RIPR2_HUMAN - dbPTM
RIPR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIPR2_HUMAN
UniProt AC Q9Y4F9
Protein Name Rho family-interacting cell polarization regulator 2
Gene Name RIPOR2
Organism Homo sapiens (Human).
Sequence Length 1068
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cell projection, filopodium . Cell projection, stereocilium . Cell projection, stereocilium membrane . Apical cell membrane . Localized in the cytoplasm in cells undergoing mitosis (PubMed:17150207). Colocalized
Protein Description Acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization. [PubMed: 17150207]
Protein Sequence MLVGSQSFSPGGPNGIIRSQSFAGFSGLQERRSRCNSFIENSSALKKPQAKLKKMHNLGHKNNNPPKEPQPKRVEEVYRALKNGLDEYLEVHQTELDKLTAQLKDMKRNSRLGVLYDLDKQIKTIERYMRRLEFHISKVDELYEAYCIQRRLQDGASKMKQAFATSPASKAARESLTEINRSFKEYTENMCTIEVELENLLGEFSIKMKGLAGFARLCPGDQYEIFMKYGRQRWKLKGKIEVNGKQSWDGEETVFLPLIVGFISIKVTELKGLATHILVGSVTCETKELFAARPQVVAVDINDLGTIKLNLEITWYPFDVEDMTASSGAGNKAAALQRRMSMYSQGTPETPTFKDHSFFRWLHPSPDKPRRLSVLSALQDTFFAKLHRSRSFSDLPSLRPSPKAVLELYSNLPDDIFENGKAAEEKMPLSLSFSDLPNGDCALTSHSTGSPSNSTNPEITITPAEFNLSSLASQNEGMDDTSSASSRNSLGEGQEPKSHLKEEDPEEPRKPASAPSEACRRQSSGAGAEHLFLENDVAEALLQESEEASELKPVELDTSEGNITKQLVKRLTSAEVPMATDRLLSEGSVGGESEGCRSFLDGSLEDAFNGLLLALEPHKEQYKEFQDLNQEVMNLDDILKCKPAVSRSRSSSLSLTVESALESFDFLNTSDFDEEEDGDEVCNVGGGADSVFSDTETEKHSYRSVHPEARGHLSEALTEDTGVGTSVAGSPLPLTTGNESLDITIVRHLQYCTQLVQQIVFSSKTPFVARSLLEKLSRQIQVMEKLAAVSDENIGNISSVVEAIPEFHKKLSLLSFWTKCCSPVGVYHSPADRVMKQLEASFARTVNKEYPGLADPVFRTLVSQILDRAEPLLSSSLSSEVVTVFQYYSYFTSHGVSDLESYLSQLARQVSMVQTLQSLRDEKLLQTMSDLAPSNLLAQQEVLRTLALLLTREDNEVSEAVTLYLAAASKNQHFREKALLYYCEALTKTNLQLQKAACLALKILEATESIKMLVTLCQSDTEEIRNVASETLLSLGEDGRLAYEQLDKFPRDCVKVGGRHGTEVATAF
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---MLVGSQSFSPGG
---CCCCCCCCCCCC
26552605
7Phosphorylation-MLVGSQSFSPGGPN
-CCCCCCCCCCCCCC
26552605
9PhosphorylationLVGSQSFSPGGPNGI
CCCCCCCCCCCCCCE
26552605
19PhosphorylationGPNGIIRSQSFAGFS
CCCCEEECCCCCCCC
23401153
21PhosphorylationNGIIRSQSFAGFSGL
CCEEECCCCCCCCCH
23927012
26PhosphorylationSQSFAGFSGLQERRS
CCCCCCCCCHHHHHH
23927012
33PhosphorylationSGLQERRSRCNSFIE
CCHHHHHHHHHHHHH
23401153
37PhosphorylationERRSRCNSFIENSSA
HHHHHHHHHHHCCHH
23401153
42PhosphorylationCNSFIENSSALKKPQ
HHHHHHCCHHCCCHH
26552605
43PhosphorylationNSFIENSSALKKPQA
HHHHHCCHHCCCHHH
26552605
