RBAK_HUMAN - dbPTM
RBAK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBAK_HUMAN
UniProt AC Q9NYW8
Protein Name RB-associated KRAB zinc finger protein
Gene Name RBAK
Organism Homo sapiens (Human).
Sequence Length 714
Subcellular Localization Nucleus .
Protein Description May repress E2F-dependent transcription. May promote AR-dependent transcription..
Protein Sequence MNTLQGPVSFKDVAVDFTQEEWQQLDPDEKITYRDVMLENYSHLVSVGYDTTKPNVIIKLEQGEEPWIMGGEFPCQHSPEAWRVDDLIERIQENEDKHSRQAACINSKTLTEEKENTFSQIYMETSLVPSSIIAHNCVSCGKNLESISQLISSDGSYARTKPDECNECGKTYHGEKMCEFNQNGDTYSHNEENILQKISILEKPFEYNECMEALDNEAVFIAHKRAYIGEKPYEWNDSGPDFIQMSNFNAYQRSQMEMKPFECSECGKSFCKKSKFIIHQRAHTGEKPYECNVCGKSFSQKGTLTVHRRSHLEEKPYKCNECGKTFCQKLHLTQHLRTHSGEKPYECSECGKTFCQKTHLTLHQRNHSGERPYPCNECGKSFSRKSALSDHQRTHTGEKLYKCNECGKSYYRKSTLITHQRTHTGEKPYQCSECGKFFSRVSYLTIHYRSHLEEKPYECNECGKTFNLNSAFIRHRKVHTEEKSHECSECGKFSQLYLTDHHTAHLEEKPYECNECGKTFLVNSAFDGHQPLPKGEKSYECNVCGKLFNELSYYTEHYRSHSEEKPYGCSECGKTFSHNSSLFRHQRVHTGEKPYECYECGKFFSQKSYLTIHHRIHSGEKPYECSKCGKVFSRMSNLTVHYRSHSGEKPYECNECGKVFSQKSYLTVHYRTHSGEKPYECNECGKKFHHRSAFNSHQRIHRRGNMNVLDVENL
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
3Phosphorylation-----MNTLQGPVSF
-----CCCCCCCCCH		21.1122985185
33PhosphorylationDPDEKITYRDVMLEN
CCCCCCCHHHHHHHH		14.3220736484
59SumoylationTKPNVIIKLEQGEEP
CCCEEEEEEECCCCC		34.5417000644
59SumoylationTKPNVIIKLEQGEEP
CCCEEEEEEECCCCC		34.54-
78PhosphorylationGEFPCQHSPEAWRVD
CCCCCCCCCCCCCHH		9.8825159151
97SumoylationRIQENEDKHSRQAAC
HHHHCCCHHHHHHHH		36.98-
97SumoylationRIQENEDKHSRQAAC
HHHHCCCHHHHHHHH		36.9828112733
108SumoylationQAACINSKTLTEEKE
HHHHHCCCCCCHHHC		42.96-
108UbiquitinationQAACINSKTLTEEKE
HHHHHCCCCCCHHHC		42.9629967540
108SumoylationQAACINSKTLTEEKE
HHHHHCCCCCCHHHC		42.96-
161SumoylationDGSYARTKPDECNEC
CCCCCCCCCHHCCCC		44.94-
161SumoylationDGSYARTKPDECNEC
CCCCCCCCCHHCCCC		44.94-
170AcetylationDECNECGKTYHGEKM
HHCCCCCCEECCCCC		58.5326051181
199PhosphorylationENILQKISILEKPFE
HHHHHHHHHHCCCCC		28.3124719451
259SumoylationQRSQMEMKPFECSEC
HHHCCCCCCEECCHH		32.99-
259SumoylationQRSQMEMKPFECSEC
HHHCCCCCCEECCHH		32.9928112733
275SumoylationKSFCKKSKFIIHQRA
HHHHHCCCEEEEECC		49.84-
275SumoylationKSFCKKSKFIIHQRA
HHHHHCCCEEEEECC		49.84-
284PhosphorylationIIHQRAHTGEKPYEC
EEEECCCCCCCCEEE		46.1628985074
301SumoylationCGKSFSQKGTLTVHR
CCCCCCCCCEEEEEC		53.30-
301SumoylationCGKSFSQKGTLTVHR
CCCCCCCCCEEEEEC		53.30-
315SumoylationRRSHLEEKPYKCNEC
CCHHCCCCCCCCCCC		44.25-
315SumoylationRRSHLEEKPYKCNEC
CCHHCCCCCCCCCCC		44.2528112733
318SumoylationHLEEKPYKCNECGKT
HCCCCCCCCCCCCHH		38.83-
318SumoylationHLEEKPYKCNECGKT
HCCCCCCCCCCCCHH		38.83-
340PhosphorylationTQHLRTHSGEKPYEC
HHHHHHCCCCCCEEC		48.2923898821
357SumoylationCGKTFCQKTHLTLHQ
CCCEEEHHHCCEEEC		38.8128112733
357SumoylationCGKTFCQKTHLTLHQ
CCCEEEHHHCCEEEC		38.81-
358PhosphorylationGKTFCQKTHLTLHQR
CCEEEHHHCCEEECC		9.0230576142
361PhosphorylationFCQKTHLTLHQRNHS
EEHHHCCEEECCCCC		18.0030576142
368PhosphorylationTLHQRNHSGERPYPC
EEECCCCCCCCCCCC		45.9925159151
381PhosphorylationPCNECGKSFSRKSAL
CCCCCCCCCCHHHHC		17.4617081983
383PhosphorylationNECGKSFSRKSALSD
CCCCCCCCHHHHCCC		45.9817081983
386PhosphorylationGKSFSRKSALSDHQR
CCCCCHHHHCCCCCC		33.07-
389PhosphorylationFSRKSALSDHQRTHT
CCHHHHCCCCCCCCC		32.53-
394PhosphorylationALSDHQRTHTGEKLY
HCCCCCCCCCCCCEE		19.74-
