SUV3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUV3_HUMAN
• UniProt AC: Q8IYB8
• Protein Name: ATP-dependent RNA helicase SUPV3L1, mitochondrial
• Gene Name: SUPV3L1
• Organism: Homo sapiens (Human).
• Sequence Length: 786
• Subcellular Localization: Nucleus . Mitochondrion matrix . Mitochondrion matrix, mitochondrion nucleoid .
• Protein Description: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA..
• Protein Sequence: MSFSRALLWARLPAGRQAGHRAAICSALRPHFGPFPGVLGQVSVLATASSSASGGSKIPNTSLFVPLTVKPQGPSADGDVGAELTRPLDKNEVKKVLDKFYKRKEIQKLGADYGLDARLFHQAFISFRNYIMQSHSLDVDIHIVLNDICFGAAHADDLFPFFLRHAKQIFPVLDCKDDLRKISDLRIPPNWYPDARAMQRKIIFHSGPTNSGKTYHAIQKYFSAKSGVYCGPLKLLAHEIFEKSNAAGVPCDLVTGEERVTVQPNGKQASHVSCTVEMCSVTTPYEVAVIDEIQMIRDPARGWAWTRALLGLCAEEVHLCGEPAAIDLVMELMYTTGEEVEVRDYKRLTPISVLDHALESLDNLRPGDCIVCFSKNDIYSVSRQIEIRGLESAVIYGSLPPGTKLAQAKKFNDPNDPCKILVATDAIGMGLNLSIRRIIFYSLIKPSINEKGERELEPITTSQALQIAGRAGRFSSRFKEGEVTTMNHEDLSLLKEILKRPVDPIRAAGLHPTAEQIEMFAYHLPDATLSNLIDIFVDFSQVDGQYFVCNMDDFKFSAELIQHIPLSLRVRYVFCTAPINKKQPFVCSSLLQFARQYSRNEPLTFAWLRRYIKWPLLPPKNIKDLMDLEAVHDVLDLYLWLSYRFMDMFPDASLIRDLQKELDGIIQDGVHNITKLIKMSETHKLLNLEGFPSGSQSRLSGTLKSQARRTRGTKALGSKATEPPSPDAGELSLASRLVQQGLLTPDMLKQLEKEWMTQQTEHNKEKTESGTHPKGTRRKKKEPDSD

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
2	Phosphorylation	------MSFSRALLW ------CCHHHHHHH	31.74	29507054
4	Phosphorylation	----MSFSRALLWAR ----CCHHHHHHHHH	14.88	29507054
99	Malonylation	EVKKVLDKFYKRKEI HHHHHHHHHHHHHHH	46.57	26320211
99	Acetylation	EVKKVLDKFYKRKEI HHHHHHHHHHHHHHH	46.57	19608861
108	2-Hydroxyisobutyrylation	YKRKEIQKLGADYGL HHHHHHHHHCCCCCC	55.33	-
183	Phosphorylation	KDDLRKISDLRIPPN CHHHHHHHCCCCCCC	33.36	24719451
201	Ubiquitination	DARAMQRKIIFHSGP CHHHHHCEEEEECCC	24.22	-
213	Ubiquitination	SGPTNSGKTYHAIQK CCCCCCCHHHHHHHH	45.81	-
220	Acetylation	KTYHAIQKYFSAKSG HHHHHHHHHHHCCCC	41.99	19608861
379	Phosphorylation	CFSKNDIYSVSRQIE ECCCCCEEEEEHHEE	13.09	-
396	Phosphorylation	GLESAVIYGSLPPGT CCCEEEEEECCCCCC	8.28	25884760
398	Phosphorylation	ESAVIYGSLPPGTKL CEEEEEECCCCCCCH	22.26	-
403	Phosphorylation	YGSLPPGTKLAQAKK EECCCCCCCHHHHHH	28.76	-
410	Acetylation	TKLAQAKKFNDPNDP CCHHHHHHCCCCCCC	53.03	27452117
441	Phosphorylation	SIRRIIFYSLIKPSI HHHHHHHHHHHCCCC	7.67	23909892
442	Phosphorylation	IRRIIFYSLIKPSIN HHHHHHHHHHCCCCC	16.93	24719451
479	Succinylation	GRFSSRFKEGEVTTM CCCHHHCCCCCCEEC	64.79	27452117
492	Phosphorylation	TMNHEDLSLLKEILK ECCHHHHHHHHHHHC	43.93	24719451
604	Phosphorylation	YSRNEPLTFAWLRRY HCCCCCCHHHHHHHH	23.25	24719451
611	Phosphorylation	TFAWLRRYIKWPLLP HHHHHHHHCCCCCCC	10.62	24719451
674	Phosphorylation	QDGVHNITKLIKMSE HHHHHHHHHHHHHHH	25.72	20068231
693	Phosphorylation	LNLEGFPSGSQSRLS CCCCCCCCCCHHHCC	49.14	23186163
695	Phosphorylation	LEGFPSGSQSRLSGT CCCCCCCCHHHCCHH	29.35	23186163
697	Phosphorylation	GFPSGSQSRLSGTLK CCCCCCHHHCCHHHH	36.56	26471730
704	Ubiquitination	SRLSGTLKSQARRTR HHCCHHHHHHHHHHH	40.12	-
719	Ubiquitination	GTKALGSKATEPPSP CCHHHCCCCCCCCCC	58.49	-
721	Phosphorylation	KALGSKATEPPSPDA HHHCCCCCCCCCCCH	53.41	29255136
725	Phosphorylation	SKATEPPSPDAGELS CCCCCCCCCCHHHHH	46.24	30266825
732	Phosphorylation	SPDAGELSLASRLVQ CCCHHHHHHHHHHHH	20.00	23403867
735	Phosphorylation	AGELSLASRLVQQGL HHHHHHHHHHHHCCC	31.29	23403867
744	Phosphorylation	LVQQGLLTPDMLKQL HHHCCCCCHHHHHHH	23.45	-
749	Ubiquitination	LLTPDMLKQLEKEWM CCCHHHHHHHHHHHH	46.31	-

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

Oops, there are no upstream regulatory protein records of SUV3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUV3_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 SUV3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LZTS2_HUMAN	LZTS2	physical	25416956
PNPT1_HUMAN	PNPT1	physical	28514442
HNRDL_HUMAN	HNRNPDL	physical	28514442
RBM3_HUMAN	RBM3	physical	28514442
USP9X_HUMAN	USP9X	physical	28514442
HNRPF_HUMAN	HNRNPF	physical	28514442
ZN703_HUMAN	ZNF703	physical	28514442
ROA1_HUMAN	HNRNPA1	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-99 AND LYS-220, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-725, AND MASSSPECTROMETRY.
PubMed: 18669648