dbPTM

PTCD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTCD3_HUMAN
UniProt AC	Q96EY7
Protein Name	Pentatricopeptide repeat domain-containing protein 3, mitochondrial
Gene Name	PTCD3
Organism	Homo sapiens (Human).
Sequence Length	689
Subcellular Localization	Mitochondrion .
Protein Description	Mitochondrial RNA-binding protein that has a role in mitochondrial translation..
Protein Sequence	MAVVSAVRWLGLRSRLGQPLTGRRAGLCEQARSCRFYSGSATLSKVEGTDVTGIEEVVIPKKKTWDKVAVLQALASTVNRDTTAVPYVFQDDPYLMPASSLESRSFLLAKKSGENVAKFIINSYPKYFQKDIAEPHIPCLMPEYFEPQIKDISEAALKERIELRKVKASVDMFDQLLQAGTTVSLETTNSLLDLLCYYGDQEPSTDYHFQQTGQSEALEEENDETSRRKAGHQFGVTWRAKNNAERIFSLMPEKNEHSYCTMIRGMVKHRAYEQALNLYTELLNNRLHADVYTFNALIEATVCAINEKFEEKWSKILELLRHMVAQKVKPNLQTFNTILKCLRRFHVFARSPALQVLREMKAIGIEPSLATYHHIIRLFDQPGDPLKRSSFIIYDIMNELMGKRFSPKDPDDDKFFQSAMSICSSLRDLELAYQVHGLLKTGDNWKFIGPDQHRNFYYSKFFDLICLMEQIDVTLKWYEDLIPSAYFPHSQTMIHLLQALDVANRLEVIPKIWKDSKEYGHTFRSDLREEILMLMARDKHPPELQVAFADCAADIKSAYESQPIRQTAQDWPATSLNCIAILFLRAGRTQEAWKMLGLFRKHNKIPRSELLNELMDSAKVSNSPSQAIEVVELASAFSLPICEGLTQRVMSDFAINQEQKEALSNLTALTSDSDTDSSSDSDSDTSEGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAVVSAVRWLGL ---CCHHHHHHHHHH	17.91	-
14	Phosphorylation	VRWLGLRSRLGQPLT HHHHHHHHHCCCCCC	36.58	24043423
37	Phosphorylation	QARSCRFYSGSATLS HHHCCCEEECCEEEE	7.86	21406692
38	Phosphorylation	ARSCRFYSGSATLSK HHCCCEEECCEEEEE	24.45	21406692
40	Phosphorylation	SCRFYSGSATLSKVE CCCEEECCEEEEEEE	16.49	21406692
42	Phosphorylation	RFYSGSATLSKVEGT CEEECCEEEEEEECC	33.01	21406692
44	Phosphorylation	YSGSATLSKVEGTDV EECCEEEEEEECCCC	30.24	21406692
45	Ubiquitination	SGSATLSKVEGTDVT ECCEEEEEEECCCCC	47.63	23503661
61	Ubiquitination	IEEVVIPKKKTWDKV CEEEEECCCCCHHHH	56.64	23503661
62	Ubiquitination	EEVVIPKKKTWDKVA EEEEECCCCCHHHHH	50.51	22817900
63	Ubiquitination	EVVIPKKKTWDKVAV EEEECCCCCHHHHHH	62.06	22817900
67 (in isoform 1)	Ubiquitination	-	24.53	21890473
67	Ubiquitination	PKKKTWDKVAVLQAL CCCCCHHHHHHHHHH	24.53	21890473
76	Phosphorylation	AVLQALASTVNRDTT HHHHHHHHHCCCCCC	33.47	22210691
77	Phosphorylation	VLQALASTVNRDTTA HHHHHHHHCCCCCCC	19.05	22210691
94	Phosphorylation	YVFQDDPYLMPASSL EEECCCCCCEECCHH	23.72	20068231
99	Phosphorylation	DPYLMPASSLESRSF CCCCEECCHHHHHHH	29.59	20068231
100	Phosphorylation	PYLMPASSLESRSFL CCCEECCHHHHHHHH	37.96	20068231
103	Phosphorylation	MPASSLESRSFLLAK EECCHHHHHHHHHHH	38.22	20068231
110	2-Hydroxyisobutyrylation	SRSFLLAKKSGENVA HHHHHHHHHCCCCHH	47.65	-
118	Acetylation	KSGENVAKFIINSYP HCCCCHHHHHHHCCH	32.58	26051181
123	Phosphorylation	VAKFIINSYPKYFQK HHHHHHHCCHHHHCC	32.19	24719451
124	Phosphorylation	AKFIINSYPKYFQKD HHHHHHCCHHHHCCC	10.15	29083192
126 (in isoform 1)	Ubiquitination	-	50.92	21890473
126	Malonylation	FIINSYPKYFQKDIA HHHHCCHHHHCCCCC	50.92	26320211
126	Acetylation	FIINSYPKYFQKDIA HHHHCCHHHHCCCCC	50.92	19608861
126	Ubiquitination	FIINSYPKYFQKDIA HHHHCCHHHHCCCCC	50.92	21890473
127	Phosphorylation	IINSYPKYFQKDIAE HHHCCHHHHCCCCCC	13.51	29083192
130	Ubiquitination	SYPKYFQKDIAEPHI CCHHHHCCCCCCCCC	41.00	22817900
139	Glutathionylation	IAEPHIPCLMPEYFE CCCCCCCCCCHHHCC	5.13	22555962
144	Phosphorylation	IPCLMPEYFEPQIKD CCCCCHHHCCHHHCC	13.84	26356563
158	Ubiquitination	DISEAALKERIELRK CCHHHHHHHHHHHHH	39.97	23503661
259	Phosphorylation	PEKNEHSYCTMIRGM CCCCCCCCHHHHHHH	8.21	28674151
261	Phosphorylation	KNEHSYCTMIRGMVK CCCCCCHHHHHHHHH	13.85	28674151
279	Phosphorylation	YEQALNLYTELLNNR HHHHHHHHHHHHHCC	9.33	-
280	Phosphorylation	EQALNLYTELLNNRL HHHHHHHHHHHHCCC	24.27	-
334	Phosphorylation	KVKPNLQTFNTILKC HCCCCHHHHHHHHHH	23.24	28842319
337	Phosphorylation	PNLQTFNTILKCLRR CCHHHHHHHHHHHHH	24.40	28842319
372	Phosphorylation	IEPSLATYHHIIRLF CCCCHHHHHHHHHHH	5.94	-
387	2-Hydroxyisobutyrylation	DQPGDPLKRSSFIIY CCCCCCCCCCHHHHH	56.47	-
387	Ubiquitination	DQPGDPLKRSSFIIY CCCCCCCCCCHHHHH	56.47	24816145
387	Acetylation	DQPGDPLKRSSFIIY CCCCCCCCCCHHHHH	56.47	25953088
406	Phosphorylation	ELMGKRFSPKDPDDD HHCCCCCCCCCCCCC	34.76	24719451
408	Succinylation	MGKRFSPKDPDDDKF CCCCCCCCCCCCCHH	79.35	23954790
433	Phosphorylation	LRDLELAYQVHGLLK HHHHHHHHHHCCHHH	24.56	-
551	Glutathionylation	LQVAFADCAADIKSA HHHHHHHHHHHHHHH	2.78	22555962
557	Phosphorylation	DCAADIKSAYESQPI HHHHHHHHHHHCCCH	36.10	28152594
559	Phosphorylation	AADIKSAYESQPIRQ HHHHHHHHHCCCHHH	24.17	28152594
561	Phosphorylation	DIKSAYESQPIRQTA HHHHHHHCCCHHHHC	28.69	28152594
604	Ubiquitination	GLFRKHNKIPRSELL HHHHHCCCCCHHHHH	54.53	24816145
650	Sulfoxidation	EGLTQRVMSDFAINQ CCHHHHHHHHHCCCH	3.29	21406390
651	Phosphorylation	GLTQRVMSDFAINQE CHHHHHHHHHCCCHH	27.07	29449344
664	Phosphorylation	QEQKEALSNLTALTS HHHHHHHHHHHHHCC	36.52	23186163
667	Phosphorylation	KEALSNLTALTSDSD HHHHHHHHHHCCCCC	24.70	30108239
670	Phosphorylation	LSNLTALTSDSDTDS HHHHHHHCCCCCCCC	28.20	25627689
671	Phosphorylation	SNLTALTSDSDTDSS HHHHHHCCCCCCCCC	35.65	26657352
673	Phosphorylation	LTALTSDSDTDSSSD HHHHCCCCCCCCCCC	42.02	25627689
675	Phosphorylation	ALTSDSDTDSSSDSD HHCCCCCCCCCCCCC	41.55	25262027
677	Phosphorylation	TSDSDTDSSSDSDSD CCCCCCCCCCCCCCC	33.56	30108239
678	Phosphorylation	SDSDTDSSSDSDSDT CCCCCCCCCCCCCCC	40.76	30108239
679	Phosphorylation	DSDTDSSSDSDSDTS CCCCCCCCCCCCCCC	45.12	30278072
681	Phosphorylation	DTDSSSDSDSDTSEG CCCCCCCCCCCCCCC	40.75	30278072
683	Phosphorylation	DSSSDSDSDTSEGK- CCCCCCCCCCCCCC-	46.90	30576142
685	Phosphorylation	SSDSDSDTSEGK--- CCCCCCCCCCCC---	32.41	30108239
686	Phosphorylation	SDSDSDTSEGK---- CCCCCCCCCCC----	49.71	30108239

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 PTCD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTCD3_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 PTCD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RT15_HUMAN	MRPS15	physical	19427859
RT29_HUMAN	DAP3	physical	26344197
RT18B_HUMAN	MRPS18B	physical	26344197
RT23_HUMAN	MRPS23	physical	26344197
RT28_HUMAN	MRPS28	physical	26344197
RT35_HUMAN	MRPS35	physical	26344197
RT09_HUMAN	MRPS9	physical	26344197
BIRC7_HUMAN	BIRC7	physical	21516116
TBD2B_HUMAN	TBC1D2B	physical	28514442
RBM38_HUMAN	RBM38	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.

Regulatory Network of PTCD3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-126, AND MASS SPECTROMETRY.	19608861 [Abstract]