Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Mitochondrial dynamics protein MID51 (Mitochondrial dynamics protein of 51 kDa) (Mitochondrial elongation factor 1) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like) (SMCR7-like protein)

 MID51_HUMAN             Reviewed;         463 AA.
Q9NQG6; Q7L890; Q9BUI3;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Mitochondrial dynamics protein MID51;
AltName: Full=Mitochondrial dynamics protein of 51 kDa;
AltName: Full=Mitochondrial elongation factor 1;
AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like;
Short=SMCR7-like protein;
Name=MIEF1; Synonyms=MID51, SMCR7L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12529303; DOI=10.1101/gr.695703;
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J.,
Knowles S., Bye J.M., Beare D.M., Dunham I.;
"Reevaluating human gene annotation: a second-generation analysis of
chromosome 22.";
Genome Res. 13:27-36(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=21508961; DOI=10.1038/embor.2011.54;
Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E.,
Ryan M.T.;
"MiD49 and MiD51, new components of the mitochondrial fission
machinery.";
EMBO Rep. 12:565-573(2011).
[10]
SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH
DNM1L AND FIS1, AND FUNCTION.
PubMed=21701560; DOI=10.1038/emboj.2011.198;
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N.,
Shupliakov O., Lendahl U., Nister M.;
"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and
promotes mitochondrial fusion rather than fission.";
EMBO J. 30:2762-2778(2011).
[11]
FUNCTION.
PubMed=23921378; DOI=10.1074/jbc.M113.479873;
Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D.,
Ryan M.T.;
"MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1
recruitment and are specific for mitochondrial fission.";
J. Biol. Chem. 288:27584-27593(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, AND INTERACTION WITH DNM1L.
PubMed=23283981; DOI=10.1091/mbc.E12-10-0721;
Loson O.C., Song Z., Chen H., Chan D.C.;
"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
fission.";
Mol. Biol. Cell 24:659-667(2013).
[14]
FUNCTION.
PubMed=23530241; DOI=10.1073/pnas.1300855110;
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A.,
Shaw J.M.;
"Interchangeable adaptors regulate mitochondrial dynamin assembly for
membrane scission.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
ALTERNATIVE INITIATION (ISOFORM 2).
PubMed=25621764; DOI=10.7554/eLife.03971;
Andreev D.E., O'Connor P.B., Fahey C., Kenny E.M., Terenin I.M.,
Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V.;
"Translation of 5' leaders is pervasive in genes resistant to eIF2
repression.";
Elife 4:E03971-E03971(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH
ADP AND GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-201; ARG-235;
238-PRO--PRO-242; ARG-342; LYS-368 AND LYS-372.
PubMed=24515348; DOI=10.1083/jcb.201311014;
Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K.,
Stroud D.A., Sesaki H., Kvansakul M., Ryan M.T.;
"Structural and functional analysis of MiD51, a dynamin receptor
required for mitochondrial fission.";
J. Cell Biol. 204:477-486(2014).
-!- FUNCTION: Mitochondrial outer membrane protein which regulates
mitochondrial fission. Promotes the recruitment and association of
the fission mediator dynamin-related protein 1 (DNM1L) to the
mitochondrial surface independently of the mitochondrial fission
FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L
oligomerization. Binds ADP and can also bind GDP, although with
lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits
DNM1L GTPase activity in the absence of bound ADP. Requires ADP to
stimulate DNM1L GTPase activity and the assembly of DNM1L into
long, oligomeric tubules with a spiral pattern, as opposed to the
ring-like DNM1L oligomers observed in the absence of bound ADP.
Does not require ADP for its function in recruiting DNM1L.
{ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241,
ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:24515348}.
-!- SUBUNIT: Homodimer. Interacts with DNM1L.
{ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:23283981,
ECO:0000269|PubMed:24515348}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-740987, EBI-740987;
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-740987, EBI-741181;
O00429:DNM1L; NbExp=9; IntAct=EBI-740987, EBI-724571;
Q9Y3D6:FIS1; NbExp=4; IntAct=EBI-740987, EBI-3385283;
P43355:MAGEA1; NbExp=6; IntAct=EBI-740987, EBI-740978;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-740987, EBI-10173939;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
ECO:0000269|PubMed:24515348}; Single-pass membrane protein
{ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
ECO:0000269|PubMed:24515348}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1;
IsoId=Q9NQG6-1; Sequence=Displayed;
Name=2;
IsoId=Q9NQG6-2; Sequence=VSP_056383, VSP_056384;
Name=3; Synonyms=uORF {ECO:0000303|PubMed:25621764};
IsoId=L0R8F8-1; Sequence=External;
Note=Product of the upstream open reading frame of this
bicistronic gene. {ECO:0000305|PubMed:25621764};
-!- TISSUE SPECIFICITY: Expression is relatively high in heart,
skeletal muscle, pancreas and kidney.
