RHBT1_HUMAN - dbPTM
RHBT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHBT1_HUMAN
UniProt AC O94844
Protein Name Rho-related BTB domain-containing protein 1
Gene Name RHOBTB1
Organism Homo sapiens (Human).
Sequence Length 696
Subcellular Localization
Protein Description
Protein Sequence MDADMDYERPNVETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFDNAIRAALISRRHLQFWKSHLKKVQKPLLQAPFLPPKAPPPVIKIPECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESPNGSEGACEKEKQSRDFQGRILSVDPEEEREEGPPRIPQADQWKSSNKSLVEALGLEAEGAVPETQTLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMNQEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSGVGIDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREKEDIALNKHRSRRKWCFWNSSPAVA
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
69PhosphorylationCQEVLERSRDVVDEV
HHHHHHHCCCCHHHH
24.37-
77PhosphorylationRDVVDEVSVSLRLWD
CCCHHHHHHEEEEHH
12.1624719451
79PhosphorylationVVDEVSVSLRLWDTF
CHHHHHHEEEEHHCC
10.5624719451
97PhosphorylationHKDRRFAYGRSDVVV
CCCCCCCCCCCCEEE
15.4521712546
119UbiquitinationPNSLNHVKSMWYPEI
CCCCHHHHHHHCHHH
27.3521906983
352PhosphorylationQWKSSNKSLVEALGL
HHHHCCHHHHHHHCC
41.7328348404
398PhosphorylationSKRMGPMTVVRMDAS
HHCCCCEEEEECCCC
20.98-
480PhosphorylationNRIKECLSKGTFSDV
HHHHHHHHCCCCCCE
40.4722817900
483PhosphorylationKECLSKGTFSDVTFK
HHHHHCCCCCCEEEE
24.5722817900
485PhosphorylationCLSKGTFSDVTFKLD
HHHCCCCCCEEEEEC
30.89-
535PhosphorylationLPNINKISMQAVLDY
CCCCCHHCHHHHHHH
13.3722210691
542PhosphorylationSMQAVLDYLYTKQLS
CHHHHHHHHHHCCCC
9.46-
544PhosphorylationQAVLDYLYTKQLSPN
HHHHHHHHHCCCCCC
12.9822210691
679UbiquitinationKEDIALNKHRSRRKW
HHHHCCHHCHHCCCC
41.04-

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 RHBT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHBT1_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 RHBT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
18835386
CUL5_HUMANCUL5physical
18835386
CUL3_HUMANCUL3physical
23040068
LRC41_MOUSELrrc41physical
22709582
BPIA2_HUMANBPIFA2physical
28514442
CYTT_HUMANCST2physical
28514442
CYTN_HUMANCST1physical
28514442
CYTS_HUMANCST4physical
28514442
IGJ_HUMANIGJphysical
28514442
PIGR_HUMANPIGRphysical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
CYTD_HUMANCST5physical
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 RHBT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-483, ANDMASS SPECTROMETRY.

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