RASEF_HUMAN - dbPTM
RASEF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RASEF_HUMAN
UniProt AC Q8IZ41
Protein Name Ras and EF-hand domain-containing protein
Gene Name RASEF
Organism Homo sapiens (Human).
Sequence Length 740
Subcellular Localization Cytoplasm, perinuclear region .
Protein Description Binds predominantly GDP, and also GTP..
Protein Sequence MEADGDGEELARLRSVFAACDANRSGRLEREEFRALCTELRVRPADAEAVFQRLDADRDGAITFQEFARGFLGSLRGGRRRDWGPLDPAPAVSEAGPETHDSEEDEGDEDAAAALATSCGPASPGRAWQDFQARLGDEAKFIPREEQVSTLYQNINLVEPRLIQPYEHVIKNFIREIRLQSTEMENLAIAVKRAQDKAAMQLSELEEEMDQRIQAAEHKTRKDEKRKAEEALSDLRRQYETEVGDLQVTIKKLRKLEEQSKRVSQKEDVAALKKQIYDLSMENQKVKKDLLEAQTNIAFLQSELDALKSDYADQSLNTERDLEIIRAYTEDRNSLERQIEILQTANRKLHDSNDGLRSALENSYSKFNRSLHINNISPGNTISRSSPKFIGHSPQPLGYDRSSRSSYVDEDCDSLALCDPLQRTNCEVDSLPESCFDSGLSTLRDPNEYDSEVEYKHQRGFQRSHGVQESFGGDASDTDVPDIRDEETFGLEDVASVLDWKPQGSVSEGSIVSSSRKPISALSPQTDLVDDNAKSFSSQKAYKIVLAGDAAVGKSSFLMRLCKNEFRENISATLGVDFQMKTLIVDGERTVLQLWDTAGQERFRSIAKSYFRKADGVLLLYDVTCEKSFLNIREWVDMIEDAAHETVPIMLVGNKADIRDTAATEGQKCVPGHFGEKLAMTYGALFCETSAKDGSNIVEAVLHLAREVKKRTDKDDSRSITNLTGTNSKKSPQMKNCCNG
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
42UbiquitinationALCTELRVRPADAEA
HHHHHCCCCHHCHHH		15.6221890473
74PhosphorylationFARGFLGSLRGGRRR
HHHHHHHHHCCCCCC		19.6224719451
93PhosphorylationLDPAPAVSEAGPETH
CCCCCCCCCCCCCCC		24.6828348404
99PhosphorylationVSEAGPETHDSEEDE
CCCCCCCCCCCCCCC		33.8326471730
102PhosphorylationAGPETHDSEEDEGDE
CCCCCCCCCCCCCCH		34.9727251275
140UbiquitinationARLGDEAKFIPREEQ
HHHCCCCCCCCHHHH		41.6033845483
152PhosphorylationEEQVSTLYQNINLVE
HHHHHHHHHHCCCCC		10.2927642862
171 (in isoform 1)Ubiquitination-44.7221890473
171UbiquitinationQPYEHVIKNFIREIR
CCHHHHHHHHHHHHH		44.7221890473
192UbiquitinationENLAIAVKRAQDKAA
HHHHHHHHHHHHHHH		32.7532015554
203PhosphorylationDKAAMQLSELEEEMD
HHHHHHHHHHHHHHH		24.20-
233PhosphorylationRKAEEALSDLRRQYE
HHHHHHHHHHHHHHH		41.4624719451
237UbiquitinationEALSDLRRQYETEVG
HHHHHHHHHHHHHHH		51.2121890473
239PhosphorylationLSDLRRQYETEVGDL
HHHHHHHHHHHHHCH		24.02-
259UbiquitinationKLRKLEEQSKRVSQK
HHHHHHHHHHHCCHH		44.8921890473
264PhosphorylationEEQSKRVSQKEDVAA
HHHHHHCCHHHHHHH		39.30-
266UbiquitinationQSKRVSQKEDVAALK
HHHHCCHHHHHHHHH		48.6633845483
273UbiquitinationKEDVAALKKQIYDLS
HHHHHHHHHHHHHHH		37.5932015554
277PhosphorylationAALKKQIYDLSMENQ
HHHHHHHHHHHHCCH		14.34-
295PhosphorylationKDLLEAQTNIAFLQS
HHHHHHHHHHHHHHH		35.3222210691
302PhosphorylationTNIAFLQSELDALKS
HHHHHHHHHHHHHHH		42.1222210691
311PhosphorylationLDALKSDYADQSLNT
HHHHHHHCCCCCCCC		21.1128674419
315PhosphorylationKSDYADQSLNTERDL
HHHCCCCCCCCHHHH		24.9225849741
328PhosphorylationDLEIIRAYTEDRNSL
HHHHHHHHHCCCCHH		10.7923312004
329PhosphorylationLEIIRAYTEDRNSLE
HHHHHHHHCCCCHHH		30.3528102081
334PhosphorylationAYTEDRNSLERQIEI
HHHCCCCHHHHHHHH		32.2823312004
343UbiquitinationERQIEILQTANRKLH
HHHHHHHHHHCHHHC		44.2021890473
348UbiquitinationILQTANRKLHDSNDG
HHHHHCHHHCCCCHH		50.4033845483
352PhosphorylationANRKLHDSNDGLRSA
HCHHHCCCCHHHHHH		26.5227251275
358PhosphorylationDSNDGLRSALENSYS
CCCHHHHHHHHHHHH		42.1030622161
363PhosphorylationLRSALENSYSKFNRS
