Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial fission factor

Gene

MFF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • mitochondrial fission Source: UniProtKB
  • mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  • mitochondrial fusion Source: UniProtKB
  • mitochondrion morphogenesis Source: MGI
  • peroxisome fission Source: UniProtKB
  • positive regulation of mitochondrial fission Source: UniProtKB
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein targeting to mitochondrion Source: UniProtKB
  • regulation of mitochondrion organization Source: UniProtKB
  • regulation of peroxisome organization Source: UniProtKB
  • release of cytochrome c from mitochondria Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial fission factor
Gene namesi
Name:MFF
Synonyms:C2orf33
ORF Names:AD030, AD033, GL004
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24858. MFF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 322322CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei323 – 34018Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini341 – 3422Mitochondrial intermembraneSequence Analysis

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of mitochondrial membrane Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • peroxisome Source: UniProtKB
  • synaptic vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395839.

Polymorphism and mutation databases

BioMutaiMFF.
DMDMi74725008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Mitochondrial fission factorPRO_0000289184Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151Phosphothreonine1 Publication
Modified residuei155 – 1551Phosphoserine3 Publications
Modified residuei157 – 1571Phosphoserine3 Publications
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei200 – 2001Phosphothreonine1 Publication
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei233 – 2331Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9GZY8.
PaxDbiQ9GZY8.
PRIDEiQ9GZY8.

PTM databases

PhosphoSiteiQ9GZY8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9GZY8.
CleanExiHS_MFF.
ExpressionAtlasiQ9GZY8. baseline and differential.
GenevestigatoriQ9GZY8.

Organism-specific databases

HPAiHPA010968.

Interactioni

Subunit structurei

Homodimer. Interacts with DNM1L (By similarity).By similarity

Protein-protein interaction databases

BioGridi121271. 9 interactions.
STRINGi9606.ENSP00000302037.

Structurei

3D structure databases

ProteinModelPortaliQ9GZY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili291 – 32232Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the Tango11 family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43415.
GeneTreeiENSGT00390000009776.
HOGENOMiHOG000285976.
HOVERGENiHBG105704.
InParanoidiQ9GZY8.
OMAiDSLWHRS.
PhylomeDBiQ9GZY8.
TreeFamiTF325506.

Family and domain databases

InterProiIPR008518. FATE/Miff/Tango-11.
[Graphical view]
PANTHERiPTHR16501. PTHR16501. 1 hit.
PfamiPF05644. Miff. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9GZY8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSKGTSSDTS LGRVSRAAFP SPTAAEMAEI SRIQYEMEYT EGISQRMRVP
60 70 80 90 100
EKLKVAPPNA DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DVSFSRPADL
110 120 130 140 150
DLIQSTPFKP LALKTPPRVL TLSERPLDFL DLERPPTTPQ NEEIRAVGRL
160 170 180 190 200
KRERSMSENA VRQNGQLVRN DSLWHRSDSA PRNKISRFQA PISAPEYTVT
210 220 230 240 250
PSPQQARVCP PHMLPEDGAN LSSARGILSL IQSSTRRAYQ QILDVLDENR
260 270 280 290 300
RPVLRGGSAA ATSNPHHDNV RYGISNIDTT IEGTSDDLTV VDAASLRRQI
310 320 330 340
IKLNRRLQLL EEENKERAKR EMVMYSITVA FWLLNSWLWF RR
Length:342
Mass (Da):38,465
Last modified:March 1, 2001 - v1
Checksum:i1DBFBBE17DB122A0
GO
Isoform 2 (identifier: Q9GZY8-2) [UniParc]FASTAAdd to basket

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. Contains a phosphoserine at position 146.3 Publications

Show »
Length:291
Mass (Da):32,973
Checksum:i1CEA83C57D1E6FE6
GO
Isoform 3 (identifier: Q9GZY8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     199-271: Missing.

Show »
Length:243
Mass (Da):27,964
Checksum:i2D2B8A36FEA1C038
GO
Isoform 4 (identifier: Q9GZY8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     174-271: Missing.

Show »
Length:218
Mass (Da):25,067
Checksum:i07B22DF970A4995F
GO
Isoform 5 (identifier: Q9GZY8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     174-251: Missing.

