RAD9A_HUMAN - dbPTM
RAD9A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD9A_HUMAN
UniProt AC Q99638
Protein Name Cell cycle checkpoint control protein RAD9A
Gene Name RAD9A
Organism Homo sapiens (Human).
Sequence Length 391
Subcellular Localization Nucleus .
Protein Description Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex..
Protein Sequence MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQYQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRKTHNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRSYHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHFDAPGRPAIFTIKDSLLDGHFVLATLSDTDSHSQDLGSPERHQPVPQLQAHSTPHPDDFANDDIDSYMIAMETTIGNEGSRVLPSISLSPGPQPPKSPGPHSEEEDEAEPSTVPGTPPPKKFRSLFFGSILAPVRSPQGPSPVLAEDSEGEG
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------MKCLVTGGN
------CCEEEECCC		35.9525953088
2Malonylation------MKCLVTGGN
------CCEEEECCC		35.9526320211
2Methylation------MKCLVTGGN
------CCEEEECCC		35.95115976059
15UbiquitinationGNVKVLGKAVHSLSR
CCEEEEHHHHHHHHH		42.97-
28PhosphorylationSRIGDELYLEPLEDG
HHCCCEEEEEECCCC		13.6322817900
79PhosphorylationRCKILMKSFLSVFRS
HHHHHHHHHHHHHHH		19.9026074081
82PhosphorylationILMKSFLSVFRSLAM
HHHHHHHHHHHHHHH		19.7326074081
86PhosphorylationSFLSVFRSLAMLEKT
HHHHHHHHHHHHHHH		14.7126074081
93PhosphorylationSLAMLEKTVEKCCIS
HHHHHHHHHHHHHHC		25.2326074081
96AcetylationMLEKTVEKCCISLNG
HHHHHHHHHHHCCCC		30.0325953088
96UbiquitinationMLEKTVEKCCISLNG
HHHHHHHHHHHCCCC		30.03-
167PhosphorylationSPALAEVTLGIGRGR
CHHHHEEEECCCCCC		15.69-
190PhosphorylationEEEADSTAKAMVTEM
HHHHHHHHHHHHHHH		11.1032142685
252PhosphorylationRPAIFTIKDSLLDGH
CCEEEEEECHHCCCE		37.9032142685
254PhosphorylationAIFTIKDSLLDGHFV
EEEEEECHHCCCEEE		26.3220873877
264PhosphorylationDGHFVLATLSDTDSH
CCEEEEEEECCCCCC		23.7230278072
266PhosphorylationHFVLATLSDTDSHSQ
EEEEEEECCCCCCCC		33.8227794612
268PhosphorylationVLATLSDTDSHSQDL
EEEEECCCCCCCCCC		35.7130278072
270PhosphorylationATLSDTDSHSQDLGS
EEECCCCCCCCCCCC		27.4221955146
272PhosphorylationLSDTDSHSQDLGSPE
ECCCCCCCCCCCCCC		29.3727794612
277PhosphorylationSHSQDLGSPERHQPV
CCCCCCCCCCCCCCC		30.7722617229
291PhosphorylationVPQLQAHSTPHPDDF
CCCCCCCCCCCCCCC		46.8026074081
292PhosphorylationPQLQAHSTPHPDDFA
CCCCCCCCCCCCCCC		18.7526074081
304PhosphorylationDFANDDIDSYMIAME
CCCCCCHHHHEEEEE		40.4833259812
324PhosphorylationEGSRVLPSISLSPGP
CCCEECCEEEECCCC		22.2025159151
326PhosphorylationSRVLPSISLSPGPQP
CEECCEEEECCCCCC		27.4230266825
328PhosphorylationVLPSISLSPGPQPPK
ECCEEEECCCCCCCC		22.4829255136
336PhosphorylationPGPQPPKSPGPHSEE
CCCCCCCCCCCCCCC		40.6430278072
341PhosphorylationPKSPGPHSEEEDEAE
CCCCCCCCCCCCCCC		50.2430278072
350PhosphorylationEEDEAEPSTVPGTPP
CCCCCCCCCCCCCCC		33.2830278072
351PhosphorylationEDEAEPSTVPGTPPP
CCCCCCCCCCCCCCC		41.2430278072
355PhosphorylationEPSTVPGTPPPKKFR
CCCCCCCCCCCHHHH		26.9325159151
363PhosphorylationPPPKKFRSLFFGSIL
CCCHHHHHHHCCCEE		32.4328176443
368PhosphorylationFRSLFFGSILAPVRS
HHHHHCCCEECCCCC		14.8526055452
375PhosphorylationSILAPVRSPQGPSPV
CEECCCCCCCCCCCC		23.0828176443
380PhosphorylationVRSPQGPSPVLAEDS
