KBTB8_HUMAN - dbPTM
KBTB8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KBTB8_HUMAN
UniProt AC Q8NFY9
Protein Name Kelch repeat and BTB domain-containing protein 8
Gene Name KBTBD8
Organism Homo sapiens (Human).
Sequence Length 601
Subcellular Localization Cytoplasm, cytoskeleton, spindle . Golgi apparatus . Translocates to the spindle apparatus during mitosis.
Protein Description Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. [PubMed: 26399832 The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1: monoubiquitination promotes the formation of a NOLC1-TCOF1 complex that acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification]
Protein Sequence MAASADLSKSSPTPNGIPSSDPASDAMDPFHACSILKQLKTMYDEGQLTDIVVEVDHGKTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMDLVLNYAYTSRVILTEANVQALFTAASIFQIPSIQDQCAKYMISHLDPQNSIGVFIFADHYGHQELGDRSKEYIRKKFLCVTKEQEFLQLTKDQLISILDSDDLNVDREEHVYESIIRWFEHEQNEREVHLPEIFAKCIRFPLMEDTFIEKIPPQFAQAIAKSCVEKGPSNTNGCTQRLGMTASEMIICFDAAHKHSGKKQTVPCLDIVTGRVFKLCKPPNDLREVGILVSPDNDIYIAGGYRPSSSEVSIDHKAENDFWMYDHSTNRWLSKPSLLRARIGCKLVYCCGKMYAIGGRVYEGDGRNSLKSVECYDSRENCWTTVCAMPVAMEFHNAVEYKEKIYVLQGEFFLFYEPQKDYWGFLTPMTVPRIQGLAAVYKDSIYYIAGTCGNHQRMFTVEAYDIELNKWTRKKDFPCDQSINPYLKLVLFQNKLHLFVRATQVTVEEHVFRTSRKNSLYQYDDIADQWMKVYETPDRLWDLGRHFECAVAKLYPQCLQKVL
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
4Phosphorylation----MAASADLSKSS
----CCCCCCCCCCC		16.8723612710
10PhosphorylationASADLSKSSPTPNGI
CCCCCCCCCCCCCCC		37.8728450419
11PhosphorylationSADLSKSSPTPNGIP
CCCCCCCCCCCCCCC		36.2124850871
13PhosphorylationDLSKSSPTPNGIPSS
CCCCCCCCCCCCCCC		31.1928450419
19PhosphorylationPTPNGIPSSDPASDA
CCCCCCCCCCCCHHC		45.5128450419
20PhosphorylationTPNGIPSSDPASDAM
CCCCCCCCCCCHHCC		42.1128450419
24PhosphorylationIPSSDPASDAMDPFH
CCCCCCCHHCCCHHH		31.1528450419
34PhosphorylationMDPFHACSILKQLKT
CCHHHHHHHHHHHHH		31.5724719451
37UbiquitinationFHACSILKQLKTMYD
HHHHHHHHHHHHHCC		52.4929967540
77PhosphorylationAISPYFRSMFTSGLT
HHCHHHHHHHHCCCC		14.35-
157UbiquitinationQNSIGVFIFADHYGH
CCCEEEEEEECCCCC		2.30-
177AcetylationRSKEYIRKKFLCVTK
HCHHHHHHHEEEEEC		38.0225953088
178AcetylationSKEYIRKKFLCVTKE
CHHHHHHHEEEEECH		33.4523749302
238UbiquitinationHLPEIFAKCIRFPLM
CHHHHHHHHCCCHHC		21.31-
248PhosphorylationRFPLMEDTFIEKIPP
CCHHCCCCHHHHCCH		17.1330622161
263UbiquitinationQFAQAIAKSCVEKGP
HHHHHHHHHHHHHCC		37.9729967540
268UbiquitinationIAKSCVEKGPSNTNG
HHHHHHHHCCCCCCC		56.58-
301UbiquitinationAHKHSGKKQTVPCLD
HHHHCCCCCCCCHHH		55.52-
332PhosphorylationREVGILVSPDNDIYI
CEEEEEECCCCCEEE		24.0827080861
338PhosphorylationVSPDNDIYIAGGYRP
ECCCCCEEEECCCCC		6.3828450419
343PhosphorylationDIYIAGGYRPSSSEV
CEEEECCCCCCCCCE		20.5928450419
346PhosphorylationIAGGYRPSSSEVSID
EECCCCCCCCCEEEE		37.1828450419
347PhosphorylationAGGYRPSSSEVSIDH
ECCCCCCCCCEEEEE		32.9528450419
348PhosphorylationGGYRPSSSEVSIDHK
CCCCCCCCCEEEEEC		46.4828450419
351PhosphorylationRPSSSEVSIDHKAEN
CCCCCCEEEEECCCC		20.4628450419
373UbiquitinationSTNRWLSKPSLLRAR
CCCCEECCHHHHHHH		36.1329967540
384UbiquitinationLRARIGCKLVYCCGK
HHHHHCCEEEEECCC		35.46-
393PhosphorylationVYCCGKMYAIGGRVY
EEECCCEEEECCEEE		9.8829496907
409UbiquitinationGDGRNSLKSVECYDS
CCCCCCCCEEEEECC		52.88-
498PhosphorylationGNHQRMFTVEAYDIE
CCCEEEEEEEEEEEE		14.2128509920
502PhosphorylationRMFTVEAYDIELNKW
EEEEEEEEEEECCCC		12.1628509920
513UbiquitinationLNKWTRKKDFPCDQS
CCCCCCCCCCCCCCC		62.4029967540
522UbiquitinationFPCDQSINPYLKLVL
CCCCCCCCHHHHHHH		25.1422505724
524PhosphorylationCDQSINPYLKLVLFQ
CCCCCCHHHHHHHCC		16.39-
541PhosphorylationLHLFVRATQVTVEEH
EEEEEECCCCEEHHH		17.0129759185
553PhosphorylationEEHVFRTSRKNSLYQ
HHHEECCCCCCCCCC		36.6829759185
572PhosphorylationADQWMKVYETPDRLW
HHHHHHHHCCCCHHH		14.4726074081
574PhosphorylationQWMKVYETPDRLWDL
HHHHHHCCCCHHHHH		16.8926074081
599UbiquitinationLYPQCLQKVL-----
HHHHHHHHHC-----		32.3422505724
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 KBTB8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KBTB8_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 KBTB8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCOF_HUMANTCOF1physical
26399832
NOLC1_HUMANNOLC1physical
26399832
ARRB1_HUMANARRB1physical
26399832
ARRB2_HUMANARRB2physical
26399832
PKN1_HUMANPKN1physical
26399832
CUL3_HUMANCUL3physical
26399832
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KBTB8_HUMAN

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Related Literatures of Post-Translational Modification

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