RASF1_HUMAN - dbPTM
RASF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASF1_HUMAN
UniProt AC Q9NS23
Protein Name Ras association domain-containing protein 1
Gene Name RASSF1 {ECO:0000312|EMBL:AAF35128.2}
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Isoform A: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Nucleus. Localizes to cytoplasmic microtubules during interphase, to bipo
Protein Description Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage..
Protein Sequence MSGEPELIELRELAPAGRAGKGRTRLERANALRIARGTACNPTRQLVPGRGHRFQPAGPATHTWCDLCGDFIWGVVRKGLQCARLSADCKFTCHYRCRALVCLDCCGPRDLGWEPAVERDTNVDEPVEWETPDLSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSVPSSKKPPSLQDARRGPGRGTSVRRRTSFYLPKDAVKHLHVLSRTRAREVIEALLRKFLVVDDPRKFALFERAERHGQVYLRKLLDDEQPLRLRLLAGPSDKALSFVLKENDSGEVNWDAFSMPELHNFLRILQREEEEHLRQILQKYSYCRQKIQEALHACPLG
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
2Acetylation------MSGEPELIE
------CCCCCCEEH		52.4419369195
2Phosphorylation------MSGEPELIE
------CCCCCCEEH		52.4419369195
18MethylationRELAPAGRAGKGRTR
HHHCCCCCCCCCCHH		42.1254558513
21AcetylationAPAGRAGKGRTRLER
CCCCCCCCCCHHHHH		44.2112429679
29UbiquitinationGRTRLERANALRIAR
CCHHHHHHHHHHHHC		9.0329967540
30UbiquitinationRTRLERANALRIARG
CHHHHHHHHHHHHCC		45.8129967540
36MethylationANALRIARGTACNPT
HHHHHHHCCCCCCCC		40.3924129315
38PhosphorylationALRIARGTACNPTRQ
HHHHHCCCCCCCCCC		23.60-
43PhosphorylationRGTACNPTRQLVPGR
CCCCCCCCCCCCCCC		19.63-
52PhosphorylationQLVPGRGHRFQPAGP
CCCCCCCCCCCCCCC		26.4832645325
61UbiquitinationFQPAGPATHTWCDLC
CCCCCCCCCCHHHHH		23.9929967540
68UbiquitinationTHTWCDLCGDFIWGV
CCCHHHHHHHHHHHH		2.9129967540
81UbiquitinationGVVRKGLQCARLSAD
HHHHHCCCHHHCCCC		27.7421890473
81UbiquitinationGVVRKGLQCARLSAD
HHHHHCCCHHHCCCC		27.7421890473
81 (in isoform 3)Ubiquitination-27.7421890473
90UbiquitinationARLSADCKFTCHYRC
HHCCCCCCCCHHHCC		44.2329967540
107UbiquitinationLVCLDCCGPRDLGWE
EEEHHHCCCHHCCCC		26.9729967540
110UbiquitinationLDCCGPRDLGWEPAV
HHHCCCHHCCCCCCC		53.3029967540
111UbiquitinationDCCGPRDLGWEPAVE
HHCCCHHCCCCCCCC		10.1729967540
126UbiquitinationRDTNVDEPVEWETPD
CCCCCCCCCCCCCCC		25.5129967540
133PhosphorylationPVEWETPDLSQAEIE
CCCCCCCCCHHHHHH		67.3932645325
135PhosphorylationEWETPDLSQAEIEQK
CCCCCCCHHHHHHHH		34.4222817900
138UbiquitinationTPDLSQAEIEQKIKE
CCCCHHHHHHHHHHH		39.1529967540
142UbiquitinationSQAEIEQKIKEYNAQ
HHHHHHHHHHHHHCC		42.8529967540
146PhosphorylationIEQKIKEYNAQINSN
HHHHHHHHHCCCCCC		15.7027067055
152PhosphorylationEYNAQINSNLFMSLN
HHHCCCCCCEEEEEC		36.2227067055
157PhosphorylationINSNLFMSLNKDGSY
CCCCEEEEECCCCCC		22.8127067055
162 (in isoform 4)Ubiquitination-24.9421890473
162UbiquitinationFMSLNKDGSYTGFIK
EEEECCCCCCEEEEE		24.9421890473
162UbiquitinationFMSLNKDGSYTGFIK
EEEECCCCCCEEEEE		24.9421890473
171UbiquitinationYTGFIKVQLKLVRPV
CEEEEEEEEEEECCC		28.0729967540
