UniProt ID | KBRS2_HUMAN | |
---|---|---|
UniProt AC | Q9NYR9 | |
Protein Name | NF-kappa-B inhibitor-interacting Ras-like protein 2 | |
Gene Name | NKIRAS2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 191 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity).. | |
Protein Sequence | MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFVYLASKMTQPQSKSAFPLSRKNKGSGSLDG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
19 | Phosphorylation | QASVGKTSILEQLLY CCCCCCHHHHHHHHH | 28.76 | 25954137 | |
33 | Phosphorylation | YGNHVVGSEMIETQE HCCCCCCCCEEECCC | 16.63 | 25954137 | |
43 | Phosphorylation | IETQEDIYVGSIETD EECCCCEEEEEEECC | 15.87 | 25954137 | |
66 (in isoform 4) | Phosphorylation | - | 43.04 | 25159151 | |
68 (in isoform 4) | Phosphorylation | - | 17.95 | 25159151 | |
77 (in isoform 4) | Phosphorylation | - | 22.85 | - | |
118 | Ubiquitination | KEVTIVVLGNKCDLQ CEEEEEEECCCCCHH | 4.30 | 21890473 | |
121 | Ubiquitination | TIVVLGNKCDLQEQR EEEEECCCCCHHHHH | 27.59 | - | |
140 | Acetylation | DVAQHWAKSEKVKLW HHHHHHHHCCCCEEE | 54.69 | 25953088 | |
140 | Ubiquitination | DVAQHWAKSEKVKLW HHHHHHHHCCCCEEE | 54.69 | - | |
150 | Phosphorylation | KVKLWEVSVADRRSL CCEEEEEEHHHHHHH | 10.48 | 28857561 | |
156 | Phosphorylation | VSVADRRSLLEPFVY EEHHHHHHHHHHHHH | 37.89 | 28857561 | |
167 | Ubiquitination | PFVYLASKMTQPQSK HHHHHHHHCCCCCCC | 40.12 | - | |
172 (in isoform 2) | Ubiquitination | - | 54.39 | 21890473 | |
174 | Ubiquitination | KMTQPQSKSAFPLSR HCCCCCCCCCCCCCC | 40.32 | 2189047 | |
174 (in isoform 1) | Ubiquitination | - | 40.32 | 21890473 | |
180 | Phosphorylation | SKSAFPLSRKNKGSG CCCCCCCCCCCCCCC | 41.25 | 27535140 | |
186 | Phosphorylation | LSRKNKGSGSLDG-- CCCCCCCCCCCCC-- | 27.15 | 19581576 | |
188 | Phosphorylation | RKNKGSGSLDG---- CCCCCCCCCCC---- | 25.61 | 19581576 |
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 KBRS2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KBRS2_HUMAN !! |
* 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 KBRS2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PAX6_HUMAN | PAX6 | physical | 21988832 | |
GFOD1_HUMAN | GFOD1 | physical | 28514442 | |
RGPA2_HUMAN | RALGAPA2 | physical | 28514442 | |
RGPA1_HUMAN | RALGAPA1 | physical | 28514442 | |
RLGPB_HUMAN | RALGAPB | physical | 28514442 | |
GFOD2_HUMAN | GFOD2 | physical | 28514442 | |
GDS1_HUMAN | RAP1GDS1 | physical | 28514442 | |
DCA10_HUMAN | DCAF10 | physical | 28514442 |
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. |
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