TOPB1_MOUSE - dbPTM
TOPB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOPB1_MOUSE
UniProt AC Q6ZQF0
Protein Name DNA topoisomerase 2-binding protein 1
Gene Name Topbp1
Organism Mus musculus (Mouse).
Sequence Length 1515
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome. Has a uniform nuclear distribution during G phase. Colocalizes with BRCA1 at stalled replication forks during S phase. In
Protein Description Required for DNA replication (By similarity). Plays a role in the rescue of stalled replication forks and checkpoint control. [PubMed: 14718568 Binds double-stranded DNA breaks and nicks as well as single-stranded DNA (By similarity Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage (By similarity Induces a large increase in the kinase activity of ATR (By similarity]
Protein Sequence MSRNDQEPFLVKFLKSSDNSECFFKALESIKELQSEDYLQIITDEEALKIRENDKSLYICDRFSGTVFDHLKQLGCRIVGPQVVTFCMRHQQCVPRAEHPVYNMIMSDVTVSCTSLDKDKREEVHKYVQMMGGRVYRDLNVSVTHLIAGEVGSKKYLVAANLKKPILLPSWIKTLWEKSQEKKITKYTDVNMEDFKCPIFLGCIICVTGLNGIHRKTVQQLTAKHGGQYMGQLKMNECTHLIVQEPKGQKYECARRWNVHCVTLQWFHDSIEKGFCQDESIYKAETRVEAKMVPDTSTPTAQSNAESHTLADVSHISNINGSCVNETMFGSTTSKLECSLENLENLDISMFQAPEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDDVRQFWSKSSHRPHVVGAKWLLECFTKGYILPEESYIHTNYQPAGIAVSDQPGNQTAVLDKSGSFSKSALVPAERLQQADEDLLAQYGNDDSTMVEAKLSEALEPEVGPCPGSAHREPCDDSTHISVQEENKSSVSHCILDDSTVREEGLFSQKSFLVLGFSVENKCNIVDIIREHAGKIVSLPSRIVADYAVVPLLGCEVDVTVGEVVTNTWLVTCIDNQTLVDPKSNPLFTPVSVMSGVTPLEDCVISFSQCVGAERDSLVFLANHLGASVQEFFVRKANAKKGMLASTHLIVKEPTGSKYEAAKKWSLPAVNISWLLETARIGKRADENHFLVDNAPKQEQVLETKIPNGVSSNPDLPAHPDAHLEIHRKKAVTPLDMNRFQSRAFRAVISQQRGQDPTFPPVRQPLTKEPSLHLDTPSKFLSKDKLFKPSFDVTDALAALETPNAASQKRKLSSPLSEVIVRNLTVALANSSRNTDSHSASPQLKGAHLEEEETRKPLDSVVVCVSKKLSKKQSELNGVAASLGAEYRWSFDETVTHFIYQGRANDSNREYKSAKERGVHIVSEHWLLECAQEYKHLPESLYPHTYNPKMSLDINTVQDGRLCNSRAPLAVSASKDDGPDHLSVEGNETNTMGTNDKESPLLNGSGRDDCKGALTQALEMRENFQKQLQEIMSATCIVKTPAQKTCMSRSSCNSASSTPDSARSVRSGRSRVLEALRQSRQAVPDVNTEPSQNEQIIWDDPTAREERARLASNLQWPSDPTQHSELQVEIKMPDDSPSRKPVYHSEIAEQASCVTQAPGHPGSEEPEPPVAERPLIPEPQAPAVASPLAKPPVAPQPADKIETQEETHRKVKKQYVFQMSSLNSQERIDYCRLIKDLGGSVIEKQCSDPSCTHMVVGYPLRNEKYLASMAAGKWVLHRSYLDACKTAGRFVQEEDYEWGSSSILDALPDVTEHQQKLALAAMRWRKRIQQSQESGIVEGAFSGWKAILRVDRPREAGFKRLLQAGGAKVLSGHPEPLLKDATHLFCDFNKLKPDDCRVFIAEATAQNMVCLKTEYIADYLMLESPPCADNYRVSEAALFHNKKGGPGLPQKRKTPAENVVKRPRVH
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
2Phosphorylation------MSRNDQEPF
------CCCCCCCCH		51.6125266776
154AcetylationIAGEVGSKKYLVAAN
EECCCCCCEEEEECC		39.247719639
164SuccinylationLVAANLKKPILLPSW
EEECCCCCCCCCHHH		40.2223806337
164AcetylationLVAANLKKPILLPSW
EEECCCCCCCCCHHH		40.2223806337
298PhosphorylationKMVPDTSTPTAQSNA
EECCCCCCCCHHCCH		27.10-
469PhosphorylationAVLDKSGSFSKSALV
EEEECCCCCCHHHCE		33.1824719451
497PhosphorylationAQYGNDDSTMVEAKL
HHHCCCCCHHHHHHH		22.6722006019
498PhosphorylationQYGNDDSTMVEAKLS
HHCCCCCHHHHHHHH		32.0325266776
505PhosphorylationTMVEAKLSEALEPEV
HHHHHHHHHHHCCCC		21.8128066266
518PhosphorylationEVGPCPGSAHREPCD
CCCCCCCCCCCCCCC		13.1725266776
548PhosphorylationSHCILDDSTVREEGL
CEEEECCCCCCCCCC		28.5925266776