98UbiquitinationVHQTELDKLTAQLKD
HHHHHHHHHHHHHHH
-
104UbiquitinationDKLTAQLKDMKRNSR
HHHHHHHHHHHHHCC
-
170UbiquitinationFATSPASKAARESLT
HHCCHHHHHHHHHHH
-
175PhosphorylationASKAARESLTEINRS
HHHHHHHHHHHHHHH
29978859
177PhosphorylationKAARESLTEINRSFK
HHHHHHHHHHHHHHH
23312004
205PhosphorylationENLLGEFSIKMKGLA
HHHHHHHHHHHCCCC
24719451
223PhosphorylationRLCPGDQYEIFMKYG
HCCCCCHHHHHHHHC
-
229PhosphorylationQYEIFMKYGRQRWKL
HHHHHHHHCCCCEEE
-
306PhosphorylationVDINDLGTIKLNLEI
EECCCCCEEEEEEEE
-
314PhosphorylationIKLNLEITWYPFDVE
EEEEEEEEEEECCHH
24275569
316PhosphorylationLNLEITWYPFDVEDM
EEEEEEEEECCHHHC
24275569
324PhosphorylationPFDVEDMTASSGAGN
ECCHHHCCCCCCCCH
24275569
341PhosphorylationAALQRRMSMYSQGTP
HHHHHHHHHHCCCCC
23401153
343PhosphorylationLQRRMSMYSQGTPET
HHHHHHHHCCCCCCC
25219547
344PhosphorylationQRRMSMYSQGTPETP
HHHHHHHCCCCCCCC
25219547
347PhosphorylationMSMYSQGTPETPTFK
HHHHCCCCCCCCCCC
25219547
350PhosphorylationYSQGTPETPTFKDHS
HCCCCCCCCCCCCCC
25219547
352PhosphorylationQGTPETPTFKDHSFF
CCCCCCCCCCCCCCH
29978859
357 (in isoform 2)Phosphorylation-24275569
357PhosphorylationTPTFKDHSFFRWLHP
CCCCCCCCCHHCCCC
24719451
373PhosphorylationPDKPRRLSVLSALQD
CCCCHHHHHHHHHHH
26503514
389PhosphorylationFFAKLHRSRSFSDLP
HHHHHHCCCCHHHCC
-
391PhosphorylationAKLHRSRSFSDLPSL
HHHHCCCCHHHCCCC
-
397PhosphorylationRSFSDLPSLRPSPKA
CCHHHCCCCCCCHHH
24719451
430PhosphorylationAEEKMPLSLSFSDLP
HHHHCCCEEECCCCC
26074081
432PhosphorylationEKMPLSLSFSDLPNG
HHCCCEEECCCCCCC
26074081
434PhosphorylationMPLSLSFSDLPNGDC
CCCEEECCCCCCCCE
26074081
444PhosphorylationPNGDCALTSHSTGSP
CCCCEEEEECCCCCC
26074081
445PhosphorylationNGDCALTSHSTGSPS
CCCEEEEECCCCCCC
26074081
447PhosphorylationDCALTSHSTGSPSNS
CEEEEECCCCCCCCC
26074081
448PhosphorylationCALTSHSTGSPSNST
EEEEECCCCCCCCCC
26074081
450PhosphorylationLTSHSTGSPSNSTNP
EEECCCCCCCCCCCC
26074081
452PhosphorylationSHSTGSPSNSTNPEI
ECCCCCCCCCCCCCE
26074081
454PhosphorylationSTGSPSNSTNPEITI
CCCCCCCCCCCCEEE
26074081
455PhosphorylationTGSPSNSTNPEITIT
CCCCCCCCCCCEEEE
26074081
489PhosphorylationSSASSRNSLGEGQEP
CCCHHHCCCCCCCCC
23401153
523PhosphorylationSEACRRQSSGAGAEH
HHHHHHHCCCCCCHH
23684312
524PhosphorylationEACRRQSSGAGAEHL
HHHHHHCCCCCCHHH
28464451
564PhosphorylationDTSEGNITKQLVKRL
CCCCCCHHHHHHHHH
23532336
572PhosphorylationKQLVKRLTSAEVPMA
HHHHHHHHHCCCCCC
28787133
573PhosphorylationQLVKRLTSAEVPMAT
