ROR2_HUMAN - dbPTM
ROR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROR2_HUMAN
UniProt AC Q01974
Protein Name Tyrosine-protein kinase transmembrane receptor ROR2
Gene Name ROR2
Organism Homo sapiens (Human).
Sequence Length 943
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Tyrosine-protein kinase receptor which may be involved in the early formation of the chondrocytes. It seems to be required for cartilage and growth plate development (By similarity). Phosphorylates YWHAB, leading to induction of osteogenesis and bone formation. [PubMed: 17717073 In contrast, has also been shown to have very little tyrosine kinase activity in vitro. May act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated signaling]
Protein Sequence MARGSALPRRPLLCIPAVWAAAALLLSVSRTSGEVEVLDPNDPLGPLDGQDGPIPTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRIIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGMKTITATGVLFVRLGPTHSPNHNFQDDYHEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCDARSRTPKPRELCRDECEVLESDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRIGIPAERLGRYHQCYNGSGMDYRGTASTTKSGHQCQPWALQHPHSHHLSSTDFPELGGGHAYCRNPGGQMEGPWCFTQNKNVRMELCDVPSCSPRDSSKMGILYILVPSIAIPLVIACLFFLVCMCRNKQKASASTPQRRQLMASPSQDMEMPLINQHKQAKLKEISLSAVRFMEELGEDRFGKVYKGHLFGPAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRARLQHPNVVCLLGVVTKDQPLSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHLVAQIAAGMEYLSSHHVVHKDLATRNVLVYDKLNVKISDLGLFREVYAADYYKLLGNSLLPIRWMAPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRNRQVLPCPDDCPAWVYALMIECWNEFPSRRPRFKDIHSRLRAWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSNVSNARYVGPKQKAPPFPQPQFIPMKGQIRPMVPPPQLYVPVNGYQPVPAYGAYLPNFYPVQIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSMADRAALLSEGADDTQNAPEDGAQSTVQEAEEEEEGSVPETELLGDCDTLQVDEAQVQLEA
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
5Phosphorylation---MARGSALPRRPL
---CCCCCCCCCCCC		22.5324719451
27PhosphorylationAAAALLLSVSRTSGE
HHHHHHHHHHCCCCE		20.3024719451
70N-linked_GlycosylationNFLEPVNNITIVQGQ
HCCCCCCCEEEEECC		32.77UniProtKB CARBOHYD
85UbiquitinationTAILHCKVAGNPPPN
EEEEEEEECCCCCCC		11.3922817900
88UbiquitinationLHCKVAGNPPPNVRW
EEEEECCCCCCCCCC		35.8521890473
97UbiquitinationPPNVRWLKNDAPVVQ
CCCCCCCCCCCCCCC		45.9129967540
157O-linked_GlycosylationLFVRLGPTHSPNHNF
EEEEECCCCCCCCCC		32.9455830597
177PhosphorylationEDGFCQPYRGIACAR
CCCCCCCCCCCEEEE		8.80-
188N-linked_GlycosylationACARFIGNRTIYVDS
EEEEEECCEEEEEEE		32.86UniProtKB CARBOHYD
318N-linked_GlycosylationGRYHQCYNGSGMDYR
CCCEECCCCCCCCCC		45.86UniProtKB CARBOHYD
346UbiquitinationPWALQHPHSHHLSST
CHHHCCCCCCCCCCC		37.3222817900
349UbiquitinationLQHPHSHHLSSTDFP
HCCCCCCCCCCCCCC		30.3521890473
435PhosphorylationCRNKQKASASTPQRR
HCCCHHHCCCCHHHH		29.7723312004
437PhosphorylationNKQKASASTPQRRQL
CCHHHCCCCHHHHHH		37.8223312004
