SEN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEN2_HUMAN
• UniProt AC: Q8NCE0
• Protein Name: tRNA-splicing endonuclease subunit Sen2
• Gene Name: TSEN2
• Organism: Homo sapiens (Human).
• Sequence Length: 465
• 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. Isoform 1 probably carries the active site for 5'-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. Isoform 2 is responsible for processing a yet unknown RNA substrate. The complex containing isoform 2 is not able to cleave pre-tRNAs properly, although it retains endonucleolytic activity..
• Protein Sequence: MAEAVFHAPKRKRRVYETYESPLPIPFGQDHGPLKEFKIFRAEMINNNVIVRNAEDIEQLYGKGYFGKGILSRSRPSFTISDPKLVAKWKDMKTNMPIITSKRYQHSVEWAAELMRRQGQDESTVRRILKDYTKPLEHPPVKRNEEAQVHDKLNSGMVSNMEGTAGGERPSVVNGDSGKSGGVGDPREPLGCLQEGSGCHPTTESFEKSVREDASPLPHVCCCKQDALILQRGLHHEDGSQHIGLLHPGDRGPDHEYVLVEEAECAMSEREAAPNEELVQRNRLICRRNPYRIFEYLQLSLEEAFFLVYALGCLSIYYEKEPLTIVKLWKAFTVVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELVDDHFEGSLRRPLSWKSLAALSRVSVNVSKELMLCYLIKPSTMTDKEMESPECMKRIKVQEVILSRWVSSRERSDQDDL

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
16	Phosphorylation	PKRKRRVYETYESPL CHHHCCCEEEECCCC	10.76	-
21	Phosphorylation	RVYETYESPLPIPFG CCEEEECCCCCCCCC	22.71	25159151
35	Ubiquitination	GQDHGPLKEFKIFRA CCCCCCHHHHEEEEE	65.32	-
63	Ubiquitination	DIEQLYGKGYFGKGI HHHHHHCCCCCCCCH	36.56	-
65	Phosphorylation	EQLYGKGYFGKGILS HHHHCCCCCCCCHHH	16.79	-
68	Ubiquitination	YGKGYFGKGILSRSR HCCCCCCCCHHHCCC	32.64	-
81	Phosphorylation	SRPSFTISDPKLVAK CCCCEEECCHHHHHH	44.81	28674419
102	Acetylation	NMPIITSKRYQHSVE CCCEEECCCHHHHHH	46.61	18529901
124	Phosphorylation	RQGQDESTVRRILKD HCCCCHHHHHHHHHH	18.91	-
134	Ubiquitination	RILKDYTKPLEHPPV HHHHHCCCCCCCCCC	41.18	-
155	Phosphorylation	QVHDKLNSGMVSNME HHHHHHHCCCCCCCC	38.41	22210691
159	Phosphorylation	KLNSGMVSNMEGTAG HHHCCCCCCCCCCCC	22.90	22210691
164	Phosphorylation	MVSNMEGTAGGERPS CCCCCCCCCCCCCCC	14.60	28555341
171	Phosphorylation	TAGGERPSVVNGDSG CCCCCCCCEECCCCC	44.94	28555341
205	Phosphorylation	GCHPTTESFEKSVRE CCCCCHHHHHHHHHC	36.29	25159151
208	Ubiquitination	PTTESFEKSVREDAS CCHHHHHHHHHCCCC	52.84	-
209	Phosphorylation	TTESFEKSVREDASP CHHHHHHHHHCCCCC	21.14	26074081
215	Phosphorylation	KSVREDASPLPHVCC HHHHCCCCCCCCEEE	39.01	23401153
240	Phosphorylation	GLHHEDGSQHIGLLH CCCCCCCCCEEEEEC	30.79	17525332
343	Phosphorylation	QPTFRTTYMAYHYFR CCCCHHHHHHHHHHH	4.52	-
346	Phosphorylation	FRTTYMAYHYFRSKG CHHHHHHHHHHHCCC	4.78	-
348	Phosphorylation	TTYMAYHYFRSKGWV HHHHHHHHHHCCCCC	6.49	-
357	Ubiquitination	RSKGWVPKVGLKYGT HCCCCCCCCCEECCC	39.04	-
362	Phosphorylation	VPKVGLKYGTDLLLY CCCCCEECCCCEEEE	30.24	30631047
369	Phosphorylation	YGTDLLLYRKGPPFY CCCCEEEEECCCCCC	15.39	-
376	Phosphorylation	YRKGPPFYHASYSVI EECCCCCCCCEEEEE	11.40	-
400	Phosphorylation	GSLRRPLSWKSLAAL CCCCCCCCHHHHHHH	34.83	23312004
408	Phosphorylation	WKSLAALSRVSVNVS HHHHHHHHCCCCCCC	26.38	15345747
411	Phosphorylation	LAALSRVSVNVSKEL HHHHHCCCCCCCHHH	13.58	15345747
415	Phosphorylation	SRVSVNVSKELMLCY HCCCCCCCHHHHHHH	18.40	15345747

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

Oops, there are no upstream regulatory protein records of SEN2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEN2_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 SEN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEN34_HUMAN	TSEN34	physical	15109492
SEN54_HUMAN	TSEN54	physical	15109492
SEN15_HUMAN	TSEN15	physical	15109492
CLP1_HUMAN	CLP1	physical	15109492
DPOD1_HUMAN	POLD1	physical	22863883
DPOD3_HUMAN	POLD3	physical	22863883
PRP39_HUMAN	PRPF39	physical	22863883
TBD2A_HUMAN	TBC1D2	physical	22863883
TBCD4_HUMAN	TBC1D4	physical	22863883
CIP4_HUMAN	TRIP10	physical	22863883
UBP8_HUMAN	USP8	physical	22863883
SEN54_HUMAN	TSEN54	physical	25416956
GRB1L_HUMAN	GREB1L	physical	28514442
TMED8_HUMAN	TMED8	physical	28514442
SEN54_HUMAN	TSEN54	physical	28514442
CLP1_HUMAN	CLP1	physical	28514442
SEN34_HUMAN	TSEN34	physical	28514442
SFSWA_HUMAN	SFSWAP	physical	28514442
XPC_HUMAN	XPC	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612389: Pontocerebellar hypoplasia 2B (PCH2B)
• 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

"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-240, AND MASSSPECTROMETRY.
PubMed: 17525332