{ECO:0000269|PubMed:21701560}.
-!- SIMILARITY: Belongs to the SMCR7 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL365515; CAB97211.1; -; mRNA.
EMBL; AK290954; BAF83643.1; -; mRNA.
EMBL; AL834205; CAD38892.2; -; mRNA.
EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60335.1; -; Genomic_DNA.
EMBL; BC002587; AAH02587.2; -; mRNA.
EMBL; BC008327; AAH08327.1; -; mRNA.
CCDS; CCDS13995.1; -. [Q9NQG6-1]
RefSeq; NP_001291493.1; NM_001304564.1.
RefSeq; NP_061881.2; NM_019008.5. [Q9NQG6-1]
RefSeq; XP_011528538.1; XM_011530236.1. [Q9NQG6-1]
RefSeq; XP_011528539.1; XM_011530237.1. [Q9NQG6-1]
RefSeq; XP_011528540.1; XM_011530238.1. [Q9NQG6-1]
RefSeq; XP_016884327.1; XM_017028838.1. [Q9NQG6-1]
UniGene; Hs.728085; -.
PDB; 4NXT; X-ray; 2.12 A; A/B/C/D=119-463.
PDB; 4NXU; X-ray; 2.30 A; A/B/C/D=119-463.
PDB; 4NXV; X-ray; 2.30 A; A/B/C/D=119-463.
PDB; 4NXW; X-ray; 2.55 A; A=119-463.
PDB; 4NXX; X-ray; 2.55 A; A=119-463.
PDBsum; 4NXT; -.
PDBsum; 4NXU; -.
PDBsum; 4NXV; -.
PDBsum; 4NXW; -.
PDBsum; 4NXX; -.
ProteinModelPortal; Q9NQG6; -.
SMR; Q9NQG6; -.
BioGrid; 119977; 14.
IntAct; Q9NQG6; 18.
MINT; MINT-1684034; -.
STRING; 9606.ENSP00000327124; -.
iPTMnet; Q9NQG6; -.
PhosphoSitePlus; Q9NQG6; -.
BioMuta; SMCR7L; -.
DMDM; 74752902; -.
EPD; Q9NQG6; -.
MaxQB; Q9NQG6; -.
PaxDb; Q9NQG6; -.
PeptideAtlas; Q9NQG6; -.
PRIDE; Q9NQG6; -.
DNASU; 54471; -.
Ensembl; ENST00000325301; ENSP00000327124; ENSG00000100335. [Q9NQG6-1]
Ensembl; ENST00000404569; ENSP00000385191; ENSG00000100335. [Q9NQG6-1]
Ensembl; ENST00000428069; ENSP00000413730; ENSG00000100335. [Q9NQG6-2]
Ensembl; ENST00000433117; ENSP00000404096; ENSG00000100335. [Q9NQG6-2]
GeneID; 54471; -.
KEGG; hsa:54471; -.
UCSC; uc003axx.4; human. [Q9NQG6-1]
CTD; 54471; -.
EuPathDB; HostDB:ENSG00000100335.12; -.
GeneCards; MIEF1; -.
H-InvDB; HIX0016492; -.
HGNC; HGNC:25979; MIEF1.
HPA; HPA061059; -.
MIM; 615497; gene.
neXtProt; NX_Q9NQG6; -.
OpenTargets; ENSG00000100335; -.
PharmGKB; PA145148068; -.
eggNOG; ENOG410IK9T; Eukaryota.
eggNOG; ENOG41109RH; LUCA.
GeneTree; ENSGT00390000013127; -.
HOGENOM; HOG000144636; -.
HOVERGEN; HBG054078; -.
InParanoid; Q9NQG6; -.
PhylomeDB; Q9NQG6; -.
