dbPTM

MTFR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MTFR1_HUMAN
UniProt AC	Q15390
Protein Name	Mitochondrial fission regulator 1
Gene Name	MTFR1
Organism	Homo sapiens (Human).
Sequence Length	333
Subcellular Localization	Mitochondrion. May be associated with the inner and the outer mitochondrial membrane..
Protein Description	May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission (By similarity)..
Protein Sequence	MLGWIKRLIRMVFQQVGVSMQSVLWSRKPYGSSRSIVRKIGTNLSLIQCPRVQFQINSHATEWSPSHPGEDAVASFADVGWVAKEEGECSARLRTEVRSRPPLQDDLLFFEKAPSRQISLPDLSQEEPQLKTPALANEEALQKICALENELAALRAQIAKIVTQQEQQNLTAGDLDSTTFGTIPPHPPPPPPPLPPPALGLHQSTSAVDLIKERREKRANAGKTLVKNNPKKPEMPNMLEILKEMNSVKLRSVKRSEQDVKPKPVDATDPAALIAEALKKKFAYRYRSDSQDEVEKGIPKSESEATSERVLFGPHMLKPTGKMKALIENVSDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	VFQQVGVSMQSVLWS HHHHHCCCHHHHHHH	12.74	-
22	Phosphorylation	QVGVSMQSVLWSRKP HHCCCHHHHHHHCCC	15.55	26503892
30	Phosphorylation	VLWSRKPYGSSRSIV HHHHCCCCCCCHHHH	32.45	22817900
32	Phosphorylation	WSRKPYGSSRSIVRK HHCCCCCCCHHHHHH	19.41	17924679
33	Phosphorylation	SRKPYGSSRSIVRKI HCCCCCCCHHHHHHH	26.19	17924679
42	Phosphorylation	SIVRKIGTNLSLIQC HHHHHHCCCCEEEEC	36.14	23312004
45	Phosphorylation	RKIGTNLSLIQCPRV HHHCCCCEEEECCCE	26.04	23312004
99	Phosphorylation	RLRTEVRSRPPLQDD EECCHHHHCCCCCCC	55.07	23312004
112	Ubiquitination	DDLLFFEKAPSRQIS CCEEEEECCCCCCCC	61.51	-
115	Phosphorylation	LFFEKAPSRQISLPD EEEECCCCCCCCCCC	41.50	25159151
119	Phosphorylation	KAPSRQISLPDLSQE CCCCCCCCCCCCCCC	26.05	29255136
124	Phosphorylation	QISLPDLSQEEPQLK CCCCCCCCCCCCCCC	42.81	30266825
132	Phosphorylation	QEEPQLKTPALANEE CCCCCCCCHHHCCHH	23.53	26074081
143	Ubiquitination	ANEEALQKICALENE CCHHHHHHHHHHHHH	40.37	-
204	Phosphorylation	PALGLHQSTSAVDLI CCCCCCCCCCHHHHH	17.37	26074081
205	Phosphorylation	ALGLHQSTSAVDLIK CCCCCCCCCHHHHHH	17.71	26074081
206	Phosphorylation	LGLHQSTSAVDLIKE CCCCCCCCHHHHHHH	31.38	26074081
217	Acetylation	LIKERREKRANAGKT HHHHHHHHHHHCCCC	55.81	7374225
223	Acetylation	EKRANAGKTLVKNNP HHHHHCCCCHHHCCC	35.95	7910681
227	Acetylation	NAGKTLVKNNPKKPE HCCCCHHHCCCCCCC	54.87	19819067
286	Phosphorylation	KKKFAYRYRSDSQDE HHHHCHHCCCCCHHH	11.20	26657352
288	Phosphorylation	KFAYRYRSDSQDEVE HHCHHCCCCCHHHHH	32.45	30278072
290	Phosphorylation	AYRYRSDSQDEVEKG CHHCCCCCHHHHHHC	40.55	23401153
301	O-linked_Glycosylation	VEKGIPKSESEATSE HHHCCCCCHHHHCCC	40.79	30620550
331	Phosphorylation	KALIENVSDS----- HHHHHCCCCC-----	43.66	28985074

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 MTFR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MTFR1_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 MTFR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MTFR1_HUMAN !!

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 MTFR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-119, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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 TYR-30; SER-32 AND SER-33,AND MASS SPECTROMETRY.	17924679 [Abstract]