KBTB2_HUMAN - dbPTM
KBTB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KBTB2_HUMAN
UniProt AC Q8IY47
Protein Name Kelch repeat and BTB domain-containing protein 2
Gene Name KBTBD2
Organism Homo sapiens (Human).
Sequence Length 623
Subcellular Localization
Protein Description
Protein Sequence MSTQDERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAATLQIIITYAYTGNLAMNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYHQDAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRIKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSTDGTEEFELDGEMVALPPV
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
51PhosphorylationCHKMVLATCSSYFRA
HHHHHHHHHHHHHHH
14.5722210691
53PhosphorylationKMVLATCSSYFRAMF
HHHHHHHHHHHHHHH
24.5822210691
54PhosphorylationMVLATCSSYFRAMFM
HHHHHHHHHHHHHHH
30.3622210691
55PhosphorylationVLATCSSYFRAMFMS
HHHHHHHHHHHHHHH
4.8422210691
62PhosphorylationYFRAMFMSGLSESKQ
HHHHHHHHCCCCCCC
25.8922210691
65PhosphorylationAMFMSGLSESKQTHV
HHHHHCCCCCCCCEE
43.2622210691
87PhosphorylationATLQIIITYAYTGNL
HHEEEEEEEEHHCCC
7.5326074081
88PhosphorylationTLQIIITYAYTGNLA
HEEEEEEEEHHCCCC
6.2926074081
90PhosphorylationQIIITYAYTGNLAMN
EEEEEEEHHCCCCCC
12.5526074081
127UbiquitinationCREYLIKKINAENCV
HHHHHHHHCCHHHHH
33.91-
149UbiquitinationLFSCEELKQSAKRMV
HHCHHHHHHHHHHHH
45.55-
251UbiquitinationVVVQGLYKSMPKFFK
HHHHHHHHHCCHHCC
45.37-
297UbiquitinationPQAEKVYKLCSPPAD
CCHHHHHHHHCCCHH
46.10-
300PhosphorylationEKVYKLCSPPADLHK
HHHHHHHCCCHHHHC
44.3425159151
307UbiquitinationSPPADLHKVGTVVTP
CCCHHHHCCCEEECC
50.05-
310PhosphorylationADLHKVGTVVTPDND
HHHHCCCEEECCCCC
18.1322817900
313PhosphorylationHKVGTVVTPDNDIYI
HCCCEEECCCCCEEE
22.1622817900
319PhosphorylationVTPDNDIYIAGGQVP
ECCCCCEEEECCEEC
6.3822817900
328UbiquitinationAGGQVPLKNTKTNHS
ECCEECCCCCCCCCC
57.4021906983
331UbiquitinationQVPLKNTKTNHSKTS
EECCCCCCCCCCHHH
57.64-
336UbiquitinationNTKTNHSKTSKLQTA
CCCCCCCHHHHHHHH
49.63-
339UbiquitinationTNHSKTSKLQTAFRT
CCCCHHHHHHHHHHH
50.25-
498PhosphorylationTVDGSSVTVEIYDVN
CCCCCEEEEEEEECC
17.8628674151
510UbiquitinationDVNKNEWKMAANIPA
ECCCCEEEEECCCCC
16.69-
518UbiquitinationMAANIPAKRYSDPCV
EECCCCCHHCCCCCH
46.65-
562PhosphorylationDLELDRWSLRQHISE
CCCCCHHHHHHHHHH
17.9924719451
587PhosphorylationRCTVGKLYPSCLEES
CCCCCCCCHHHHCCC
9.1525690035

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 KBTB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KBTB2_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 KBTB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
27708159
P85A_HUMANPIK3R1physical
27708159

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 KBTB2_HUMAN

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Related Literatures of Post-Translational Modification

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