ITFG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ITFG2_HUMAN
• UniProt AC: Q969R8
• Protein Name: KICSTOR complex protein ITFG2 {ECO:0000305}
• Gene Name: ITFG2 {ECO:0000312|HGNC:HGNC:30879}
• Organism: Homo sapiens (Human).
• Sequence Length: 447
• Subcellular Localization: Lysosome membrane . Localization to lysosomes is amino acid-independent.
• 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: MRSVSYVQRVALEFSGSLFPHAICLGDVDNDTLNELVVGDTSGKVSVYKNDDSRPWLTCSCQGMLTCVGVGDVCNKGKNLLVAVSAEGWFHLFDLTPAKVLDASGHHETLIGEEQRPVFKQHIPANTKVMLISDIDGDGCRELVVGYTDRVVRAFRWEELGEGPEHLTGQLVSLKKWMLEGQVDSLSVTLGPLGLPELMVSQPGCAYAILLCTWKKDTGSPPASEGPTDGSRETPAARDVVLHQTSGRIHNKNVSTHLIGNIKQGHGTESSGSGLFALCTLDGTLKLMEEMEEADKLLWSVQVDHQLFALEKLDVTGNGHEEVVACAWDGQTYIIDHNRTVVRFQVDENIRAFCAGLYACKEGRNSPCLVYVTFNQKIYVYWEVQLERMESTNLVKLLETKPEYHSLLQELGVDPDDLPVTRALLHQTLYHPDQPPQCAPSSLQDPT

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
48	Phosphorylation	TSGKVSVYKNDDSRP CCCEEEEEECCCCCC	9.14	-
49	Ubiquitination	SGKVSVYKNDDSRPW CCEEEEEECCCCCCE	52.31	-
49	Ubiquitination	SGKVSVYKNDDSRPW CCEEEEEECCCCCCE	52.31	-
53	Phosphorylation	SVYKNDDSRPWLTCS EEEECCCCCCEEEEE	43.01	-
104	Phosphorylation	PAKVLDASGHHETLI HHEEEECCCCCCCCC	38.02	23401153
109	Phosphorylation	DASGHHETLIGEEQR ECCCCCCCCCCCCCC	21.22	23403867
120	Ubiquitination	EEQRPVFKQHIPANT CCCCCHHHHCCCCCC	41.00	-
207	Phosphorylation	VSQPGCAYAILLCTW HCCCCEEEEEEEEEE	9.76	-
218	Phosphorylation	LCTWKKDTGSPPASE EEEEECCCCCCCCCC	48.73	21955146
220	Phosphorylation	TWKKDTGSPPASEGP EEECCCCCCCCCCCC	29.78	29255136
224	Phosphorylation	DTGSPPASEGPTDGS CCCCCCCCCCCCCCC	49.19	30576142
228	Phosphorylation	PPASEGPTDGSRETP CCCCCCCCCCCCCCH	64.94	25850435
234	Phosphorylation	PTDGSRETPAARDVV CCCCCCCCHHHHHEE	19.67	-
245	Phosphorylation	RDVVLHQTSGRIHNK HHEEEEECCCCCCCC	23.54	-
246	Phosphorylation	DVVLHQTSGRIHNKN HEEEEECCCCCCCCC	21.36	-
252	Ubiquitination	TSGRIHNKNVSTHLI CCCCCCCCCCEEEEE	44.56	-
255	Phosphorylation	RIHNKNVSTHLIGNI CCCCCCCEEEEEECE	21.36	28985074
256	Phosphorylation	IHNKNVSTHLIGNIK CCCCCCEEEEEECEE	19.20	28985074
270	Phosphorylation	KQGHGTESSGSGLFA ECCCCCCCCCCCEEE	39.58	28985074
280	Phosphorylation	SGLFALCTLDGTLKL CCEEEEEECHHHHHH	28.83	28985074
340	Phosphorylation	YIIDHNRTVVRFQVD EEEECCCEEEEEEEC	28.77	30576142
361	Ubiquitination	CAGLYACKEGRNSPC HHHHHHCCCCCCCCE	55.84	-
401	Ubiquitination	LVKLLETKPEYHSLL HHHHHHCCHHHHHHH	26.86	-
404	Phosphorylation	LLETKPEYHSLLQEL HHHCCHHHHHHHHHH	12.77	27642862

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ITFG2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ITFG2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ITFG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CL066_HUMAN	C12orf66	physical	28514442
SZT2_HUMAN	SZT2	physical	28514442
SPD2B_HUMAN	SH3PXD2B	physical	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.