OXSM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OXSM_HUMAN
• UniProt AC: Q9NWU1
• Protein Name: 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
• Gene Name: OXSM
• Organism: Homo sapiens (Human).
• Sequence Length: 459
• Subcellular Localization: Mitochondrion .
• Protein Description: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function..
• Protein Sequence: MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL

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
12	Phosphorylation	LQNFLKITSTRLLCS HHHHHHHHHHHHHHH	23.58	20068231
13	Phosphorylation	QNFLKITSTRLLCSR HHHHHHHHHHHHHHH	18.27	20068231
14	Phosphorylation	NFLKITSTRLLCSRL HHHHHHHHHHHHHHH	19.38	20068231
19	Phosphorylation	TSTRLLCSRLCQQLR HHHHHHHHHHHHHHH	28.40	20068231
34	Phosphorylation	SKRKFFGTVPISRLH HCCCCCCCCCHHHHC	20.25	20068231
38	Phosphorylation	FFGTVPISRLHRRVV CCCCCCHHHHCCCEE	23.79	20068231
71	Phosphorylation	DRLIGGESGIVSLVG HHHHCCCCCEEEECC	36.77	20068231
75	Phosphorylation	GGESGIVSLVGEEYK CCCCCEEEECCCEEC	18.54	20068231
81	Phosphorylation	VSLVGEEYKSIPCSV EEECCCEECCCCEEE	13.01	20068231
82	Acetylation	SLVGEEYKSIPCSVA EECCCEECCCCEEEE	45.23	25038526
109	Ubiquitination	NEQNFVSKSDIKSMS CCCCCCCHHHHCCCC	47.01	-
109	Succinylation	NEQNFVSKSDIKSMS CCCCCCCHHHHCCCC	47.01	-
109	Malonylation	NEQNFVSKSDIKSMS CCCCCCCHHHHCCCC	47.01	26320211
109	Acetylation	NEQNFVSKSDIKSMS CCCCCCCHHHHCCCC	47.01	23236377
109	Succinylation	NEQNFVSKSDIKSMS CCCCCCCHHHHCCCC	47.01	-
113	Succinylation	FVSKSDIKSMSSPTI CCCHHHHCCCCCCCH	45.13	-
113	Succinylation	FVSKSDIKSMSSPTI CCCHHHHCCCCCCCH	45.13	-
131	Acetylation	GAAELAMKDSGWHPQ HHHHHHHHCCCCCCC	43.04	30591089
174	Succinylation	FQTKGYNKVSPFFVP CCCCCCCCCCCCHHH	35.29	-
174	Acetylation	FQTKGYNKVSPFFVP CCCCCCCCCCCCHHH	35.29	19608861
174	Malonylation	FQTKGYNKVSPFFVP CCCCCCCCCCCCHHH	35.29	26320211
174	Succinylation	FQTKGYNKVSPFFVP CCCCCCCCCCCCHHH	35.29	23954790
182	Acetylation	VSPFFVPKILVNMAA CCCCHHHHHHHCCCC	43.29	25038526
199	Acetylation	VSIRYKLKGPNHAVS EEEEEEECCCCCCEE	69.07	26051181
255	Phosphorylation	FSRARALSTNSDPKL HHHHCHHCCCCCCCC	25.26	-
256	Phosphorylation	SRARALSTNSDPKLA HHHCHHCCCCCCCCC	39.32	-
258	Phosphorylation	ARALSTNSDPKLACR HCHHCCCCCCCCCCC	56.21	-
261	Acetylation	LSTNSDPKLACRPFH HCCCCCCCCCCCCCC	54.42	26051181
270	Acetylation	ACRPFHPKRDGFVMG CCCCCCCCCCEEEEE	55.33	30591083
333	Acetylation	RCMAAALKDAGVQPE HHHHHHHHHCCCCHH	40.58	26051181
361	Acetylation	LGDAAENKAIKHLFK CHHHHHHHHHHHHHC	42.89	23954790
368	Acetylation	KAIKHLFKDHAYALA HHHHHHHCCCCEEEE	55.77	25038526
377	Phosphorylation	HAYALAVSSTKGATG CCEEEEECCCCCHHH	27.04	30631047
428	Acetylation	DLNYVPLKAQEWKTE CCCCCCCCHHHCCCC	41.79	25038526

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of OXSM_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 OXSM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DHRS4_HUMAN	DHRS4	physical	26344197

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-174, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASSSPECTROMETRY.
PubMed: 17924679