ATRIP_HUMAN - dbPTM
ATRIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATRIP_HUMAN
UniProt AC Q8WXE1
Protein Name ATR-interacting protein
Gene Name ATRIP
Organism Homo sapiens (Human).
Sequence Length 791
Subcellular Localization Nucleus . Redistributes to discrete nuclear foci upon DNA damage.
Protein Description Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein..
Protein Sequence MAGTSAPGSKRRSEPPAPRPGPPPGTGHPPSKRARGFSAAAAPDPDDPFGAHGDFTADDLEELDTLASQALSQCPAAARDVSSDHKVHRLLDGMSKNPSGKNRETVPIKDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQSELQFKDAEMNELRTKLQTSERANKLAAPSVSHVSPRKNPSVVIKPEACSPQFGKTSFPTKESFSANMSLPHPCQTESGYKPLVGREDSKPHSLRGDSIKQEEAQKSFVDSWRQRSNTQGSILINLLLKQPLIPGSSLSLCHLLSSSSESPAGTPLQPPGFGSTLAGMSGLRTTGSYDGSFSLSALREAQNLAFTGLNLVARNECSRDGDPAEGGRRAFPLCQLPGAVHFLPLVQFFIGLHCQALQDLAAAKRSGAPGDSPTHSSCVSSGVETNPEDSVCILEGFSVTALSILQHLVCHSGAVVSLLLSGVGADSAAGEGNRSLVHRLSDGDMTSALRGVADDQGQHPLLKMLLHLLAFSSAATGHLQASVLTQCLKVLVKLAENTSCDFLPRFQCVFQVLPKCLSPETPLPSVLLAVELLSLLADHDQLAPQLCSHSEGCLLLLLYMYITSRPDRVALETQWLQLEQEVVWLLAKLGVQSPLPPVTGSNCQCNVEVVRALTVMLHRQWLTVRRAGGPPRTDQQRRTVRCLRDTVLLLHGLSQKDKLFMMHCVEVLHQFDQVMPGVSMLIRGLPDVTDCEEAALDDLCAAETDVEDPEVECG
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
4Phosphorylation----MAGTSAPGSKR
----CCCCCCCCCCC		16.5123312004
5Phosphorylation---MAGTSAPGSKRR
---CCCCCCCCCCCC		31.3923312004
9PhosphorylationAGTSAPGSKRRSEPP
CCCCCCCCCCCCCCC		23.1723312004
13PhosphorylationAPGSKRRSEPPAPRP
CCCCCCCCCCCCCCC		59.4925159151
26PhosphorylationRPGPPPGTGHPPSKR
CCCCCCCCCCCCCHH		37.7824719451
31PhosphorylationPGTGHPPSKRARGFS
CCCCCCCCHHCCCCC		38.9424719451
32AcetylationGTGHPPSKRARGFSA
CCCCCCCHHCCCCCC		56.7112435493
38PhosphorylationSKRARGFSAAAAPDP
CHHCCCCCCCCCCCC		21.5928387310
68PhosphorylationEELDTLASQALSQCP
HHHHHHHHHHHHCCC		21.0622817900
72PhosphorylationTLASQALSQCPAAAR
HHHHHHHHCCCHHHH		32.5222817900
96UbiquitinationRLLDGMSKNPSGKNR
HHHHCCCCCCCCCCC		65.0817203973
122UbiquitinationEVLQAQYKELKEKMK
HHHHHHHHHHHHHHH		44.48-
148PhosphorylationEIKILRDSLHQTESV
CEEEEECCHHCHHHH		22.7129083192
152PhosphorylationLRDSLHQTESVLEEQ
EECCHHCHHHHHHHH		21.3429083192
154PhosphorylationDSLHQTESVLEEQRR
CCHHCHHHHHHHHHH		35.0829083192
162PhosphorylationVLEEQRRSHFLLEQE
HHHHHHHHHHHHHHH		22.3025159151
205UbiquitinationEMNELRTKLQTSERA
HHHHHHHHHHHHHHH		31.96-
214UbiquitinationQTSERANKLAAPSVS
HHHHHHHHHCCCCCC		38.22-
219PhosphorylationANKLAAPSVSHVSPR
HHHHCCCCCCCCCCC		31.3730278072
221PhosphorylationKLAAPSVSHVSPRKN
HHCCCCCCCCCCCCC		23.6230278072
224PhosphorylationAPSVSHVSPRKNPSV
CCCCCCCCCCCCCCE		17.3529255136
230PhosphorylationVSPRKNPSVVIKPEA
CCCCCCCCEEECCCC		38.1130108239
239PhosphorylationVIKPEACSPQFGKTS
EECCCCCCCCCCCCC		28.8723401153
