UniProt ID | KPTN_HUMAN | |
---|---|---|
UniProt AC | Q9Y664 | |
Protein Name | KICSTOR complex protein kaptin {ECO:0000305|PubMed:10099934} | |
Gene Name | KPTN {ECO:0000312|HGNC:HGNC:6404} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 436 | |
Subcellular Localization | Lysosome membrane . Cell projection, lamellipodium . Cell projection, stereocilium . Localization to lysosomes is amino acid-independent (PubMed:28199306). Colocalizes with F-actin (PubMed:24239382). | |
Protein Description | As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose.. | |
Protein Sequence | MMGEAAVAAGPCPLREDSFTRFSSQSNVYGLAGGAGGRGELLAATLKGKVLGFRYQDLRQKIRPVAKELQFNYIPVDAEIVSIDTFNKSPPKRGLVVGITFIKDSGDKGSPFLNIYCDYEPGSEYNLDSIAQSCLNLELQFTPFQLCHAEVQVGDQLETVFLLSGNDPAIHLYKENEGLHQFEEQPVENLFPELTNLTSSVLWLDVHNFPGTSRRLSALGCQSGYVRVAHVDQRSREVLQMWSVLQDGPISRVIVFSLSAAKETKDRPLQDEYSVLVASMLEPAVVYRDLLNRGLEDQLLLPGSDQFDSVLCSLVTDVDLDGRPEVLVATYGQELLCYKYRGPESGLPEAQHGFHLLWQRSFSSPLLAMAHVDLTGDGLQELAVVSLKGVHILQHSLIQASELVLTRLRHQVEQRRRRLQGLEDGAGAGPAENAAS | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MMGEAAVA -------CCCCCHHH | 7.60 | 22814378 | |
23 | Phosphorylation | EDSFTRFSSQSNVYG CCCCCCCCCCCCCCE | 24.95 | 21406692 | |
24 | Phosphorylation | DSFTRFSSQSNVYGL CCCCCCCCCCCCCEE | 34.61 | 21406692 | |
25 | Ubiquitination | SFTRFSSQSNVYGLA CCCCCCCCCCCCEEC | 37.51 | - | |
26 | Phosphorylation | FTRFSSQSNVYGLAG CCCCCCCCCCCEECC | 30.15 | 21406692 | |
29 | Phosphorylation | FSSQSNVYGLAGGAG CCCCCCCCEECCCCC | 15.63 | 21406692 | |
38 | Methylation | LAGGAGGRGELLAAT ECCCCCCHHHHHHHH | 34.20 | 82955125 | |
47 | Ubiquitination | ELLAATLKGKVLGFR HHHHHHHCCCEECCC | 52.94 | - | |
49 | Ubiquitination | LAATLKGKVLGFRYQ HHHHHCCCEECCCHH | 32.47 | - | |
67 | Ubiquitination | QKIRPVAKELQFNYI HHHHHHHHHCCCCCC | 60.22 | - | |
88 | Ubiquitination | VSIDTFNKSPPKRGL EEEECCCCCCCCCCE | 61.21 | - | |
100 | Phosphorylation | RGLVVGITFIKDSGD CCEEEEEEEEECCCC | 17.24 | - | |
223 | Phosphorylation | LSALGCQSGYVRVAH HHHCCCCCCEEEEEE | 35.85 | - | |
257 | Phosphorylation | ISRVIVFSLSAAKET CCEEEEEEECCCCCC | 15.55 | 26270265 | |
259 | Phosphorylation | RVIVFSLSAAKETKD EEEEEEECCCCCCCC | 25.61 | 26270265 | |
265 | Ubiquitination | LSAAKETKDRPLQDE ECCCCCCCCCCCCCH | 53.48 | - | |
287 | Phosphorylation | MLEPAVVYRDLLNRG HCCHHHHHHHHHHCC | 7.57 | - | |
361 | Phosphorylation | FHLLWQRSFSSPLLA HEEEEEECCCCCEEE | 17.87 | - | |
363 | Phosphorylation | LLWQRSFSSPLLAMA EEEEECCCCCEEEEE | 32.09 | - | |
364 | Phosphorylation | LWQRSFSSPLLAMAH EEEECCCCCEEEEEC | 19.98 | - | |
375 | Phosphorylation | AMAHVDLTGDGLQEL EEECEECCCCCHHHE | 28.85 | - |
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 KPTN_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KPTN_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 KPTN_HUMAN !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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