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Q9GZY8 (MFF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial fission factor
Gene names
Name:MFF
Synonyms:C2orf33
ORF Names:AD030, AD033, GL004
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.17

Subunit structure

Homodimer. Interacts with DNM1L By similarity. Ref.17

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein. Peroxisome. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle By similarity Ref.1 Ref.16.

Tissue specificity

Highly expressed in heart, kidney, liver, brain, muscle, and stomach. Ref.1

Sequence similarities

Belongs to the Tango11 family.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasmic vesicle
Membrane
Mitochondrion
Mitochondrion outer membrane
Peroxisome
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrial fission

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial fragmentation involved in apoptotic process

Inferred from mutant phenotype Ref.1PubMed 21149567. Source: UniProtKB

mitochondrial fusion

Inferred from mutant phenotype Ref.16. Source: UniProtKB

mitochondrion morphogenesis

Inferred from mutant phenotype PubMed 21149567. Source: MGI

peroxisome fission

Inferred from mutant phenotype Ref.1PubMed 21149567. Source: UniProtKB

positive regulation of mitochondrial fission

Inferred from direct assay PubMed 23283981Ref.17. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from direct assay PubMed 23283981. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 21149567. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.1. Source: UniProtKB

protein targeting to mitochondrion

Inferred from mutant phenotype PubMed 21149567. Source: UniProtKB

regulation of mitochondrion organization

Inferred from mutant phenotype Ref.1PubMed 21149567. Source: UniProtKB

regulation of peroxisome organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of mitochondrial membrane

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 21149567. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.1Ref.16. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 21149567. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9GZY8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9GZY8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     174-198: Missing.
Note: Contains a phosphothreonine at position 149. Contains a phosphoserine at position 151.
Isoform 3 (identifier: Q9GZY8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     199-271: Missing.
Isoform 4 (identifier: Q9GZY8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     174-271: Missing.
Isoform 5 (identifier: Q9GZY8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     174-251: Missing.
Note: Contains a phosphoserine at position 146.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Mitochondrial fission factor
PRO_0000289184

Regions

Topological domain1 – 322322Cytoplasmic Potential
Transmembrane323 – 34018Helical; Anchor for type IV membrane protein; Potential
Topological domain341 – 3422Mitochondrial intermembrane Potential
Coiled coil291 – 32232 Potential

Amino acid modifications

Modified residue1151Phosphothreonine Ref.12
Modified residue1551Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue1571Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue1721Phosphoserine By similarity
Modified residue2001Phosphothreonine Ref.12
Modified residue2021Phosphoserine Ref.12
Modified residue2291Phosphoserine Ref.12
Modified residue2331Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 2626Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_025954
Alternative sequence174 – 27198Missing in isoform 4.
VSP_025955
Alternative sequence174 – 25178Missing in isoform 5.
VSP_025956
Alternative sequence174 – 19825Missing in isoform 2.
VSP_025957
Alternative sequence199 – 27173Missing in isoform 3.
VSP_025958
Natural variant71S → C.
Corresponds to variant rs3211097 [ dbSNP | Ensembl ].
VAR_053915
Natural variant71S → I.
Corresponds to variant rs3211098 [ dbSNP | Ensembl ].
VAR_053916
Natural variant291E → K in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036028

Experimental info

Sequence conflict2121H → Y in CAH56328. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 1DBFBBE17DB122A0

FASTA34238,465
        10         20         30         40         50         60 
MSKGTSSDTS LGRVSRAAFP SPTAAEMAEI SRIQYEMEYT EGISQRMRVP EKLKVAPPNA 

        70         80         90        100        110        120 
DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DVSFSRPADL DLIQSTPFKP LALKTPPRVL 

       130        140        150        160        170        180 
TLSERPLDFL DLERPPTTPQ NEEIRAVGRL KRERSMSENA VRQNGQLVRN DSLWHRSDSA 

       190        200        210        220        230        240 
PRNKISRFQA PISAPEYTVT PSPQQARVCP PHMLPEDGAN LSSARGILSL IQSSTRRAYQ 

       250        260        270        280        290        300 
QILDVLDENR RPVLRGGSAA ATSNPHHDNV RYGISNIDTT IEGTSDDLTV VDAASLRRQI 

       310        320        330        340 
IKLNRRLQLL EEENKERAKR EMVMYSITVA FWLLNSWLWF RR 

« Hide

Isoform 2 [UniParc].

Checksum: 1CEA83C57D1E6FE6
Show »

FASTA29132,973
Isoform 3 [UniParc].

Checksum: 2D2B8A36FEA1C038
Show »

FASTA24327,964
Isoform 4 [UniParc].

Checksum: 07B22DF970A4995F
Show »

FASTA21825,067
Isoform 5 [UniParc].

