RASA1_HUMAN - dbPTM
RASA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASA1_HUMAN
UniProt AC P20936
Protein Name Ras GTPase-activating protein 1
Gene Name RASA1
Organism Homo sapiens (Human).
Sequence Length 1047
Subcellular Localization Cytoplasm .
Protein Description Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1..
Protein Sequence MMAAEAGSEEGGPVTAGAGGGGAAAGSSAYPAVCRVKIPAALPVAAAPYPGLVETGVAGTLGGGAALGSEFLGAGSVAGALGGAGLTGGGTAAGVAGAAAGVAGAAVAGPSGDMALTKLPTSLLAETLGPGGGFPPLPPPPYLPPLGAGLGTVDEGDSLDGPEYEEEEVAIPLTAPPTNQWYHGKLDRTIAEERLRQAGKSGSYLIRESDRRPGSFVLSFLSQMNVVNHFRIIAMCGDYYIGGRRFSSLSDLIGYYSHVSCLLKGEKLLYPVAPPEPVEDRRRVRAILPYTKVPDTDEISFLKGDMFIVHNELEDGWMWVTNLRTDEQGLIVEDLVEEVGREEDPHEGKIWFHGKISKQEAYNLLMTVGQVCSFLVRPSDNTPGDYSLYFRTNENIQRFKICPTPNNQFMMGGRYYNSIGDIIDHYRKEQIVEGYYLKEPVPMQDQEQVLNDTVDGKEIYNTIRRKTKDAFYKNIVKKGYLLKKGKGKRWKNLYFILEGSDAQLIYFESEKRATKPKGLIDLSVCSVYVVHDSLFGRPNCFQIVVQHFSEEHYIFYFAGETPEQAEDWMKGLQAFCNLRKSSPGTSNKRLRQVSSLVLHIEEAHKLPVKHFTNPYCNIYLNSVQVAKTHAREGQNPVWSEEFVFDDLPPDINRFEITLSNKTKKSKDPDILFMRCQLSRLQKGHATDEWFLLSSHIPLKGIEPGSLRVRARYSMEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLRIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLTHLLNILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNTTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLILVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGAQQHVLKKLLAITELLQQKQNQYTKTNDVR
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-------MMAAEAGS
-------CCCCCCCC
20.1522223895
5 (in isoform 4)Phosphorylation-43.9829116813
15PhosphorylationSEEGGPVTAGAGGGG
CCCCCCCCCCCCCCC
23.6222210691
27PhosphorylationGGGAAAGSSAYPAVC
CCCCCCCCCCCCCEE
13.6822210691
164PhosphorylationDSLDGPEYEEEEVAI
CCCCCCCCCEEEEEC
31.6022817900
239PhosphorylationIIAMCGDYYIGGRRF
HHHHHCCEEECCCCC
5.1427259358
240PhosphorylationIAMCGDYYIGGRRFS
HHHHCCEEECCCCCC
9.6024961811
300PhosphorylationVPDTDEISFLKGDMF
CCCCCCCCEECCCEE
23.6024719451
418PhosphorylationMGGRYYNSIGDIIDH
CCCCCCCCHHHHHHH
16.3023898821
443SulfoxidationYLKEPVPMQDQEQVL
ECCCCCCCCCHHHHH
7.5530846556
453PhosphorylationQEQVLNDTVDGKEIY
HHHHHHHCCCHHHHH
21.30-
460PhosphorylationTVDGKEIYNTIRRKT
CCCHHHHHHHHHHHC
13.821850098
462PhosphorylationDGKEIYNTIRRKTKD
CHHHHHHHHHHHCHH
10.0128152594
472PhosphorylationRKTKDAFYKNIVKKG
HHCHHHHHHHHHHHC
12.59-
480PhosphorylationKNIVKKGYLLKKGKG
HHHHHHCCEEECCCC
20.1029341593
581PhosphorylationAFCNLRKSSPGTSNK
HHHHHCCCCCCCCHH
35.0224719451
585PhosphorylationLRKSSPGTSNKRLRQ
HCCCCCCCCHHHHHH
32.2924719451
586PhosphorylationRKSSPGTSNKRLRQV
CCCCCCCCHHHHHHH
46.3928348404
612PhosphorylationKLPVKHFTNPYCNIY
CCCCCCCCCCCCCEE
34.7028152594
615PhosphorylationVKHFTNPYCNIYLNS
CCCCCCCCCCEEECC
10.5321082442
619PhosphorylationTNPYCNIYLNSVQVA
CCCCCCEEECCHHHH
5.9529341593
622PhosphorylationYCNIYLNSVQVAKTH
CCCEEECCHHHHHHC
16.0129341593
705PhosphorylationLKGIEPGSLRVRARY
CCCCCCCCCEEEEEE
24.5823403867
750PhosphorylationHVCGQDRTLLASILL
HHHCCCHHHHHHHHH
34.1223403867
754PhosphorylationQDRTLLASILLRIFL
CCHHHHHHHHHHHHH
17.4623403867
767PhosphorylationFLHEKLESLLLCTLN
HHHHHHHHHHHCCCC
34.4521955146
772PhosphorylationLESLLLCTLNDREIS
HHHHHHCCCCCCEEC
28.6821955146
779PhosphorylationTLNDREISMEDEATT
CCCCCEECCHHHHHH
16.0321955146
780SulfoxidationLNDREISMEDEATTL
CCCCEECCHHHHHHH
10.3930846556
785PhosphorylationISMEDEATTLFRATT
ECCHHHHHHHHHHHH
23.2221955146
786PhosphorylationSMEDEATTLFRATTL
CCHHHHHHHHHHHHH
30.8321955146
791PhosphorylationATTLFRATTLASTLM
HHHHHHHHHHHHHHH
20.3421955146
792PhosphorylationTTLFRATTLASTLME
HHHHHHHHHHHHHHH
21.2421955146
795PhosphorylationFRATTLASTLMEQYM
HHHHHHHHHHHHHHH
25.7821955146
796PhosphorylationRATTLASTLMEQYMK
HHHHHHHHHHHHHHH
25.2321955146
801PhosphorylationASTLMEQYMKATATQ
HHHHHHHHHHHHHHH
6.3021955146
817PhosphorylationVHHALKDSILKIMES
HHHHHHHHHHHHHHH
28.3824719451
824PhosphorylationSILKIMESKQSCELS
HHHHHHHHHCCCCCC
20.7229449344
827PhosphorylationKIMESKQSCELSPSK
HHHHHHCCCCCCHHH
17.1923927012
831PhosphorylationSKQSCELSPSKLEKN
HHCCCCCCHHHHCCC
12.5830266825
833PhosphorylationQSCELSPSKLEKNED
CCCCCCHHHHCCCCC
46.6330266825
834MalonylationSCELSPSKLEKNEDV
CCCCCHHHHCCCCCC
65.1426320211
863PhosphorylationVEKIFMASEILPPTL
HHHHHHHHHCCCHHH
17.2419845377
874PhosphorylationPPTLRYIYGCLQKSV
CHHHHHHHHHHHHHH
7.8919845377
952PhosphorylationEFGAKEPYMEGVNPF
HHCCCCCHHCCCCHH
14.6427259358

