SEN34_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEN34_HUMAN
• UniProt AC: Q9BSV6
• Protein Name: tRNA-splicing endonuclease subunit Sen34
• Gene Name: TSEN34
• Organism: Homo sapiens (Human).
• Sequence Length: 310
• Subcellular Localization: Nucleus . Nucleus, nucleolus . May be transiently localized in the nucleolus.
• Protein Description: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. It probably carries the active site for 3'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events..
• Protein Sequence: MLVVEVANGRSLVWGAEAVQALRERLGVGGRTVGALPRGPRQNSRLGLPLLLMPEEARLLAEIGAVTLVSAPRPDSRHHSLALTSFKRQQEESFQEQSALAAEARETRRQELLEKITEGQAAKKQKLEQASGASSSQEAGSSQAAKEDETSDGQASGEQEEAGPSSSQAGPSNGVAPLPRSALLVQLATARPRPVKARPLDWRVQSKDWPHAGRPAHELRYSIYRDLWERGFFLSAAGKFGGDFLVYPGDPLRFHAHYIAQCWAPEDTIPLQDLVAAGRLGTSVRKTLLLCSPQPDGKVVYTSLQWASLQ

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
38	Methylation	RTVGALPRGPRQNSR CCCCCCCCCCCCCCC	69.47	54560365
67	Phosphorylation	LAEIGAVTLVSAPRP HHHHCCEEEEECCCC	22.40	28348404
70	Phosphorylation	IGAVTLVSAPRPDSR HCCEEEEECCCCCCC	35.35	28348404
76	Phosphorylation	VSAPRPDSRHHSLAL EECCCCCCCCCHHHH	35.88	28348404
80	Phosphorylation	RPDSRHHSLALTSFK CCCCCCCHHHHHHHH	14.82	20873877
84	Phosphorylation	RHHSLALTSFKRQQE CCCHHHHHHHHHHHH	26.89	26434776
85	Phosphorylation	HHSLALTSFKRQQEE CCHHHHHHHHHHHHH	29.62	26434776
87	Acetylation	SLALTSFKRQQEESF HHHHHHHHHHHHHHH	49.41	24469671
87	Methylation	SLALTSFKRQQEESF HHHHHHHHHHHHHHH	49.41	24469671
87	Sumoylation	SLALTSFKRQQEESF HHHHHHHHHHHHHHH	49.41	-
87	Ubiquitination	SLALTSFKRQQEESF HHHHHHHHHHHHHHH	49.41	21906983
87	Sumoylation	SLALTSFKRQQEESF HHHHHHHHHHHHHHH	49.41	-
93	Phosphorylation	FKRQQEESFQEQSAL HHHHHHHHHHHHHHH	31.32	28555341
115	Ubiquitination	RRQELLEKITEGQAA HHHHHHHHHHHHHHH	55.70	21906983
123	Ubiquitination	ITEGQAAKKQKLEQA HHHHHHHHHHHHHHH	59.77	21906983
123	2-Hydroxyisobutyrylation	ITEGQAAKKQKLEQA HHHHHHHHHHHHHHH	59.77	-
126	Sumoylation	GQAAKKQKLEQASGA HHHHHHHHHHHHHCC	63.97	-
126	Sumoylation	GQAAKKQKLEQASGA HHHHHHHHHHHHHCC	63.97	-
126	Ubiquitination	GQAAKKQKLEQASGA HHHHHHHHHHHHHCC	63.97	21906983
131	Phosphorylation	KQKLEQASGASSSQE HHHHHHHHCCCCCHH	34.29	23090842
134	Phosphorylation	LEQASGASSSQEAGS HHHHHCCCCCHHHCC	33.76	29255136
135	Phosphorylation	EQASGASSSQEAGSS HHHHCCCCCHHHCCC	35.19	29255136
136	Phosphorylation	QASGASSSQEAGSSQ HHHCCCCCHHHCCCH	29.55	29255136
141	Phosphorylation	SSSQEAGSSQAAKED CCCHHHCCCHHHHCC	26.73	29255136
142	Phosphorylation	SSQEAGSSQAAKEDE CCHHHCCCHHHHCCC	23.95	29255136
150	Phosphorylation	QAAKEDETSDGQASG HHHHCCCCCCCCCCC	44.43	23090842
151	Phosphorylation	AAKEDETSDGQASGE HHHCCCCCCCCCCCC	37.38	23090842
156	Phosphorylation	ETSDGQASGEQEEAG CCCCCCCCCCCCCCC	34.67	23090842
207	Ubiquitination	LDWRVQSKDWPHAGR CCCCEECCCCCCCCC	46.88	21906983
221	Phosphorylation	RPAHELRYSIYRDLW CCHHHHHHHHHHHHH	16.43	29496907
222	Phosphorylation	PAHELRYSIYRDLWE CHHHHHHHHHHHHHH	13.50	29496907
224	Phosphorylation	HELRYSIYRDLWERG HHHHHHHHHHHHHHC	7.67	29496907
286	Ubiquitination	RLGTSVRKTLLLCSP CCCCCCEEEEEEECC	41.17	-

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

Oops, there are no upstream regulatory protein records of SEN34_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEN34_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 SEN34_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEN2_HUMAN	TSEN2	physical	15109492
SEN54_HUMAN	TSEN54	physical	15109492
ARMX3_HUMAN	ARMCX3	physical	22863883
RBGPR_HUMAN	RAB3GAP2	physical	22863883

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612390: Pontocerebellar hypoplasia 2C (PCH2C)
• 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

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-135 ANDSER-136, AND MASS SPECTROMETRY.
PubMed: 19413330