Note: Contains a phosphoserine at position 146.1 Publication

Show »
Length:238
Mass (Da):27,105
Checksum:i3F647B952DAE2A05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121H → Y in CAH56328 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71S → C.
Corresponds to variant rs3211097 [ dbSNP | Ensembl ].
VAR_053915
Natural varianti7 – 71S → I.
Corresponds to variant rs3211098 [ dbSNP | Ensembl ].
VAR_053916
Natural varianti29 – 291E → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036028

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_025954Add
BLAST
Alternative sequencei174 – 27198Missing in isoform 4. 1 PublicationVSP_025955Add
BLAST
Alternative sequencei174 – 25178Missing in isoform 5. 1 PublicationVSP_025956Add
BLAST
Alternative sequencei174 – 19825Missing in isoform 2. 1 PublicationVSP_025957Add
BLAST
Alternative sequencei199 – 27173Missing in isoform 3. 1 PublicationVSP_025958Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2465.1. [Q9GZY8-1]
CCDS63139.1. [Q9GZY8-3]
CCDS63140.1. [Q9GZY8-2]
CCDS63141.1. [Q9GZY8-5]
CCDS63142.1. [Q9GZY8-4]
RefSeqiNP_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_006712639.2. [Q9GZY8-5]
UniGeneiHs.471528.

Genome annotation databases

EnsembliENST00000304593; ENSP00000304898; ENSG00000168958. [Q9GZY8-2]
ENST00000337110; ENSP00000338412; ENSG00000168958. [Q9GZY8-3]
ENST00000349901; ENSP00000304134; ENSG00000168958. [Q9GZY8-5]
ENST00000353339; ENSP00000302037; ENSG00000168958. [Q9GZY8-1]
ENST00000354503; ENSP00000346498; ENSG00000168958. [Q9GZY8-4]
ENST00000409565; ENSP00000386964; ENSG00000168958. [Q9GZY8-4]
ENST00000409616; ENSP00000386641; ENSG00000168958. [Q9GZY8-5]
GeneIDi56947.
KEGGihsa:56947.
UCSCiuc002vos.4. human. [Q9GZY8-1]
uc002vot.4. human. [Q9GZY8-2]
uc002vow.4. human. [Q9GZY8-3]
uc002voz.4. human. [Q9GZY8-4]
uc021vxu.2. human. [Q9GZY8-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2465.1. [Q9GZY8-1]
CCDS63139.1. [Q9GZY8-3]
CCDS63140.1. [Q9GZY8-2]
CCDS63141.1. [Q9GZY8-5]
CCDS63142.1. [Q9GZY8-4]
RefSeqiNP_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_006712639.2. [Q9GZY8-5]
UniGeneiHs.471528.

3D structure databases

ProteinModelPortaliQ9GZY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121271. 9 interactions.
STRINGi9606.ENSP00000302037.

PTM databases

PhosphoSiteiQ9GZY8.

Polymorphism and mutation databases

BioMutaiMFF.
DMDMi74725008.

Proteomic databases

MaxQBiQ9GZY8.
PaxDbiQ9GZY8.
PRIDEiQ9GZY8.

Protocols and materials databases

DNASUi56947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304593; ENSP00000304898; ENSG00000168958. [Q9GZY8-2]
ENST00000337110; ENSP00000338412; ENSG00000168958. [Q9GZY8-3]
ENST00000349901; ENSP00000304134; ENSG00000168958. [Q9GZY8-5]
ENST00000353339; ENSP00000302037; ENSG00000168958. [Q9GZY8-1]
ENST00000354503; ENSP00000346498; ENSG00000168958. [Q9GZY8-4]
ENST00000409565; ENSP00000386964; ENSG00000168958. [Q9GZY8-4]
ENST00000409616; ENSP00000386641; ENSG00000168958. [Q9GZY8-5]
GeneIDi56947.
KEGGihsa:56947.
UCSCiuc002vos.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

CTDi56947.
GeneCardsiGC02P228189.
HGNCiHGNC:24858. MFF.
HPAiHPA010968.
MIMi614785. gene.
neXtProtiNX_Q9GZY8.
PharmGKBiPA162395839.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43415.
GeneTreeiENSGT00390000009776.
HOGENOMiHOG000285976.
HOVERGENiHBG105704.
InParanoidiQ9GZY8.
OMAiDSLWHRS.
PhylomeDBiQ9GZY8.
TreeFamiTF325506.

Miscellaneous databases

ChiTaRSiMFF. human.
GeneWikiiMitochondrial_fission_factor.
GenomeRNAii56947.
NextBioi62537.
PROiQ9GZY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZY8.
CleanExiHS_MFF.
ExpressionAtlasiQ9GZY8. baseline and differential.
GenevestigatoriQ9GZY8.

Family and domain databases

InterProiIPR008518. FATE/Miff/Tango-11.
[Graphical view]
PANTHERiPTHR16501. PTHR16501. 1 hit.
PfamiPF05644. Miff. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. "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.
  16. "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.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-29.

Entry informationi

Entry nameiMFF_HUMAN
AccessioniPrimary (citable) accession number: Q9GZY8
Secondary accession number(s): Q567U1
, Q658R6, Q9BVZ1, Q9H690, Q9NRG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.