TreeFam; TF331032; -.
GeneWiki; SMCR7L; -.
GenomeRNAi; 54471; -.
PRO; PR:Q9NQG6; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100335; -.
CleanEx; HS_SMCR7L; -.
ExpressionAtlas; Q9NQG6; baseline and differential.
Genevisible; Q9NQG6; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IDA:MGI.
GO; GO:0019003; F:GDP binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
InterPro; IPR024810; Mab-21_dom.
Pfam; PF03281; Mab-21; 1.
SMART; SM01265; Mab-21; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Complete proteome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 463 Mitochondrial dynamics protein MID51.
/FTId=PRO_0000310448.
TOPO_DOM 1 23 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 24 46 Helical. {ECO:0000255}.
TOPO_DOM 47 463 Cytoplasmic. {ECO:0000255}.
REGION 49 195 Dimerization.
REGION 160 169 Important for interaction with DNM1L.
REGION 234 242 Important for interaction with DNM1L.
BINDING 187 187 ADP.
BINDING 189 189 ADP.
BINDING 201 201 ADP.
BINDING 340 340 ADP.
BINDING 342 342 ADP.
BINDING 368 368 ADP.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BGV8}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 108 148 DTFCPPRPKPVARKGQVDLKKSRLRMSLQEKLLTYYRNRAA
-> GETSYLLPEPGSHPCWRAGSGQASCCGHMCRAPELPAG
QVA (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_056383.
VAR_SEQ 149 463 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_056384.
VARIANT 78 78 G -> R (in dbSNP:rs2272830).
/FTId=VAR_037040.
VARIANT 89 89 T -> M (in dbSNP:rs17001213).
/FTId=VAR_037041.
VARIANT 169 169 R -> W (in dbSNP:rs2232088).
/FTId=VAR_037042.
VARIANT 264 264 D -> N (in dbSNP:rs2232091).
/FTId=VAR_037043.
MUTAGEN 201 201 H->D: Abolishes nucleotide-binding, but
not DNM1L recruitment; when associated
with E-342; E-368 and E-372.
{ECO:0000269|PubMed:24515348}.
MUTAGEN 235 235 R->A: No effect on mitochondrial
localization. Impairs DNM1L recruitment.
{ECO:0000269|PubMed:24515348}.
MUTAGEN 238 242 Missing: No effect on mitochondrial
localization. Impairs DNM1L recruitment.
{ECO:0000269|PubMed:24515348}.
MUTAGEN 342 342 R->E: Abolishes nucleotide-binding, but
not DNM1L recruitment; when associated
with D-201; E-368 and E-372.
{ECO:0000269|PubMed:24515348}.
MUTAGEN 368 368 K->E: Abolishes nucleotide-binding, but
not DNM1L recruitment; when associated
with D-201; E-342 and E-372.
{ECO:0000269|PubMed:24515348}.
MUTAGEN 372 372 K->E: Abolishes nucleotide-binding, but
not DNM1L recruitment; when associated
with D-201; E-342 and E-368.
{ECO:0000269|PubMed:24515348}.
HELIX 126 145 {ECO:0000244|PDB:4NXT}.
HELIX 151 175 {ECO:0000244|PDB:4NXT}.
STRAND 179 181 {ECO:0000244|PDB:4NXT}.
STRAND 185 188 {ECO:0000244|PDB:4NXT}.
TURN 189 193 {ECO:0000244|PDB:4NXT}.
STRAND 201 208 {ECO:0000244|PDB:4NXT}.
HELIX 212 214 {ECO:0000244|PDB:4NXT}.
STRAND 215 219 {ECO:0000244|PDB:4NXT}.
HELIX 220 222 {ECO:0000244|PDB:4NXT}.
STRAND 223 225 {ECO:0000244|PDB:4NXT}.
STRAND 230 235 {ECO:0000244|PDB:4NXT}.
TURN 238 240 {ECO:0000244|PDB:4NXT}.
HELIX 247 251 {ECO:0000244|PDB:4NXT}.
HELIX 259 271 {ECO:0000244|PDB:4NXT}.
HELIX 272 274 {ECO:0000244|PDB:4NXW}.
HELIX 276 283 {ECO:0000244|PDB:4NXT}.
STRAND 286 289 {ECO:0000244|PDB:4NXT}.
