTANNSAGV
CCCEEEEECCCCCCE
24.3421712546
487N-linked_GlycosylationGVYRCTANNSAGVVL
CEEEEECCCCCCEEE
25.49UniProtKB CARBOHYD
495PhosphorylationNSAGVVLYQARINVR
CCCCEEEEEEEEECC
6.6321712546
512N-linked_GlycosylationASIRPMKNITAIAGR
CCCCCCCCEEEEECC
30.50UniProtKB CARBOHYD
530PhosphorylationIHCRVIGYPYYSIKW
EEEEECCCCEEEEEE
4.12-
532PhosphorylationCRVIGYPYYSIKWYK
EEECCCCEEEEEEEE
11.02-
533PhosphorylationRVIGYPYYSIKWYKN
EECCCCEEEEEEEEC
10.22-
534PhosphorylationVIGYPYYSIKWYKNS
ECCCCEEEEEEEECC
16.3224719451
556N-linked_GlycosylationRQVAFENNGTLKLSD
CEEEEECCCEEEEHH
37.31UniProtKB CARBOHYD
560AcetylationFENNGTLKLSDVQKE
EECCCEEEEHHHEEE
45.877934559
658N-linked_GlycosylationTSSLRISNLSLMHNG
CCCEEECCEEEEECC
31.14UniProtKB CARBOHYD
666N-linked_GlycosylationLSLMHNGNYTCIARN
EEEEECCCEEEEEEC
33.97UniProtKB CARBOHYD
703PhosphorylationPRDQDGIYGKAVILN
CCCCCCCCCEEEEEE
20.36-
710N-linked_GlycosylationYGKAVILNCSAEGYP
CCEEEEEECCCCCCC
13.43UniProtKB CARBOHYD
748N-linked_GlycosylationGRIQVLSNGSLLIKH
CEEEEEECCCEEEEE
39.65UniProtKB CARBOHYD
769PhosphorylationGYYLCKVSNDVGADV
CEEEEEEECCCCCCC
16.89-
781PhosphorylationADVSKSMYLTVKIPA
CCCCHHCEEEEEECE
13.3021214269
793PhosphorylationIPAMITSYPNTTLAT
ECEEEECCCCCEECC
7.5826503892
795N-linked_GlycosylationAMITSYPNTTLATQG
EEEECCCCCEECCCC
37.15UniProtKB CARBOHYD
796PhosphorylationMITSYPNTTLATQGQ
EEECCCCCEECCCCC
20.7726503892
797PhosphorylationITSYPNTTLATQGQK
EECCCCCEECCCCCC
22.4921214269
848PhosphorylationEVGEEVISTLQILPT
HHHHHHHHHHEECCC
28.39-
860PhosphorylationLPTVREDSGFFSCHA
CCCCCCCCCCEEEEE
32.52-
864PhosphorylationREDSGFFSCHAINSY
CCCCCCEEEEEECCC
11.6128634120
870PhosphorylationFSCHAINSYGEDRGI
EEEEEECCCCCCCEE
28.5328634120
924N-linked_GlycosylationGYDIECKNKSDSWDS
EEEEEECCCCCCCCC
61.80UniProtKB CARBOHYD
928PhosphorylationECKNKSDSWDSAQRT
EECCCCCCCCCHHHH
39.6130576142
931PhosphorylationNKSDSWDSAQRTKDV
CCCCCCCCHHHHCCC
21.75-
935PhosphorylationSWDSAQRTKDVSPQL
CCCCHHHHCCCCCCC
21.37-
957PhosphorylationIHPSSTYSIRMYAKN
ECCCCCCEEEEEEEC
12.1024719451
1142N-linked_GlycosylationGELGEIKNITTTQPS
CCCCCEECCEECCCC
42.36UniProtKB CARBOHYD
1160N-linked_GlycosylationDGLEKYTNYSIQVLA
CCHHHCCCCEEEEEE
26.01UniProtKB CARBOHYD
1222PhosphorylationLNGIIRKYTVFCSHP
ECCEEEEEEEECCCC
9.7828634298
1223PhosphorylationNGIIRKYTVFCSHPY
CCEEEEEEEECCCCC
15.3328634298
1227PhosphorylationRKYTVFCSHPYPTVI
EEEEEECCCCCCEEE
18.9428634298
1230PhosphorylationTVFCSHPYPTVISEF
EEECCCCCCEEEEEE
13.2028634298
1232PhosphorylationFCSHPYPTVISEFEA
ECCCCCCEEEEEEEC
25.3228634298
1235PhosphorylationHPYPTVISEFEASPD
CCCCEEEEEEECCCC
31.7128634298
1240PhosphorylationVISEFEASPDSFSYR
EEEEEECCCCCCEEE
23.2628634298
