RHDF2_HUMAN - dbPTM
RHDF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHDF2_HUMAN
UniProt AC Q6PJF5
Protein Name Inactive rhomboid protein 2
Gene Name RHBDF2
Organism Homo sapiens (Human).
Sequence Length 856
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. Cell membrane .
Protein Description Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration (By similarity)..
Protein Sequence MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH
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
10PhosphorylationSADKNGGSVSSVSSS
CCCCCCCCCCCCCHH
21.8923090842
12PhosphorylationDKNGGSVSSVSSSRL
CCCCCCCCCCCHHHC
27.0723090842
13PhosphorylationKNGGSVSSVSSSRLQ
CCCCCCCCCCHHHCC
24.7023090842
15PhosphorylationGGSVSSVSSSRLQSR
CCCCCCCCHHHCCCC
25.2523090842
16PhosphorylationGSVSSVSSSRLQSRK
CCCCCCCHHHCCCCC
19.8123090842
17PhosphorylationSVSSVSSSRLQSRKP
CCCCCCHHHCCCCCC
29.5123090842
21PhosphorylationVSSSRLQSRKPPNLS
CCHHHCCCCCCCCCE
47.0323090842
28PhosphorylationSRKPPNLSITIPPPE
CCCCCCCEEECCCCC
25.0723312004
30PhosphorylationKPPNLSITIPPPEKE
CCCCCEEECCCCCCC
24.8523312004
46PhosphorylationQAPGEQDSMLPEGFQ
CCCCCCCCCCCHHHH
23.1622210691
52UbiquitinationDSMLPEGFQNRRLKK
CCCCCHHHHHCCCCC
5.7729967540
58UbiquitinationGFQNRRLKKSQPRTW
HHHHCCCCCCCCCCH
48.8729967540
61 (in isoform 2)Phosphorylation-40.1329507054
61PhosphorylationNRRLKKSQPRTWAAH
HCCCCCCCCCCHHHC
40.1332645325
75UbiquitinationHTTACPPSFLPKRKN
CCCCCCHHHCCCCCC
25.2629967540
81UbiquitinationPSFLPKRKNPAYLKS
HHHCCCCCCCHHHHC
73.70-
87UbiquitinationRKNPAYLKSVSLQEP
CCCCHHHHCCCCCCC
35.81-
88PhosphorylationKNPAYLKSVSLQEPR
CCCHHHHCCCCCCCH
17.8430266825
90PhosphorylationPAYLKSVSLQEPRSR
CHHHHCCCCCCCHHH
31.2725159151
96PhosphorylationVSLQEPRSRWQESSE
CCCCCCHHHHHHHHH
48.8928102081
101PhosphorylationPRSRWQESSEKRPGF
CHHHHHHHHHCCCCH
28.7928857561
102PhosphorylationRSRWQESSEKRPGFR
HHHHHHHHHCCCCHH
46.5128857561
104UbiquitinationRWQESSEKRPGFRRQ
HHHHHHHCCCCHHHH
66.8829967540
113PhosphorylationPGFRRQASLSQSIRK
CCHHHHHHHHHHHHH
21.8823401153
115PhosphorylationFRRQASLSQSIRKGA
HHHHHHHHHHHHHCC
21.2730266825
117PhosphorylationRQASLSQSIRKGAAQ
HHHHHHHHHHHCCHH
22.4520164059
120MethylationSLSQSIRKGAAQWFG
HHHHHHHHCCHHHHC
51.75115976631
129PhosphorylationAAQWFGVSGDWEGQR
CHHHHCCCCCCCHHH
31.2629507054
143PhosphorylationRQQWQRRSLHHCSMR
HHHHHHHHHHHHHHH
33.9527251275
148PhosphorylationRRSLHHCSMRYGRLK
HHHHHHHHHHHHHHH
11.2628348404
150UbiquitinationSLHHCSMRYGRLKAS
HHHHHHHHHHHHHHH
17.9229967540
166PhosphorylationQRDLELPSQEAPSFQ
HCCCCCCCCCCCCCC
53.9623927012
171PhosphorylationLPSQEAPSFQGTESP
CCCCCCCCCCCCCCC
36.9323401153
175PhosphorylationEAPSFQGTESPKPCK
CCCCCCCCCCCCCCC
23.6223401153
177PhosphorylationPSFQGTESPKPCKMP
CCCCCCCCCCCCCCC
37.7530266825
179UbiquitinationFQGTESPKPCKMPKI
CCCCCCCCCCCCCCC
72.7829967540
192MethylationKIVDPLARGRAFRHP
CCCCHHHCCCCCCCH
42.7054558769
213PhosphorylationHAPHPPLTPGVLSLT
CCCCCCCCCCEEEEC
24.6224719451
227PhosphorylationTSFTSVRSGYSHLPR
CCCCCCCCCCCCCCH
39.6730266825
229PhosphorylationFTSVRSGYSHLPRRK
CCCCCCCCCCCCHHH
8.3130266825
230PhosphorylationTSVRSGYSHLPRRKR
CCCCCCCCCCCHHHC
23.2930266825
239PhosphorylationLPRRKRMSVAHMSLQ
CCHHHCCCHHHHHHH
21.8622617229
244PhosphorylationRMSVAHMSLQAAAAL
CCCHHHHHHHHHHHH