HHHHHHHHHHHCCCC		22.7728348404
364PhosphorylationRSALENSYSKFNRSL
HHHHHHHHHHCCCCC		27.7130622161
365UbiquitinationSALENSYSKFNRSLH
HHHHHHHHHCCCCCC		30.5021890473
365PhosphorylationSALENSYSKFNRSLH
HHHHHHHHHCCCCCC		30.5030622161
366UbiquitinationALENSYSKFNRSLHI
HHHHHHHHCCCCCCC		38.1222817900
366 (in isoform 1)Ubiquitination-38.1221890473
370PhosphorylationSYSKFNRSLHINNIS
HHHHCCCCCCCCCCC		25.9623312004
377PhosphorylationSLHINNISPGNTISR
CCCCCCCCCCCCCCC		28.9530266825
381PhosphorylationNNISPGNTISRSSPK
CCCCCCCCCCCCCCC		26.6730266825
383PhosphorylationISPGNTISRSSPKFI
CCCCCCCCCCCCCCC		24.8730266825
385PhosphorylationPGNTISRSSPKFIGH
CCCCCCCCCCCCCCC		44.1727251275
386PhosphorylationGNTISRSSPKFIGHS
CCCCCCCCCCCCCCC		30.8827251275
388 (in isoform 1)Ubiquitination-52.1121890473
388UbiquitinationTISRSSPKFIGHSPQ
CCCCCCCCCCCCCCC		52.1122817900
393PhosphorylationSPKFIGHSPQPLGYD
CCCCCCCCCCCCCCC		21.7323312004
399PhosphorylationHSPQPLGYDRSSRSS
CCCCCCCCCCCCCCC		18.8323898821
402PhosphorylationQPLGYDRSSRSSYVD
CCCCCCCCCCCCCCC		27.4924260401
403PhosphorylationPLGYDRSSRSSYVDE
CCCCCCCCCCCCCCC		36.7624719451
405PhosphorylationGYDRSSRSSYVDEDC
CCCCCCCCCCCCCCC		28.1528348404
406PhosphorylationYDRSSRSSYVDEDCD
CCCCCCCCCCCCCCH		28.2424719451
407PhosphorylationDRSSRSSYVDEDCDS
CCCCCCCCCCCCCHH		17.1126657352
414PhosphorylationYVDEDCDSLALCDPL
CCCCCCHHHHCCCHH		23.1327251275
424PhosphorylationLCDPLQRTNCEVDSL
CCCHHHCCCCCCCCC		31.1222210691
430PhosphorylationRTNCEVDSLPESCFD
CCCCCCCCCCHHHHC		51.5022210691
434PhosphorylationEVDSLPESCFDSGLS
CCCCCCHHHHCCCCC		20.3922210691
438PhosphorylationLPESCFDSGLSTLRD
CCHHHHCCCCCCCCC		22.7528102081
441PhosphorylationSCFDSGLSTLRDPNE
HHHCCCCCCCCCCCC		28.9928102081
442PhosphorylationCFDSGLSTLRDPNEY
HHCCCCCCCCCCCCC		30.7528102081
449PhosphorylationTLRDPNEYDSEVEYK
CCCCCCCCCCHHHHH		31.2627642862
451PhosphorylationRDPNEYDSEVEYKHQ
CCCCCCCCHHHHHHH		42.5127499020
470PhosphorylationRSHGVQESFGGDASD
HHCCCCCCCCCCCCC		16.4626657352
476PhosphorylationESFGGDASDTDVPDI
CCCCCCCCCCCCCCC		45.8723312004
478PhosphorylationFGGDASDTDVPDIRD
CCCCCCCCCCCCCCC		36.0827251275
520PhosphorylationSSSRKPISALSPQTD
CCCCCCCCCCCCCCC		31.5223898821
523PhosphorylationRKPISALSPQTDLVD
CCCCCCCCCCCCCCC		18.0616094384
526PhosphorylationISALSPQTDLVDDNA
CCCCCCCCCCCCCCC		34.3816094384
534UbiquitinationDLVDDNAKSFSSQKA
CCCCCCCCCCCCCCC		59.2832015554
535PhosphorylationLVDDNAKSFSSQKAY
CCCCCCCCCCCCCCC		28.13-
573PhosphorylationFRENISATLGVDFQM
HHHHHHHHHCCCEEE		19.77-
597PhosphorylationTVLQLWDTAGQERFR
HHHHHHHCCCHHHHH		22.5528857561
717PhosphorylationKRTDKDDSRSITNLT
HHCCCCCCCCCCCCC		37.7522496350
719PhosphorylationTDKDDSRSITNLTGT
CCCCCCCCCCCCCCC		37.4025849741
721PhosphorylationKDDSRSITNLTGTNS
CCCCCCCCCCCCCCC		25.9730266825
729UbiquitinationNLTGTNSKKSPQMKN
CCCCCCCCCCHHHCC		60.3832015554
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 RASEF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of RASEF_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 RASEF_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-526, ANDMASS SPECTROMETRY.

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