IKBZ_HUMAN - dbPTM
IKBZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IKBZ_HUMAN
UniProt AC Q9BYH8
Protein Name NF-kappa-B inhibitor zeta
Gene Name NFKBIZ
Organism Homo sapiens (Human).
Sequence Length 718
Subcellular Localization Nucleus . Aggregated in dot-like structures. Colocalizes with NCOR2.
Protein Description Involved in regulation of NF-kappa-B transcription factor complexes. Inhibits NF-kappa-B activity without affecting its nuclear translocation upon stimulation. Inhibits DNA-binding of RELA and NFKB1/p50, and of the NF-kappa-B p65-p50 heterodimer and the NF-kappa-B p50-p50 homodimer. Seems also to activate NF-kappa-B-mediated transcription. In vitro, upon association with NFKB1/p50 has transcriptional activation activity and, together with NFKB1/p50 and RELA, is recruited to LCN2 promoters. Promotes transcription of LCN2 and DEFB4. Is recruited to IL-6 promoters and activates IL-6 but decreases TNF-alpha production in response to LPS. Seems to be involved in the induction of inflammatory genes activated through TLR/IL-1 receptor signaling. May promote apoptosis (By similarity). Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR) (By similarity)..
Protein Sequence MIVDKLLDDSRGGEGLRDAAGGCGLMTSPLNLSYFYGASPPAAAPGACDASCSVLGPSAPGSPGSDSSDFSSASSVSSCGAVESRSRGGARAERQPVEPHMGVGRQQRGPFQGVRVKNSVKELLLHIRSHKQKASGQAVDDFKTQGVNIEQFRELKNTVSYSGKRKGPDSLSDGPACKRPALLHSQFLTPPQTPTPGESMEDVHLNEPKQESSADLLQNIINIKNECSPVSLNTVQVSWLNPVVVPQSSPAEQCQDFHGGQVFSPPQKCQPFQVRGSQQMIDQASLYQYSPQNQHVEQQPHYTHKPTLEYSPFPIPPQSPAYEPNLFDGPESQFCPNQSLVSLLGDQRESENIANPMQTSSSVQQQNDAHLHSFSMMPSSACEAMVGHEMASDSSNTSLPFSNMGNPMNTTQLGKSLFQWQVEQEESKLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGAVGSNQFVDLEATNYDGLTPLHCAVIAHNAVVHELQRNQQPHSPEVQELLLKNKSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSCLSFVNAKAYNGNTALHVAASLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVHLVPDGPVGEQIRRILKGKSIQQRAPPY
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
10PhosphorylationVDKLLDDSRGGEGLR
CCCCCCCCCCCCCHH
32.2724505115
56UbiquitinationDASCSVLGPSAPGSP
CCCCEECCCCCCCCC
16.3829967540
156UbiquitinationIEQFRELKNTVSYSG
HHHHHHHHCCCCCCC
45.9129967540
158PhosphorylationQFRELKNTVSYSGKR
HHHHHHCCCCCCCCC
14.8329083192
160PhosphorylationRELKNTVSYSGKRKG
HHHHCCCCCCCCCCC
16.1429083192
161PhosphorylationELKNTVSYSGKRKGP
HHHCCCCCCCCCCCC
19.6729083192
162PhosphorylationLKNTVSYSGKRKGPD
HHCCCCCCCCCCCCC
30.2729083192
170PhosphorylationGKRKGPDSLSDGPAC
CCCCCCCCCCCCCCC
32.67-
172PhosphorylationRKGPDSLSDGPACKR
CCCCCCCCCCCCCCC
44.46-
189PhosphorylationLLHSQFLTPPQTPTP
HHCCCCCCCCCCCCC
33.9224719451
193PhosphorylationQFLTPPQTPTPGESM
CCCCCCCCCCCCCCH
34.6024719451
661PhosphorylationHVAASLQYRLTQLDA
HHHHHHHHHHHHHHH
16.94-

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 IKBZ_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IKBZ_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 IKBZ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFKB1_HUMANNFKB1physical
11356851
STAT3_HUMANSTAT3physical
19595668
STAT3_HUMANSTAT3physical
21988832

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IKBZ_HUMAN

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Related Literatures of Post-Translational Modification

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