RN207_HUMAN - dbPTM
RN207_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN207_HUMAN
UniProt AC Q6ZRF8
Protein Name RING finger protein 207
Gene Name RNF207
Organism Homo sapiens (Human).
Sequence Length 634
Subcellular Localization Cytoplasm . Probably located in the endoplasmic reticulum and/or possibly the cis-Golgi apparatus.
Protein Description Plays a role in cardiac repolarization possibly by stabilizing membrane expression of the potassium channel KCNH2/HERG, or by assisting its synthesis, folding or export from the endoplasmic reticulum, in a heat shock protein-dependent manner..
Protein Sequence MSGAIFGPLEGPSSLDAPSIHPLVCPLCHVQYERPCLLDCFHDFCAGCLRGRATDGRLTCPLCQHQTVLKGPSGLPPVDRLLQFLVDSSGDGVEAVRCANCDLECSEQDVETTYFCNTCGQPLCARCRDETHRARMFARHDIVALGQRSRDVPQKCTLHAEPYLLFSTDKKLLLCIRCFRDMQKESRAHCVDLESAYVQGCERLEQAVLAVKALQTATREAIALLQAMVEEVRHSAAEEEDAIHALFGSMQDRLAERKALLLQAVQSQYEEKDKAFKEQLSHLATLLPTLQVHLVICSSFLSLANKAEFLDLGYELMERLQGIVTRPHHLRPIQSSKIASDHRAEFARCLEPLLLLGPRRVAAAASGANTLAGGLGPKALTGPHCPSPVGKMSGSPVQKPTLHRSISTKVLLAEGENTPFAEHCRHYEDSYRHLQAEMQSLKDQVQELHRDLTKHHSLIKAEIMGDVLHKSLQLDVQIASEHASLEGMRVVFQEIWEEAYQRVANEQEIYEAQLHDLLQLRQENAYLTTITKQITPYVRSIAKVKERLEPRFQAPVDEQSESLQNTHDDSRNNAASARNNPGSVPEKREKTSEPKGNSWAPNGLSEEPLLKNMDHHRSKQKNGGDVPTWREHPT
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
131PhosphorylationCARCRDETHRARMFA
HHHHCCHHHHHHHHH
22.43-
289PhosphorylationHLATLLPTLQVHLVI
HHHHHHHHHHHHHHH
29.7722817900
302PhosphorylationVICSSFLSLANKAEF
HHHHHHHHHHCHHHH
24.3524173317
325PhosphorylationERLQGIVTRPHHLRP
HHHHCCCCCCCCCCC
36.24-
370PhosphorylationAAASGANTLAGGLGP
HHHCCCCCCCCCCCC
19.9022210691
387PhosphorylationLTGPHCPSPVGKMSG
CCCCCCCCCCCCCCC
37.3022210691
430PhosphorylationHCRHYEDSYRHLQAE
HHHHHHHHHHHHHHH
16.4827251275
457PhosphorylationRDLTKHHSLIKAEIM
HHHHHHHHHHHHHHH
31.3524719451
560PhosphorylationQAPVDEQSESLQNTH
CCCCCHHHHHHHHCC
27.4025850435
562PhosphorylationPVDEQSESLQNTHDD
CCCHHHHHHHHCCCC
40.2725850435

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 RN207_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN207_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 RN207_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNH2_HUMANKCNH2physical
25281747

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 RN207_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 THR-289, AND MASSSPECTROMETRY.

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