UniProt ID | KTBL1_HUMAN | |
---|---|---|
UniProt AC | Q9H079 | |
Protein Name | KATNB1-like protein 1 | |
Gene Name | KATNBL1 {ECO:0000303|PubMed:26929214} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 304 | |
Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, spindle pole . Localizes to the spindle poles only during mitosis. Sequestered to the nucleus during interphase. | |
Protein Description | Regulates microtubule-severing activity of KATNAL1 in a concentration-dependent manner in vitro.. | |
Protein Sequence | MASETHNVKKRNFCNKIEDHFIDLPRKKISNFTNKNMKEVKKSPKQLAAYINRTVGQTVKSPDKLRKVIYRRKKVHHPFPNPCYRKKQSPGSGGCDMANKENELACAGHLPEKLHHDSRTYLVNSSDSGSSQTESPSSKYSGFFSEVSQDHETMAQVLFSRNMRLNVALTFWRKRSISELVAYLLRIEDLGVVVDCLPVLTNCLQEEKQYISLGCCVDLLPLVKSLLKSKFEEYVIVGLNWLQAVIKRWWSELSSKTEIINDGNIQILKQQLSGLWEQENHLTLVPGYTGNIAKDVDAYLLQLH | |
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 |
---|---|---|---|---|---|
43 | Phosphorylation | NMKEVKKSPKQLAAY CHHHHHCCHHHHHHH | 24719451 | ||
50 | Phosphorylation | SPKQLAAYINRTVGQ CHHHHHHHHHCHHCC | 24719451 | ||
54 | Phosphorylation | LAAYINRTVGQTVKS HHHHHHCHHCCCCCC | 23927012 | ||
58 | Phosphorylation | INRTVGQTVKSPDKL HHCHHCCCCCCHHHH | 23927012 | ||
61 | Phosphorylation | TVGQTVKSPDKLRKV HHCCCCCCHHHHHHH | 25159151 | ||
89 | Phosphorylation | PCYRKKQSPGSGGCD CCCCCCCCCCCCCCC | 28985074 | ||
92 | Phosphorylation | RKKQSPGSGGCDMAN CCCCCCCCCCCCCCC | 28102081 | ||
128 | Phosphorylation | YLVNSSDSGSSQTES EEEECCCCCCCCCCC | 27251275 | ||
130 | Phosphorylation | VNSSDSGSSQTESPS EECCCCCCCCCCCCC | 27251275 | ||
131 | Phosphorylation | NSSDSGSSQTESPSS ECCCCCCCCCCCCCC | 27251275 | ||
133 | Phosphorylation | SDSGSSQTESPSSKY CCCCCCCCCCCCCCC | 27251275 | ||
135 | Phosphorylation | SGSSQTESPSSKYSG CCCCCCCCCCCCCCC | 21815630 | ||
137 | Phosphorylation | SSQTESPSSKYSGFF CCCCCCCCCCCCCCC | 25159151 | ||
138 | Phosphorylation | SQTESPSSKYSGFFS CCCCCCCCCCCCCCC | 27251275 | ||
225 | Phosphorylation | DLLPLVKSLLKSKFE HHHHHHHHHHHHCCC | 24719451 | ||
229 | Phosphorylation | LVKSLLKSKFEEYVI HHHHHHHHCCCCEEE | - | ||
234 | Phosphorylation | LKSKFEEYVIVGLNW HHHCCCCEEEEHHHH | - | ||
247 | Acetylation | NWLQAVIKRWWSELS HHHHHHHHHHHHHHH | 20167786 | ||
251 | Phosphorylation | AVIKRWWSELSSKTE HHHHHHHHHHHCCEE | 29449344 | ||
254 | Phosphorylation | KRWWSELSSKTEIIN HHHHHHHHCCEEEEE | 29449344 | ||
255 | Phosphorylation | RWWSELSSKTEIIND HHHHHHHCCEEEEEC | 29449344 |
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 KTBL1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KTBL1_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 KTBL1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KAT7_HUMAN | KAT7 | physical | 16169070 | |
HAP1_HUMAN | HAP1 | physical | 16169070 | |
KTBL1_HUMAN | KATNBL1 | physical | 25416956 | |
KATL1_HUMAN | KATNAL1 | physical | 25416956 | |
KTNA1_HUMAN | KATNA1 | physical | 26186194 | |
KTNB1_HUMAN | KATNB1 | physical | 26186194 | |
KTNA1_HUMAN | KATNA1 | physical | 28514442 | |
KTNB1_HUMAN | KATNB1 | 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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