SEN54_HUMAN - dbPTM
SEN54_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEN54_HUMAN
UniProt AC Q7Z6J9
Protein Name tRNA-splicing endonuclease subunit Sen54
Gene Name TSEN54
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization Nucleus . Nucleus, nucleolus . May be transiently localized in the nucleolus.
Protein Description Non-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. 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 MEPEPEPAAVEVPAGRVLSARELFAARSRSQKLPQRSHGPKDFLPDGSAAQAERLRRCREELWQLLAEQRVERLGSLVAAEWRPEEGFVELKSPAGKFWQTMGFSEQGRQRLHPEEALYLLECGSIHLFHQDLPLSIQEAYQLLLTDHTVTFLQYQVFSHLKRLGYVVRRFQPSSVLSPYERQLNLDASVQHLEDGDGKRKRSSSSPRSINKKAKALDNSLQPKSLAASSPPPCSQPSQCPEEKPQESSPMKGPGGPFQLLGSLGPSPGPAREGVGCSWESGRAENGVTGAGKRRWNFEQISFPNMASDSRHTLLRAPAPELLPANVAGRETDAESWCQKLNQRKEKLSRREREHHAEAAQFQEDVNADPEVQRCSSWREYKELLQRRQVQRSQRRAPHLWGQPVTPLLSPGQASSPAVVLQHISVLQTTHLPDGGARLLEKSGGLEIIFDVYQADAVATFRKNNPGKPYARMCISGFDEPVPDLCSLKRLSYQSGDVPLIFALVDHGDISFYSFRDFTLPQDVGH
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 Orthologous
Protein Cluster
1Acetylation-------MEPEPEPA
-------CCCCCCCC		20.4822814378
76PhosphorylationQRVERLGSLVAAEWR
HHHHHHHHHHEEECC		25.0222617229
92UbiquitinationEEGFVELKSPAGKFW
CCCCEEEECCCCCHH		40.6722817900
97 (in isoform 2)Ubiquitination-45.6021906983
97UbiquitinationELKSPAGKFWQTMGF
EEECCCCCHHHHCCC		45.6022817900
97 (in isoform 1)Ubiquitination-45.6021906983
166PhosphorylationSHLKRLGYVVRRFQP
HHHHHHCCHHHHCCC		10.6028857561
174PhosphorylationVVRRFQPSSVLSPYE
HHHHCCCHHCCCHHH		23.4629396449
175PhosphorylationVRRFQPSSVLSPYER
HHHCCCHHCCCHHHH		33.4928450419
178PhosphorylationFQPSSVLSPYERQLN
CCCHHCCCHHHHHCC		24.2316964243
180PhosphorylationPSSVLSPYERQLNLD
CHHCCCHHHHHCCCC		21.9929396449
189PhosphorylationRQLNLDASVQHLEDG
HHCCCCHHHEECCCC		23.2129214152
199AcetylationHLEDGDGKRKRSSSS
ECCCCCCCCCCCCCC		60.5324468191
203PhosphorylationGDGKRKRSSSSPRSI
CCCCCCCCCCCCCHH		37.2922798277
204PhosphorylationDGKRKRSSSSPRSIN
CCCCCCCCCCCCHHH		38.5827690223
205PhosphorylationGKRKRSSSSPRSINK
CCCCCCCCCCCHHHH		45.6822798277
206PhosphorylationKRKRSSSSPRSINKK
CCCCCCCCCCHHHHH		26.7022798277
209PhosphorylationRSSSSPRSINKKAKA
CCCCCCCHHHHHHHH		33.6227690223
220PhosphorylationKAKALDNSLQPKSLA
HHHHHCCCCCCCHHH		28.2228555341
225PhosphorylationDNSLQPKSLAASSPP
CCCCCCCHHHCCCCC		29.8919413330
229PhosphorylationQPKSLAASSPPPCSQ
CCCHHHCCCCCCCCC		37.4623401153
230PhosphorylationPKSLAASSPPPCSQP
CCHHHCCCCCCCCCC		36.3817525332
235PhosphorylationASSPPPCSQPSQCPE
CCCCCCCCCCCCCCC		51.4023401153
238PhosphorylationPPPCSQPSQCPEEKP
CCCCCCCCCCCCCCC		36.4630576142
248PhosphorylationPEEKPQESSPMKGPG
CCCCCCCCCCCCCCC		34.2025159151
249PhosphorylationEEKPQESSPMKGPGG
CCCCCCCCCCCCCCC		28.4125159151
263PhosphorylationGPFQLLGSLGPSPGP
CCHHEECCCCCCCCC		30.0729396449
267PhosphorylationLLGSLGPSPGPAREG
EECCCCCCCCCCCCC		40.4625159151
293AcetylationNGVTGAGKRRWNFEQ
CCCCCCCCCCCCCCC		37.9525953088
316MethylationDSRHTLLRAPAPELL
CCCCCCCCCCCCCCC		41.4524129315
340UbiquitinationDAESWCQKLNQRKEK
CHHHHHHHHHHHHHH		46.3929967540
382UbiquitinationCSSWREYKELLQRRQ
CCHHHHHHHHHHHHH		36.81-
410PhosphorylationQPVTPLLSPGQASSP
CCCCCCCCCCCCCCC		34.3726074081
415PhosphorylationLLSPGQASSPAVVLQ
CCCCCCCCCCHHHHH		29.0326074081
443PhosphorylationGARLLEKSGGLEIIF
HHHHHHHCCCEEEEE		28.81-
489UbiquitinationVPDLCSLKRLSYQSG
CCCHHHCHHCEECCC		34.6922505724
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

Oops, there are no upstream regulatory protein records of SEN54_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEN54_HUMAN !!
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 SEN54_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEN2_HUMANTSEN2physical
15109492
SEN34_HUMANTSEN34physical
15109492
SEN15_HUMANTSEN15physical
15109492
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
225753Pontocerebellar hypoplasia 4 (PCH4)
277470Pontocerebellar hypoplasia 2A (PCH2A)
610204Pontocerebellar hypoplasia 5 (PCH5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEN54_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-225 AND SER-249, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-225 AND SER-249, AND MASS SPECTROMETRY.
"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-230 AND SER-235, ANDMASS SPECTROMETRY.

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