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
460YPhosphorylationKinaseEGFRP00533
PhosphoELM
460YPhosphorylationKinaseSRCP12931
GPS
460YPhosphorylationKinasePDGFR-FAMILY-GPS
460YPhosphorylationKinasePDGFR_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RASA1_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 RASA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOK1_HUMANDOK1physical
10822173
DOK2_HUMANDOK2physical
10822173
PAXI_HUMANPXNphysical
10092539
KHDR1_HUMANKHDRBS1physical
11604231
KHDR1_HUMANKHDRBS1physical
9743338
YES_HUMANYES1physical
1544885
NCK1_HUMANNCK1physical
9233798
EPHB2_HUMANEPHB2physical
9233798
HD_HUMANHTTphysical
9079622
SRC_HUMANSRCphysical
1717825
DOK1_HUMANDOK1physical
10799545
ANXA6_HUMANANXA6physical
10571081
EPHB3_HUMANEPHB3physical
9674711
EPHB2_HUMANEPHB2physical
10644995
CAV2_HUMANCAV2physical
12091389
G3BP1_HUMANG3BP1physical
9632780
RASH_HUMANHRASphysical
7628625
RASH_HUMANHRASphysical
9219684
PGFRB_HUMANPDGFRBphysical
11896619
RASH_HUMANHRASphysical
11389730
IKBA_HUMANNFKBIAgenetic
12151397
FBW1A_HUMANBTRCgenetic
12151397
NCK1_HUMANNCK1physical
21664272
TRM2A_HUMANTRMT2Aphysical
21900206
BBS10_HUMANBBS10physical
21900206
ZN579_HUMANZNF579physical
21900206
KAIN_HUMANSERPINA4physical
21900206
XRCC6_HUMANXRCC6physical
21900206
EIF1_HUMANEIF1physical
21900206
EZH2_HUMANEZH2physical
21900206
SOCS1_HUMANSOCS1physical
18556463
A4_HUMANAPPphysical
21832049
ERBB3_HUMANERBB3physical
16273093
ERBB4_HUMANERBB4physical
16273093
ABL1_HUMANABL1physical
1571536
PLCG1_HUMANPLCG1physical
8977179
DOK2_HUMANDOK2physical
9478921
DOK1_HUMANDOK1physical
9478921
KHDR1_HUMANKHDRBS1physical
1385407
EGFR_HUMANEGFRphysical
1385407
DOK1_MOUSEDok1physical
10202139
RHG35_HUMANARHGAP35physical
8419471
KHDR1_HUMANKHDRBS1physical
8419471
RHG35_HUMANARHGAP35physical
8189062
KHDR1_HUMANKHDRBS1physical
8189062
OLIG1_HUMANOLIG1physical
25814554
RASH_HUMANHRASphysical
26721396

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Mutations in the SH2 domain of RASA seem to be oncogenic and cause basal cell carcinomas.
608354
608355Parkes Weber syndrome (PKWS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RASA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND MASSSPECTROMETRY.

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