179PhosphorylationLKLVRPVSVPSSKKP
EEEECCCCCCCCCCC		30.87-
180UbiquitinationKLVRPVSVPSSKKPP
EEECCCCCCCCCCCC		5.6229967540
181UbiquitinationLVRPVSVPSSKKPPS
EECCCCCCCCCCCCC		25.9429967540
182PhosphorylationVRPVSVPSSKKPPSL
ECCCCCCCCCCCCCH		53.2728555341
183PhosphorylationRPVSVPSSKKPPSLQ
CCCCCCCCCCCCCHH		38.33-
184UbiquitinationPVSVPSSKKPPSLQD
CCCCCCCCCCCCHHH		73.8929967540
185UbiquitinationVSVPSSKKPPSLQDA
CCCCCCCCCCCHHHH		65.2029967540
188PhosphorylationPSSKKPPSLQDARRG
CCCCCCCCHHHHHCC		47.3822817900
188UbiquitinationPSSKKPPSLQDARRG
CCCCCCCCHHHHHCC		47.3829967540
198MethylationDARRGPGRGTSVRRR
HHHCCCCCCCCCCCC		48.64115490345
201PhosphorylationRGPGRGTSVRRRTSF
CCCCCCCCCCCCCCE		19.22-
203PhosphorylationPGRGTSVRRRTSFYL
CCCCCCCCCCCCEEC		23.3332645325
206PhosphorylationGTSVRRRTSFYLPKD
CCCCCCCCCEECCHH		22.7530266825
207UbiquitinationTSVRRRTSFYLPKDA
CCCCCCCCEECCHHH		15.3029967540
207PhosphorylationTSVRRRTSFYLPKDA
CCCCCCCCEECCHHH		15.3030266825
209PhosphorylationVRRRTSFYLPKDAVK
CCCCCCEECCHHHHH		23.1230266825
212UbiquitinationRTSFYLPKDAVKHLH
CCCEECCHHHHHHHH		56.5829967540
216UbiquitinationYLPKDAVKHLHVLSR
ECCHHHHHHHHHHCH		42.0129967540
222PhosphorylationVKHLHVLSRTRAREV
HHHHHHHCHHHHHHH		30.4322817900
224PhosphorylationHLHVLSRTRAREVIE
HHHHHCHHHHHHHHH		25.8822817900
232UbiquitinationRAREVIEALLRKFLV
HHHHHHHHHHHHHCC		10.7721890473
232 (in isoform 2)Ubiquitination-10.7721890473
232UbiquitinationRAREVIEALLRKFLV
HHHHHHHHHHHHHCC		10.7721890473
236UbiquitinationVIEALLRKFLVVDDP
HHHHHHHHHCCCCCH		42.9122817900
236 (in isoform 5)Ubiquitination-42.9121890473
236 (in isoform 1)Ubiquitination-42.9121890473
241UbiquitinationLRKFLVVDDPRKFAL
HHHHCCCCCHHHHHH		53.3629967540
245UbiquitinationLVVDDPRKFALFERA
CCCCCHHHHHHHHHH		40.1429967540
252UbiquitinationKFALFERAERHGQVY
HHHHHHHHHHHCCEE		15.8129967540
258UbiquitinationRAERHGQVYLRKLLD
HHHHHCCEEHHHHCC		6.0229967540
259PhosphorylationAERHGQVYLRKLLDD
HHHHCCEEHHHHCCC		7.9128152594
262UbiquitinationHGQVYLRKLLDDEQP
HCCEEHHHHCCCCCC		51.2929967540
277UbiquitinationLRLRLLAGPSDKALS
CEEEEECCCCCHHHH		23.3929967540
281UbiquitinationLLAGPSDKALSFVLK
EECCCCCHHHHEEEE		56.4129967540
284PhosphorylationGPSDKALSFVLKEND
CCCCHHHHEEEECCC		20.4027067055
322UbiquitinationEEEEHLRQILQKYSY
HHHHHHHHHHHHHHH		47.2929967540
326UbiquitinationHLRQILQKYSYCRQK
HHHHHHHHHHHHHHH		32.4929967540
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
38TPhosphorylationKinaseCHEK1O14757
GPS
43TPhosphorylationKinaseCHEK1O14757
GPS
131SPhosphorylationKinaseATMQ13315
PSP
131SPhosphorylationKinaseATRQ13535
PSP
135SPhosphorylationKinaseATMQ13315
PSP
175SPhosphorylationKinaseGSK3BP49841
PSP
178SPhosphorylationKinaseGSK3BP49841
PSP
179SPhosphorylationKinaseGSK3BP49841
PSP
184SPhosphorylationKinaseCHEK1O14757
GPS
197SPhosphorylationKinasePRKCAP17252
GPS
202TPhosphorylationKinaseAURKAO14965
GPS
203SPhosphorylationKinaseAURKAO14965
