dbPTM

TTI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTI1_HUMAN
UniProt AC	O43156
Protein Name	TELO2-interacting protein 1 homolog
Gene Name	TTI1
Organism	Homo sapiens (Human).
Sequence Length	1089
Subcellular Localization	Cytoplasm .
Protein Description	Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals..
Protein Sequence	MAVFDTPEEAFGVLRPVCVQLTKTQTVENVEHLQTRLQAVSDSALQELQQYILFPLRFTLKTPGPKRERLIQSVVECLTFVLSSTCVKEQELLQELFSELSACLYSPSSQKPAAVSEELKLAVIQGLSTLMHSAYGDIILTFYEPSILPRLGFAVSLLLGLAEQEKSKQIKIAALKCLQVLLLQCDCQDHPRSLDELEQKQLGDLFASFLPGISTALTRLITGDFKQGHSIVVSSLKIFYKTVSFIMADEQLKRISKVQAKPAVEHRVAELMVYREADWVKKTGDKLTILIKKIIECVSVHPHWKVRLELVELVEDLLLKCSQSLVECAGPLLKALVGLVNDESPEIQAQCNKVLRHFADQKVVVGNKALADILSESLHSLATSLPRLMNSQDDQGKFSTLSLLLGYLKLLGPKINFVLNSVAHLQRLSKALIQVLELDVADIKIVEERRWNSDDLNASPKTSATQPWNRIQRRYFRFFTDERIFMLLRQVCQLLGYYGNLYLLVDHFMELYHQSVVYRKQAAMILNELVTGAAGLEVEDLHEKHIKTNPEELREIVTSILEEYTSQENWYLVTCLETEEMGEELMMEHPGLQAITSGEHTCQVTSFLAFSKPSPTICSMNSNIWQICIQLEGIGQFAYALGKDFCLLLMSALYPVLEKAGDQTLLISQVATSTMMDVCRACGYDSLQHLINQNSDYLVNGISLNLRHLALHPHTPKVLEVMLRNSDANLLPLVADVVQDVLATLDQFYDKRAASFVSVLHALMAALAQWFPDTGNLGHLQEQSLGEEGSHLNQRPAALEKSTTTAEDIEQFLLNYLKEKDVADGNVSDFDNEEEEQSVPPKVDENDTRPDVEPPLPLQIQIAMDVMERCIHLLSDKNLQIRLKVLDVLDLCVVVLQSHKNQLLPLAHQAWPSLVHRLTRDAPLAVLRAFKVLRTLGSKCGDFLRSRFCKDVLPKLAGSLVTQAPISARAGPVYSHTLAFKLQLAVLQGLGPLCERLDLGEGDLNKVADACLIYLSVKQPVKLQEAARSVFLHLMKVDPDSTWFLLNELYCPVQFTPPHPSLHPVQLHGASGQQNPYTTNVLQLLKELQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
61	Ubiquitination	FPLRFTLKTPGPKRE HHHEEECCCCCHHHH	50.01	33845483
106	Phosphorylation	ELSACLYSPSSQKPA HHHHHHCCCCCCCCC	12.83	25627689
116	Phosphorylation	SQKPAAVSEELKLAV CCCCCCCCHHHHHHH	22.19	28348404
167	Phosphorylation	GLAEQEKSKQIKIAA HHHHHHHCHHHHHHH	29.10	-
253	Ubiquitination	IMADEQLKRISKVQA HHCHHHHHHHHHCCC	47.59	29967540
256	Phosphorylation	DEQLKRISKVQAKPA HHHHHHHHHCCCCHH	30.70	30576142
257	Ubiquitination	EQLKRISKVQAKPAV HHHHHHHHCCCCHHH	35.67	27667366
261	Ubiquitination	RISKVQAKPAVEHRV HHHHCCCCHHHHHHH	19.20	29967540
274	Phosphorylation	RVAELMVYREADWVK HHHHHHHHHHCHHHH	6.70	20071362
283	Phosphorylation	EADWVKKTGDKLTIL HCHHHHHHCCHHHHH	44.91	-
353	Ubiquitination	EIQAQCNKVLRHFAD HHHHHHHHHHHHHCC	50.72	21963094
362	Ubiquitination	LRHFADQKVVVGNKA HHHHCCCEEEECCHH	37.23	27667366
368	Ubiquitination	QKVVVGNKALADILS CEEEECCHHHHHHHH	38.56	29967540
453	Phosphorylation	VEERRWNSDDLNASP EEHHCCCCCCCCCCC	26.07	29978859
459	Phosphorylation	NSDDLNASPKTSATQ CCCCCCCCCCCCCCC	26.34	19664994
461	Ubiquitination	DDLNASPKTSATQPW CCCCCCCCCCCCCHH	53.25	21906983
462	Phosphorylation	DLNASPKTSATQPWN CCCCCCCCCCCCHHH	27.29	26074081
463	Phosphorylation	LNASPKTSATQPWNR CCCCCCCCCCCHHHH	35.13	26074081
547	Ubiquitination	DLHEKHIKTNPEELR HHHHHHCCCCHHHHH	41.80	-
802	Phosphorylation	RPAALEKSTTTAEDI CCHHHHCCCCCHHHH	22.93	25627689
803	Phosphorylation	PAALEKSTTTAEDIE CHHHHCCCCCHHHHH	38.95	25627689
804	Phosphorylation	AALEKSTTTAEDIEQ HHHHCCCCCHHHHHH	30.97	25627689
805	Phosphorylation	ALEKSTTTAEDIEQF HHHCCCCCHHHHHHH	28.30	25627689
818	Ubiquitination	QFLLNYLKEKDVADG HHHHHHHHHCCCCCC	52.97	29967540
828	Phosphorylation	DVADGNVSDFDNEEE CCCCCCCCCCCCHHH	36.24	25159151
838	Phosphorylation	DNEEEEQSVPPKVDE CCHHHHHCCCCCCCC	39.61	26074081
877	Ubiquitination	CIHLLSDKNLQIRLK HHHHHCCCCHHHHHH	57.07	29967540
939	Ubiquitination	VLRTLGSKCGDFLRS HHHHHHHHHHHHHHH	40.20	29967540
946	Phosphorylation	KCGDFLRSRFCKDVL HHHHHHHHHHCHHHH	31.68	20068231
955	Ubiquitination	FCKDVLPKLAGSLVT HCHHHHHHHCCCHHH	46.97	29967540
959	Phosphorylation	VLPKLAGSLVTQAPI HHHHHCCCHHHCCCC	17.66	20068231
962	Phosphorylation	KLAGSLVTQAPISAR HHCCCHHHCCCCCCC	25.06	20068231
967	Phosphorylation	LVTQAPISARAGPVY HHHCCCCCCCCCCCC	15.62	20068231
1029	Phosphorylation	KLQEAARSVFLHLMK CHHHHHHHHHHHHCC	16.70	27067055
1077	Phosphorylation	ASGQQNPYTTNVLQL CCCCCCCCHHHHHHH	33.47	-

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
828	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
828	S	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO9	Q9UK97	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
828	S	Phosphorylation	23186163
Phosphorylated at Ser-828 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex.
828	S	ubiquitylation	23186163
Phosphorylated at Ser-828 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex.

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 TTI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MTOR_HUMAN	MTOR	physical	20427287
TELO2_HUMAN	TELO2	physical	20427287
ATM_HUMAN	ATM	physical	20427287
ATR_HUMAN	ATR	physical	20427287
PRKDC_HUMAN	PRKDC	physical	20427287
SMG1_HUMAN	SMG1	physical	20427287
TRRAP_HUMAN	TRRAP	physical	20427287
RUVB1_HUMAN	RUVBL1	physical	20801936
TTI2_HUMAN	TTI2	physical	20801936
RUVB2_HUMAN	RUVBL2	physical	20801936
HSP74_HUMAN	HSPA4	physical	20801936
PIHD1_HUMAN	PIH1D1	physical	20801936
RUVB1_HUMAN	RUVBL1	physical	20371770
RUVB2_HUMAN	RUVBL2	physical	20371770
RPAB1_HUMAN	POLR2E	physical	20371770
SMG1_HUMAN	SMG1	physical	20371770
PRKDC_HUMAN	PRKDC	physical	20371770
TRRAP_HUMAN	TRRAP	physical	20371770
TELO2_HUMAN	TELO2	physical	20371770
RPAP3_HUMAN	RPAP3	physical	20371770
RMP_HUMAN	URI1	physical	20371770
HSP74_HUMAN	HSPA4	physical	20371770
TBA1A_HUMAN	TUBA1A	physical	20371770
PIHD1_HUMAN	PIH1D1	physical	20371770
RPAB1_HUMAN	POLR2E	physical	22863883
PSME4_HUMAN	PSME4	physical	22863883
ATM_HUMAN	ATM	physical	20810650
ATR_HUMAN	ATR	physical	20810650
PRKDC_HUMAN	PRKDC	physical	20810650
SMG1_HUMAN	SMG1	physical	20810650
MTOR_HUMAN	MTOR	physical	20810650
TELO2_HUMAN	TELO2	physical	20810650
STOM_HUMAN	STOM	physical	27173435

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 TTI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND MASSSPECTROMETRY.	17081983 [Abstract]

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