NPRL2_HUMAN - dbPTM
NPRL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPRL2_HUMAN
UniProt AC Q8WTW4
Protein Name GATOR complex protein NPRL2 {ECO:0000305}
Gene Name NPRL2 {ECO:0000312|HGNC:HGNC:24969}
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization Lysosome membrane . Localization to lysosomes is amino acid-independent.
Protein Description As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway.; Suppresses Src-dependent tyrosine phosphorylation and activation of PDPK1 and its downstream signaling. Down-regulates PDPK1 kinase activity by interfering with tyrosine phosphorylation at 'Tyr-9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor. Suppresses cell growth and enhances sensitivity to various anticancer drugs..
Protein Sequence MGSGCRIECIFFSEFHPTLGPKITYQVPEDFISRELFDTVQVYIITKPELQNKLITVTAMEKKLIGCPVCIEHKKYSRNALLFNLGFVCDAQAKTCALEPIVKKLAGYLTTLELESSFVSMEESKQKLVPIMTILLEELNASGRCTLPIDESNTIHLKVIEQRPDPPVAQEYDVPVFTKDKEDFFNSQWDLTTQQILPYIDGFRHIQKISAEADVELNLVRIAIQNLLYYGVVTLVSILQYSNVYCPTPKVQDLVDDKSLQEACLSYVTKQGHKRASLRDVFQLYCSLSPGTTVRDLIGRHPQQLQHVDERKLIQFGLMKNLIRRLQKYPVRVTREEQSHPARLYTGCHSYDEICCKTGMSYHELDERLENDPNIIICWK
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
59UbiquitinationNKLITVTAMEKKLIG
CCEEEEECCHHHHHC
10.3722817900
59 (in isoform 2)Ubiquitination-10.3721906983
61UbiquitinationLITVTAMEKKLIGCP
EEEEECCHHHHHCCC
44.5722817900
62 (in isoform 1)Ubiquitination-39.5321906983
62UbiquitinationITVTAMEKKLIGCPV
EEEECCHHHHHCCCE
39.5322817900
63UbiquitinationTVTAMEKKLIGCPVC
EEECCHHHHHCCCEE
31.8422817900
74UbiquitinationCPVCIEHKKYSRNAL
CCEECCCCCCCCCCE
40.3929967540
94UbiquitinationFVCDAQAKTCALEPI
EECCHHHCHHCHHHH
31.86-
100UbiquitinationAKTCALEPIVKKLAG
HCHHCHHHHHHHHHH
37.2121963094
101UbiquitinationKTCALEPIVKKLAGY
CHHCHHHHHHHHHHH
5.3222817900
103UbiquitinationCALEPIVKKLAGYLT
HCHHHHHHHHHHHHH
42.6721963094
104UbiquitinationALEPIVKKLAGYLTT
CHHHHHHHHHHHHHH
32.4522817900
110PhosphorylationKKLAGYLTTLELESS
HHHHHHHHHHHHHHH
22.3522210691
111PhosphorylationKLAGYLTTLELESSF
HHHHHHHHHHHHHHC
18.6822210691
117PhosphorylationTTLELESSFVSMEES
HHHHHHHHCCCHHHH
21.9422210691
120PhosphorylationELESSFVSMEESKQK
HHHHHCCCHHHHHHH
20.61-
138UbiquitinationIMTILLEELNASGRC
HHHHHHHHHCCCCCC
47.4921963094
158UbiquitinationESNTIHLKVIEQRPD
CCCEEEEEEEECCCC
27.31-
176UbiquitinationAQEYDVPVFTKDKED
CCCCCCCCEECCHHH
10.7922817900
178UbiquitinationEYDVPVFTKDKEDFF
CCCCCCEECCHHHHH
38.2722817900
179 (in isoform 1)Ubiquitination-56.1721906983
179UbiquitinationYDVPVFTKDKEDFFN
CCCCCEECCHHHHHH
56.1722817900
181UbiquitinationVPVFTKDKEDFFNSQ
CCCEECCHHHHHHCC
61.8222817900
200UbiquitinationTQQILPYIDGFRHIQ
HHHHHHHHCCCCCHH
3.8421963094
237UbiquitinationYGVVTLVSILQYSNV
HHHHHHHHHHHHCCC
22.2421963094
255UbiquitinationTPKVQDLVDDKSLQE
CCCHHHHCCCHHHHH
13.8921963094
258UbiquitinationVQDLVDDKSLQEACL
HHHHCCCHHHHHHHH
48.9121963094
270UbiquitinationACLSYVTKQGHKRAS
HHHHHHHHHCCCCCC
44.2129967540
277PhosphorylationKQGHKRASLRDVFQL
HHCCCCCCHHHHHHH
28.1532142685
287PhosphorylationDVFQLYCSLSPGTTV
HHHHHHHCCCCCCCH
20.5122210691
289PhosphorylationFQLYCSLSPGTTVRD
HHHHHCCCCCCCHHH
12.6522210691
292PhosphorylationYCSLSPGTTVRDLIG
HHCCCCCCCHHHHHC
26.0422210691
293PhosphorylationCSLSPGTTVRDLIGR
HCCCCCCCHHHHHCC
21.3222210691
312UbiquitinationLQHVDERKLIQFGLM
HCCCCHHHHHHHHHH
48.14-
317UbiquitinationERKLIQFGLMKNLIR
HHHHHHHHHHHHHHH
14.4221963094
320UbiquitinationLIQFGLMKNLIRRLQ
HHHHHHHHHHHHHHH
54.3621963094
328UbiquitinationNLIRRLQKYPVRVTR
HHHHHHHHCCCCCCH
56.99-
345PhosphorylationQSHPARLYTGCHSYD
HCCCCEEECCCCCHH
8.7829496907
350PhosphorylationRLYTGCHSYDEICCK
EEECCCCCHHHHHHC
38.0529496907
354UbiquitinationGCHSYDEICCKTGMS
CCCCHHHHHHCCCCC
2.8221963094
357UbiquitinationSYDEICCKTGMSYHE
CHHHHHHCCCCCHHH
43.6421963094

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 NPRL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NPRL2_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 NPRL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAP0_HUMANPRKAR1Aphysical
17353931
UBC12_HUMANUBE2Mphysical
17353931
NPRL3_HUMANNPRL3physical
19521502
DEPD5_HUMANDEPDC5physical
23723238
NPRL3_HUMANNPRL3physical
23723238
WDR59_HUMANWDR59physical
23723238
WDR24_HUMANWDR24physical
23723238
SEH1_HUMANSEH1Lphysical
23723238
HERC2_HUMANHERC2physical
25480944
RRAGA_HUMANRRAGAphysical
25936802
DEPD5_HUMANDEPDC5physical
25936802
DEPD5_HUMANDEPDC5physical
28514442
NPRL3_HUMANNPRL3physical
28514442
ZBTB5_HUMANZBTB5physical
28514442
APBP2_HUMANAPPBP2physical
28514442
LRCH2_HUMANLRCH2physical
28514442

Drug and Disease Associations
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.
Regulatory Network of NPRL2_HUMAN

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Related Literatures of Post-Translational Modification

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