MFF_HUMAN - dbPTM
MFF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MFF_HUMAN
UniProt AC Q9GZY8
Protein Name Mitochondrial fission factor
Gene Name MFF
Organism Homo sapiens (Human).
Sequence Length 342
Subcellular Localization Mitochondrion outer membrane
Single-pass type IV membrane protein. Peroxisome. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle.
Protein Description Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles..
Protein Sequence MSKGTSSDTSLGRVSRAAFPSPTAAEMAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVPNASVIMQVPERIVVAGNNEDVSFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPPTTPQNEEIRAVGRLKRERSMSENAVRQNGQLVRNDSLWHRSDSAPRNKISRFQAPISAPEYTVTPSPQQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNIDTTIEGTSDDLTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR
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 Orthologous
Protein Cluster
2Phosphorylation------MSKGTSSDT
------CCCCCCCCC		39.5329083192
5Phosphorylation---MSKGTSSDTSLG
---CCCCCCCCCCHH		28.8829083192
6Phosphorylation--MSKGTSSDTSLGR
--CCCCCCCCCCHHH		34.5829083192
7Phosphorylation-MSKGTSSDTSLGRV
-CCCCCCCCCCHHHH		44.7529083192
7O-linked_Glycosylation-MSKGTSSDTSLGRV
-CCCCCCCCCCHHHH		44.7530379171
9PhosphorylationSKGTSSDTSLGRVSR
CCCCCCCCCHHHHHH		28.0029083192
10PhosphorylationKGTSSDTSLGRVSRA
CCCCCCCCHHHHHHC		33.5429083192
21PhosphorylationVSRAAFPSPTAAEMA
HHHCCCCCCCHHHHH		28.5621815630
23PhosphorylationRAAFPSPTAAEMAEI
HCCCCCCCHHHHHHH		42.7226552605
28 (in isoform 5)Ubiquitination-11.5021906983
28 (in isoform 4)Ubiquitination-11.5021906983
28 (in isoform 3)Ubiquitination-11.5021906983
28 (in isoform 2)Ubiquitination-11.5021906983
31PhosphorylationAAEMAEISRIQYEME
HHHHHHHHHHHHHHH		18.1626552605
35PhosphorylationAEISRIQYEMEYTEG
HHHHHHHHHHHHCCC		18.1828796482
39PhosphorylationRIQYEMEYTEGISQR
HHHHHHHHCCCCHHH		14.5828796482
40PhosphorylationIQYEMEYTEGISQRM
HHHHHHHCCCCHHHC		17.9028796482
44PhosphorylationMEYTEGISQRMRVPE
HHHCCCCHHHCCCCH		23.6928796482
52AcetylationQRMRVPEKLKVAPPN
HHCCCCHHCCCCCCC		47.7625953088
54UbiquitinationMRVPEKLKVAPPNAD
CCCCHHCCCCCCCCC		47.632190698
54 (in isoform 1)Ubiquitination-47.6321906983
74PhosphorylationQEGVPNASVIMQVPE
HCCCCCCEEEEECCC		20.8620873877
88 (in isoform 2)Ubiquitination-38.69-
93PhosphorylationAGNNEDVSFSRPADL
ECCCCCCCCCCCCCC		29.8120873877
95PhosphorylationNNEDVSFSRPADLDL
CCCCCCCCCCCCCCC		29.8325159151
95O-linked_GlycosylationNNEDVSFSRPADLDL
CCCCCCCCCCCCCCC		29.8330379171
105PhosphorylationADLDLIQSTPFKPLA
CCCCCCCCCCCCCCC		30.9325850435
106PhosphorylationDLDLIQSTPFKPLAL
CCCCCCCCCCCCCCC		19.1725850435
109UbiquitinationLIQSTPFKPLALKTP
CCCCCCCCCCCCCCC		40.08-
114UbiquitinationPFKPLALKTPPRVLT
CCCCCCCCCCCCEEE		54.07-
115PhosphorylationFKPLALKTPPRVLTL
CCCCCCCCCCCEEEC		39.1029255136
121PhosphorylationKTPPRVLTLSERPLD
CCCCCEEECCCCCCC		25.9424732914
123PhosphorylationPPRVLTLSERPLDFL
CCCEEECCCCCCCHH		26.7325159151
137PhosphorylationLDLERPPTTPQNEEI
HCCCCCCCCCCCHHH		54.5129255136
138PhosphorylationDLERPPTTPQNEEIR
CCCCCCCCCCCHHHH		28.7529255136
146PhosphorylationPQNEEIRAVGRLKRE
CCCHHHHHHHHHHHH		17.4927251275
146 (in isoform 2)Phosphorylation-17.4922167270
146 (in isoform 4)Phosphorylation-17.4927732954
146 (in isoform 5)Phosphorylation-17.4922167270
148 (in isoform 4)Phosphorylation-28.3727251275
149 (in isoform 2)Phosphorylation-30.3630266825
151 (in isoform 4)Phosphorylation-51.3427732954
151 (in isoform 2)Phosphorylation-51.3430266825
154 (in isoform 5)Phosphorylation-41.5125159151
155PhosphorylationGRLKRERSMSENAVR
HHHHHHHCCCHHHHH		23.1629255136
155 (in isoform 4)Phosphorylation-23.1627732954
156 (in isoform 4)Phosphorylation-7.9427732954
157PhosphorylationLKRERSMSENAVRQN
HHHHHCCCHHHHHHC		29.0129255136
159 (in isoform 5)Phosphorylation-36.1125159151
160 (in isoform 4)Phosphorylation-8.2027732954
161 (in isoform 4)Phosphorylation-11.0327732954
165 (in isoform 4)Phosphorylation-17.5427732954
168 (in isoform 5)Phosphorylation-4.0622210691
172PhosphorylationGQLVRNDSLWHRSDS
CEEECCCCHHCCCCC		36.5923401153
177PhosphorylationNDSLWHRSDSAPRNK
CCCHHCCCCCCCCCC		24.0325159151
179PhosphorylationSLWHRSDSAPRNKIS
CHHCCCCCCCCCCCC		41.2325159151
193PhosphorylationSRFQAPISAPEYTVT
CCCCCCCCCCCCEEC		36.3927174698
197PhosphorylationAPISAPEYTVTPSPQ
CCCCCCCCEECCCHH		12.8827174698
198PhosphorylationPISAPEYTVTPSPQQ
CCCCCCCEECCCHHH		19.0827174698
200O-linked_GlycosylationSAPEYTVTPSPQQAR
CCCCCEECCCHHHCC		15.3930379171
200PhosphorylationSAPEYTVTPSPQQAR
CCCCCEECCCHHHCC		15.3926055452
202O-linked_GlycosylationPEYTVTPSPQQARVC
CCCEECCCHHHCCCC		26.4430379171
202PhosphorylationPEYTVTPSPQQARVC
CCCEECCCHHHCCCC		26.4426055452
222PhosphorylationPEDGANLSSARGILS
CCCCCCCHHHHHHHH		23.0425159151
223PhosphorylationEDGANLSSARGILSL
CCCCCCHHHHHHHHH		25.7529396449
229PhosphorylationSSARGILSLIQSSTR
HHHHHHHHHHHHHHH		22.8526055452
233PhosphorylationGILSLIQSSTRRAYQ
HHHHHHHHHHHHHHH		27.0425159151
234PhosphorylationILSLIQSSTRRAYQQ
HHHHHHHHHHHHHHH		15.0122199227
235PhosphorylationLSLIQSSTRRAYQQI
HHHHHHHHHHHHHHH		29.4421815630
239PhosphorylationQSSTRRAYQQILDVL
HHHHHHHHHHHHHHH		10.1127642862
251 (in isoform 2)Ubiquitination-36.94-
251 (in isoform 2)Malonylation-36.9426320211
258PhosphorylationRPVLRGGSAAATSNP
CCCCCCCCCCCCCCC		19.9825159151
262PhosphorylationRGGSAAATSNPHHDN
CCCCCCCCCCCCCCC		25.0629396449
263PhosphorylationGGSAAATSNPHHDNV
CCCCCCCCCCCCCCC		43.5725159151
264 (in isoform 2)Ubiquitination-35.25-
275PhosphorylationDNVRYGISNIDTTIE
CCCEECCCCCCCEEE		24.3030622161
279PhosphorylationYGISNIDTTIEGTSD
ECCCCCCCEEECCCC		26.3530622161
295PhosphorylationLTVVDAASLRRQIIK
CEEECHHHHHHHHHH		24.91-
302UbiquitinationSLRRQIIKLNRRLQL
HHHHHHHHHHHHHHH		41.14-
302AcetylationSLRRQIIKLNRRLQL
HHHHHHHHHHHHHHH		41.1425953088
302MalonylationSLRRQIIKLNRRLQL
HHHHHHHHHHHHHHH		41.1426320211
3152-HydroxyisobutyrylationQLLEEENKERAKREM
HHHHHHHHHHHHHHH		52.43-
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
172SPhosphorylationKinaseAMPKA2P54646
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MFF_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 MFF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MFF_HUMANMFFphysical
23530241
CC126_HUMANCCDC126physical
28514442
MGT5A_HUMANMGAT5physical
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 MFF_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-172, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-157; THR-200AND SER-202, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137, AND MASSSPECTROMETRY.

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