13.8922985185
256PhosphorylationAALLKGRSVLDATGQ
HHHHCCCHHHHCCCC
35.3828857561
261PhosphorylationGRSVLDATGQRCRVV
CCHHHHCCCCCEEEE
33.2527470641
271PhosphorylationRCRVVKRSFAFPSFL
CEEEEEHHHCCCCCC
18.4029523821
276PhosphorylationKRSFAFPSFLEEDVV
EHHHCCCCCCCCCCC
35.6929523821
288PhosphorylationDVVDGADTFDSSFFS
CCCCCCCCCCHHHCC
28.89-
300PhosphorylationFFSKEEMSSMPDDVF
HCCHHHHCCCCCCCC
27.1127050516
301PhosphorylationFSKEEMSSMPDDVFE
CCHHHHCCCCCCCCC
32.7820639409
308UbiquitinationSMPDDVFESPPLSAS
CCCCCCCCCCCCCHH
63.2821890473
308 (in isoform 2)Ubiquitination-63.2821890473
309PhosphorylationMPDDVFESPPLSASY
CCCCCCCCCCCCHHH
21.9820639409
313PhosphorylationVFESPPLSASYFRGI
CCCCCCCCHHHHCCC
22.4229116813
315PhosphorylationESPPLSASYFRGIPH
CCCCCCHHHHCCCCC
22.7920639409
316PhosphorylationSPPLSASYFRGIPHS
CCCCCHHHHCCCCCC
9.3020639409
323PhosphorylationYFRGIPHSASPVSPD
HHCCCCCCCCCCCCC
25.7023401153
325PhosphorylationRGIPHSASPVSPDGV
CCCCCCCCCCCCCCC
28.9323927012
328PhosphorylationPHSASPVSPDGVQIP
CCCCCCCCCCCCEEC
22.2125159151
329UbiquitinationHSASPVSPDGVQIPL
CCCCCCCCCCCEECH
42.4833845483
337 (in isoform 1)Ubiquitination-43.4621890473
337UbiquitinationDGVQIPLKEYGRAPV
CCCEECHHHHCCCCC
43.4622817900
339PhosphorylationVQIPLKEYGRAPVPG
CEECHHHHCCCCCCC
15.4327642862
355PhosphorylationRRGKRIASKVKHFAF
CCCHHHHHHCCEECC
35.2924719451
356PhosphorylationRGKRIASKVKHFAFD
CCHHHHHHCCEECCC
46.4033259812
358UbiquitinationKRIASKVKHFAFDRK
HHHHHHCCEECCCCC
36.4233845483
381PhosphorylationVGNWLNRSYRRSISS
HHHHHCHHHHHHHHH
23.1724719451
385PhosphorylationLNRSYRRSISSTVQR
HCHHHHHHHHHHHHH
20.1630266825
387PhosphorylationRSYRRSISSTVQRQL
HHHHHHHHHHHHHHH
22.6229255136
388PhosphorylationSYRRSISSTVQRQLE
HHHHHHHHHHHHHHH
30.8130266825
389PhosphorylationYRRSISSTVQRQLES
HHHHHHHHHHHHHHH
17.5430266825
443UbiquitinationTQLVLRNKGVYESVK
HHHHHCCCCHHHHHH
43.2321963094
472UbiquitinationDLIHLGAKFSPCIRK
EEEECCCCCCCCCCC
44.5721963094
530PhosphorylationFVKWQDDTGPPMDKS
HHHHCCCCCCCCCHH
60.93-
544UbiquitinationSDLGQKRTSGAVCHQ
HHHCCCCCCCCCCCC
38.2521963094
573UbiquitinationIWPDDITKWPICTEQ
CCCCCCCCCCCCCHH
51.8421963094
576UbiquitinationDDITKWPICTEQARS
CCCCCCCCCCHHHHH
4.3921963094
605UbiquitinationRPCCIGTKGSCEITT
CEEECCCCCCEEEEH
43.5521963094
607PhosphorylationCCIGTKGSCEITTRE
EECCCCCCEEEEHHH
15.33-
700PhosphorylationIAIIFILSGITGNLA
HHHHHHHHCCCCCHH
24.27-
703PhosphorylationIFILSGITGNLASAI
HHHHHCCCCCHHHHH
24.44-
708PhosphorylationGITGNLASAIFLPYR
CCCCCHHHHHHCCCC
25.68-
819UbiquitinationFAGLFAALVLWLYIY
HHHHHHHHHHHHHHC
2.6721963094
848UbiquitinationFTSRFCEKYELDQVL
CCHHHHHHCCHHHHC
45.2521963094

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 RHDF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHDF2_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 RHDF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2V1_HUMANUBE2V1physical
29069608
UBE2N_HUMANUBE2Nphysical
29069608
CHIP_HUMANSTUB1physical
29069608

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
148500Tylosis with esophageal cancer (TOC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHDF2_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-90; SER-325 AND SER-328,AND MASS SPECTROMETRY.

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