R51A1_HUMAN - dbPTM
R51A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID R51A1_HUMAN
UniProt AC Q96B01
Protein Name RAD51-associated protein 1
Gene Name RAD51AP1 {ECO:0000312|EMBL:AAH16330.1, ECO:0000312|HGNC:HGNC:16956}
Organism Homo sapiens (Human).
Sequence Length 352
Subcellular Localization Nucleus. Colocalizes with RAD51 to multiple nuclear foci..
Protein Description May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Functionally cooperates with PALB2 in promoting of D-loop formation by RAD51. Binds to single and double stranded DNA, and is capable of aggregating DNA. Also binds RNA..
Protein Sequence MVRPVRHKKPVNYSQFDHSDSDDDFVSATVPLNKKSRTAPKELKQDKPKPNLNNLRKEEIPVQEKTPKKRLPEGTFSIPASAVPCTKMALDDKLYQRDLEVALALSVKELPTVTTNVQNSQDKSIEKHGSSKIETMNKSPHISNCSVASDYLDLDKITVEDDVGGVQGKRKAASKAAAQQRKILLEGSDGDSANDTEPDFAPGEDSEDDSDFCESEDNDEDFSMRKSKVKEIKKKEVKVKSPVEKKEKKSKSKCNALVTSVDSAPAAVKSESQSLPKKVSLSSDTTRKPLEIRSPSAESKKPKWVPPAASGGSRSSSSPLVVVSVKSPNQSLRLGLSRLARVKPLHPNATST
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
8SumoylationMVRPVRHKKPVNYSQ
CCCCCCCCCCCCHHH		48.48-
8SumoylationMVRPVRHKKPVNYSQ
CCCCCCCCCCCCHHH		48.48-
13PhosphorylationRHKKPVNYSQFDHSD
CCCCCCCHHHCCCCC		12.2325159151
13 (in isoform 2)Phosphorylation-12.23-
14 (in isoform 2)Phosphorylation-21.11-
14PhosphorylationHKKPVNYSQFDHSDS
CCCCCCHHHCCCCCC		21.1125159151
19 (in isoform 2)Phosphorylation-40.43-
19PhosphorylationNYSQFDHSDSDDDFV
CHHHCCCCCCCCCCE		40.4325159151
21 (in isoform 2)Phosphorylation-46.05-
21PhosphorylationSQFDHSDSDDDFVSA
HHCCCCCCCCCCEEE		46.0525159151
27PhosphorylationDSDDDFVSATVPLNK
CCCCCCEEEECCCCC		20.4422115753
29PhosphorylationDDDFVSATVPLNKKS
CCCCEEEECCCCCCC		18.3628102081
29 (in isoform 2)Phosphorylation-18.36-
44UbiquitinationRTAPKELKQDKPKPN
CCCCHHHCCCCCCCC		58.5024816145
57AcetylationPNLNNLRKEEIPVQE
CCHHHCCHHCCCCCC		63.9725038526
65UbiquitinationEEIPVQEKTPKKRLP
HCCCCCCCCCCCCCC		53.7033845483
65AcetylationEEIPVQEKTPKKRLP
HCCCCCCCCCCCCCC		53.7026051181
66PhosphorylationEIPVQEKTPKKRLPE
CCCCCCCCCCCCCCC		39.3229255136
66 (in isoform 2)Phosphorylation-39.3218669648
69UbiquitinationVQEKTPKKRLPEGTF
CCCCCCCCCCCCCCC		61.4424816145
75PhosphorylationKKRLPEGTFSIPASA
CCCCCCCCCCCCHHH		16.7320068231
77PhosphorylationRLPEGTFSIPASAVP
CCCCCCCCCCHHHCC		27.7420068231
81PhosphorylationGTFSIPASAVPCTKM
CCCCCCHHHCCCCHH		25.1720068231
86PhosphorylationPASAVPCTKMALDDK
CHHHCCCCHHHCCCH		20.1320068231
95PhosphorylationMALDDKLYQRDLEVA
HHCCCHHHHCHHHHH		13.7727642862
103 (in isoform 2)Phosphorylation-6.26-
106UbiquitinationLEVALALSVKELPTV
HHHHHHHHCHHCCEE		26.0733845483