1243PhosphorylationEFEASPDSFSYRIPN
EEECCCCCCEEECCC
21.3428634298
1245PhosphorylationEASPDSFSYRIPNLS
ECCCCCCEEECCCCC
19.9028634298
1246PhosphorylationASPDSFSYRIPNLSR
CCCCCCEEECCCCCC
15.5628634298
1250N-linked_GlycosylationSFSYRIPNLSRNRQY
CCEEECCCCCCCCCE
48.56UniProtKB CARBOHYD
1271N-linked_GlycosylationVTSAGRGNSSEIITV
EEECCCCCCCCEEEE
40.79UniProtKB CARBOHYD
1323PhosphorylationAVKWMKDSNGTPSLV
HHHCEECCCCCCCEE
31.4730576142
1326PhosphorylationWMKDSNGTPSLVTID
CEECCCCCCCEEEEC
17.6030576142
1341N-linked_GlycosylationGRRSIFSNGSFIIRT
CCEEECCCCCEEEEE
39.10UniProtKB CARBOHYD
1343PhosphorylationRSIFSNGSFIIRTVK
EEECCCCCEEEEEEE
19.9530576142
1463PhosphorylationGVGPGRISEIIEAKT
CCCCCHHHHHHHHHC
22.7622210691
1488N-linked_GlycosylationQELFASINTTRVRLN
HHHHHHCCCCEEEEE
32.66UniProtKB CARBOHYD
1640PhosphorylationSLAEMLMSKNTRTSD
HHHHHHHCCCCCCCH
20.8423403867
1641 (in isoform 1)Ubiquitination-48.6621906983
1641UbiquitinationLAEMLMSKNTRTSDT
HHHHHHCCCCCCCHH
48.662190698
1643PhosphorylationEMLMSKNTRTSDTLS
HHHHCCCCCCCHHHH
38.7823403867
1644MethylationMLMSKNTRTSDTLSK
HHHCCCCCCCHHHHH
41.44-
1645PhosphorylationLMSKNTRTSDTLSKQ
HHCCCCCCCHHHHHH
28.9928270605
1646PhosphorylationMSKNTRTSDTLSKQQ
HCCCCCCCHHHHHHH
25.8828270605
1648PhosphorylationKNTRTSDTLSKQQQT
CCCCCCHHHHHHHHH
32.4728270605
1650PhosphorylationTRTSDTLSKQQQTLR
CCCCHHHHHHHHHHH
30.4328270605
1803PhosphorylationRARSSMVSTESASST
HHHHHCCCCHHHHHH
20.16-
1891UbiquitinationVMNMAVPKAHRPGDL
EEEEECCCCCCCCCC
50.67-
1904PhosphorylationDLIHLPPYLRMDFLL
CCCCCCCCCCHHHHH
12.6622210691
1936PhosphorylationLEPQKSRTLKRPTVL
CCCCCCCCCCCCCEE
43.66-
1941PhosphorylationSRTLKRPTVLEPIPM
CCCCCCCCEEECCCH
41.58-
1953PhosphorylationIPMEAASSASSTREG
CCHHHHCCCCCCCCC
27.6922210691
1956PhosphorylationEAASSASSTREGQSW
HHHCCCCCCCCCCCC
31.0622210691
1986PhosphorylationLGQAAKMSSSQESLL
HHHHHHCCCCHHHHH
26.5724719451
1988PhosphorylationQAAKMSSSQESLLDS
HHHHCCCCHHHHHHC
30.57-
2005PhosphorylationHLKGNNPYAKSYTLV
CCCCCCCCCCCEEEC
28.8724719451
2008PhosphorylationGNNPYAKSYTLV---
CCCCCCCCEEEC---
18.3822210691
2009PhosphorylationNNPYAKSYTLV----
CCCCCCCEEEC----
11.9122210691
2010PhosphorylationNPYAKSYTLV-----
CCCCCCEEEC-----
28.3024719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DSCAM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DSCAM_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DSCAM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DSCAM_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DSCAM_HUMAN

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Related Literatures of Post-Translational Modification

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