ROBO3_HUMAN - dbPTM
ROBO3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROBO3_HUMAN
UniProt AC Q96MS0
Protein Name Roundabout homolog 3
Gene Name ROBO3
Organism Homo sapiens (Human).
Sequence Length 1386
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1 (By similarity). Required for hindbrain axon midline crossing..
Protein Sequence MLRYLLKTLLQMNLFADSLAGDISNSSELLLGFNSSLAALNHTLLPPGDPSLNGSRVGPEDAMPRIVEQPPDLLVSRGEPATLPCRAEGRPRPNIEWYKNGARVATVREDPRAHRLLLPSGALFFPRIVHGRRARPDEGVYTCVARNYLGAAASRNASLEVAVLRDDFRQSPGNVVVAVGEPAVLECVPPRGHPEPSVSWRKDGARLKEEEGRITIRGGKLMMSHTLKSDAGMYVCVASNMAGERESAAAEVMVLERPSFLRRPVNQVVLADAPVTFLCEVKGDPPPRLRWRKEDGELPTGRYEIRSDHSLWIGHVSAEDEGTYTCVAENSVGRAEASGSLSVHVPPQLVTQPQDQMAAPGESVAFQCETKGNPPPAIFWQKEGSQVLLFPSQSLQPTGRFSVSPRGQLNITAVQRGDAGYYVCQAVSVAGSILAKALLEIKGASLDGLPPVILQGPANQTLVLGSSVWLPCRVTGNPQPSVRWKKDGQWLQGDDLQFKTMANGTLYIANVQEMDMGFYSCVAKSSTGEATWSGWLKMREDWGVSPDPPTEPSSPPGAPSQPVVTEITKNSITLTWKPNPQTGAAVTSYVIEAFSPAAGNTWRTVADGVQLETHTVSGLQPNTIYLFLVRAVGAWGLSEPSPVSEPVRTQDSSPSRPVEDPWRGQQGLAEVAVRLQEPIVLGPRTLQVSWTVDGPVQLVQGFRVSWRVAGPEGGSWTMLDLQSPSQQSTVLRGLPPGTQIQIKVQAQGQEGLGAESLSVTRSIPEEAPSGPPQGVAVALGGDGNSSITVSWEPPLPSQQNGVITEYQIWCLGNESRFHLNRSAAGWARSAMLRGLVPGLLYRTLVAAATSAGVGVPSAPVLVQLPSPPDLEPGLEVGAGLAVRLARVLREPAFLAGSGAACGALLLGLCAALYWRRKQRKELSHYTASFAYTPAVSFPHSEGLSGASSRPPMGLGPAPYSWLADSWPHPSRSPSAQEPRGSCCPSNPDPDDRYYNEAGISLYLAQTARGTAAPGEGPVYSTIDPAGEELQTFHGGFPQHPSGDLGPWSQYAPPEWSQGDSGAKGGKVKLLGKPVQMPSLNWPEALPPPPPSCELSCLEGPEEELEGSSEPEEWCPPMPERSHLTEPSSSGGCLVTPSRRETPSPTPSYGQQSTATLTPSPPDPPQPPTDMPHLHQMPRRVPLGPSSPLSVSQPMLGIREARPAGLGAGPAASPHLSPSPAPSTASSAPGRTWQGNGEMTPPLQGPRARFRKKPKALPYRRENSPGDLPPPPLPPPEEEASWALELRAAGSMSSLERERSGERKAVQAVPLAAQRVLHPDEEAWLPYSRPSFLSRGQGTSTCSTAGSNSSRGSSSSRGSRGPGRSRSRSQSRSQSQRPGQKRREEPR
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
25N-linked_GlycosylationSLAGDISNSSELLLG
HHCCCCCCCHHHHHH		50.30UniProtKB CARBOHYD
34N-linked_GlycosylationSELLLGFNSSLAALN
HHHHHHCCHHHHHHC		28.96UniProtKB CARBOHYD
41N-linked_GlycosylationNSSLAALNHTLLPPG
CHHHHHHCCCCCCCC		22.75UniProtKB CARBOHYD
53N-linked_GlycosylationPPGDPSLNGSRVGPE
CCCCCCCCCCCCCHH		51.21UniProtKB CARBOHYD
76PhosphorylationQPPDLLVSRGEPATL
CCCCEEEECCCCCCC		34.2424719451
99UbiquitinationRPNIEWYKNGARVAT
CCCCEEEECCEEEEE		50.40-
156N-linked_GlycosylationLGAAASRNASLEVAV
HHHHHHCCCEEEEEE		31.24UniProtKB CARBOHYD
202UbiquitinationEPSVSWRKDGARLKE
CCCCCCCCCCCCCEE		55.01-
215PhosphorylationKEEEGRITIRGGKLM
EEECCCEEEECCEEE		11.85-
300PhosphorylationKEDGELPTGRYEIRS
CCCCCCCCCCEEECC		47.09-
310PhosphorylationYEIRSDHSLWIGHVS
EEECCCCEEEEEEEE		30.3222468782
317PhosphorylationSLWIGHVSAEDEGTY
EEEEEEEEECCCCEE		21.9222468782
323PhosphorylationVSAEDEGTYTCVAEN
EEECCCCEEEEEEEC		17.3822468782
398PhosphorylationPSQSLQPTGRFSVSP
ECCCCCCCCCCEECC		28.20-
402PhosphorylationLQPTGRFSVSPRGQL
CCCCCCCEECCCCCE		21.9627067055
404PhosphorylationPTGRFSVSPRGQLNI
CCCCCEECCCCCEEE		14.0027067055
410N-linked_GlycosylationVSPRGQLNITAVQRG
ECCCCCEEEEEEECC		22.98UniProtKB CARBOHYD
459N-linked_GlycosylationVILQGPANQTLVLGS
EEEECCCCCEEEECC		38.20UniProtKB CARBOHYD
503N-linked_GlycosylationLQFKTMANGTLYIAN
EEEEEECCCEEEEEC		32.91UniProtKB CARBOHYD
550PhosphorylationGVSPDPPTEPSSPPG
CCCCCCCCCCCCCCC		66.95-
560PhosphorylationSSPPGAPSQPVVTEI
CCCCCCCCCCEEEEE		46.73-
565PhosphorylationAPSQPVVTEITKNSI
CCCCCEEEEEECCEE		23.15-
715PhosphorylationVAGPEGGSWTMLDLQ
EECCCCCCEEEEECC		30.1730206219
717PhosphorylationGPEGGSWTMLDLQSP
CCCCCCEEEEECCCH		15.0030206219
723PhosphorylationWTMLDLQSPSQQSTV
EEEEECCCHHHCCEE		33.5430206219
725PhosphorylationMLDLQSPSQQSTVLR
EEECCCHHHCCEEEC		46.2130206219
728PhosphorylationLQSPSQQSTVLRGLP
CCCHHHCCEEECCCC		16.9122210691
729PhosphorylationQSPSQQSTVLRGLPP
CCHHHCCEEECCCCC		21.1524719451
784N-linked_GlycosylationVALGGDGNSSITVSW
EEECCCCCCCEEEEE		37.01UniProtKB CARBOHYD
813N-linked_GlycosylationYQIWCLGNESRFHLN
EEEEECCCCCCCCCC		30.99UniProtKB CARBOHYD
820N-linked_GlycosylationNESRFHLNRSAAGWA
CCCCCCCCCCHHHHH		27.56UniProtKB CARBOHYD
843PhosphorylationVPGLLYRTLVAAATS
HHHHHHHHHHHHHHH		16.42-
1066UbiquitinationDSGAKGGKVKLLGKP
CCCCCCCCEEECCEE		44.88-
1068UbiquitinationGAKGGKVKLLGKPVQ
CCCCCCEEECCEECC		41.2921890473
1068 (in isoform 1)Ubiquitination-41.2921890473
1157PhosphorylationQQSTATLTPSPPDPP
CCCCCEECCCCCCCC		19.84-
1159PhosphorylationSTATLTPSPPDPPQP
CCCEECCCCCCCCCC		43.77-
1185PhosphorylationRRVPLGPSSPLSVSQ
CCCCCCCCCCCCCCC		42.6729978859
1186PhosphorylationRVPLGPSSPLSVSQP
CCCCCCCCCCCCCCC		32.7527050516
1189PhosphorylationLGPSSPLSVSQPMLG
CCCCCCCCCCCCCCC		24.0929978859
1191PhosphorylationPSSPLSVSQPMLGIR
CCCCCCCCCCCCCCC		25.7829978859
1212PhosphorylationLGAGPAASPHLSPSP
CCCCCCCCCCCCCCC		18.2429214152
1216PhosphorylationPAASPHLSPSPAPST
CCCCCCCCCCCCCCC		21.9429214152
1239PhosphorylationWQGNGEMTPPLQGPR
CCCCCCCCCCCCCCC		19.9028985074
1263PhosphorylationLPYRRENSPGDLPPP
CCCCCCCCCCCCCCC		26.0530266825
1292PhosphorylationLRAAGSMSSLERERS
HHHHCCCCHHHHHHC		33.2123312004
1293PhosphorylationRAAGSMSSLERERSG
HHHCCCCHHHHHHCC		26.1323312004
1314MethylationAVPLAAQRVLHPDEE
HHHHHHHHHCCCCCC		28.3954558849
1330PhosphorylationWLPYSRPSFLSRGQG
CCCCCCHHHHCCCCC		37.40-
1333PhosphorylationYSRPSFLSRGQGTST
CCCHHHHCCCCCCCC		32.1424719451
1334MethylationSRPSFLSRGQGTSTC
CCHHHHCCCCCCCCC		43.53115491491
1338PhosphorylationFLSRGQGTSTCSTAG
HHCCCCCCCCCCCCC		16.99-
1352PhosphorylationGSNSSRGSSSSRGSR
CCCCCCCCCCCCCCC		26.41-
1353PhosphorylationSNSSRGSSSSRGSRG
CCCCCCCCCCCCCCC		34.85-
1358PhosphorylationGSSSSRGSRGPGRSR
CCCCCCCCCCCCCCC		32.71-
1363MethylationRGSRGPGRSRSRSQS
CCCCCCCCCCCHHHC		31.8424396641
1364PhosphorylationGSRGPGRSRSRSQSR
CCCCCCCCCCHHHCC		40.29-
1365MethylationSRGPGRSRSRSQSRS
CCCCCCCCCHHHCCC		34.4324396647
1367MethylationGPGRSRSRSQSRSQS
CCCCCCCHHHCCCCC		37.2924396653
1370PhosphorylationRSRSRSQSRSQSQRP
CCCCHHHCCCCCCCC		34.84-
1372PhosphorylationRSRSQSRSQSQRPGQ
CCHHHCCCCCCCCCC		39.1629978859
1374PhosphorylationRSQSRSQSQRPGQKR
HHHCCCCCCCCCCCC		29.4229978859
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
1330SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROBO3_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 ROBO3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LNX1_HUMANLNX1physical
25416956
CCD57_HUMANCCDC57physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607313Familial horizontal gaze palsy with progressive scoliosis (HGPPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROBO3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1263, AND MASSSPECTROMETRY.

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