549PhosphorylationHCILDDSTVREEGLF
EEEECCCCCCCCCCC		30.4925266776
557PhosphorylationVREEGLFSQKSFLVL
CCCCCCCCCCEEEEE		41.5625266776
695PhosphorylationAKKGMLASTHLIVKE
HHCCCEEEEEEEEEC		16.6417203969
696PhosphorylationKKGMLASTHLIVKEP
HCCCEEEEEEEEECC		18.3317203969
782PhosphorylationIHRKKAVTPLDMNRF
HHHCCCCCCCCHHHH		24.0028066266
820PhosphorylationQPLTKEPSLHLDTPS
CCCCCCCCCCCCCCH		29.5228418008
825PhosphorylationEPSLHLDTPSKFLSK
CCCCCCCCCHHHCCC		35.5026824392
827PhosphorylationSLHLDTPSKFLSKDK
CCCCCCCHHHCCCCC		37.8328066266
839PhosphorylationKDKLFKPSFDVTDAL
CCCCCCCCCCHHHHH		34.3726643407
843PhosphorylationFKPSFDVTDALAALE
CCCCCCHHHHHHHHC		19.8726643407
851PhosphorylationDALAALETPNAASQK
HHHHHHCCCCHHHHH		23.7726643407
856PhosphorylationLETPNAASQKRKLSS
HCCCCHHHHHHCCCC		33.5522006019
862PhosphorylationASQKRKLSSPLSEVI
HHHHHCCCCCHHHHH		32.7022942356
863PhosphorylationSQKRKLSSPLSEVIV
HHHHCCCCCHHHHHH		40.0526824392
866PhosphorylationRKLSSPLSEVIVRNL
HCCCCCHHHHHHHHH		32.9521082442
874PhosphorylationEVIVRNLTVALANSS
HHHHHHHHHHHHCCC		13.7929899451
880PhosphorylationLTVALANSSRNTDSH
HHHHHHCCCCCCCCC		25.6830482847
884PhosphorylationLANSSRNTDSHSASP
HHCCCCCCCCCCCCC		37.4630635358
886PhosphorylationNSSRNTDSHSASPQL
CCCCCCCCCCCCCCC		19.8030635358
888PhosphorylationSRNTDSHSASPQLKG
CCCCCCCCCCCCCCC		34.1026745281
890PhosphorylationNTDSHSASPQLKGAH
CCCCCCCCCCCCCCC		19.0526824392
903PhosphorylationAHLEEEETRKPLDSV
CCCCHHHHCCCCCEE		47.4724719451
1000PhosphorylationHTYNPKMSLDINTVQ
CCCCCCCCEECCCCC		29.0828066266
1021PhosphorylationSRAPLAVSASKDDGP
CCCCEEEECCCCCCC		22.6319854140
1023PhosphorylationAPLAVSASKDDGPDH
CCEEEECCCCCCCCC		29.1624759943
1032PhosphorylationDDGPDHLSVEGNETN
CCCCCCCEECCCCCC		18.0726370283
1064PhosphorylationDDCKGALTQALEMRE
CCHHHHHHHHHHHHH		15.9717525332
1089PhosphorylationSATCIVKTPAQKTCM
HCCEEEECHHHCCCC		16.9826745281
1128PhosphorylationVLEALRQSRQAVPDV
HHHHHHHHHCCCCCC		21.67-
1140PhosphorylationPDVNTEPSQNEQIIW
CCCCCCCCCCCCCCC		39.1326370283
1185PhosphorylationEIKMPDDSPSRKPVY
EEECCCCCCCCCCCC		31.9622817900
1187PhosphorylationKMPDDSPSRKPVYHS
ECCCCCCCCCCCCCH		57.8128066266
1235PhosphorylationPQAPAVASPLAKPPV
CCCCCCCCCCCCCCC		17.5328066266
1269PhosphorylationKQYVFQMSSLNSQER
HHHEEEHHCCCHHHH		22.38-
1284AcetylationIDYCRLIKDLGGSVI
HHHHHHHHHHCCCEE		52.0422826441
1417AcetylationLLQAGGAKVLSGHPE
HHHCCCCEECCCCCC		47.166571469
1428AcetylationGHPEPLLKDATHLFC
CCCCCHHHCCCCHHC		53.666571445
1503PhosphorylationGLPQKRKTPAENVVK
CCCCCCCCCHHHHCC		31.5928059163
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 TOPB1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOPB1_MOUSE !!
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 TOPB1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRIC3_HUMANPRICKLE3physical
26496610
POP7_HUMANPOP7physical
26496610
RM03_HUMANMRPL3physical
26496610
RBM25_HUMANRBM25physical
26496610
TTC31_HUMANTTC31physical
26496610
ERI1_HUMANERI1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOPB1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-1064, AND MASSSPECTROMETRY.

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