270UbiquitinationCQTESGYKPLVGRED
CCCCCCCCCCCCCCC		35.09-
270AcetylationCQTESGYKPLVGRED
CCCCCCCCCCCCCCC		35.0926051181
278PhosphorylationPLVGREDSKPHSLRG
CCCCCCCCCCCCCCC		43.2528555341
282PhosphorylationREDSKPHSLRGDSIK
CCCCCCCCCCCCCCC		28.4329449344
295UbiquitinationIKQEEAQKSFVDSWR
CCHHHHHHHHHHHHH		53.56-
305PhosphorylationVDSWRQRSNTQGSIL
HHHHHHHCCCCCCHH		35.5718452278
307PhosphorylationSWRQRSNTQGSILIN
HHHHHCCCCCCHHHH		35.2418452278
310PhosphorylationQRSNTQGSILINLLL
HHCCCCCCHHHHHHH		12.3818452278
512PhosphorylationAAGEGNRSLVHRLSD
CCCCCCHHHEEECCC		38.4523403867
518PhosphorylationRSLVHRLSDGDMTSA
HHHEEECCCCCHHHH		39.2329255136
523PhosphorylationRLSDGDMTSALRGVA
ECCCCCHHHHHHCCC		18.6523927012
524PhosphorylationLSDGDMTSALRGVAD
CCCCCHHHHHHCCCC		20.7623927012
575PhosphorylationLVKLAENTSCDFLPR
HHHHHHCCCCCCHHH		23.4123403867
576PhosphorylationVKLAENTSCDFLPRF
HHHHHCCCCCCHHHH		24.2223403867
636PhosphorylationGCLLLLLYMYITSRP
HHHHHHHHHHHHCCC		6.45-
664 (in isoform 2)Phosphorylation-11.67-
735UbiquitinationHGLSQKDKLFMMHCV
CCCCHHHHHHHHHHH		51.14-
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
68SPhosphorylationKinaseATRQ13535
PSP
72SPhosphorylationKinaseATRQ13535
PSP
224SPhosphorylationKinaseCDK2P24941
PSP
239SPhosphorylationKinaseCDK2P24941
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATRIP_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 ATRIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSH2_HUMANMSH2physical
14657349
ATR_HUMANATRphysical
14657349
MCM7_HUMANMCM7physical
15210935
ATR_HUMANATRphysical
15210935
RFA1_HUMANRPA1physical
12791985
ATR_HUMANATRphysical
11721054
ATR_HUMANATRphysical
18344416
ATR_HUMANATRphysical
18283122
CE164_HUMANCEP164physical
18283122
ATR_HUMANATRphysical
15451423
ATR_HUMANATRphysical
17384638
ATR_HUMANATRphysical
20847938
ATR_HUMANATRphysical
15758953
ATM_HUMANATMphysical
15758953
PRKDC_HUMANPRKDCphysical
15758953
NBN_HUMANNBNphysical
15758953
HERC2_HUMANHERC2physical
21775519
MCM2_HUMANMCM2physical
21775519
CINP_HUMANCINPphysical
19889979
LNX1_HUMANLNX1physical
25416956
CA094_HUMANC1orf94physical
25416956
MT21A_HUMANMETTL21Aphysical
25416956
PEPL1_HUMANNPEPL1physical
26344197
ATR_HUMANATRphysical
28514442
MUL1_HUMANMUL1physical
28514442
PEX14_HUMANPEX14physical
28514442
FANCL_HUMANFANCLphysical
23723247
FP100_HUMANC17orf70physical
23723247
ATRIP_HUMANATRIPphysical
23723247
RFA1_HUMANRPA1physical
22258451
TELO2_HUMANTELO2physical
17384638
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 ATRIP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-518, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, AND MASSSPECTROMETRY.

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