RASF2_HUMAN - dbPTM
RASF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASF2_HUMAN
UniProt AC P50749
Protein Name Ras association domain-containing protein 2
Gene Name RASSF2
Organism Homo sapiens (Human).
Sequence Length 326
Subcellular Localization Nucleus. Cytoplasm. Chromosome, centromere, kinetochore . Translocates to the cytoplasm in the presence of STK3/MST2 AND STK4/MST1.
Protein Description Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation..
Protein Sequence MDYSHQTSLVPCGQDKYISKNELLLHLKTYNLYYEGQNLQLRHREEEDEFIVEGLLNISWGLRRPIRLQMQDDNERIRPPPSSSSWHSGCNLGAQGTTLKPLTVPKVQISEVDAPPEGDQMPSSTDSRGLKPLQEDTPQLMRTRSDVGVRRRGNVRTPSDQRRIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYVVHTSGEKQKLKATDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPVLKSFIQKLQEEEDREVKKLMRKYTVLRLMIRQRLEEIAETPATI
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
3Phosphorylation-----MDYSHQTSLV
-----CCCCCCCCCC		13.5227642862
4Phosphorylation----MDYSHQTSLVP
----CCCCCCCCCCC		12.5925907765
7Phosphorylation-MDYSHQTSLVPCGQ
-CCCCCCCCCCCCCC		20.7125907765
8PhosphorylationMDYSHQTSLVPCGQD
CCCCCCCCCCCCCCC		22.3125907765
20UbiquitinationGQDKYISKNELLLHL
CCCCEECCCHHHHEE		44.9029967540
24UbiquitinationYISKNELLLHLKTYN
EECCCHHHHEEEEEE		2.0021890473
85PhosphorylationRPPPSSSSWHSGCNL
CCCCCCCCCCCCCCC		30.6524247654
100UbiquitinationGAQGTTLKPLTVPKV
CCCCCCCCCCCCCEE		35.5721906983
103PhosphorylationGTTLKPLTVPKVQIS
CCCCCCCCCCEEEEE		43.2024719451
130UbiquitinationSSTDSRGLKPLQEDT
CCCCCCCCCCCCCCC		5.1221890473
131UbiquitinationSTDSRGLKPLQEDTP
CCCCCCCCCCCCCCH		46.6424816145
133UbiquitinationDSRGLKPLQEDTPQL
CCCCCCCCCCCCHHH		9.2324816145
137PhosphorylationLKPLQEDTPQLMRTR
CCCCCCCCHHHHHHH		16.5124719451
141SulfoxidationQEDTPQLMRTRSDVG
CCCCHHHHHHHHHHC		3.2821406390
142DimethylationEDTPQLMRTRSDVGV
CCCHHHHHHHHHHCC		35.26-
142MethylationEDTPQLMRTRSDVGV
CCCHHHHHHHHHHCC		35.2618938733
143PhosphorylationDTPQLMRTRSDVGVR
CCHHHHHHHHHHCCC		22.1426552605
144DimethylationTPQLMRTRSDVGVRR
CHHHHHHHHHHCCCC		22.09-
144MethylationTPQLMRTRSDVGVRR
CHHHHHHHHHHCCCC		22.0918938739
145PhosphorylationPQLMRTRSDVGVRRR
HHHHHHHHHHCCCCC		35.7122115753
151DimethylationRSDVGVRRRGNVRTP
HHHHCCCCCCCCCCH		48.75-
151MethylationRSDVGVRRRGNVRTP
HHHHCCCCCCCCCCH		48.7518938745
157PhosphorylationRRRGNVRTPSDQRRI
CCCCCCCCHHHHHHH		23.9029052541
159PhosphorylationRGNVRTPSDQRRIRR
CCCCCCHHHHHHHHH		45.8424719451
165DimethylationPSDQRRIRRHRFSIN
HHHHHHHHHHEEEEC		26.92-
165MethylationPSDQRRIRRHRFSIN
HHHHHHHHHHEEEEC		26.9218938751
170PhosphorylationRIRRHRFSINGHFYN
HHHHHEEEECCEECC		18.3323401153
180PhosphorylationGHFYNHKTSVFTPAY
CEECCCCCCEEECCC		23.6728857561
181PhosphorylationHFYNHKTSVFTPAYG
