RHPN2_HUMAN - dbPTM
RHPN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHPN2_HUMAN
UniProt AC Q8IUC4
Protein Name Rhophilin-2
Gene Name RHPN2
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization Cytoplasm, perinuclear region .
Protein Description Binds specifically to GTP-Rho. May function in a Rho pathway to limit stress fiber formation and/or increase the turnover of F-actin structures in the absence of high levels of RhoA activity..
Protein Sequence MTDALLPAAPQPLEKENDGYFRKGCNPLAQTGRSKLQNQRAALNQQILKAVRMRTGAENLLKVATNSKVREQVRLELSFVNSDLQMLKEELEGLNISVGVYQNTEEAFTIPLIPLGLKETKDVDFAVVLKDFILEHYSEDGYLYEDEIADLMDLRQACRTPSRDEAGVELLMTYFIQLGFVESRFFPPTRQMGLLFTWYDSLTGVPVSQQNLLLEKASVLFNTGALYTQIGTRCDRQTQAGLESAIDAFQRAAGVLNYLKDTFTHTPSYDMSPAMLSVLVKMMLAQAQESVFEKISLPGIRNEFFMLVKVAQEAAKVGEVYQQLHAAMSQAPVKENIPYSWASLACVKAHHYAALAHYFTAILLIDHQVKPGTDLDHQEKCLSQLYDHMPEGLTPLATLKNDQQRRQLGKSHLRRAMAHHEESVREASLCKKLRSIEVLQKVLCAAQERSRLTYAQHQEEDDLLNLIDAPSVVAKTEQEVDIILPQFSKLTVTDFFQKLGPLSVFSANKRWTPPRSIRFTAEEGDLGFTLRGNAPVQVHFLDPYCSASVAGAREGDYIVSIQLVDCKWLTLSEVMKLLKSFGEDEIEMKVVSLLDSTSSMHNKSATYSVGMQKTYSMICLAIDDDDKTDKTKKISKKLSFLSWGTNKNRQKSASTLCLPSVGAARPQVKKKLPSPFSLLNSDSSWY
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
20PhosphorylationLEKENDGYFRKGCNP
CCCCCCCCCCCCCCH		11.7728674419
23UbiquitinationENDGYFRKGCNPLAQ
CCCCCCCCCCCHHHH		58.8929967540
31PhosphorylationGCNPLAQTGRSKLQN
CCCHHHHHCHHHHHH		29.0225849741
34PhosphorylationPLAQTGRSKLQNQRA
HHHHHCHHHHHHHHH		38.7828258704
35UbiquitinationLAQTGRSKLQNQRAA
HHHHCHHHHHHHHHH		53.3727667366
49UbiquitinationALNQQILKAVRMRTG
HHHHHHHHHHHHHHC		46.6021963094
62UbiquitinationTGAENLLKVATNSKV
HCHHHHHHHHCCHHH		32.7529967540
68UbiquitinationLKVATNSKVREQVRL
HHHHCCHHHHHHHHH		47.59-
82PhosphorylationLELSFVNSDLQMLKE
HHHHHHHHHHHHHHH		34.1027499020
258NitrationRAAGVLNYLKDTFTH
HHHHHHHHHHHCCCC		15.80-
258Nitrated tyrosineRAAGVLNYLKDTFTH
HHHHHHHHHHHCCCC		15.80-
262PhosphorylationVLNYLKDTFTHTPSY
HHHHHHHCCCCCCCC		28.9222210691
269PhosphorylationTFTHTPSYDMSPAML
CCCCCCCCCCCHHHH		19.5022210691
272PhosphorylationHTPSYDMSPAMLSVL
CCCCCCCCHHHHHHH		13.4522210691
410UbiquitinationQQRRQLGKSHLRRAM
HHHHHHCHHHHHHHH		43.2129967540
423PhosphorylationAMAHHEESVREASLC
HHHHCHHHHHHHHHH		24.40-
441UbiquitinationRSIEVLQKVLCAAQE
HHHHHHHHHHHHHHH		32.77-
498UbiquitinationTVTDFFQKLGPLSVF
CHHHHHHHHCCCCCE		50.70-
529PhosphorylationEEGDLGFTLRGNAPV
EECCCCEEEECCCCE		17.4724719451
544PhosphorylationQVHFLDPYCSASVAG
EEEEECCCCCHHHCC		9.9427642862
576UbiquitinationLTLSEVMKLLKSFGE
ECHHHHHHHHHHCCC		56.7133845483
579UbiquitinationSEVMKLLKSFGEDEI
HHHHHHHHHCCCCHH		54.92-
580PhosphorylationEVMKLLKSFGEDEIE
HHHHHHHHCCCCHHH		38.15-
592PhosphorylationEIEMKVVSLLDSTSS
HHHHHHHHHHHCCCC		26.6323186163
596PhosphorylationKVVSLLDSTSSMHNK
HHHHHHHCCCCCCCC		30.1123911959
597PhosphorylationVVSLLDSTSSMHNKS
HHHHHHCCCCCCCCC		25.2028857561
598PhosphorylationVSLLDSTSSMHNKSA
HHHHHCCCCCCCCCC		29.6225849741
599PhosphorylationSLLDSTSSMHNKSAT
HHHHCCCCCCCCCCE		24.9325849741
603UbiquitinationSTSSMHNKSATYSVG
CCCCCCCCCCEEEEC		27.1329967540
604PhosphorylationTSSMHNKSATYSVGM
CCCCCCCCCEEEECC		31.0321945579
606PhosphorylationSMHNKSATYSVGMQK
CCCCCCCEEEECCCC		24.3419664994
607PhosphorylationMHNKSATYSVGMQKT
CCCCCCEEEECCCCE		10.9021945579
608PhosphorylationHNKSATYSVGMQKTY
CCCCCEEEECCCCEE		14.0821945579
614PhosphorylationYSVGMQKTYSMICLA
EEECCCCEEEEEEEE		12.1628387310
615PhosphorylationSVGMQKTYSMICLAI
EECCCCEEEEEEEEE		11.8626657352
616PhosphorylationVGMQKTYSMICLAID
ECCCCEEEEEEEEEC		13.6028355574
628PhosphorylationAIDDDDKTDKTKKIS
EECCCCCCCHHHHHH		50.1223312004
631PhosphorylationDDDKTDKTKKISKKL
CCCCCCHHHHHHHHH		40.1423312004
639PhosphorylationKKISKKLSFLSWGTN
HHHHHHHHHHHCCCC		32.7828355574
642PhosphorylationSKKLSFLSWGTNKNR
HHHHHHHHCCCCCCC		22.8128355574
645PhosphorylationLSFLSWGTNKNRQKS
HHHHHCCCCCCCCCC		36.4430206219
647UbiquitinationFLSWGTNKNRQKSAS
HHHCCCCCCCCCCCH		54.03-
651MethylationGTNKNRQKSASTLCL
CCCCCCCCCCHHEEC		44.76115976635
652PhosphorylationTNKNRQKSASTLCLP
CCCCCCCCCHHEECC		21.0730266825
654PhosphorylationKNRQKSASTLCLPSV
CCCCCCCHHEECCCC		29.0719664994
655PhosphorylationNRQKSASTLCLPSVG
CCCCCCHHEECCCCC		22.6230266825
660PhosphorylationASTLCLPSVGAARPQ
CHHEECCCCCCCCHH		21.8930266825
674PhosphorylationQVKKKLPSPFSLLNS
HHHHHCCCCCHHCCC		49.3522199227
677PhosphorylationKKLPSPFSLLNSDSS
HHCCCCCHHCCCCCC		35.0223090842
681PhosphorylationSPFSLLNSDSSWY--
CCCHHCCCCCCCC--		38.5523090842
683PhosphorylationFSLLNSDSSWY----
CHHCCCCCCCC----		23.6928102081
684PhosphorylationSLLNSDSSWY-----
HHCCCCCCCC-----		35.0728102081
686PhosphorylationLNSDSSWY-------
CCCCCCCC-------		15.6028102081
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 RHPN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHPN2_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 RHPN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOB_HUMANRHOBphysical
12473120
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 RHPN2_HUMAN

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-258, AND MASS SPECTROMETRY.
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-639, AND MASSSPECTROMETRY.

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