RASA2_HUMAN - dbPTM
RASA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASA2_HUMAN
UniProt AC Q15283
Protein Name Ras GTPase-activating protein 2
Gene Name RASA2
Organism Homo sapiens (Human).
Sequence Length 850
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region.
Protein Description Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4)..
Protein Sequence MAAAAPAAAAASSEAPAASATAEPEAGDQDSREVRVLQSLRGKICEAKNLLPYLGPHKMRDCFCTINLDQEEVYRTQVVEKSLSPFFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVAIKKEDLCNHSGKETWFSLQPVDSNSEVQGKVHLELKLNELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQFQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIKVPVNVLRTDSSHQAWYLLQPRDNGNKSSKTDDLGSLRLNICYTEDYVLPSEYYGPLKTLLLKSPDVQPISASAAYILSEICRDKNDAVLPLVRLLLHHDKLVPFATAVAELDLKDTQDANTIFRGNSLATRCLDEMMKIVGGHYLKVTLKPILDEICDSSKSCEIDPIKLKEGDNVENNKENLRYYVDKLFNTIVKSSMSCPTVMCDIFYSLRQMATQRFPNDPHVQYSAVSSFVFLRFFAVAVVSPHTFHLRPHHPDAQTIRTLTLISKTIQTLGSWGSLSKSKSSFKETFMCEFFKMFQEEGYIIAVKKFLDEISSTETKESSGTSEPVHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTYHKQPGSKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSRCNQNRLSFYHPSVYLNGNWLCCQETGENTLGCKPCTAGVPADIQIDIDEDRETERIYSLFTLSLLKLQKMEEACGTIAVYQGPQKEPDDYSNFVIEDSVTTFKTIQQIKSIIEKLDEPHEKYRKKRSSSAKYGSKENPIVGKAS
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------MAAAAPAAA
------CCCHHHHHH		13.0522223895
48SumoylationRGKICEAKNLLPYLG
CCCHHHHHCCHHHCC		26.32-
58AcetylationLPYLGPHKMRDCFCT
HHHCCCCCCCCEEEE		38.4725953088
124AcetylationRIGKVAIKKEDLCNH
CCCCEEEEHHHHCCC		40.1370509
134UbiquitinationDLCNHSGKETWFSLQ
HHCCCCCCCCEEEEE		55.7929967540
208AcetylationGPSRNDQKKTKVKKK
CCCCCHHHCCCCCCC		66.3319608861
209AcetylationPSRNDQKKTKVKKKT
CCCCHHHCCCCCCCC		48.2019608861
211AcetylationRNDQKKTKVKKKTSN
CCHHHCCCCCCCCCC		62.0219608861
213AcetylationDQKKTKVKKKTSNPQ
HHHCCCCCCCCCCCC		50.5419608861
214AcetylationQKKTKVKKKTSNPQF
HHCCCCCCCCCCCCC		65.36133589
216PhosphorylationKTKVKKKTSNPQFNE
CCCCCCCCCCCCCCE		42.4928464451
217PhosphorylationTKVKKKTSNPQFNEI
CCCCCCCCCCCCCEE		56.2328464451
226PhosphorylationPQFNEIFYFEVTRSS
CCCCEEEEEEEECCC		12.4227642862
233PhosphorylationYFEVTRSSSYTRKSQ
EEEEECCCCCCCCCC		24.8726074081
234PhosphorylationFEVTRSSSYTRKSQF
EEEECCCCCCCCCCE		31.6026074081
235PhosphorylationEVTRSSSYTRKSQFQ
EEECCCCCCCCCCEE		16.7126074081
239PhosphorylationSSSYTRKSQFQVEEE
CCCCCCCCCEEECHH		32.7029514088
302UbiquitinationDNGNKSSKTDDLGSL
CCCCCCCCCCCCCCE		64.1624816145
305UbiquitinationNKSSKTDDLGSLRLN
CCCCCCCCCCCEEEE		59.1524816145
308PhosphorylationSKTDDLGSLRLNICY
CCCCCCCCEEEEEEE		20.0124719451
324UbiquitinationEDYVLPSEYYGPLKT
CCCCCCHHHHCCHHH		40.6124816145
357UbiquitinationLSEICRDKNDAVLPL
HHHHCCCCCCCHHHH		37.0624816145
360UbiquitinationICRDKNDAVLPLVRL
HCCCCCCCHHHHHHH		17.7224816145
379UbiquitinationDKLVPFATAVAELDL
CCHHCHHHEEEECCC		23.2624816145
419UbiquitinationIVGGHYLKVTLKPIL
HHCCCEEEEEEHHHH		26.4732015554
423UbiquitinationHYLKVTLKPILDEIC
CEEEEEEHHHHHHHH		22.2032015554
440UbiquitinationSKSCEIDPIKLKEGD
CCCCCCCCCCCCCCC		31.1324816145
442UbiquitinationSCEIDPIKLKEGDNV
CCCCCCCCCCCCCCC		59.9229967540
462UbiquitinationNLRYYVDKLFNTIVK
HHHHHHHHHHHHHHH		44.96-
484PhosphorylationVMCDIFYSLRQMATQ
HHHHHHHHHHHHHHH		13.3124719451
501PhosphorylationPNDPHVQYSAVSSFV
CCCCCCCHHHHHHHH		9.4827251275
502PhosphorylationNDPHVQYSAVSSFVF
CCCCCCHHHHHHHHH		12.7127251275
