DCBD2_HUMAN - dbPTM
DCBD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCBD2_HUMAN
UniProt AC Q96PD2
Protein Name Discoidin, CUB and LCCL domain-containing protein 2
Gene Name DCBLD2
Organism Homo sapiens (Human).
Sequence Length 775
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MASRAVVRARRCPQCPQVRAAAAAPAWAALPLSRSLPPCSNSSSFSMPLFLLLLLVLLLLLEDAGAQQGDGCGHTVLGPESGTLTSINYPQTYPNSTVCEWEIRVKMGERVRIKFGDFDIEDSDSCHFNYLRIYNGIGVSRTEIGKYCGLGLQMNHSIESKGNEITLLFMSGIHVSGRGFLASYSVIDKQDLITCLDTASNFLEPEFSKYCPAGCLLPFAEISGTIPHGYRDSSPLCMAGVHAGVVSNTLGGQISVVISKGIPYYESSLANNVTSVVGHLSTSLFTFKTSGCYGTLGMESGVIADPQITASSVLEWTDHTGQENSWKPKKARLKKPGPPWAAFATDEYQWLQIDLNKEKKITGIITTGSTMVEHNYYVSAYRILYSDDGQKWTVYREPGVEQDKIFQGNKDYHQDVRNNFLPPIIARFIRVNPTQWQQKIAMKMELLGCQFIPKGRPPKLTQPPPPRNSNDLKNTTAPPKIAKGRAPKFTQPLQPRSSNEFPAQTEQTTASPDIRNTTVTPNVTKDVALAAVLVPVLVMVLTTLILILVCAWHWRNRKKKTEGTYDLPYWDRAGWWKGMKQFLPAKAVDHEETPVRYSSSEVNHLSPREVTTVLQADSAEYAQPLVGGIVGTLHQRSTFKPEEGKEAGYADLDPYNSPGQEVYHAYAEPLPITGPEYATPIIMDMSGHPTTSVGQPSTSTFKATGNQPPPLVGTYNTLLSRTDSCSSAQAQYDTPKAGKPGLPAPDELVYQVPQSTQEVSGAGRDGECDVFKEIL
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
3Phosphorylation-----MASRAVVRAR
-----CCCHHHHHHH		21.34-
35PhosphorylationAALPLSRSLPPCSNS
HHCCCCCCCCCCCCC		41.68-
95N-linked_GlycosylationNYPQTYPNSTVCEWE
ECCCCCCCCCEEEEE		39.64UniProtKB CARBOHYD
134PhosphorylationHFNYLRIYNGIGVSR
CCEEEEEECCCCCCH		10.8218083107
155N-linked_GlycosylationCGLGLQMNHSIESKG
CCCCCCCCCCCCCCC		16.88UniProtKB CARBOHYD
272N-linked_GlycosylationYESSLANNVTSVVGH
HHHHHHHCCHHHHHH		32.60UniProtKB CARBOHYD
315UbiquitinationITASSVLEWTDHTGQ
EEHHHEEEECCCCCC		46.2927667366
328UbiquitinationGQENSWKPKKARLKK
CCCCCCCCCCCCCCC		36.8027667366
334UbiquitinationKPKKARLKKPGPPWA
CCCCCCCCCCCCCCH		51.9027667366
345PhosphorylationPPWAAFATDEYQWLQ
CCCHHEECCCCEEEE		23.9426074081
348PhosphorylationAAFATDEYQWLQIDL
HHEECCCCEEEEEEC		14.0626074081
360UbiquitinationIDLNKEKKITGIITT
EECCCCCCEEEEEEC		46.74-
363UbiquitinationNKEKKITGIITTGST
CCCCCEEEEEECCCC		16.8723503661
366PhosphorylationKKITGIITTGSTMVE
CCEEEEEECCCCHHC		24.16-
367UbiquitinationKITGIITTGSTMVEH
CEEEEEECCCCHHCC		20.8023503661
391UbiquitinationLYSDDGQKWTVYREP
EECCCCCEEEEEECC		50.8121906983
391 (in isoform 1)Ubiquitination-50.8121890473
391 (in isoform 2)Ubiquitination-50.8121890473
397UbiquitinationQKWTVYREPGVEQDK
CEEEEEECCCCCCCC		28.8127667366
404UbiquitinationEPGVEQDKIFQGNKD
CCCCCCCCCCCCCCC		45.1521906983
404 (in isoform 1)Ubiquitination-45.1521890473