HHHHHHHHCCCCCCH
23401153
580PhosphorylationSAEVPMATDRLLSEG
HCCCCCCHHHHHHCC
30108239
585PhosphorylationMATDRLLSEGSVGGE
CCHHHHHHCCCCCCC
23401153
588PhosphorylationDRLLSEGSVGGESEG
HHHHHCCCCCCCCHH
23401153
593PhosphorylationEGSVGGESEGCRSFL
CCCCCCCCHHHHHHC
26552605
603PhosphorylationCRSFLDGSLEDAFNG
HHHHCCCCHHHHHHH
22617229
623AcetylationEPHKEQYKEFQDLNQ
CCCHHHHHHHHHHCH
19814999
714PhosphorylationPEARGHLSEALTEDT
HHHHCCHHHHHHCCC
27080861
718PhosphorylationGHLSEALTEDTGVGT
CCHHHHHHCCCCCCC
27080861
721PhosphorylationSEALTEDTGVGTSVA
HHHHHCCCCCCCCCC
27080861
725PhosphorylationTEDTGVGTSVAGSPL
HCCCCCCCCCCCCCC
27080861
726PhosphorylationEDTGVGTSVAGSPLP
CCCCCCCCCCCCCCC
27080861
730PhosphorylationVGTSVAGSPLPLTTG
CCCCCCCCCCCCCCC
27080861
735PhosphorylationAGSPLPLTTGNESLD
CCCCCCCCCCCCCCC
27080861
762PhosphorylationLVQQIVFSSKTPFVA
HHHHHHHCCCCHHHH
30631047
763PhosphorylationVQQIVFSSKTPFVAR
HHHHHHCCCCHHHHH
30631047
771PhosphorylationKTPFVARSLLEKLSR
CCHHHHHHHHHHHHH
24719451
809UbiquitinationEAIPEFHKKLSLLSF
HHCHHHHHHHHHHHH
-
848UbiquitinationSFARTVNKEYPGLAD
HHHHHHCCCCCCCCC
-
860PhosphorylationLADPVFRTLVSQILD
CCCHHHHHHHHHHHH
23090842
863PhosphorylationPVFRTLVSQILDRAE
HHHHHHHHHHHHHHH
23090842
874PhosphorylationDRAEPLLSSSLSSEV
HHHHHHHCCCCCCCC
29759185
911PhosphorylationSQLARQVSMVQTLQS
HHHHHHHHHHHHHHH
22817900
915PhosphorylationRQVSMVQTLQSLRDE
HHHHHHHHHHHHCHH
22817900
918PhosphorylationSMVQTLQSLRDEKLL
HHHHHHHHHCHHHHH
30622161
945PhosphorylationAQQEVLRTLALLLTR
HHHHHHHHHHHHHHC
-
951O-linked_GlycosylationRTLALLLTREDNEVS
HHHHHHHHCCCCHHH
30379171
1043PhosphorylationGEDGRLAYEQLDKFP
CCCCCHHHHHHHCCC
28796482
1048UbiquitinationLAYEQLDKFPRDCVK
HHHHHHHCCCHHHHE
-

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 RIPR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIPR2_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 RIPR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
21988832
PER1_HUMANPER1physical
21988832
MP2K2_HUMANMAP2K2physical
21988832
1433Z_HUMANYWHAZphysical
24687993
HDAC6_HUMANHDAC6physical
24687993
DYSF_HUMANDYSFphysical
24687993
MYOF_HUMANMYOFphysical
24687993

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIPR2_HUMAN

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Related Literatures of Post-Translational Modification

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