CCCCCCCCCCCCCCC		34.1724260401
387PhosphorylationSPVLAEDSEGEG---
CCCCCCCCCCCC---		38.7228176443
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
28YPhosphorylationKinaseABL1P00519
PhosphoELM
28YPhosphorylationKinaseABL-FAMILY-GPS
272SPhosphorylationKinaseATMQ13315
PSP
277SPhosphorylationKinaseCDK1P06493
PSP
292TPhosphorylationKinaseCDK1P06493
PSP
328SPhosphorylationKinaseCDK1P06493
PSP
328SPhosphorylationKinaseCDK2P24941
PSP
328SPhosphorylationKinaseTLK1Q9UKI8
PSP
336SPhosphorylationKinaseCDK1P06493
PSP
341SPhosphorylationKinaseCSNK2A1P68400
GPS
355TPhosphorylationKinaseCDK1P06493
PSP
355TPhosphorylationKinaseTLK1Q9UKI8
PSP
387SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD9A_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 RAD9A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANDR_HUMANARphysical
14966297
RAD1_HUMANRAD1physical
14611806
HUS1_HUMANHUS1physical
14611806
RAD17_HUMANRAD17physical
14611806
HUS1B_HUMANHUS1Bphysical
14611806
CLSPN_HUMANCLSPNphysical
12766152
HDAC1_HUMANHDAC1physical
10846170
RAD17_HUMANRAD17physical
12578958
ABL1_HUMANABL1physical
11971963
BCL2_HUMANBCL2physical
10620799
B2CL1_HUMANBCL2L1physical
10620799
HUS1_HUMANHUS1physical
9872989
RAD1_HUMANRAD1physical
9872989
HUS1_HUMANHUS1physical
11907025
RAD1_HUMANRAD1physical
11907025
TOPB1_HUMANTOPBP1physical
11395493
HUS1_HUMANHUS1physical
11994305
RAD1_HUMANRAD1physical
11994305
RAD17_HUMANRAD17physical
11572977
RAD1_HUMANRAD1physical
11572977
RFA1_HUMANRPA1physical
15897895
RFA2_HUMANRPA2physical
15897895
TOPB1_HUMANTOPBP1physical
12941802
SETMR_HUMANSETMARphysical
20457750
CSN5_HUMANCOPS5physical
17583730
MSH2_HUMANMSH2physical
20188637
MSH6_HUMANMSH6physical
20188637
MSH3_HUMANMSH3physical
20188637
RAD17_HUMANRAD17physical
20424596
CLSPN_HUMANCLSPNphysical
20424596
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 RAD9A_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-277; SER-375 ANDSER-387, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND SER-387, ANDMASS SPECTROMETRY.
"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-277; SER-375 ANDSER-387, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380 ANDSER-387, AND MASS SPECTROMETRY.
"Phosphorylation of human Rad9 is required for genotoxin-activatedcheckpoint signaling.";
Roos-Mattjus P., Hopkins K.M., Oestreich A.J., Vroman B.T.,Johnson K.L., Naylor S., Lieberman H.B., Karnitz L.M.;
J. Biol. Chem. 278:24428-24437(2003).
Cited for: PROTEIN SEQUENCE OF 270-280; 326-329; 373-383 AND 385-390,IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-272;SER-277; SER-328; SER-341; SER-375; SER-380 AND SER-387, ANDMUTAGENESIS OF SER-272; SER-277; SER-328; SER-341; SER-375; SER-380AND SER-387.
"c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein inresponse to DNA damage.";
Yoshida K., Komatsu K., Wang H.-G., Kufe D.;
Mol. Cell. Biol. 22:3292-3300(2002).
Cited for: INTERACTION WITH ABL1 AND BCL2L1, PHOSPHORYLATION, PHOSPHORYLATION ATTYR-28, AND MUTAGENESIS OF TYR-28.

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