404 (in isoform 2)Ubiquitination-45.1521890473
410AcetylationDKIFQGNKDYHQDVR
CCCCCCCCCHHHHHH		67.5020167786
410UbiquitinationDKIFQGNKDYHQDVR
CCCCCCCCCHHHHHH		67.5021906983
410 (in isoform 1)Ubiquitination-67.5021890473
410 (in isoform 2)Ubiquitination-67.5021890473
412UbiquitinationIFQGNKDYHQDVRNN
CCCCCCCHHHHHHHC		11.7327667366
439UbiquitinationNPTQWQQKIAMKMEL
CCHHHHHHHHHHHHH		19.8221906983
439 (in isoform 1)Ubiquitination-19.8221890473
439 (in isoform 2)Ubiquitination-19.8221890473
443UbiquitinationWQQKIAMKMELLGCQ
HHHHHHHHHHHHCCE		21.8723503661
454AcetylationLGCQFIPKGRPPKLT
HCCEECCCCCCCCCC		63.847927387
461PhosphorylationKGRPPKLTQPPPPRN
CCCCCCCCCCCCCCC		45.1923403867
473UbiquitinationPRNSNDLKNTTAPPK
CCCCCCCCCCCCCCC		55.9321906983
473 (in isoform 1)Ubiquitination-55.9321890473
473 (in isoform 2)Ubiquitination-55.9321890473
474N-linked_GlycosylationRNSNDLKNTTAPPKI
CCCCCCCCCCCCCCC		50.38UniProtKB CARBOHYD
480UbiquitinationKNTTAPPKIAKGRAP
CCCCCCCCCCCCCCC		54.9927667366
482UbiquitinationTTAPPKIAKGRAPKF
CCCCCCCCCCCCCCC		17.8723503661
483UbiquitinationTAPPKIAKGRAPKFT
CCCCCCCCCCCCCCC		53.0223503661
484UbiquitinationAPPKIAKGRAPKFTQ
CCCCCCCCCCCCCCC		23.2027667366
488UbiquitinationIAKGRAPKFTQPLQP
CCCCCCCCCCCCCCC		61.1227667366
490O-linked_GlycosylationKGRAPKFTQPLQPRS
CCCCCCCCCCCCCCC		35.0955833799
497PhosphorylationTQPLQPRSSNEFPAQ
CCCCCCCCCCCCCCC		44.1728634120
498PhosphorylationQPLQPRSSNEFPAQT
CCCCCCCCCCCCCCC		41.4828634120
501UbiquitinationQPRSSNEFPAQTEQT
CCCCCCCCCCCCCCC		7.7023000965
504UbiquitinationSSNEFPAQTEQTTAS
CCCCCCCCCCCCCCC		45.8923000965
505PhosphorylationSNEFPAQTEQTTASP
CCCCCCCCCCCCCCC		31.9728634120
510UbiquitinationAQTEQTTASPDIRNT
CCCCCCCCCCCCCCC		23.5823000965
516N-linked_GlycosylationTASPDIRNTTVTPNV
CCCCCCCCCCCCCCC		40.20UniProtKB CARBOHYD
517O-linked_GlycosylationASPDIRNTTVTPNVT
CCCCCCCCCCCCCCC		16.88OGP
522N-linked_GlycosylationRNTTVTPNVTKDVAL
CCCCCCCCCCHHHHH		44.73UniProtKB CARBOHYD
558UbiquitinationAWHWRNRKKKTEGTY
HHHHHCCCCCCCCCC		63.2723503661
559UbiquitinationWHWRNRKKKTEGTYD
HHHHCCCCCCCCCCC		62.7923503661
560UbiquitinationHWRNRKKKTEGTYDL
HHHCCCCCCCCCCCC		55.6421906983
560 (in isoform 1)Ubiquitination-55.6421890473
560 (in isoform 2)Ubiquitination-55.6421890473
561PhosphorylationWRNRKKKTEGTYDLP
HHCCCCCCCCCCCCC		48.8328152594
564PhosphorylationRKKKTEGTYDLPYWD
CCCCCCCCCCCCCHH		13.9725884760
564UbiquitinationRKKKTEGTYDLPYWD
CCCCCCCCCCCCCHH		13.9727667366
564 (in isoform 2)Phosphorylation-13.9727642862
565PhosphorylationKKKTEGTYDLPYWDR
