DCC_HUMAN - dbPTM
DCC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCC_HUMAN
UniProt AC P43146
Protein Name Netrin receptor DCC
Gene Name DCC
Organism Homo sapiens (Human).
Sequence Length 1447
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene..
Protein Sequence MENSLRCVWVPKLAFVLFGASLFSAHLQVTGFQIKAFTALRFLSEPSDAVTMRGGNVLLDCSAESDRGVPVIKWKKDGIHLALGMDERKQQLSNGSLLIQNILHSRHHKPDEGLYQCEASLGDSGSIISRTAKVAVAGPLRFLSQTESVTAFMGDTVLLKCEVIGEPMPTIHWQKNQQDLTPIPGDSRVVVLPSGALQISRLQPGDIGIYRCSARNPASSRTGNEAEVRILSDPGLHRQLYFLQRPSNVVAIEGKDAVLECCVSGYPPPSFTWLRGEEVIQLRSKKYSLLGGSNLLISNVTDDDSGMYTCVVTYKNENISASAELTVLVPPWFLNHPSNLYAYESMDIEFECTVSGKPVPTVNWMKNGDVVIPSDYFQIVGGSNLRILGVVKSDEGFYQCVAENEAGNAQTSAQLIVPKPAIPSSSVLPSAPRDVVPVLVSSRFVRLSWRPPAEAKGNIQTFTVFFSREGDNRERALNTTQPGSLQLTVGNLKPEAMYTFRVVAYNEWGPGESSQPIKVATQPELQVPGPVENLQAVSTSPTSILITWEPPAYANGPVQGYRLFCTEVSTGKEQNIEVDGLSYKLEGLKKFTEYSLRFLAYNRYGPGVSTDDITVVTLSDVPSAPPQNVSLEVVNSRSIKVSWLPPPSGTQNGFITGYKIRHRKTTRRGEMETLEPNNLWYLFTGLEKGSQYSFQVSAMTVNGTGPPSNWYTAETPENDLDESQVPDQPSSLHVRPQTNCIIMSWTPPLNPNIVVRGYIIGYGVGSPYAETVRVDSKQRYYSIERLESSSHYVISLKAFNNAGEGVPLYESATTRSITDPTDPVDYYPLLDDFPTSVPDLSTPMLPPVGVQAVALTHDAVRVSWADNSVPKNQKTSEVRLYTVRWRTSFSASAKYKSEDTTSLSYTATGLKPNTMYEFSVMVTKNRRSSTWSMTAHATTYEAAPTSAPKDLTVITREGKPRAVIVSWQPPLEANGKITAYILFYTLDKNIPIDDWIMETISGDRLTHQIMDLNLDTMYYFRIQARNSKGVGPLSDPILFRTLKVEHPDKMANDQGRHGDGGYWPVDTNLIDRSTLNEPPIGQMHPPHGSVTPQKNSNLLVIIVVTVGVITVLVVVIVAVICTRRSSAQQRKKRATHSAGKRKGSQKDLRPPDLWIHHEEMEMKNIEKPSGTDPAGRDSPIQSCQDLTPVSHSQSETQLGSKSTSHSGQDTEEAGSSMSTLERSLAARRAPRAKLMIPMDAQSNNPAVVSAIPVPTLESAQYPGILPSPTCGYPHPQFTLRPVPFPTLSVDRGFGAGRSQSVSEGPTTQQPPMLPPSQPEHSSSEEAPSRTIPTACVRPTHPLRSFANPLLPPPMSAIEPKVPYTPLLSQPGPTLPKTHVKTASLGLAGKARSPLLPVSVPTAPEVSEESHKPTEDSANVYEQDDLSEQMASLEGLMKQLNAITGSAF
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
94N-linked_GlycosylationERKQQLSNGSLLIQN
HHHHHHHCCCHHHHH		53.30UniProtKB CARBOHYD
115PhosphorylationHKPDEGLYQCEASLG
CCCCCCCEEEECCCC		23.2121214269
126PhosphorylationASLGDSGSIISRTAK
CCCCCCCCCCEEEEE		22.2424719451
129PhosphorylationGDSGSIISRTAKVAV
CCCCCCCEEEEEEEE		23.1621214269
156PhosphorylationVTAFMGDTVLLKCEV
EEEECCCEEEEEEEE		13.8123312004
287PhosphorylationIQLRSKKYSLLGGSN
EHHCCCCEEECCCCC		14.3226074081
288PhosphorylationQLRSKKYSLLGGSNL
HHCCCCEEECCCCCE		26.4626074081
293PhosphorylationKYSLLGGSNLLISNV
CEEECCCCCEEECCC		23.6226074081
298PhosphorylationGGSNLLISNVTDDDS
CCCCEEECCCCCCCC		25.8026074081
299N-linked_GlycosylationGSNLLISNVTDDDSG
CCCEEECCCCCCCCC		33.44UniProtKB CARBOHYD
301PhosphorylationNLLISNVTDDDSGMY
CEEECCCCCCCCCCE		37.6526074081
305PhosphorylationSNVTDDDSGMYTCVV
CCCCCCCCCCEEEEE		32.2426074081
308PhosphorylationTDDDSGMYTCVVTYK