396PhosphorylationSDHQRTHTGEKLYKC
CCCCCCCCCCCEEEC		46.56-
399UbiquitinationQRTHTGEKLYKCNEC
CCCCCCCCEEECCCC		59.4629967540
409PhosphorylationKCNECGKSYYRKSTL
ECCCCCCCEECCCEE		16.8123607784
410PhosphorylationCNECGKSYYRKSTLI
CCCCCCCEECCCEEE		15.6923607784
411PhosphorylationNECGKSYYRKSTLIT
CCCCCCEECCCEEEE		20.7523607784
422PhosphorylationTLITHQRTHTGEKPY
EEEEECCCCCCCCCE		19.7428111955
424PhosphorylationITHQRTHTGEKPYQC
EEECCCCCCCCCEEC		46.5628111955
427SumoylationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
427UbiquitinationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
427SumoylationQRTHTGEKPYQCSEC
CCCCCCCCCEECCCC		50.82-
429PhosphorylationTHTGEKPYQCSECGK
CCCCCCCEECCCCHH		32.9728111955
439PhosphorylationSECGKFFSRVSYLTI
CCCHHHHHHEEEHHH		34.6023403867
442PhosphorylationGKFFSRVSYLTIHYR
HHHHHHEEEHHHCCH		17.2023403867
443PhosphorylationKFFSRVSYLTIHYRS
HHHHHEEEHHHCCHH		12.6623403867
445PhosphorylationFSRVSYLTIHYRSHL
HHHEEEHHHCCHHHH		9.4723403867
455UbiquitinationYRSHLEEKPYECNEC
CHHHHCCCCEECCCC		43.45-
470PhosphorylationGKTFNLNSAFIRHRK
CCEEECCHHHHHCCC		27.9428555341
509UbiquitinationHTAHLEEKPYECNEC
CCCCCCCCCEECCCC		43.45-
534SumoylationDGHQPLPKGEKSYEC
CCCCCCCCCCCCEEC		83.6928112733
534SumoylationDGHQPLPKGEKSYEC
CCCCCCCCCCCCEEC		83.69-
537SumoylationQPLPKGEKSYECNVC
CCCCCCCCCEECCCH		67.9928112733
537UbiquitinationQPLPKGEKSYECNVC
CCCCCCCCCEECCCH		67.99-
560PhosphorylationYYTEHYRSHSEEKPY
HHHHHHHCCCCCCCC		24.97-
562PhosphorylationTEHYRSHSEEKPYGC
HHHHHCCCCCCCCCC		49.01-
565SumoylationYRSHSEEKPYGCSEC
HHCCCCCCCCCCCCC		39.22-
565SumoylationYRSHSEEKPYGCSEC
HHCCCCCCCCCCCCC		39.22-
567PhosphorylationSHSEEKPYGCSECGK
CCCCCCCCCCCCCCC		41.66-
570PhosphorylationEEKPYGCSECGKTFS
CCCCCCCCCCCCCCC		31.40-
577PhosphorylationSECGKTFSHNSSLFR
CCCCCCCCCCCCCCC		27.3028555341
580PhosphorylationGKTFSHNSSLFRHQR
CCCCCCCCCCCCCCC		24.0128555341
581PhosphorylationKTFSHNSSLFRHQRV
CCCCCCCCCCCCCCC		36.5224719451
590PhosphorylationFRHQRVHTGEKPYEC
CCCCCCCCCCCCEEE		44.1521712546
595PhosphorylationVHTGEKPYECYECGK
CCCCCCCEEEECCCC		29.69-
598PhosphorylationGEKPYECYECGKFFS
CCCCEEEECCCCCCC		11.4320736484
609PhosphorylationKFFSQKSYLTIHHRI
CCCCCCCEEEEEEEC		18.2018083107
618PhosphorylationTIHHRIHSGEKPYEC
EEEEECCCCCCCEEC		46.4028674419
633PhosphorylationSKCGKVFSRMSNLTV
CCCCCHHHHHCCCEE		30.0227251275
636PhosphorylationGKVFSRMSNLTVHYR
CCHHHHHCCCEEEEC		27.8128555341
639PhosphorylationFSRMSNLTVHYRSHS
HHHHCCCEEEECCCC		14.97-
642PhosphorylationMSNLTVHYRSHSGEK
HCCCEEEECCCCCCC		14.96-
646PhosphorylationTVHYRSHSGEKPYEC
EEEECCCCCCCCEEE		50.3121857030
649UbiquitinationYRSHSGEKPYECNEC
ECCCCCCCCEEECCC		57.32-
658SumoylationYECNECGKVFSQKSY
EEECCCCCEEECCCE		52.33-
658SumoylationYECNECGKVFSQKSY
EEECCCCCEEECCCE		52.33-
663SumoylationCGKVFSQKSYLTVHY
CCCEEECCCEEEEEE		39.61-
663SumoylationCGKVFSQKSYLTVHY
CCCEEECCCEEEEEE		39.61-
674PhosphorylationTVHYRTHSGEKPYEC
EEEEECCCCCCCEEE		48.2923898821
677UbiquitinationYRTHSGEKPYECNEC
EECCCCCCCEEECCC		57.32-
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 RBAK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of RBAK_HUMAN !!
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 RBAK_HUMAN

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Related Literatures of Post-Translational Modification

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