DBR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DBR1_HUMAN
• UniProt AC: Q9UK59
• Protein Name: Lariat debranching enzyme
• Gene Name: DBR1
• Organism: Homo sapiens (Human).
• Sequence Length: 544
• Subcellular Localization: Nucleus .
• Protein Description: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis..
• Protein Sequence: MRVAVAGCCHGELDKIYETLALAERRGPGPVDLLLCCGDFQAVRNEADLRCMAVPPKYRHMQTFYRYYSGEKKAPVLTLFIGGNHEASNHLQELPYGGWVAPNIYYLGLAGVVKYRGVRIGGISGIFKSHDYRKGHFECPPYNSSTIRSIYHVRNIEVYKLKQLKQPIDIFLSHDWPRSIYHYGNKKQLLKTKSFFRQEVENNTLGSPAASELLEHLKPTYWFSAHLHVKFAALMQHQAKDKGQTARATKFLALDKCLPHRDFLQILEIEHDPSAPDYLEYDIEWLTILRATDDLINVTGRLWNMPENNGLHARWDYSATEEGMKEVLEKLNHDLKVPCNFSVTAACYDPSKPQTQMQLIHRINPQTTEFCAQLGIIDINVRLQKSKEEHHVCGEYEEQDDVESNDSGEDQSEYNTDTSALSSINPDEIMLDEEEDEDSIVSAHSGMNTPSVEPSDQASEFSASFSDVRILPGSMIVSSDDTVDSTIDREGKPGGTVESGNGEDLTKVPLKRLSDEHEPEQRKKIKRRNQAIYAAVDDDDDDAA

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
58	Phosphorylation	CMAVPPKYRHMQTFY CEECCCHHCCHHHHH	16.12	29759185
63	Phosphorylation	PKYRHMQTFYRYYSG CHHCCHHHHHHHHCC	18.30	29759185
68	Phosphorylation	MQTFYRYYSGEKKAP HHHHHHHHCCCCCCC	10.95	29759185
69	Phosphorylation	QTFYRYYSGEKKAPV HHHHHHHCCCCCCCE	31.38	-
128	Acetylation	GGISGIFKSHDYRKG CCEEEECCCCCCCCC	44.98	19608861
128	Malonylation	GGISGIFKSHDYRKG CCEEEECCCCCCCCC	44.98	26320211
183	Phosphorylation	WPRSIYHYGNKKQLL CCCCCEECCCHHHHH	12.86	24275569
186	Ubiquitination	SIYHYGNKKQLLKTK CCEECCCHHHHHHCH	37.22	29967540
194	Phosphorylation	KQLLKTKSFFRQEVE HHHHHCHHHHHHHHH	34.54	24719451
240	Ubiquitination	ALMQHQAKDKGQTAR HHHHHHHHCCCCHHH	54.10	29967540
245	O-linked_Glycosylation	QAKDKGQTARATKFL HHHCCCCHHHHHHHH	27.12	30379171
250	Acetylation	GQTARATKFLALDKC CCHHHHHHHHHHHHH	37.08	25953088
250	Ubiquitination	GQTARATKFLALDKC CCHHHHHHHHHHHHH	37.08	-
256	Ubiquitination	TKFLALDKCLPHRDF HHHHHHHHHCCCCCH	38.22	-
256	Acetylation	TKFLALDKCLPHRDF HHHHHHHHHCCCCCH	38.22	26051181
260 (in isoform 2)	Ubiquitination	-	29.06	21906983
330	Ubiquitination	GMKEVLEKLNHDLKV HHHHHHHHHCCCCCC	50.89	29967540
336	Acetylation	EKLNHDLKVPCNFSV HHHCCCCCCCCCEEE	50.63	25953088
352	Acetylation	AACYDPSKPQTQMQL EECCCCCCCCHHHHH	46.67	26051181
396	Phosphorylation	EHHVCGEYEEQDDVE HCCCCCCCCCCCCCC	15.28	-
445	Phosphorylation	DSIVSAHSGMNTPSV CCCCCCCCCCCCCCC	39.18	26074081
449	Phosphorylation	SAHSGMNTPSVEPSD CCCCCCCCCCCCCCC	14.19	26074081
451	Phosphorylation	HSGMNTPSVEPSDQA CCCCCCCCCCCCCHH	36.75	26074081
464	Phosphorylation	QASEFSASFSDVRIL HHHHHCCCCCCCEEC	24.88	24275569
474	Phosphorylation	DVRILPGSMIVSSDD CCEECCCCEEECCCC	11.91	28176443
478	Phosphorylation	LPGSMIVSSDDTVDS CCCCEEECCCCCCCC	19.68	25159151
479	Phosphorylation	PGSMIVSSDDTVDST CCCEEECCCCCCCCC	28.72	29255136
482	Phosphorylation	MIVSSDDTVDSTIDR EEECCCCCCCCCCCC	31.07	23663014
485	Phosphorylation	SSDDTVDSTIDREGK CCCCCCCCCCCCCCC	23.95	29255136
486	Phosphorylation	SDDTVDSTIDREGKP CCCCCCCCCCCCCCC	23.57	29255136
492 (in isoform 1)	Ubiquitination	-	35.42	21906983
492	Ubiquitination	STIDREGKPGGTVES CCCCCCCCCCCEEEC	35.42	22817900
499	Phosphorylation	KPGGTVESGNGEDLT CCCCEEECCCCCCCC	32.97	25159151
506	Phosphorylation	SGNGEDLTKVPLKRL CCCCCCCCCCCHHHC	42.17	26074081
507	Ubiquitination	GNGEDLTKVPLKRLS CCCCCCCCCCHHHCC	49.50	24816145
514	Phosphorylation	KVPLKRLSDEHEPEQ CCCHHHCCCCCCHHH	45.01	29255136
533	Phosphorylation	KRRNQAIYAAVDDDD HHHHHHHHEEECCCC	7.48	28796482

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

Oops, there are no upstream regulatory protein records of DBR1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DBR1_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 DBR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRP16_HUMAN	DHX38	physical	26344197
SK2L2_HUMAN	SKIV2L2	physical	26344197
MPLKI_HUMAN	MPLKIP	physical	28514442
C19L1_HUMAN	CWF19L1	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

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-128, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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 SER-474, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-474; SER-478; SER-479AND SER-514, AND MASS SPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASSSPECTROMETRY.
PubMed: 17081983