438PhosphorylationKQKASASTPQRRQLM
CHHHCCCCHHHHHHH		24.1323312004
447PhosphorylationQRRQLMASPSQDMEM
HHHHHHCCCCCCCCC		15.8925159151
449PhosphorylationRQLMASPSQDMEMPL
HHHHCCCCCCCCCCC		36.0017525332
466UbiquitinationQHKQAKLKEISLSAV
HHHHHHHHHCCHHHH		52.9029967540
469SulfationQAKLKEISLSAVRFM
HHHHHHCCHHHHHHH		19.8414752058
469SulfoserineQAKLKEISLSAVRFM
HHHHHHCCHHHHHHH		19.84-
469PhosphorylationQAKLKEISLSAVRFM
HHHHHHCCHHHHHHH		19.8420068231
471SulfoserineKLKEISLSAVRFMEE
HHHHCCHHHHHHHHH		20.23-
471SulfationKLKEISLSAVRFMEE
HHHHCCHHHHHHHHH		20.2314752058
471PhosphorylationKLKEISLSAVRFMEE
HHHHCCHHHHHHHHH		20.2320068231
483UbiquitinationMEELGEDRFGKVYKG
HHHHCCCCCCEEECC		37.6022817900
486UbiquitinationLGEDRFGKVYKGHLF
HCCCCCCEEECCCCC		39.4121890473
489UbiquitinationDRFGKVYKGHLFGPA
CCCCEEECCCCCCCC		42.7322817900
507UbiquitinationQTQAVAIKTLKDKAE
CHHHEEEEHHHHHCC		37.7629967540
512UbiquitinationAIKTLKDKAEGPLRE
EEEHHHHHCCCCCCH		46.9129967540
569PhosphorylationHEFLVMRSPHSDVGS
HHHEEECCCCCCCCC		14.6321955146
572PhosphorylationLVMRSPHSDVGSTDD
EEECCCCCCCCCCCC		37.0626699800
576PhosphorylationSPHSDVGSTDDDRTV
CCCCCCCCCCCCCHH		28.6330576142
577PhosphorylationPHSDVGSTDDDRTVK
CCCCCCCCCCCCHHH		37.2030576142
582PhosphorylationGSTDDDRTVKSALEP
CCCCCCCHHHHHCCC		39.0030576142
624PhosphorylationATRNVLVYDKLNVKI
CCCCEEEEECCCCCH		11.82-
626UbiquitinationRNVLVYDKLNVKISD
CCEEEEECCCCCHHH		25.0329967540
646PhosphorylationEVYAADYYKLLGNSL
HHHHHHHHHHHCCCC		8.84-
647UbiquitinationVYAADYYKLLGNSLL
HHHHHHHHHHCCCCC		30.89-
652PhosphorylationYYKLLGNSLLPIRWM
HHHHHCCCCCCCEEC		29.5025003641
666PhosphorylationMAPEAIMYGKFSIDS
CCCCHHHHCCCCCCH		15.8522817900
755PhosphorylationAWGNLSNYNSSAQTS
HHCCCCCCCCCCCCC		17.04-
758PhosphorylationNLSNYNSSAQTSGAS
CCCCCCCCCCCCCCC		22.28-
762PhosphorylationYNSSAQTSGASNTTQ
CCCCCCCCCCCCCCC		21.93-
768PhosphorylationTSGASNTTQTSSLST
CCCCCCCCCCCCCCC		33.8230175587
782PhosphorylationTSPVSNVSNARYVGP
CCCCCCCCCCEECCC		29.08-
785Asymmetric dimethylarginineVSNVSNARYVGPKQK
CCCCCCCEECCCCCC		30.81-
785MethylationVSNVSNARYVGPKQK
CCCCCCCEECCCCCC		30.81-
792UbiquitinationRYVGPKQKAPPFPQP
EECCCCCCCCCCCCC		69.8229967540
824PhosphorylationLYVPVNGYQPVPAYG
CEEECCCEECCCCCC		12.39-
860PhosphorylationPQMVPKPSSHHSGSG
CCCCCCCCCCCCCCC		48.7227732954
861PhosphorylationQMVPKPSSHHSGSGS
CCCCCCCCCCCCCCC		33.4727732954
864PhosphorylationPKPSSHHSGSGSTST
CCCCCCCCCCCCCCC		29.2727732954
866PhosphorylationPSSHHSGSGSTSTGY
CCCCCCCCCCCCCEE		32.3627732954
868PhosphorylationSHHSGSGSTSTGYVT
CCCCCCCCCCCEEEE		22.3827732954
869PhosphorylationHHSGSGSTSTGYVTT
CCCCCCCCCCEEEEC		33.5622468782
870PhosphorylationHSGSGSTSTGYVTTA
CCCCCCCCCEEEECC		22.8727732954
871PhosphorylationSGSGSTSTGYVTTAP
CCCCCCCCEEEECCC		32.4022468782
873PhosphorylationSGSTSTGYVTTAPSN
CCCCCCEEEECCCCC		8.4925884760
875PhosphorylationSTSTGYVTTAPSNTS
CCCCEEEECCCCCCC		14.5723312004
876PhosphorylationTSTGYVTTAPSNTSM
CCCEEEECCCCCCCH		26.9123312004
879PhosphorylationGYVTTAPSNTSMADR
EEEECCCCCCCHHHH		50.7223312004
881PhosphorylationVTTAPSNTSMADRAA
EECCCCCCCHHHHHH		24.9823312004
882PhosphorylationTTAPSNTSMADRAAL
ECCCCCCCHHHHHHH		19.0723312004
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 ROR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROR2_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
824Phosphorylation819 (5)V ⇒ Irs10761129
  • Nose size
  • Lobe attachment (rater-scored or self-reported)
27182965
29198719
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGD1_HUMANMAGED1physical
12754255
M3K7_HUMANMAP3K7physical
18762249
DAZP2_HUMANDAZAP2physical
18762249
WNT1_HUMANWNT1physical
18762249
HS90A_HUMANHSP90AA1physical
22939624
ROR2_HUMANROR2physical
25416956
ZMYM4_HUMANZMYM4physical
25416956
DAZP2_HUMANDAZAP2physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
CA094_HUMANC1orf94physical
25416956
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
PP2BB_HUMANPPP3CBphysical
28065597
PPM1A_HUMANPPM1Aphysical
28065597
PPM1B_HUMANPPM1Bphysical
28065597
PPM1F_HUMANPPM1Fphysical
28065597
ILKAP_HUMANILKAPphysical
28065597
TAB1_HUMANTAB1physical
28065597
PTPRR_HUMANPTPRRphysical
28065597
PTN6_HUMANPTPN6physical
28065597
PTN7_HUMANPTPN7physical
28065597
PTN11_HUMANPTPN11physical
28065597
PTN12_HUMANPTPN12physical
28065597
PTN20_HUMANPTPN20Bphysical
28065597
DUS1_HUMANDUSP1physical
28065597
DUS6_HUMANDUSP6physical
28065597
DUS10_HUMANDUSP10physical
28065597
DUS14_HUMANDUSP14physical
28065597
DUS18_HUMANDUSP18physical
28065597
DUS19_HUMANDUSP19physical
28065597
DUS21_HUMANDUSP21physical
28065597
DUPD1_HUMANDUPD1physical
28065597
STYX_HUMANSTYXphysical
28065597
CC14A_HUMANCDC14Aphysical
28065597
TPTE_HUMANTPTEphysical
28065597
MTMR1_HUMANMTMR1physical
28065597
MTMR2_HUMANMTMR2physical
28065597
MTMR6_HUMANMTMR6physical
28065597
MTMR9_HUMANMTMR9physical
28065597
MPIP3_HUMANCDC25Cphysical
28065597
EYA2_HUMANEYA2physical
28065597
Drug and Disease Associations
Kegg Disease
H00482 Brachydactyly, including: type A; type B; type D; type E
H00485 Robinow syndrome
OMIM Disease
113000Brachydactyly B1 (BDB1)
268310Robinow syndrome autosomal recessive (RRS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.
Sulfation
ReferencePubMed
"O-sulfonation of serine and threonine: mass spectrometric detectionand characterization of a new posttranslational modification indiverse proteins throughout the eukaryotes.";
Medzihradszky K.F., Darula Z., Perlson E., Fainzilber M.,Chalkley R.J., Ball H., Greenbaum D., Bogyo M., Tyson D.R.,Bradshaw R.A., Burlingame A.L.;
Mol. Cell. Proteomics 3:429-440(2004).
Cited for: PROTEIN SEQUENCE OF 465-474, SULFATION AT SER-469 AND SER-471, ANDMASS SPECTROMETRY.

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