GPS
203SPhosphorylationKinaseAURKBQ96GD4
GPS
203SPhosphorylationKinaseCDK4P11802
PSP
203SPhosphorylationKinasePRKACAP17612
GPS
203SPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseCDC20Q12834
PMID:21874044
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:18071316
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASF1_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 RASF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAP1B_HUMANMAP1Bphysical
15205320
MAP1S_HUMANMAP1Sphysical
15205320
CNKR1_HUMANCNKSR1physical
15075335
TBG1_HUMANTUBG1physical
14603253
TBB5_HUMANTUBBphysical
14603253
RASH_HUMANHRASphysical
10998413
RASF1_HUMANRASSF1physical
11857081
DAXX_HUMANDAXXphysical
16810318
CUL1_HUMANCUL1physical
18071316
SKP2_HUMANSKP2physical
18071316
SKP1_HUMANSKP1physical
18071316
CDC20_HUMANCDC20physical
21874044
DDB1_HUMANDDB1physical
21205828
CUL4A_HUMANCUL4Aphysical
21205828
MAST2_HUMANMAST2physical
22195963
SAV1_HUMANSAV1physical
17379520
STK3_HUMANSTK3physical
17379520
LATS1_HUMANLATS1physical
17379520
SAV1_HUMANSAV1physical
21489991
FBW1A_HUMANBTRCphysical
21910689
GSK3B_HUMANGSK3Bphysical
21910689
CDC20_HUMANCDC20physical
18372912
ID1_HUMANID1physical
18372912
STK4_HUMANSTK4physical
17598981
STK3_HUMANSTK3physical
17598981
STK3_HUMANSTK3physical
20086174
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
DAXX_HUMANDAXXphysical
23038753
MDM2_HUMANMDM2physical
23038753
E4F1_HUMANE4F1physical
14729613
E4F1_HUMANE4F1genetic
14729613
HGFL_HUMANMST1physical
14729613
STK3_HUMANSTK3physical
14729613
NDUV2_HUMANNDUFV2physical
26186194
MAP1B_HUMANMAP1Bphysical
26186194
STK3_HUMANSTK3physical
26186194
STK4_HUMANSTK4physical
26186194
MAP1S_HUMANMAP1Sphysical
26186194
IPRI_HUMANITPRIPphysical
26186194
MTHR_HUMANMTHFRphysical
26186194
LRP6_HUMANLRP6physical
26186194
SNX27_HUMANSNX27physical
26186194
H2A2B_HUMANHIST2H2ABphysical
26186194
IPRI_HUMANITPRIPphysical
24366813
MAP1B_HUMANMAP1Bphysical
24366813
MAP1S_HUMANMAP1Sphysical
24366813
STK4_HUMANSTK4physical
24366813
STK3_HUMANSTK3physical
24366813
XPO6_HUMANXPO6physical
24366813
RASF1_HUMANRASSF1physical
26578655
RHOA_HUMANRHOAphysical
26825171
SMUF1_HUMANSMURF1physical
26825171
TGFR1_HUMANTGFBR1physical
27292796
TGFR2_HUMANTGFBR2physical
27292796
ITCH_HUMANITCHphysical
27292796
STK4_HUMANSTK4physical
28514442
STK3_HUMANSTK3physical
28514442
MAP1S_HUMANMAP1Sphysical
28514442
SNX27_HUMANSNX27physical
28514442
MTHR_HUMANMTHFRphysical
28514442
MAP1B_HUMANMAP1Bphysical
28514442
IPRI_HUMANITPRIPphysical
28514442
LRP6_HUMANLRP6physical
28514442
NDUV2_HUMANNDUFV2physical
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 RASF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-188, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND MASSSPECTROMETRY.

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