MCTS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MCTS1_HUMAN
• UniProt AC: Q9ULC4
• Protein Name: Malignant T-cell-amplified sequence 1
• Gene Name: MCTS1
• Organism: Homo sapiens (Human).
• Sequence Length: 181
• Subcellular Localization: Cytoplasm . Nuclear relocalization after DNA damage.
• Protein Description: Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constitutively expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3. Involved in translation initiation; promotes aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits..
• Protein Sequence: MFKKFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQIMPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTIVAIMAEGKQHALCVGVMKMSAEDIEKVNKGIGIENIHYLNDGLWHMKTYK

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
4	Acetylation	----MFKKFDEKENV ----CCCCCCCCCCH	46.94	25953088
8	Ubiquitination	MFKKFDEKENVSNCI CCCCCCCCCCHHHHH	57.33	29967540
14	S-nitrosylation	EKENVSNCIQLKTSV CCCCHHHHHHHHHHH	1.31	22178444
18	Malonylation	VSNCIQLKTSVIKGI HHHHHHHHHHHHHHH	23.52	26320211
18	Acetylation	VSNCIQLKTSVIKGI HHHHHHHHHHHHHHH	23.52	25953088
18	Ubiquitination	VSNCIQLKTSVIKGI HHHHHHHHHHHHHHH	23.52	33845483
19 (in isoform 3)	Malonylation	-	36.50	26320211
23	Acetylation	QLKTSVIKGIKNQLI HHHHHHHHHHHHHHH	53.05	26051181
23	Ubiquitination	QLKTSVIKGIKNQLI HHHHHHHHHHHHHHH	53.05	33845483
24 (in isoform 3)	Ubiquitination	-	25.61	-
24	Ubiquitination	LKTSVIKGIKNQLIE HHHHHHHHHHHHHHH	25.61	33845483
44	Sulfoxidation	EPWLNQIMPKKDPVK HHHHHHHCCCCCCCE	2.61	28183972
51	Acetylation	MPKKDPVKIVRCHEH CCCCCCCEEEECCCC	40.65	23749302
52	Acetylation	PKKDPVKIVRCHEHI CCCCCCEEEECCCCE	2.11	19608861
75 (in isoform 2)	Ubiquitination	-	63.98	21890473
79	Phosphorylation	RQREGPFYPTLRLLH ECCCCCCHHHHHHHH	9.84	20068231
81	Phosphorylation	REGPFYPTLRLLHKY CCCCCHHHHHHHHCC	17.09	20068231
87 (in isoform 1)	Ubiquitination	-	55.37	21890473
87	Ubiquitination	PTLRLLHKYPFILPH HHHHHHHCCCCCCCC	55.37	23000965
87	Acetylation	PTLRLLHKYPFILPH HHHHHHHCCCCCCCC	55.37	23236377
88	Ubiquitination	TLRLLHKYPFILPHQ HHHHHHCCCCCCCCC	7.82	21890473
88	Ubiquitination	TLRLLHKYPFILPHQ HHHHHHCCCCCCCCC	7.82	21890473
88 (in isoform 3)	Ubiquitination	-	7.82	-
99	Ubiquitination	LPHQQVDKGAIKFVL CCCCCCCCCHHHHHH	51.92	29967540
99	2-Hydroxyisobutyrylation	LPHQQVDKGAIKFVL CCCCCCCCCHHHHHH	51.92	-
99	Acetylation	LPHQQVDKGAIKFVL CCCCCCCCCHHHHHH	51.92	19608861
100	Acetylation	PHQQVDKGAIKFVLS CCCCCCCCHHHHHHC	28.24	19608861
100	Ubiquitination	PHQQVDKGAIKFVLS CCCCCCCCHHHHHHC	28.24	29967540
103	Acetylation	QVDKGAIKFVLSGAN CCCCCHHHHHHCCCC	28.96	25953088
103	Ubiquitination	QVDKGAIKFVLSGAN CCCCCHHHHHHCCCC	28.96	-
107	Phosphorylation	GAIKFVLSGANIMCP CHHHHHHCCCCEECC	30.47	30622161
112	Sulfoxidation	VLSGANIMCPGLTSP HHCCCCEECCCCCCC	1.95	21406390
117	Phosphorylation	NIMCPGLTSPGAKLY CEECCCCCCCCCCCC	38.50	25159151
118	Phosphorylation	IMCPGLTSPGAKLYP EECCCCCCCCCCCCH	26.78	25159151
124	Phosphorylation	TSPGAKLYPAAVDTI CCCCCCCCHHHHHHH	7.07	28348404
157	Acetylation	MSAEDIEKVNKGIGI CCHHHHHHHHCCCCC	51.98	23236377
157	Ubiquitination	MSAEDIEKVNKGIGI CCHHHHHHHHCCCCC	51.98	29967540
158	Ubiquitination	SAEDIEKVNKGIGIE CHHHHHHHHCCCCCE	6.08	29967540
160	Ubiquitination	EDIEKVNKGIGIENI HHHHHHHCCCCCEEE	55.69	21963094
161 (in isoform 3)	Ubiquitination	-	20.39	-
161	Ubiquitination	DIEKVNKGIGIENIH HHHHHHCCCCCEEEE	20.39	21963094
177	Sulfoxidation	LNDGLWHMKTYK--- ECCCEECEEECC---	2.04	30846556
178	Acetylation	NDGLWHMKTYK---- CCCEECEEECC----	35.50	25953088
178	Ubiquitination	NDGLWHMKTYK---- CCCEECEEECC----	35.50	-
179 (in isoform 3)	Ubiquitination	-	29.03	-
181	Ubiquitination	LWHMKTYK------- EECEEECC-------	60.12	-
182 (in isoform 3)	Ubiquitination	-		-

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
81	T	Phosphorylation	Kinase	ERK2	P28482	PSP
81	T	Phosphorylation	Kinase	ERK1	P27361	PSP
118	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MCTS1_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 MCTS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DENR_HUMAN	DENR	physical	16169070
ASB6_HUMAN	ASB6	physical	22863883
PUR9_HUMAN	ATIC	physical	22863883
HDGF_HUMAN	HDGF	physical	22863883
HMGB3_HUMAN	HMGB3	physical	22863883
IPO5_HUMAN	IPO5	physical	22863883
IPO9_HUMAN	IPO9	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
UBA1_HUMAN	UBA1	physical	22863883
UBP5_HUMAN	USP5	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
COR1C_HUMAN	CORO1C	physical	26344197
DENR_HUMAN	DENR	physical	26344197
DENR_HUMAN	DENR	physical	21516116

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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Phosphorylation of MCT-1 by p44/42 MAPK is required for itsstabilization in response to DNA damage.";
Nandi S., Reinert L.S., Hachem A., Mazan-Mamczarz K., Hagner P.,He H., Gartenhaus R.B.;
Oncogene 26:2283-2289(2007).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-81 AND SER-118, AND MUTAGENESIS OFTHR-81 AND SER-118.
PubMed: 17016429