112PhosphorylationLSVKELPTVTTNVQN
HHCHHCCEEEECCCC		43.0130108239
114PhosphorylationVKELPTVTTNVQNSQ
CHHCCEEEECCCCCC		18.3530108239
115PhosphorylationKELPTVTTNVQNSQD
HHCCEEEECCCCCCC		29.1130108239
115UbiquitinationKELPTVTTNVQNSQD
HHCCEEEECCCCCCC		29.1129967540
120PhosphorylationVTTNVQNSQDKSIEK
EEECCCCCCCCCHHH		23.7529255136
122 (in isoform 2)Phosphorylation-46.63-
123AcetylationNVQNSQDKSIEKHGS
CCCCCCCCCHHHHCC		45.7725953088
123UbiquitinationNVQNSQDKSIEKHGS
CCCCCCCCCHHHHCC		45.7733845483
124PhosphorylationVQNSQDKSIEKHGSS
CCCCCCCCHHHHCCC		44.2430108239
132AcetylationIEKHGSSKIETMNKS
HHHHCCCHHHCCCCC		46.3826051181
132UbiquitinationIEKHGSSKIETMNKS
HHHHCCCHHHCCCCC		46.3829967540
135PhosphorylationHGSSKIETMNKSPHI
HCCCHHHCCCCCCCC		29.5327080861
139UbiquitinationKIETMNKSPHISNCS
HHHCCCCCCCCCCCC		19.3929967540
139PhosphorylationKIETMNKSPHISNCS
HHHCCCCCCCCCCCC		19.3925159151
143PhosphorylationMNKSPHISNCSVASD
CCCCCCCCCCCCCHH		28.8430576142
146PhosphorylationSPHISNCSVASDYLD
CCCCCCCCCCHHCCC		25.6030576142
149PhosphorylationISNCSVASDYLDLDK
CCCCCCCHHCCCCCC		25.3230576142
151PhosphorylationNCSVASDYLDLDKIT
CCCCCHHCCCCCCCE		10.3020068231
152UbiquitinationCSVASDYLDLDKITV
CCCCHHCCCCCCCEE		6.7333845483
156UbiquitinationSDYLDLDKITVEDDV
HHCCCCCCCEEECCC		47.8029967540
158PhosphorylationYLDLDKITVEDDVGG
CCCCCCCEEECCCCC		24.4728122231
158UbiquitinationYLDLDKITVEDDVGG
CCCCCCCEEECCCCC		24.4724816145
169AcetylationDVGGVQGKRKAASKA
CCCCCCCHHHHHHHH		33.3725953088
169UbiquitinationDVGGVQGKRKAASKA
CCCCCCCHHHHHHHH		33.3733845483
174PhosphorylationQGKRKAASKAAAQQR
CCHHHHHHHHHHHHH		27.90-
175UbiquitinationGKRKAASKAAAQQRK
CHHHHHHHHHHHHHH		37.0024816145
224 (in isoform 2)Phosphorylation-6.71-
241PhosphorylationKKEVKVKSPVEKKEK
HHCCCCCCCHHHCHH		36.8526055452
260 (in isoform 3)Phosphorylation-19.2220068231
263 (in isoform 3)Phosphorylation-33.7120068231
263 (in isoform 2)Phosphorylation-33.71-
263PhosphorylationALVTSVDSAPAAVKS
EEEECCCCCCHHHHC		33.7120068231
265 (in isoform 3)Phosphorylation-25.3820068231
266 (in isoform 3)Phosphorylation-25.3020068231
267 (in isoform 3)Phosphorylation-14.2820068231
268 (in isoform 3)Phosphorylation-8.3420068231
269AcetylationDSAPAAVKSESQSLP
CCCCHHHHCCCCCCC		43.7226051181
274 (in isoform 3)Phosphorylation-56.7920068231
277 (in isoform 3)Phosphorylation-71.7220068231
277 (in isoform 2)Phosphorylation-71.72-
280PhosphorylationQSLPKKVSLSSDTTR
CCCCCCEECCCCCCC		31.2625159151
281 (in isoform 3)Phosphorylation-6.7720068231
282PhosphorylationLPKKVSLSSDTTRKP
CCCCEECCCCCCCCC		20.7529978859
283PhosphorylationPKKVSLSSDTTRKPL
CCCEECCCCCCCCCC		44.2429978859
285PhosphorylationKVSLSSDTTRKPLEI
CEECCCCCCCCCCEE		30.3727251275
286PhosphorylationVSLSSDTTRKPLEIR
EECCCCCCCCCCEEC		41.5127251275
294PhosphorylationRKPLEIRSPSAESKK
CCCCEECCCCCCCCC		28.9424260401
296PhosphorylationPLEIRSPSAESKKPK
CCEECCCCCCCCCCC		46.0125159151
299PhosphorylationIRSPSAESKKPKWVP
ECCCCCCCCCCCCCC		45.7728176443
301 (in isoform 2)Phosphorylation-62.20-
310PhosphorylationKWVPPAASGGSRSSS
CCCCCCCCCCCCCCC		45.8820068231
310 (in isoform 2)Phosphorylation-45.88-
315PhosphorylationAASGGSRSSSSPLVV
CCCCCCCCCCCCEEE		35.9524732914
316PhosphorylationASGGSRSSSSPLVVV
CCCCCCCCCCCEEEE		33.4524732914
317PhosphorylationSGGSRSSSSPLVVVS
CCCCCCCCCCEEEEE		36.9025159151
318PhosphorylationGGSRSSSSPLVVVSV
CCCCCCCCCEEEEEE		24.9725159151
324PhosphorylationSSPLVVVSVKSPNQS
CCCEEEEEECCCCHH		16.5324732914
326AcetylationPLVVVSVKSPNQSLR
CEEEEEECCCCHHHH		53.3319608861
326 (in isoform 2)Acetylation-53.33-
327PhosphorylationLVVVSVKSPNQSLRL
EEEEEECCCCHHHHH		27.2525159151
331PhosphorylationSVKSPNQSLRLGLSR
EECCCCHHHHHCHHH		23.3022617229
333 (in isoform 2)Phosphorylation-31.77-
334 (in isoform 2)Phosphorylation-11.11-
335 (in isoform 2)Phosphorylation-18.38-
343AcetylationLSRLARVKPLHPNAT
HHHHHHCCCCCCCCC		35.9923749302
350PhosphorylationKPLHPNATST-----
CCCCCCCCCC-----		39.2720068231
351PhosphorylationPLHPNATST------
CCCCCCCCC------		29.7018669648
352PhosphorylationLHPNATST-------
CCCCCCCC-------		37.9720068231
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 R51A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of R51A1_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 R51A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD51_HUMANRAD51physical
9396801
RAD51_HUMANRAD51physical
16920159
A4_HUMANAPPphysical
21832049
PLAK_HUMANJUPphysical
26186194
WDR48_HUMANWDR48physical
26186194
UBP1_HUMANUSP1physical
26186194
UBP46_HUMANUSP46physical
26186194
UBP1_HUMANUSP1physical
27463890
WDR48_HUMANWDR48physical
27463890
UBP46_HUMANUSP46physical
28514442
WDR48_HUMANWDR48physical
28514442
PLAK_HUMANJUPphysical
28514442
UBP1_HUMANUSP1physical
28514442
WDR48_HUMANWDR48physical
27239033
RAD51_HUMANRAD51physical
27239033
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 R51A1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-343, AND MASS SPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, 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-19; SER-21; THR-66;SER-280 AND SER-327, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.

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