CCCCCCCCCCCCHHC		26.7527273156
565 (in isoform 2)Phosphorylation-26.7527642862
569PhosphorylationEGTYDLPYWDRAGWW
CCCCCCCCHHCCCHH		27.5225884760
569 (in isoform 2)Phosphorylation-27.5227642862
577UbiquitinationWDRAGWWKGMKQFLP
HHCCCHHHHHHHHCC		42.4923000965
577 (in isoform 1)Ubiquitination-42.4921890473
580UbiquitinationAGWWKGMKQFLPAKA
CCHHHHHHHHCCCCC		46.7123000965
580 (in isoform 1)Ubiquitination-46.7121890473
586UbiquitinationMKQFLPAKAVDHEET
HHHHCCCCCCCCCCC		47.1823000965
586 (in isoform 1)Ubiquitination-47.1821890473
593PhosphorylationKAVDHEETPVRYSSS
CCCCCCCCCCCCCCC		24.8929255136
594 (in isoform 2)Ubiquitination-16.3321890473
597PhosphorylationHEETPVRYSSSEVNH
CCCCCCCCCCCCCCC		17.0927273156
598PhosphorylationEETPVRYSSSEVNHL
CCCCCCCCCCCCCCC		19.4723927012
599PhosphorylationETPVRYSSSEVNHLS
CCCCCCCCCCCCCCC		22.9127273156
600PhosphorylationTPVRYSSSEVNHLSP
CCCCCCCCCCCCCCH		39.3623927012
600 (in isoform 2)Ubiquitination-39.3621890473
606PhosphorylationSSEVNHLSPREVTTV
CCCCCCCCHHHEEEE		17.8526846344
611PhosphorylationHLSPREVTTVLQADS
CCCHHHEEEEEECCC		13.3626356563
611 (in isoform 2)Phosphorylation-13.3627642862
612PhosphorylationLSPREVTTVLQADSA
CCHHHEEEEEECCCH		25.1326356563
618PhosphorylationTTVLQADSAEYAQPL
EEEEECCCHHHHHHH		26.4728796482
621PhosphorylationLQADSAEYAQPLVGG
EECCCHHHHHHHHHH		15.3927273156
632PhosphorylationLVGGIVGTLHQRSTF
HHHHHHHHHHCCCCC		15.3529255136
635 (in isoform 2)Phosphorylation-44.1027642862
640UbiquitinationLHQRSTFKPEEGKEA
HHCCCCCCCCCCCCC		52.1621906983
640 (in isoform 1)Ubiquitination-52.1621890473
646 (in isoform 2)Phosphorylation-59.1727642862
649PhosphorylationEEGKEAGYADLDPYN
CCCCCCCCCCCCCCC		12.1825884760
654 (in isoform 2)Ubiquitination-37.1921890473
655PhosphorylationGYADLDPYNSPGQEV
CCCCCCCCCCCCCEE		28.1225884760
657PhosphorylationADLDPYNSPGQEVYH
CCCCCCCCCCCEEEE		25.27-
660UbiquitinationDPYNSPGQEVYHAYA
CCCCCCCCEEEEEEC		40.1323503661
663PhosphorylationNSPGQEVYHAYAEPL
CCCCCEEEEEECCCC		4.6820736484
663UbiquitinationNSPGQEVYHAYAEPL
CCCCCEEEEEECCCC		4.6823503661
666PhosphorylationGQEVYHAYAEPLPIT
CCEEEEEECCCCCCC		9.7420736484
677PhosphorylationLPITGPEYATPIIMD
CCCCCCCCCCCEEEE		20.93-
679PhosphorylationITGPEYATPIIMDMS
CCCCCCCCCEEEECC		17.70-
704PhosphorylationSTSTFKATGNQPPPL
CCCCEECCCCCCCCC		36.9422199227
714PhosphorylationQPPPLVGTYNTLLSR
CCCCCEEEHHHHHHC		13.2021945579
715PhosphorylationPPPLVGTYNTLLSRT
CCCCEEEHHHHHHCC		10.5421945579
717PhosphorylationPLVGTYNTLLSRTDS
CCEEEHHHHHHCCCC		20.7521945579