505PhosphorylationHVQYSAVSSFVFLRF
CCCHHHHHHHHHHHH		20.1327251275
506PhosphorylationVQYSAVSSFVFLRFF
CCHHHHHHHHHHHHH		20.8727251275
537PhosphorylationPDAQTIRTLTLISKT
CCHHHHHHHHHHHHH		21.9030576142
542PhosphorylationIRTLTLISKTIQTLG
HHHHHHHHHHHHHHH		27.1930576142
544PhosphorylationTLTLISKTIQTLGSW
HHHHHHHHHHHHHCC		16.13-
550PhosphorylationKTIQTLGSWGSLSKS
HHHHHHHCCCCCCCC		31.2328348404
553PhosphorylationQTLGSWGSLSKSKSS
HHHHCCCCCCCCHHH		24.1825159151
555PhosphorylationLGSWGSLSKSKSSFK
HHCCCCCCCCHHHHH		36.2628348404
557PhosphorylationSWGSLSKSKSSFKET
CCCCCCCCHHHHHHH		34.1028450419
559PhosphorylationGSLSKSKSSFKETFM
CCCCCCHHHHHHHHH		48.3628450419
560PhosphorylationSLSKSKSSFKETFMC
CCCCCHHHHHHHHHH		44.0428464451
564PhosphorylationSKSSFKETFMCEFFK
CHHHHHHHHHHHHHH		19.7728450419
584UbiquitinationGYIIAVKKFLDEISS
CEEEEEHHHHHHHCC		44.5629967540
591PhosphorylationKFLDEISSTETKESS
HHHHHHCCCCCCCCC		35.6024719451
597PhosphorylationSSTETKESSGTSEPV
CCCCCCCCCCCCCCE		35.3129255136
598PhosphorylationSTETKESSGTSEPVH
CCCCCCCCCCCCCEE		47.3729255136
600PhosphorylationETKESSGTSEPVHLK
CCCCCCCCCCCEECC		31.6829255136
601PhosphorylationTKESSGTSEPVHLKE
CCCCCCCCCCEECCC		43.3528348404
607UbiquitinationTSEPVHLKEGEMYKR
CCCCEECCCCHHHHH		49.1229967540
612PhosphorylationHLKEGEMYKRAQGRT
ECCCCHHHHHCCCCC		7.94-
651PhosphorylationPGSKDAIYTIPVKNI
CCCCCCEEEEEHHHE		16.8227642862
656UbiquitinationAIYTIPVKNILAVEK
CEEEEEHHHEEEEEE		34.4429967540
759PhosphorylationDIDEDRETERIYSLF
ECCCCCCHHHHHHHH		32.12-
769PhosphorylationIYSLFTLSLLKLQKM
HHHHHHHHHHHHHHH		5.7120860994
782PhosphorylationKMEEACGTIAVYQGP
HHHHHHCEEEEEECC		1.1622817900
786PhosphorylationACGTIAVYQGPQKEP
HHCEEEEEECCCCCC		50.9522817900
796PhosphorylationPQKEPDDYSNFVIED
CCCCCCCCCCCEEEC		30.6822817900
808UbiquitinationIEDSVTTFKTIQQIK
EECCCCCHHHHHHHH		42.5029967540
809UbiquitinationEDSVTTFKTIQQIKS
ECCCCCHHHHHHHHH		21.5929967540
812UbiquitinationVTTFKTIQQIKSIIE
CCCHHHHHHHHHHHH		41.0229967540
814UbiquitinationTFKTIQQIKSIIEKL
CHHHHHHHHHHHHHC		31.1229967540
815UbiquitinationFKTIQQIKSIIEKLD
HHHHHHHHHHHHHCC		30.3529967540
816PhosphorylationKTIQQIKSIIEKLDE
HHHHHHHHHHHHCCC		3.9122210691
818UbiquitinationIQQIKSIIEKLDEPH
HHHHHHHHHHCCCHH		45.9929967540
833PhosphorylationEKYRKKRSSSAKYGS
HHHHHHHCCCCCCCC		38.0528634298
834PhosphorylationKYRKKRSSSAKYGSK
HHHHHHCCCCCCCCC		29.9928634298
835PhosphorylationYRKKRSSSAKYGSKE
HHHHHCCCCCCCCCC		15.8428634298
838PhosphorylationKRSSSAKYGSKENPI
HHCCCCCCCCCCCCC		31.3829759185
840PhosphorylationSSSAKYGSKENPIVG
CCCCCCCCCCCCCCC		58.0928122231
847UbiquitinationSKENPIVGKAS----
CCCCCCCCCCC----		34.2624816145
848UbiquitinationKENPIVGKAS-----
CCCCCCCCCC-----		17.9724816145
851UbiquitinationPIVGKAS--------
CCCCCCC--------		24816145
869Ubiquitination--------------------------
--------------------------		24816145
870Ubiquitination---------------------------
---------------------------		24816145
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 RASA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASA2_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 RASA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RASA2_HUMAN !!
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 RASA2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208; LYS-209; LYS-211 ANDLYS-213, AND MASS SPECTROMETRY.

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