PDS5B_MOUSE - dbPTM
PDS5B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDS5B_MOUSE
UniProt AC Q4VA53
Protein Name Sister chromatid cohesion protein PDS5 homolog B
Gene Name Pds5b
Organism Mus musculus (Mouse).
Sequence Length 1446
Subcellular Localization Nucleus .
Protein Description Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells (By similarity)..
Protein Sequence MAHSKTRTNDGKITYPPGVKEISDKISKEEMVRRLKMVVKTFMDMDQDSEEEKELYLNLALHLASDFFLKHPDKDVRLLVACCLADIFRIYAPEAPYTSPDKLKDIFMFITRQLKGLEDTKSPQFNRYFYLLENIAWVKSYNICFELEDSNEIFTQLYRTLFSVINNGHNQKVHMHMVDLMSSIICEGDTVSQELLDTVLVNLVPAHKNLNKQAYDLAKALLKRTAQAIEPYITNFFNQVLMLGKTSISDLSEHVFDLILELYNIDSHLLLSVLPQLEFKLKSNDNEERLQVVKLLAKMFGAKDSELASQNKPLWQCYLGRFNDIHVPIRLECVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVSIVTAAKKDILLVNDHLLNFVRERTLDKRWRVRKEAMMGLAQIYKKYSLQSAAGKDAAKQISWVKDKLLHIYYQNSIDDRLLVERIFAQYMVPHNLETTERMKCLYYLYATLDLNAVKALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKVMVITRNLPDPGKAQDFMKKFTQVLEDDEKIRKQLEALVSPTCSCKQAEGCVREITKKLGNPKQPTNPFLEMIKFLLERIAPVHIDTESISALIKQVNKSIDGTADDEDEGVPTDQAIRAGLELLKVLSFTHPISFHSAETFESLLACLKMDDEKVAEAALQIFKNTGSKIEEDFPHIRSALLPVLHHKSKKGPPRQAKYAIHCIHAIFSSKETQFAQIFEPLHKSLDPSNLEHLITPLVTIGHIALLAPDQFAAPLKSLVATFIVKDLLMNDRLPGKKTTKLWVPDEEVSPETMVKIQAIKMMVRWLLGMKNNHSKSGTSTLRLLTTILHSDGDLTEQGKISKPDMSRLRLAAGSAIVKLAQEPCYHEIITLEQYQLCALAINDECYQVRQVFAQKLHKGLSRLRLPLEYMAICALCAKDPVKERRAHARQCLVKNITVRREYLKQHAAVSEKLLSLLPEYVVPYTIHLLAHDPDYVKVQDIEQLKDVKECLWFVLEILMAKNENNSHAFIRKMVENIKQTKDAQGPDDTKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTANVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSSEMDHSENEDYTMSSPLPGKKSDKREDPDLSELEKPRSRKKAPVTDPEEKLGMDDLTKLVQEQKPKGSQRGRKRGRTASDSDEQQWPEEKRHKEELLENEDEQNSPPKKGKRGRPPKPLGGGTSKEEPTMKTSKKGNKKKLVPPVVDDDEEEERQIGNTEHKSKSKQHRTSKRAQQRAESPETSAVESTQSTPQKGRGRPSKAPSPSQPPKKIRVGRSKQVATKENDSSEEMDVLQASSPVSDDTTQEGAEEEDISVGNVRRRSSKRERR
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
215PhosphorylationKNLNKQAYDLAKALL
CCCCHHHHHHHHHHH		14.7022802335
252PhosphorylationKTSISDLSEHVFDLI
CCCHHHHHHHHHHHH		30.55-
294UbiquitinationEERLQVVKLLAKMFG
HHHHHHHHHHHHHHC		38.64-
335AcetylationPIRLECVKFASHCLM
CEEHHHHHHHHHHHH		47.0422826441
352PhosphorylationPDLAKDLTEYLKVRS
HHHHHHHHHHHHHHC		32.4925367039
354PhosphorylationLAKDLTEYLKVRSHD
HHHHHHHHHHHHCCC		13.4425367039
356UbiquitinationKDLTEYLKVRSHDPE
HHHHHHHHHHCCCHH		34.40-
434PhosphorylationKDAAKQISWVKDKLL
CCHHHHHHHHHHHHH		24.2728059163
444PhosphorylationKDKLLHIYYQNSIDD
HHHHHHHHHCCCCCH		6.5625159016
445PhosphorylationDKLLHIYYQNSIDDR
HHHHHHHHCCCCCHH		10.7025159016
448PhosphorylationLHIYYQNSIDDRLLV
HHHHHCCCCCHHHHH		16.3325159016
478PhosphorylationTERMKCLYYLYATLD
HHHHHHHHHHHHHCC		10.8222871156
479PhosphorylationERMKCLYYLYATLDL
HHHHHHHHHHHHCCH		4.7422871156
481PhosphorylationMKCLYYLYATLDLNA
HHHHHHHHHHCCHHH		4.9622871156
507UbiquitinationNLLRHQVKDLLDLIK
HHHHHHHHHHHHHHH		35.77-
533PhosphorylationFSKVMVITRNLPDPG
HHHEEEEECCCCCCC		11.33-
872UbiquitinationTEQGKISKPDMSRLR
CCCCCCCCCCHHHHH		48.81-
884PhosphorylationRLRLAAGSAIVKLAQ
HHHHHHHCHHHHHHC		15.3129176673
1089UbiquitinationTYSLESPKDPVLPAR
CCCCCCCCCCCCCCH		81.56-
1118PhosphorylationYLPPEMKSFFTPGKP
CCCHHHHHCCCCCCC		25.0423984901
1121PhosphorylationPEMKSFFTPGKPKTA
HHHHHCCCCCCCCCH		29.1727600695
1136AcetylationNVLGAVNKPLSSAGK
HHHHHHCCCCHHCCC		40.5123806337
1139PhosphorylationGAVNKPLSSAGKQSQ
HHHCCCCHHCCCCCC		27.0325266776
1140PhosphorylationAVNKPLSSAGKQSQT
HHCCCCHHCCCCCCC		49.0426745281
1154PhosphorylationTKSSRMETVSNASSS
CCCCCCHHHHCCCCC		21.6423375375
1156PhosphorylationSSRMETVSNASSSSN
CCCCHHHHCCCCCCC		33.8123684622
1159PhosphorylationMETVSNASSSSNPSS
CHHHHCCCCCCCCCC		34.7023684622
1160PhosphorylationETVSNASSSSNPSSP
HHHHCCCCCCCCCCC		35.0627087446
1161PhosphorylationTVSNASSSSNPSSPG
HHHCCCCCCCCCCCC		31.4727087446
1162PhosphorylationVSNASSSSNPSSPGR
HHCCCCCCCCCCCCC		55.5025521595
1165PhosphorylationASSSSNPSSPGRIKG
CCCCCCCCCCCCCCC		54.1127087446
1166PhosphorylationSSSSNPSSPGRIKGR
CCCCCCCCCCCCCCC		32.4127087446
1176PhosphorylationRIKGRLDSSEMDHSE
CCCCCCCCCCCCCCC		32.5627087446
1177PhosphorylationIKGRLDSSEMDHSEN
CCCCCCCCCCCCCCC		36.2925521595
1182PhosphorylationDSSEMDHSENEDYTM
CCCCCCCCCCCCCCC		37.5425521595
1187PhosphorylationDHSENEDYTMSSPLP
CCCCCCCCCCCCCCC		9.7327087446
1188PhosphorylationHSENEDYTMSSPLPG
CCCCCCCCCCCCCCC		23.9327087446
1190PhosphorylationENEDYTMSSPLPGKK
CCCCCCCCCCCCCCC		22.4727087446
1191PhosphorylationNEDYTMSSPLPGKKS
CCCCCCCCCCCCCCC		21.4525521595
1207PhosphorylationKREDPDLSELEKPRS
CCCCCCHHHCCCCCC		47.7322817900
1244PhosphorylationQEQKPKGSQRGRKRG
HHHCCCCCCCCHHCC		23.8826824392
1253PhosphorylationRGRKRGRTASDSDEQ
CCHHCCCCCCCCCCC		33.0825521595
1255PhosphorylationRKRGRTASDSDEQQW
HHCCCCCCCCCCCCC		36.7127087446
1257PhosphorylationRGRTASDSDEQQWPE
CCCCCCCCCCCCCCH		40.3225521595
1281PhosphorylationENEDEQNSPPKKGKR
HCCCCCCCCCCCCCC		42.1225521595
1356PhosphorylationRAQQRAESPETSAVE
HHHHHHHCCCCCHHH		27.3524925903
1359PhosphorylationQRAESPETSAVESTQ
HHHHCCCCCHHHCCC		25.9325521595
1360PhosphorylationRAESPETSAVESTQS
HHHCCCCCHHHCCCC		28.7625521595
1364PhosphorylationPETSAVESTQSTPQK
CCCCHHHCCCCCCCC		25.7524925903
1365PhosphorylationETSAVESTQSTPQKG
CCCHHHCCCCCCCCC		17.0324925903
1367PhosphorylationSAVESTQSTPQKGRG
CHHHCCCCCCCCCCC		41.9924925903
1368PhosphorylationAVESTQSTPQKGRGR
HHHCCCCCCCCCCCC		21.6624925903
1377PhosphorylationQKGRGRPSKAPSPSQ
CCCCCCCCCCCCCCC		39.8425619855
1381PhosphorylationGRPSKAPSPSQPPKK
CCCCCCCCCCCCCCC		41.8825521595
1383PhosphorylationPSKAPSPSQPPKKIR
CCCCCCCCCCCCCEE		60.7127149854
1404PhosphorylationVATKENDSSEEMDVL
CCCCCCCCHHHHHHH		51.7521149613
1405PhosphorylationATKENDSSEEMDVLQ
CCCCCCCHHHHHHHH		40.2023429704
1414PhosphorylationEMDVLQASSPVSDDT
HHHHHHHCCCCCCCC		23.3921149613
1415PhosphorylationMDVLQASSPVSDDTT
HHHHHHCCCCCCCCC		32.1323429704
1418PhosphorylationLQASSPVSDDTTQEG
HHHCCCCCCCCCCCC		32.9016141072
1421PhosphorylationSSPVSDDTTQEGAEE
CCCCCCCCCCCCCHH		35.0621149613
1422PhosphorylationSPVSDDTTQEGAEEE
CCCCCCCCCCCCHHH		31.4521149613
1440PhosphorylationVGNVRRRSSKRERR-
HHHHCCCCCCCCCC-		38.10-
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 PDS5B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDS5B_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 PDS5B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PDS5B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDS5B_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1381, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1257 ANDSER-1356, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory