dbPTM

TFAM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFAM_HUMAN
UniProt AC	Q00059
Protein Name	Transcription factor A, mitochondrial
Gene Name	TFAM
Organism	Homo sapiens (Human).
Sequence Length	246
Subcellular Localization	Mitochondrion . Mitochondrion matrix, mitochondrion nucleoid .
Protein Description	Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. [PubMed: 29445193 Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA.]
Protein Sequence	MAFLRSMWGVLSALGRSGAELCTGCGSRLRSPFSFVYLPRWFSSVLASCPKKPVSSYLRFSKEQLPIFKAQNPDAKTTELIRRIAQRWRELPDSKKKIYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKKELTLLGKPKRPRSAYNVYVAERFQEAKGDSPQEKLKTVKENWKNLSDSEKELYIQHAKEDETRYHNEMKSWEEQMIEVGRKDLLRRTIKKQRKYGAEEC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAFLRSMWGVLSA --CHHHHHHHHHHHH	22.49	24043423
12	Phosphorylation	RSMWGVLSALGRSGA HHHHHHHHHHHCCHH	21.02	24043423
17	Phosphorylation	VLSALGRSGAELCTG HHHHHHCCHHHHCCC	40.32	24043423
23	Phosphorylation	RSGAELCTGCGSRLR CCHHHHCCCCCCCCC	48.40	24043423
27	Phosphorylation	ELCTGCGSRLRSPFS HHCCCCCCCCCCCCE	32.02	24043423
31	Phosphorylation	GCGSRLRSPFSFVYL CCCCCCCCCCEEEEC	34.58	30622161
34	Phosphorylation	SRLRSPFSFVYLPRW CCCCCCCEEEECHHH	19.72	30622161
43	Phosphorylation	VYLPRWFSSVLASCP EECHHHHHHHHHHCC	16.75	30622161
44	Phosphorylation	YLPRWFSSVLASCPK ECHHHHHHHHHHCCC	16.21	30622161
52	Ubiquitination	VLASCPKKPVSSYLR HHHHCCCCCHHHHCC	35.48	21890473
55	Phosphorylation	SCPKKPVSSYLRFSK HCCCCCHHHHCCCCH	23.07	28152594
56	Phosphorylation	CPKKPVSSYLRFSKE CCCCCHHHHCCCCHH	28.55	28152594
57	Phosphorylation	PKKPVSSYLRFSKEQ CCCCHHHHCCCCHHH	8.39	28152594
61	Phosphorylation	VSSYLRFSKEQLPIF HHHHCCCCHHHCCCH	28.93	23201127
62	Ubiquitination	SSYLRFSKEQLPIFK HHHCCCCHHHCCCHH	46.93	20972266
62	Acetylation	SSYLRFSKEQLPIFK HHHCCCCHHHCCCHH	46.93	26051181
62	Ubiquitination	SSYLRFSKEQLPIFK HHHCCCCHHHCCCHH	46.93	21890473
62	Ubiquitination	SSYLRFSKEQLPIFK HHHCCCCHHHCCCHH	46.93	21890473
69	Methylation	KEQLPIFKAQNPDAK HHHCCCHHCCCCCHH	50.19	115980001
69	Acetylation	KEQLPIFKAQNPDAK HHHCCCHHCCCCCHH	50.19	26051181
76	Acetylation	KAQNPDAKTTELIRR HCCCCCHHHHHHHHH	64.46	26051181
76	Ubiquitination	KAQNPDAKTTELIRR HCCCCCHHHHHHHHH	64.46	20972266
76	2-Hydroxyisobutyrylation	KAQNPDAKTTELIRR HCCCCCHHHHHHHHH	64.46	-
77	Phosphorylation	AQNPDAKTTELIRRI CCCCCHHHHHHHHHH	27.50	28509920
78	Phosphorylation	QNPDAKTTELIRRIA CCCCHHHHHHHHHHH	28.25	28509920
82	Methylation	AKTTELIRRIAQRWR HHHHHHHHHHHHHHH	36.26	115918377
95	Succinylation	WRELPDSKKKIYQDA HHCCCHHHCHHHHHH	66.52	23954790
99	Phosphorylation	PDSKKKIYQDAYRAE CHHHCHHHHHHHHHH	14.82	25884760
111	Ubiquitination	RAEWQVYKEEISRFK HHHHHHHHHHHHHHH	50.44	-
111	Acetylation	RAEWQVYKEEISRFK HHHHHHHHHHHHHHH	50.44	25825284
118	Ubiquitination	KEEISRFKEQLTPSQ HHHHHHHHHHCCHHH	43.36	21890473
118	Ubiquitination	KEEISRFKEQLTPSQ HHHHHHHHHHCCHHH	43.36	21890473
118	Ubiquitination	KEEISRFKEQLTPSQ HHHHHHHHHHCCHHH	43.36	21890473
122	Phosphorylation	SRFKEQLTPSQIMSL HHHHHHCCHHHHHHH	22.16	30266825
124	Phosphorylation	FKEQLTPSQIMSLEK HHHHCCHHHHHHHHH	27.40	30266825
127	Sulfoxidation	QLTPSQIMSLEKEIM HCCHHHHHHHHHHHH	2.65	21406390
128	Phosphorylation	LTPSQIMSLEKEIMD CCHHHHHHHHHHHHH	34.70	30266825
136	2-Hydroxyisobutyrylation	LEKEIMDKHLKRKAM HHHHHHHHHHHHHHH	33.19	-
146	Methylation	KRKAMTKKKELTLLG HHHHHCCCHHHHHCC	42.17	-
146	Trimethylation	KRKAMTKKKELTLLG HHHHHCCCHHHHHCC	42.17	-
147	Methylation	RKAMTKKKELTLLGK HHHHCCCHHHHHCCC	60.56	-
147	Trimethylation	RKAMTKKKELTLLGK HHHHCCCHHHHHCCC	60.56	-
160	Phosphorylation	GKPKRPRSAYNVYVA CCCCCCCCHHCHHHH	37.48	28152594
161 (in isoform 2)	Phosphorylation	-	10.95	29116813
162	Phosphorylation	PKRPRSAYNVYVAER CCCCCCHHCHHHHHH	13.35	28152594
165	Phosphorylation	PRSAYNVYVAERFQE CCCHHCHHHHHHHHH	7.12	28152594
174	Acetylation	AERFQEAKGDSPQEK HHHHHHHCCCCHHHH	63.60	26051181
177	Phosphorylation	FQEAKGDSPQEKLKT HHHHCCCCHHHHHHH	36.83	29978859
186	Ubiquitination	QEKLKTVKENWKNLS HHHHHHHHHHHHCCC	51.03	-
190	Ubiquitination	KTVKENWKNLSDSEK HHHHHHHHCCCHHHH	60.64	-
190	Succinylation	KTVKENWKNLSDSEK HHHHHHHHCCCHHHH	60.64	23954790
193	Phosphorylation	KENWKNLSDSEKELY HHHHHCCCHHHHHHH	48.78	23927012
195	Phosphorylation	NWKNLSDSEKELYIQ HHHCCCHHHHHHHHH	47.38	23401153
197	2-Hydroxyisobutyrylation	KNLSDSEKELYIQHA HCCCHHHHHHHHHHC	57.90	-
197	Ubiquitination	KNLSDSEKELYIQHA HCCCHHHHHHHHHHC	57.90	-
197	Acetylation	KNLSDSEKELYIQHA HCCCHHHHHHHHHHC	57.90	26051181
200	Phosphorylation	SDSEKELYIQHAKED CHHHHHHHHHHCHHC	10.30	28464451
205	2-Hydroxyisobutyrylation	ELYIQHAKEDETRYH HHHHHHCHHCCHHHH	64.67	-
205	Acetylation	ELYIQHAKEDETRYH HHHHHHCHHCCHHHH	64.67	26051181
205	Succinylation	ELYIQHAKEDETRYH HHHHHHCHHCCHHHH	64.67	23954790
216	Acetylation	TRYHNEMKSWEEQMI HHHHHHHHHHHHHHH	46.36	26051181

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
55	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
55	S	Phosphorylation	Kinase	PKA	-	Uniprot
56	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
56	S	Phosphorylation	Kinase	PKA	-	Uniprot
61	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
61	S	Phosphorylation	Kinase	PKA	-	Uniprot
160	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
160	S	Phosphorylation	Kinase	PKA	-	Uniprot
177	S	Phosphorylation	Kinase	ERK2	P28482	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:23045728

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFB1M_HUMAN	TFB1M	physical	12897151
TFB2M_HUMAN	TFB2M	physical	12897151
AR6P1_HUMAN	ARL6IP1	physical	25416956
ATRAP_HUMAN	AGTRAP	physical	25416956

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 TFAM_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-193, AND MASSSPECTROMETRY.	18669648 [Abstract]