718 (in isoform 2)Phosphorylation-3.4927642862
720PhosphorylationGTYNTLLSRTDSCSS
EEHHHHHHCCCCCCC		35.9321945579
722PhosphorylationYNTLLSRTDSCSSAQ
HHHHHHCCCCCCCCC		28.9622617229
724PhosphorylationTLLSRTDSCSSAQAQ
HHHHCCCCCCCCCCC		18.4525159151
726PhosphorylationLSRTDSCSSAQAQYD
HHCCCCCCCCCCCCC		32.4322617229
727PhosphorylationSRTDSCSSAQAQYDT
HCCCCCCCCCCCCCC		28.8222617229
728 (in isoform 2)Phosphorylation-7.7627642862
729 (in isoform 2)Phosphorylation-30.8327642862
731 (in isoform 2)Phosphorylation-25.2627642862
732PhosphorylationCSSAQAQYDTPKAGK
CCCCCCCCCCCCCCC		25.4627273156
734PhosphorylationSAQAQYDTPKAGKPG
CCCCCCCCCCCCCCC		23.0428102081
734 (in isoform 2)Phosphorylation-23.0427642862
736UbiquitinationQAQYDTPKAGKPGLP
CCCCCCCCCCCCCCC		72.3833845483
736 (in isoform 2)Phosphorylation-72.3827642862
738 (in isoform 2)Phosphorylation-42.7027642862
739UbiquitinationYDTPKAGKPGLPAPD
CCCCCCCCCCCCCCH		40.5533845483
739 (in isoform 1)Ubiquitination-40.5521890473
740 (in isoform 2)Phosphorylation-48.9427642862
741 (in isoform 2)Phosphorylation-48.0227642862
746 (in isoform 2)Phosphorylation-65.0627642862
748 (in isoform 2)Phosphorylation-5.9127642862
749PhosphorylationLPAPDELVYQVPQST
CCCCHHHEEECCCCC		2.7117016520
750PhosphorylationPAPDELVYQVPQSTQ
CCCHHHEEECCCCCC		19.2027273156
753 (in isoform 2)Ubiquitination-13.5921890473
755PhosphorylationLVYQVPQSTQEVSGA
HEEECCCCCCCCCCC		26.4528152594
756PhosphorylationVYQVPQSTQEVSGAG
EEECCCCCCCCCCCC		24.4128152594
760PhosphorylationPQSTQEVSGAGRDGE
CCCCCCCCCCCCCCC		23.3626356563
764 (in isoform 2)Phosphorylation-48.5027642862
774 (in isoform 2)Phosphorylation-5.9627642862
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
565YPhosphorylationKinaseFYNP06241
PSP
621YPhosphorylationKinaseFYNP06241
PSP
655YPhosphorylationKinaseFYNP06241
PSP
666YPhosphorylationKinaseFYNP06241
PSP
677YPhosphorylationKinaseFYNP06241
PSP
732YPhosphorylationKinaseFYNP06241
PSP
750YPhosphorylationKinaseFYNP06241
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCBD2_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 DCBD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF6_HUMANTRAF6physical
25061874
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 DCBD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-715 AND TYR-732, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-750, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-750, AND MASSSPECTROMETRY.

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