Checksum: 3F647B952DAE2A05
Show »

FASTA23827,105

References

« Hide 'large scale' references
[1]"The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
Gandre-Babbe S., van der Bliek A.M.
Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"A novel gene expressed in human liver non-tumor tissues."
Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Liver.
[4]Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
Tissue: Placenta.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-342.
Tissue: Stomach.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-155; SER-157; THR-200; SER-202; SER-229 AND SER-233, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-29.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK026137 mRNA. Translation: BAB15373.1.
AF246239 mRNA. Translation: AAG44486.1.
AF226049 mRNA. Translation: AAF86949.1.
AF258660 mRNA. Translation: AAG44658.1.
AC097662 Genomic DNA. Translation: AAY24252.1.
BC000797 mRNA. Translation: AAH00797.1.
BC093024 mRNA. Translation: AAH93024.1.
AL833032 mRNA. Translation: CAH56328.1.
CCDSCCDS2465.1. [Q9GZY8-1]
CCDS63139.1. [Q9GZY8-3]
CCDS63140.1. [Q9GZY8-2]
CCDS63141.1. [Q9GZY8-5]
CCDS63142.1. [Q9GZY8-4]
RefSeqNP_001263990.1. NM_001277061.1. [Q9GZY8-1]
NP_001263991.1. NM_001277062.1. [Q9GZY8-2]
NP_001263992.1. NM_001277063.1. [Q9GZY8-3]
NP_001263993.1. NM_001277064.1. [Q9GZY8-5]
NP_001263994.1. NM_001277065.1. [Q9GZY8-4]
NP_001263995.1. NM_001277066.1. [Q9GZY8-4]
NP_001263996.1. NM_001277067.1.
NP_001263997.1. NM_001277068.1.
NP_064579.3. NM_020194.5. [Q9GZY8-1]
XP_006712701.1. XM_006712638.1. [Q9GZY8-2]
XP_006712702.1. XM_006712639.1. [Q9GZY8-5]
UniGeneHs.471528.

3D structure databases

ProteinModelPortalQ9GZY8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121271. 6 interactions.
STRING9606.ENSP00000302037.

PTM databases

PhosphoSiteQ9GZY8.

Polymorphism databases

DMDM74725008.

Proteomic databases

MaxQBQ9GZY8.
PaxDbQ9GZY8.
PRIDEQ9GZY8.

Protocols and materials databases

DNASU56947.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304593; ENSP00000304898; ENSG00000168958. [Q9GZY8-2]
ENST00000337110; ENSP00000338412; ENSG00000168958. [Q9GZY8-3]
ENST00000349901; ENSP00000304134; ENSG00000168958. [Q9GZY8-5]
ENST00000353339; ENSP00000302037; ENSG00000168958. [Q9GZY8-1]
ENST00000354503; ENSP00000346498; ENSG00000168958. [Q9GZY8-4]
ENST00000392059; ENSP00000375912; ENSG00000168958. [Q9GZY8-1]
ENST00000409565; ENSP00000386964; ENSG00000168958. [Q9GZY8-4]
ENST00000409616; ENSP00000386641; ENSG00000168958. [Q9GZY8-5]
GeneID56947.
KEGGhsa:56947.
UCSCuc002vos.4. human. [Q9GZY8-1]
uc002vot.4. human. [Q9GZY8-2]
uc002vow.4. human. [Q9GZY8-3]
uc002voz.4. human. [Q9GZY8-4]
uc021vxu.2. human. [Q9GZY8-5]

Organism-specific databases

CTD56947.
GeneCardsGC02P228189.
HGNCHGNC:24858. MFF.
HPAHPA010968.
MIM614785. gene.
neXtProtNX_Q9GZY8.
PharmGKBPA162395839.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43415.
HOGENOMHOG000285976.
HOVERGENHBG105704.
InParanoidQ9GZY8.
OMAISAPEYT.
PhylomeDBQ9GZY8.
TreeFamTF325506.

Gene expression databases

ArrayExpressQ9GZY8.
BgeeQ9GZY8.
CleanExHS_MFF.
GenevestigatorQ9GZY8.

Family and domain databases

InterProIPR008518. FATE/Miff/Tango-11.
[Graphical view]
PANTHERPTHR16501. PTHR16501. 1 hit.
PfamPF05644. Miff. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMFF. human.
GeneWikiMitochondrial_fission_factor.
GenomeRNAi56947.
NextBio62537.
PROQ9GZY8.
SOURCESearch...

Entry information

Entry nameMFF_HUMAN
AccessionPrimary (citable) accession number: Q9GZY8
Secondary accession number(s): Q567U1 expand/collapse secondary AC list , Q658R6, Q9BVZ1, Q9H690, Q9NRG8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM