RHOF_HUMAN - dbPTM
RHOF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOF_HUMAN
UniProt AC Q9HBH0
Protein Name Rho-related GTP-binding protein RhoF
Gene Name RHOF
Organism Homo sapiens (Human).
Sequence Length 211
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm, cytoskeleton.
Protein Description Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Causes the formation of thin, actin-rich surface projections called filopodia. Functions cooperatively with CDC42 and Rac to generate additional structures, increasing the diversity of actin-based morphology..
Protein Sequence MDAPGALAQTAAPGPGRKELKIVIVGDGGCGKTSLLMVYSQGSFPEHYAPSVFEKYTASVTVGSKEVTLNLYDTAGQEDYDRLRPLSYQNTHLVLICYDVMNPTSYDNVLIKWFPEVTHFCRGIPMVLIGCKTDLRKDKEQLRKLRAAQLEPITYMQGLSACEQIRAALYLECSAKFRENVEDVFREAAKVALSALKKAQRQKKRRLCLLL
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
1Acetylation-------MDAPGALA
-------CCCCCCCC
10.0122814378
10PhosphorylationAPGALAQTAAPGPGR
CCCCCCCCCCCCCCC
21.1220068231
33PhosphorylationGDGGCGKTSLLMVYS
ECCCCCCEEEEEEEE
15.1923403867
34PhosphorylationDGGCGKTSLLMVYSQ
CCCCCCEEEEEEEEC
24.0023403867
40PhosphorylationTSLLMVYSQGSFPEH
EEEEEEEECCCCCCC
19.3623403867
43PhosphorylationLMVYSQGSFPEHYAP
EEEEECCCCCCCCCC
29.9523403867
48PhosphorylationQGSFPEHYAPSVFEK
CCCCCCCCCCCHHHE
20.67-
51PhosphorylationFPEHYAPSVFEKYTA
CCCCCCCCHHHEEEE
31.1323403867
56PhosphorylationAPSVFEKYTASVTVG
CCCHHHEEEEEEEEC
10.5923403867
59PhosphorylationVFEKYTASVTVGSKE
HHHEEEEEEEECCEE
15.5523403867
61PhosphorylationEKYTASVTVGSKEVT
HEEEEEEEECCEEEE
19.3623403867
64PhosphorylationTASVTVGSKEVTLNL
EEEEEECCEEEEEEE
22.7023403867
72PhosphorylationKEVTLNLYDTAGQED
EEEEEEEEECCCCCC
15.3527259358
74PhosphorylationVTLNLYDTAGQEDYD
EEEEEEECCCCCCHH
21.09-
80PhosphorylationDTAGQEDYDRLRPLS
ECCCCCCHHHHCCCC
11.3814506284
132UbiquitinationPMVLIGCKTDLRKDK
CEEEEEECCCCCCCH
39.60-
176UbiquitinationLYLECSAKFRENVED
HHHHHHHHHHHCHHH
28.7633845483
190UbiquitinationDVFREAAKVALSALK
HHHHHHHHHHHHHHH
34.7833845483
197UbiquitinationKVALSALKKAQRQKK
HHHHHHHHHHHHHHH
45.8633845483
1972-HydroxyisobutyrylationKVALSALKKAQRQKK
HHHHHHHHHHHHHHH
45.86-
208MethylationRQKKRRLCLLL----
HHHHHHEECCC----
2.09-
208GeranylgeranylationRQKKRRLCLLL----
HHHHHHEECCC----
2.09-

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 RHOF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOF_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 RHOF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANFY1_HUMANANKFY1physical
24102721
NAA25_HUMANNAA25physical
28514442
GDS1_HUMANRAP1GDS1physical
28514442
TCPW_HUMANCCT6Bphysical
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 RHOF_HUMAN

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Related Literatures of Post-Translational Modification

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