CCCCCCCEEEEEEEE		10.6626074081
309PhosphorylationDDDSGMYTCVVTYKN
CCCCCCEEEEEEEEC		7.0226074081
313PhosphorylationGMYTCVVTYKNENIS
CCEEEEEEEECCCEE		14.3726074081
314PhosphorylationMYTCVVTYKNENISA
CEEEEEEEECCCEEE		10.5423532336
318N-linked_GlycosylationVVTYKNENISASAEL
EEEEECCCEEEEEEE		42.80UniProtKB CARBOHYD
374PhosphorylationNGDVVIPSDYFQIVG
CCCEECCCCCEEEEC		33.5428122231
376PhosphorylationDVVIPSDYFQIVGGS
CEECCCCCEEEECCC		11.1728122231
383PhosphorylationYFQIVGGSNLRILGV
CEEEECCCCEEEEEE		27.1128122231
441PhosphorylationDVVPVLVSSRFVRLS
CCEEEEEECCEEEEE		16.1924719451
448PhosphorylationSSRFVRLSWRPPAEA
ECCEEEEEECCCHHH		15.5224719451
478N-linked_GlycosylationDNRERALNTTQPGSL
CCCCEECCCCCCCCE		39.84UniProtKB CARBOHYD
479PhosphorylationNRERALNTTQPGSLQ
CCCEECCCCCCCCEE		27.88-
488PhosphorylationQPGSLQLTVGNLKPE
CCCCEEEEECCCCCC		17.26-
521PhosphorylationSQPIKVATQPELQVP
CCCEEEECCCCCCCC		47.87-
595PhosphorylationLKKFTEYSLRFLAYN
HHHHHHHHHHHHHHC		13.5624719451
628N-linked_GlycosylationVPSAPPQNVSLEVVN
CCCCCCCCEEEEEEC		30.99UniProtKB CARBOHYD
642PhosphorylationNSRSIKVSWLPPPSG
CCCCEEEEEECCCCC		20.21-
681PhosphorylationLEPNNLWYLFTGLEK
ECCCCCEEEEECCCC		8.6329083192
684PhosphorylationNNLWYLFTGLEKGSQ
CCCEEEEECCCCCCE		37.9629083192
702N-linked_GlycosylationQVSAMTVNGTGPPSN
EEEEEEECCCCCCCC		32.89UniProtKB CARBOHYD
723PhosphorylationPENDLDESQVPDQPS
CCCCCCHHHCCCCCC		35.8222210691
730PhosphorylationSQVPDQPSSLHVRPQ
HHCCCCCCCCEECCC		39.6422210691
731PhosphorylationQVPDQPSSLHVRPQT
HCCCCCCCCEECCCC		29.2222210691
795PhosphorylationSSSHYVISLKAFNNA
CCCEEEEEEEEECCC		17.4924719451
809PhosphorylationAGEGVPLYESATTRS
CCCCCCCCCCCCCCC		11.19-
811PhosphorylationEGVPLYESATTRSIT
CCCCCCCCCCCCCCC		19.84-
813PhosphorylationVPLYESATTRSITDP
CCCCCCCCCCCCCCC		31.83-
814PhosphorylationPLYESATTRSITDPT
CCCCCCCCCCCCCCC		23.33-
868PhosphorylationRVSWADNSVPKNQKT
EEECCCCCCCCCCCC		40.1019413330
881PhosphorylationKTSEVRLYTVRWRTS
CCCCEEEEEEEEEEC		7.82-
904PhosphorylationSEDTTSLSYTATGLK
CCCCCEEEEEECCCC		21.8722468782
906PhosphorylationDTTSLSYTATGLKPN
CCCEEEEEECCCCCC		17.8622468782
914PhosphorylationATGLKPNTMYEFSVM
ECCCCCCCEEEEEEE		29.6522468782
1034PhosphorylationSKGVGPLSDPILFRT
CCCCCCCCCCCEEEE		44.4627422710
1073PhosphorylationDTNLIDRSTLNEPPI
CCCCCCCCCCCCCCC		33.2318187866
1074PhosphorylationTNLIDRSTLNEPPIG
CCCCCCCCCCCCCCC		34.2018187866
1121S-palmitoylationVVIVAVICTRRSSAQ
HHHHHHHHCCCCHHH		1.6215811950
1142AcetylationTHSAGKRKGSQKDLR
HHHHHCCCCCCCCCC		67.417705767
1178PhosphorylationTDPAGRDSPIQSCQD
CCCCCCCCCCCCCCC		23.6527732954
1182PhosphorylationGRDSPIQSCQDLTPV
CCCCCCCCCCCCCCC		17.9227732954
1187PhosphorylationIQSCQDLTPVSHSQS
