R3HC1_HUMAN - dbPTM
R3HC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID R3HC1_HUMAN
UniProt AC Q9Y3T6
Protein Name R3H and coiled-coil domain-containing protein 1 {ECO:0000312|HGNC:HGNC:27329}
Gene Name R3HCC1 {ECO:0000312|HGNC:HGNC:27329}
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization
Protein Description
Protein Sequence MALLCLDGVFLSSAENDFVHRIQEELDRFLLQKQLSKVLLFPPLSSRLRYLIHRTAENFDLLSSFSVGEGWKRRTVICHQDIRVPSSDGLSGPCRAPASCPSRYHGPRPISNQGAAAVPRGARAGRWYRGRKPDQPLYVPRVLRRQEEWGLTSTSVLKREAPAGRDPEEPGDVGAGDPNSDQGLPVLMTQGTEDLKGPGQRCENEPLLDPVGPEPLGPESQSGKGDMVEMATRFGSTLQLDLEKGKESLLEKRLVAEEEEDEEEVEEDGPSSCSEDDYSELLQEITDNLTKKEIQIEKIHLDTSSFVEELPGEKDLAHVVEIYDFEPALKTEDLLATFSEFQEKGFRIQWVDDTHALGIFPCLASAAEALTREFSVLKIRPLTQGTKQSKLKALQRPKLLRLVKERPQTNATVARRLVARALGLQHKKKERPAVRGPLPP
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
36PhosphorylationFLLQKQLSKVLLFPP
HHHHHHHHHHHHCCC		4.17-
45PhosphorylationVLLFPPLSSRLRYLI
HHHCCCHHHHHHHHH		3.19-
46PhosphorylationLLFPPLSSRLRYLIH
HHCCCHHHHHHHHHH		6.92-
49PhosphorylationPPLSSRLRYLIHRTA
CCHHHHHHHHHHHCH		4.3324719451
76PhosphorylationEGWKRRTVICHQDIR
CCCEECEEEECCCCC		20.44-
85PhosphorylationCHQDIRVPSSDGLSG
ECCCCCCCCCCCCCC		21.13-
86PhosphorylationHQDIRVPSSDGLSGP
CCCCCCCCCCCCCCC		42.91-
104PhosphorylationPASCPSRYHGPRPIS
CCCCCCCCCCCCCCC		22.8524905233
108MethylationPSRYHGPRPISNQGA
CCCCCCCCCCCCCCC		26.88115489811
111PhosphorylationYHGPRPISNQGAAAV
CCCCCCCCCCCCCCC		6.1524905233
120MethylationQGAAAVPRGARAGRW
CCCCCCCCCCCCCCC		43.33115389517
123MethylationAAVPRGARAGRWYRG
CCCCCCCCCCCCCCC		42.45115489817
141MethylationDQPLYVPRVLRRQEE
CCCCCHHHHCCCHHH		21.24115489805
154UbiquitinationEEWGLTSTSVLKREA
HHHCCCCHHHHCCCC		22.7924816145
178PhosphorylationGDVGAGDPNSDQGLP
CCCCCCCCCCCCCCC		18.3227642862
189PhosphorylationQGLPVLMTQGTEDLK
CCCCEEEECCCCCCC		13.32-
192PhosphorylationPVLMTQGTEDLKGPG
CEEEECCCCCCCCCC		26.48-
194PhosphorylationLMTQGTEDLKGPGQR
EEECCCCCCCCCCCC		20.0232142685
195PhosphorylationMTQGTEDLKGPGQRC
EECCCCCCCCCCCCC		25.8132142685
196UbiquitinationTQGTEDLKGPGQRCE
ECCCCCCCCCCCCCC		8.0724816145
229PhosphorylationSGKGDMVEMATRFGS
CCCCCHHHHHHHHCC		21.49-
232PhosphorylationGDMVEMATRFGSTLQ
CCHHHHHHHHCCEEE		19.26-
236PhosphorylationEMATRFGSTLQLDLE
HHHHHHCCEEEEEHH		75.3223401153
237PhosphorylationMATRFGSTLQLDLEK
HHHHHCCEEEEEHHH		38.5829255136
248PhosphorylationDLEKGKESLLEKRLV
EHHHHHHHHHHHHHH		11.6424719451
271PhosphorylationEVEEDGPSSCSEDDY
HHHHCCCCCCCCCHH		5.1126552605
272PhosphorylationVEEDGPSSCSEDDYS
HHHCCCCCCCCCHHH		25.8126552605
274PhosphorylationEDGPSSCSEDDYSEL
HCCCCCCCCCHHHHH		8.6626552605
276PhosphorylationGPSSCSEDDYSELLQ
CCCCCCCCHHHHHHH		24.1925850435
277PhosphorylationPSSCSEDDYSELLQE
CCCCCCCHHHHHHHH		20.9220736484
278PhosphorylationSSCSEDDYSELLQEI
CCCCCCHHHHHHHHH		5.2226552605
279PhosphorylationSCSEDDYSELLQEIT
CCCCCHHHHHHHHHH		32.7826552605
286PhosphorylationSELLQEITDNLTKKE
HHHHHHHHHCCCHHH		56.0226552605
290PhosphorylationQEITDNLTKKEIQIE
HHHHHCCCHHHEEEE		11.5326552605
337PhosphorylationKTEDLLATFSEFQEK
CHHHHHHHHHHHHHC		29.58-
339PhosphorylationEDLLATFSEFQEKGF
HHHHHHHHHHHHCCC		2.24-
344AcetylationTFSEFQEKGFRIQWV
HHHHHHHCCCEEEEC		22.8023236377
363PhosphorylationALGIFPCLASAAEAL
HHCHHHHHHHHHHHH		10.9027642862
377PhosphorylationLTREFSVLKIRPLTQ
HHHHCCEEEEEECCC		27.88-
379PhosphorylationREFSVLKIRPLTQGT
HHCCEEEEEECCCCC		32.90-
384AcetylationLKIRPLTQGTKQSKL
EEEEECCCCCCHHHH		53.1925953088
404UbiquitinationPKLLRLVKERPQTNA
HHHHHHHHHCCCCCH		12.11-
409PhosphorylationLVKERPQTNATVARR
HHHHCCCCCHHHHHH		14.9826699800
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 R3HC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of R3HC1_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 R3HC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of R3HC1_HUMAN !!
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 R3HC1_HUMAN

loading...

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 SER-276, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory