TIPIN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIPIN_HUMAN
• UniProt AC: Q9BVW5
• Protein Name: TIMELESS-interacting protein
• Gene Name: TIPIN
• Organism: Homo sapiens (Human).
• Sequence Length: 301
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Plays an important role in the control of DNA replication and the maintenance of replication fork stability. Important for cell survival after DNA damage or replication stress. May be specifically required for the ATR-CHEK1 pathway in the replication checkpoint induced by hydroxyurea or ultraviolet light. Forms a complex with TIMELESS and this complex regulates DNA replication processes under both normal and stress conditions, stabilizes replication forks and influences both CHEK1 phosphorylation and the intra-S phase checkpoint in response to genotoxic stress..
• Protein Sequence: MLEPQENGVIDLPDYEHVEDETFPPFPPPASPERQDGEGTEPDEESGNGAPVRVPPKRTVKRNIPKLDAQRLISERGLPALRHVFDKAKFKGKGHEAEDLKMLIRHMEHWAHRLFPKLQFEDFIDRVEYLGSKKEVQTCLKRIRLDLPILHEDFVSNNDEVAENNEHDVTSTELDPFLTNLSESEMFASELSRSLTEEQQQRIERNKQLALERRQAKLLSNSQTLGNDMLMNTPRAHTVEEVNTDEDQKEESNGLNEDILDNPCNDAIANTLNEEETLLDQSFKNVQQQLDATSRNITEAR

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
22	Phosphorylation	YEHVEDETFPPFPPP CCCCCCCCCCCCCCC	54.48	26074081
31	Phosphorylation	PPFPPPASPERQDGE CCCCCCCCCCCCCCC	32.82	26074081
40	Phosphorylation	ERQDGEGTEPDEESG CCCCCCCCCCCCCCC	39.79	26074081
76	Methylation	AQRLISERGLPALRH HHHHHHHCCHHHHHH	45.20	115918517
87	Ubiquitination	ALRHVFDKAKFKGKG HHHHHHHHHHHCCCC	41.85	-
93	Ubiquitination	DKAKFKGKGHEAEDL HHHHHCCCCCCHHHH	58.65	-
101	Ubiquitination	GHEAEDLKMLIRHME CCCHHHHHHHHHHHH	43.94	21890473
117	Ubiquitination	WAHRLFPKLQFEDFI HHHHHHCCCCHHHHH	47.81	21890473
126	Methylation	QFEDFIDRVEYLGSK CHHHHHHHHHHHCCH	20.53	115918513
133	Ubiquitination	RVEYLGSKKEVQTCL HHHHHCCHHHHHHHH	51.67	-
134	Ubiquitination	VEYLGSKKEVQTCLK HHHHCCHHHHHHHHH	65.89	-
141	Ubiquitination	KEVQTCLKRIRLDLP HHHHHHHHHHCCCCC	48.18	-
182	Phosphorylation	DPFLTNLSESEMFAS CHHHHCCCHHHHHHH	40.94	26074081
184	Phosphorylation	FLTNLSESEMFASEL HHHCCCHHHHHHHHH	30.87	26074081
192	Phosphorylation	EMFASELSRSLTEEQ HHHHHHHHHHCCHHH	18.77	-
194	Phosphorylation	FASELSRSLTEEQQQ HHHHHHHHCCHHHHH	35.95	25159151
196	Phosphorylation	SELSRSLTEEQQQRI HHHHHHCCHHHHHHH	38.43	25262027
207	Ubiquitination	QQRIERNKQLALERR HHHHHHHHHHHHHHH	53.57	-
217	Ubiquitination	ALERRQAKLLSNSQT HHHHHHHHHHHCCCC	41.44	-
220	Phosphorylation	RRQAKLLSNSQTLGN HHHHHHHHCCCCCCC	44.89	25159151
222	Phosphorylation	QAKLLSNSQTLGNDM HHHHHHCCCCCCCCC	22.59	17525332
224	Phosphorylation	KLLSNSQTLGNDMLM HHHHCCCCCCCCCCC	36.13	25159151
233	Phosphorylation	GNDMLMNTPRAHTVE CCCCCCCCCCCCCEE	10.53	25159151
238	Phosphorylation	MNTPRAHTVEEVNTD CCCCCCCCEEECCCC	28.73	25159151
244	Phosphorylation	HTVEEVNTDEDQKEE CCEEECCCCHHHHHH	46.04	25159151
271	Phosphorylation	CNDAIANTLNEEETL HHHHHHHHCCHHHHH	23.18	28102081
277	Phosphorylation	NTLNEEETLLDQSFK HHCCHHHHHHHHHHH	35.58	28102081
282	Phosphorylation	EETLLDQSFKNVQQQ HHHHHHHHHHHHHHH	37.54	26074081
293	Phosphorylation	VQQQLDATSRNITEA HHHHHHHHHCCHHHC	28.08	28555341

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TIPIN_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 TIPIN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFA1_HUMAN	RPA1	physical	17296725
TIM_HUMAN	TIMELESS	physical	17102137
A4_HUMAN	APP	physical	21832049
PRDX1_HUMAN	PRDX1	physical	17141802
TEX11_HUMAN	TEX11	physical	25416956
SP16H_HUMAN	SUPT16H	physical	26186194
TIM_HUMAN	TIMELESS	physical	26186194
MCM7_HUMAN	MCM7	physical	26186194
MCM2_HUMAN	MCM2	physical	26186194
PSF1_HUMAN	GINS1	physical	26186194
MCM3_HUMAN	MCM3	physical	26186194
SLD5_HUMAN	GINS4	physical	26186194
TIM_HUMAN	TIMELESS	physical	28514442
SLD5_HUMAN	GINS4	physical	28514442
PSF1_HUMAN	GINS1	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
MCM3_HUMAN	MCM3	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY.
PubMed: 18669648

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASSSPECTROMETRY.
PubMed: 17525332

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND MASSSPECTROMETRY.
PubMed: 19690332