KPTN_HUMAN - dbPTM
KPTN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MMGEAAVA
-------CCCCCHHH
7.6022814378
23PhosphorylationEDSFTRFSSQSNVYG
CCCCCCCCCCCCCCE
24.9521406692
24PhosphorylationDSFTRFSSQSNVYGL
CCCCCCCCCCCCCEE
34.6121406692
25UbiquitinationSFTRFSSQSNVYGLA
CCCCCCCCCCCCEEC
37.51-
26PhosphorylationFTRFSSQSNVYGLAG
CCCCCCCCCCCEECC
30.1521406692
29PhosphorylationFSSQSNVYGLAGGAG
CCCCCCCCEECCCCC
15.6321406692
38MethylationLAGGAGGRGELLAAT
ECCCCCCHHHHHHHH
34.2082955125
47UbiquitinationELLAATLKGKVLGFR
HHHHHHHCCCEECCC
52.94-
49UbiquitinationLAATLKGKVLGFRYQ
HHHHHCCCEECCCHH
32.47-
67UbiquitinationQKIRPVAKELQFNYI
HHHHHHHHHCCCCCC
60.22-
88UbiquitinationVSIDTFNKSPPKRGL
EEEECCCCCCCCCCE
61.21-
100PhosphorylationRGLVVGITFIKDSGD
CCEEEEEEEEECCCC
17.24-
223PhosphorylationLSALGCQSGYVRVAH
HHHCCCCCCEEEEEE
35.85-
257PhosphorylationISRVIVFSLSAAKET
CCEEEEEEECCCCCC
15.5526270265
259PhosphorylationRVIVFSLSAAKETKD
EEEEEEECCCCCCCC
25.6126270265
265UbiquitinationLSAAKETKDRPLQDE
ECCCCCCCCCCCCCH
53.48-
287PhosphorylationMLEPAVVYRDLLNRG
HCCHHHHHHHHHHCC
7.57-
361PhosphorylationFHLLWQRSFSSPLLA
HEEEEEECCCCCEEE
17.87-
363PhosphorylationLLWQRSFSSPLLAMA
EEEEECCCCCEEEEE
32.09-
364PhosphorylationLWQRSFSSPLLAMAH
EEEECCCCCEEEEEC
19.98-
375PhosphorylationAMAHVDLTGDGLQEL
EEECEECCCCCHHHE
28.85-

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 KPTN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPTN_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 KPTN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB25_HUMANRAB25physical
17353931
ITFG2_HUMANITFG2physical
17353931
TSN7_HUMANTSPAN7physical
17353931
AUP1_HUMANAUP1physical
17353931
A4_HUMANAPPphysical
21832049
ELP1_HUMANIKBKAPphysical
26186194
NFRKB_HUMANNFRKBphysical
26186194
DCAM_HUMANAMD1physical
26186194
CL066_HUMANC12orf66physical
26186194
IF4G3_HUMANEIF4G3physical
26186194
ELP2_HUMANELP2physical
26186194
KLC1_HUMANKLC1physical
26186194
KLC2_HUMANKLC2physical
26186194
KLC4_HUMANKLC4physical
26186194
KINH_HUMANKIF5Bphysical
26186194
KIF5C_HUMANKIF5Cphysical
26186194
S14L1_HUMANSEC14L1physical
26186194
ITFG2_HUMANITFG2physical
26186194
RNH2A_HUMANRNASEH2Aphysical
26186194
TES_HUMANTESphysical
26186194
UBP19_HUMANUSP19physical
26186194
SZT2_HUMANSZT2physical
26186194
KLH15_HUMANKLHL15physical
26186194
ELP3_HUMANELP3physical
26186194
GTSE1_HUMANGTSE1physical
26186194
TMCO4_HUMANTMCO4physical
26186194
COX16_HUMANCOX16physical
26186194
MAVS_HUMANMAVSphysical
26186194
DPH1_HUMANDPH1physical
26186194
FMN2_HUMANFMN2physical
26186194
ITFG2_HUMANITFG2physical
28514442
SZT2_HUMANSZT2physical
28514442
CL066_HUMANC12orf66physical
28514442
TMCO4_HUMANTMCO4physical
28514442
S14L1_HUMANSEC14L1physical
28514442
NFRKB_HUMANNFRKBphysical
28514442
KLC4_HUMANKLC4physical
28514442
TES_HUMANTESphysical
28514442
RNH2A_HUMANRNASEH2Aphysical
28514442
ELP3_HUMANELP3physical
28514442
KLC2_HUMANKLC2physical
28514442
KLC1_HUMANKLC1physical
28514442
GTSE1_HUMANGTSE1physical
28514442
MAVS_HUMANMAVSphysical
28514442
FMN2_HUMANFMN2physical
28514442
IF4G3_HUMANEIF4G3physical
28514442
DCAM_HUMANAMD1physical
28514442
KINH_HUMANKIF5Bphysical
28514442
ELP2_HUMANELP2physical
28514442
KLH15_HUMANKLHL15physical
28514442
DPH1_HUMANDPH1physical
28514442

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

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Related Literatures of Post-Translational Modification

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