RHPN1_HUMAN - dbPTM
RHPN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHPN1_HUMAN
UniProt AC Q8TCX5
Protein Name Rhophilin-1
Gene Name RHPN1
Organism Homo sapiens (Human).
Sequence Length 695
Subcellular Localization
Protein Description Has no enzymatic activity. May serve as a target for Rho, and interact with some cytoskeletal component upon Rho binding or relay a Rho signal to other molecules (By similarity)..
Protein Sequence MILEERPDGAGAGEESPRLQGCDSLTQIQCGQLQSRRAQIHQQIDKELQMRTGAENLYRATSNNRVRETVALELSYVNSNLQLLKEELEELSGGVDPGRHGSEAVTVPMIPLGLKETKELDWSTPLKELISVHFGEDGASYEAEIRELEALRQAMRTPSRNESGLELLTAYYNQLCFLDARFLTPARSLGLFFHWYDSLTGVPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGARRAMEAFQRAAGAFSLLRENFSHAPSPDMSAASLCALEQLMMAQAQECVFEGLSPPASMAPQDCLAQLRLAQEAAQVAAEYRLVHRTMAQPPVHDYVPVSWTALVHVKAEYFRSLAHYHVAMALCDGSRECPPHLPMVLPRPPRAGSQPLCPPAATEGELPTHEQVFLQPPTSSKPRGPVLPQELEERRQLGKAHLKRAILGQEEALRLHALCRVLREVDLLRAVISQTLQRSLAKYAELDREDDFCEAAEAPDIQPKTHQKPEARMPRLSQGKGPDIFHRLGPLSVFSAKNRWRLVGPVHLTRGEGGFGLTLRGDSPVLIAAVIPGSQAAAAGLKEGDYIVSVNGQPCRWWRHAEVVTELKAAGEAGASLQVVSLLPSSRLPSLGDRRPVLLGPRGLLRSQREHGCKTPASTWASPRPLLNWSRKAQQGKTGGCPQPCAPVKPAPPSSLKHPGWP
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
16PhosphorylationGAGAGEESPRLQGCD
CCCCCCCCCCCCCCC
15.8330266825
24PhosphorylationPRLQGCDSLTQIQCG
CCCCCCCCCCCHHCH
37.0827251275
26PhosphorylationLQGCDSLTQIQCGQL
CCCCCCCCCHHCHHH
27.8127251275
92PhosphorylationKEELEELSGGVDPGR
HHHHHHHCCCCCCCC
36.46-
118UbiquitinationPLGLKETKELDWSTP
CCCCCCCCCCCCCCC
58.3229967540
157PhosphorylationALRQAMRTPSRNESG
HHHHHHCCCCCCHHH
16.72-
159PhosphorylationRQAMRTPSRNESGLE
HHHHCCCCCCHHHHH
47.31-
163PhosphorylationRTPSRNESGLELLTA
CCCCCCHHHHHHHHH
52.83-
188PhosphorylationRFLTPARSLGLFFHW
HCCCCHHHHCCHHHH
28.9727251275
436AcetylationQLGKAHLKRAILGQE
HHHHHHHHHHHCCHH
29.897589111
450UbiquitinationEEALRLHALCRVLRE
HHHHHHHHHHHHHHH
16.98-
475UbiquitinationTLQRSLAKYAELDRE
HHHHHHHHHHHCCCC
50.73-
498PhosphorylationAPDIQPKTHQKPEAR
CCCCCCCCCCCCCCC
35.9026074081
505UbiquitinationTHQKPEARMPRLSQG
CCCCCCCCCCCHHCC
33.70-
510PhosphorylationEARMPRLSQGKGPDI
CCCCCCHHCCCCCCH
37.8626074081
530UbiquitinationPLSVFSAKNRWRLVG
CCEEEECCCCEEEEC
45.94-
609PhosphorylationAAGEAGASLQVVSLL
HHHHCCCCEEEEECC
20.5827732954
614PhosphorylationGASLQVVSLLPSSRL
CCCEEEEECCCCCCC
25.9027732954
618PhosphorylationQVVSLLPSSRLPSLG
EEEECCCCCCCCCCC
28.2327732954
619PhosphorylationVVSLLPSSRLPSLGD
EEECCCCCCCCCCCC
35.5827732954
632MethylationGDRRPVLLGPRGLLR
CCCCCCCCCHHHHHH
10.13-
655PhosphorylationTPASTWASPRPLLNW
CCCCCCCCCCCCCCC
17.0128509920
657DimethylationASTWASPRPLLNWSR
CCCCCCCCCCCCCHH
31.81-
657MethylationASTWASPRPLLNWSR
CCCCCCCCCCCCCHH
31.8154561735
663PhosphorylationPRPLLNWSRKAQQGK
CCCCCCCHHHHHCCC
23.8824719451

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 RHPN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHPN1_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 RHPN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNKR1_HUMANCNKSR1physical
14749388
CEP70_HUMANCEP70physical
21516116
PTN14_HUMANPTPN14physical
28514442
PTN21_HUMANPTPN21physical
28514442
KIBRA_HUMANWWC1physical
28514442
WWC2_HUMANWWC2physical
28514442
GOGA2_HUMANGOLGA2physical
28514442
KLH11_HUMANKLHL11physical
28514442
PDXL2_HUMANPODXL2physical
28514442
TTC19_HUMANTTC19physical
28514442
PODXL_HUMANPODXLphysical
28514442
ZBT10_HUMANZBTB10physical
28514442
SNTB2_HUMANSNTB2physical
28514442
CTNL1_HUMANCTNNAL1physical
28514442
MELK_HUMANMELKphysical
28514442
NDUB9_HUMANNDUFB9physical
28514442
DTNB_HUMANDTNBphysical
28514442
MK09_HUMANMAPK9physical
28514442
UBP15_HUMANUSP15physical
28514442
SPAG5_HUMANSPAG5physical
28514442
UTRO_HUMANUTRNphysical
28514442
MCMBP_HUMANMCMBPphysical
28514442
LZTS2_HUMANLZTS2physical
28514442
UBP47_HUMANUSP47physical
28514442
IFT81_HUMANIFT81physical
28514442
PPCE_HUMANPREPphysical
28514442
MTMR4_HUMANMTMR4physical
28514442
WDR47_HUMANWDR47physical
28514442
IFT74_HUMANIFT74physical
28514442
P4R3A_HUMANSMEK1physical
28514442
GORS1_HUMANGORASP1physical
28514442

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 RHPN1_HUMAN

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Related Literatures of Post-Translational Modification

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