EECCCCCCEEECCCC		21.7528857561
184PhosphorylationNHKTSVFTPAYGSVT
CCCCCEEECCCCCEE		12.5930108239
187PhosphorylationTSVFTPAYGSVTNVR
CCEEECCCCCEEEEE		15.9030108239
189PhosphorylationVFTPAYGSVTNVRIN
EEECCCCCEEEEEEC		17.0628857561
191PhosphorylationTPAYGSVTNVRINST
ECCCCCEEEEEECCC		29.6930108239
198PhosphorylationTNVRINSTMTTPQVL
EEEEECCCCCCHHHH		17.6628857561
206UbiquitinationMTTPQVLKLLLNKFK
CCCHHHHHHHHHHHC		37.9322817900
208UbiquitinationTPQVLKLLLNKFKIE
CHHHHHHHHHHHCCC		4.7821890473
211UbiquitinationVLKLLLNKFKIENSA
HHHHHHHHHCCCCCH		48.2622817900
213UbiquitinationKLLLNKFKIENSAEE
HHHHHHHCCCCCHHH		51.2022817900
224PhosphorylationSAEEFALYVVHTSGE
CHHHEEEEEEECCCC		9.30-
270PhosphorylationDQVEEVTYDVAQYIK
HHEEEEEHHHHHHHH		17.37-
289UbiquitinationVLKSFIQKLQEEEDR
HHHHHHHHHHHHHHH		47.5229967540
305PhosphorylationVKKLMRKYTVLRLMI
HHHHHHHHHHHHHHH		7.5424719451
306PhosphorylationKKLMRKYTVLRLMIR
HHHHHHHHHHHHHHH		18.9924719451
325PhosphorylationEIAETPATI------
HHHCCCCCC------		28.5528450419
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 RASF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASF2_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 RASF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASK_HUMANKRASphysical
12732644
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV91_HUMANSUV39H1physical
23455924
AKAP9_HUMANAKAP9physical
24255178
CP131_HUMANCEP131physical
24255178
BIRC6_HUMANBIRC6physical
24255178
C1QBP_HUMANC1QBPphysical
24255178
HDAC6_HUMANHDAC6physical
24255178
OFD1_HUMANOFD1physical
24255178
COA7_HUMANCOA7physical
24255178
STK3_HUMANSTK3physical
24255178
STK4_HUMANSTK4physical
24255178
1433B_HUMANYWHABphysical
24255178
1433E_HUMANYWHAEphysical
24255178
1433G_HUMANYWHAGphysical
24255178
1433F_HUMANYWHAHphysical
24255178
1433T_HUMANYWHAQphysical
24255178
1433Z_HUMANYWHAZphysical
24255178
ANM3_HUMANPRMT3physical
23455924
RASF5_HUMANRASSF5physical
25416956
STK3_HUMANSTK3physical
26186194
STK4_HUMANSTK4physical
26186194
NEB1_HUMANPPP1R9Aphysical
26186194
PP2BA_HUMANPPP3CAphysical
26186194
PP2BB_HUMANPPP3CBphysical
26186194
1433F_HUMANYWHAHphysical
24366813
1433G_HUMANYWHAGphysical
24366813
CALL3_HUMANCALML3physical
24366813
STK4_HUMANSTK4physical
24366813
STK3_HUMANSTK3physical
24366813
SPR2E_HUMANSPRR2Ephysical
24366813
STK3_HUMANSTK3physical
28514442
STK4_HUMANSTK4physical
28514442
NEB1_HUMANPPP1R9Aphysical
28514442
PP2BA_HUMANPPP3CAphysical
28514442
1433G_HUMANYWHAGphysical
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 RASF2_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-145 AND THR-325, ANDMASS SPECTROMETRY.

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