CCCCCCCCCCCCCCC		29.9027732954
1267PhosphorylationQYPGILPSPTCGYPH
CCCCCCCCCCCCCCC		29.42-
1278PhosphorylationGYPHPQFTLRPVPFP
CCCCCCCEEECCCCC		19.3324719451
1286PhosphorylationLRPVPFPTLSVDRGF
EECCCCCEEEEECCC		31.8527732954
1288PhosphorylationPVPFPTLSVDRGFGA
CCCCCEEEEECCCCC		25.1727732954
1306PhosphorylationQSVSEGPTTQQPPML
CCCCCCCCCCCCCCC		48.3622210691
1328PhosphorylationSSSEEAPSRTIPTAC
CCCCCCCCCCCCCCC		49.4522210691
1363PhosphorylationAIEPKVPYTPLLSQP
CCCCCCCCCCCCCCC		24.7918253061
1377PhosphorylationPGPTLPKTHVKTASL
CCCCCCCCCCEECCC		29.9321964256
1420PhosphorylationTEDSANVYEQDDLSE
CCCCCCCHHCCCHHH		14.0018253061
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
1178SPhosphorylationKinaseMAPK1P28482
Uniprot
1187TPhosphorylationKinaseMAPK1P28482
Uniprot
1267SPhosphorylationKinaseMAPK1P28482
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:9334332
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:9858595
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCC_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 DCC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANDR_HUMANARphysical
12864730
NET1_HUMANNTN1physical
12810718
CASP3_HUMANCASP3physical
11248093
MK03_HUMANMAPK3physical
11986622
MAZ_HUMANMAZphysical
11527412
SIAH1_HUMANSIAH1physical
9858595
DP13A_HUMANAPPL1physical
12011067
FAK1_HUMANPTK2physical
15494733
RL5_HUMANRPL5physical
20434207
EI2BB_HUMANEIF2B2physical
20434207
RL10A_HUMANRPL10Aphysical
20434207
RL23_HUMANRPL23physical
20434207
RL13_HUMANRPL13physical
20434207
IF2G_HUMANEIF2S3physical
20434207
EI2BD_HUMANEIF2B4physical
20434207
RL38_HUMANRPL38physical
20434207
RS24_HUMANRPS24physical
20434207
IF1AX_HUMANEIF1AXphysical
20434207
RS10_HUMANRPS10physical
20434207
RL28_HUMANRPL28physical
20434207
RS13_HUMANRPS13physical
20434207
IF5A2_HUMANEIF5A2physical
20434207
MK01_HUMANMAPK1physical
20434207
IF2B_HUMANEIF2S2physical
20434207
EIF3E_HUMANEIF3Ephysical
20434207
NET1_HUMANNTN1physical
20434207
EZRI_HUMANEZRphysical
20434207
EI2BA_HUMANEIF2B1physical
20434207
IF4E3_HUMANEIF4E3physical
20434207
FAK1_HUMANPTK2physical
20434207
RS6_HUMANRPS6physical
20434207
IF4E_HUMANEIF4Ephysical
20434207
EIF2A_HUMANEIF2Aphysical
20434207
RS4X_HUMANRPS4Xphysical
20434207
SIAH2_HUMANSIAH2physical
9334332
SINA_DROMEsinaphysical
9334332
Drug and Disease Associations
Kegg Disease
H00018 Gastric cancer
H00020 Colorectal cancer
H00044 Cancer of the anal canal
H01287 Congenital mirror movements (CMM)
OMIM Disease
157600Mirror movements 1 (MRMV1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073 AND THR-1074, ANDMASS SPECTROMETRY.

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