STRAND 297 303 {ECO:0000244|PDB:4NXT}.
STRAND 306 318 {ECO:0000244|PDB:4NXT}.
STRAND 321 324 {ECO:0000244|PDB:4NXT}.
HELIX 331 333 {ECO:0000244|PDB:4NXT}.
STRAND 337 339 {ECO:0000244|PDB:4NXT}.
HELIX 342 354 {ECO:0000244|PDB:4NXT}.
TURN 355 357 {ECO:0000244|PDB:4NXT}.
HELIX 360 373 {ECO:0000244|PDB:4NXT}.
HELIX 375 377 {ECO:0000244|PDB:4NXT}.
HELIX 382 395 {ECO:0000244|PDB:4NXT}.
HELIX 401 403 {ECO:0000244|PDB:4NXT}.
HELIX 404 421 {ECO:0000244|PDB:4NXT}.
TURN 434 437 {ECO:0000244|PDB:4NXT}.
HELIX 440 451 {ECO:0000244|PDB:4NXT}.
HELIX 457 460 {ECO:0000244|PDB:4NXT}.
SEQUENCE 463 AA; 51293 MW; 0824AD44305C234D CRC64;
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT DSSTFDTDTF CPPRPKPVAR
KGQVDLKKSR LRMSLQEKLL TYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY
FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
QYERDKHLFI DFLPSVTLGD TVLVAKPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS PDMLADRFLQ ALRGLISYLE
AGVLPSALNP KVNLFAELTP EEIDELGYTL YCSLSEPEVL LQT


Related products :

Catalog number Product name Quantity
CSB-EL021826HU Human Smith-Magenis syndrome chromosomal region candidate gene 7 protein(SMCR7) ELISA kit 96T
H1302 Smith-Magenis syndrome chromosomal region candidate gene 7 protein (SMCR7), Mouse, ELISA Kit 96T
H1301 Smith-Magenis syndrome chromosomal region candidate gene 7 protein (SMCR7), Human, ELISA Kit 96T
CSB-EL021826MO Mouse Smith-Magenis syndrome chromosomal region candidate gene 7 protein(SMCR7) ELISA kit 96T
CSB-EL021826HU Human Smith-Magenis syndrome chromosomal region candidate gene 7 protein(SMCR7) ELISA kit SpeciesHuman 96T
CSB-EL021826MO Mouse Smith-Magenis syndrome chromosomal region candidate gene 7 protein(SMCR7) ELISA kit SpeciesMouse 96T
H1305 Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like (SMCR7L), Rat, ELISA Kit 96T
CSB-EL021827RA Rat Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like(SMCR7L) ELISA kit 96T
SMCR5_HUMAN Human ELISA Kit FOR Smith-Magenis syndrome chromosomal region candidate gene 5 protein 96T
H1300 Smith-Magenis syndrome chromosomal region candidate gene 5 protein (SMCR5), Human, ELISA Kit 96T
CSB-EL021827HU Human Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like(SMCR7L) ELISA kit 96T
CSB-EL021828MO Mouse Smith-Magenis syndrome chromosomal region candidate gene 8 protein(SMCR8) ELISA kit 96T
CSB-EL021824HU Human Smith-Magenis syndrome chromosomal region candidate gene 5 protein(SMCR5) ELISA kit 96T
H1306 Smith-Magenis syndrome chromosomal region candidate gene 8 protein (SMCR8), Human, ELISA Kit 96T
H1303 Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like (SMCR7L), Human, ELISA Kit 96T
CSB-EL021827MO Mouse Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like(SMCR7L) ELISA kit 96T
CSB-EL021827RA Rat Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like(SMCR7L) ELISA kit SpeciesRat 96T
H1307 Smith-Magenis syndrome chromosomal region candidate gene 8 protein (SMCR8), Mouse, ELISA Kit 96T
H1304 Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like (SMCR7L), Mouse, ELISA Kit 96T
CSB-EL021828HU Human Smith-Magenis syndrome chromosomal region candidate gene 8 protein(SMCR8) ELISA kit 96T
EIAAB38787 Mouse,Mus musculus,Smcr8,Smith-Magenis syndrome chromosomal region candidate gene 8 protein homolog
CSB-EL021827HU Human Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like(SMCR7L) ELISA kit SpeciesHuman 96T
CSB-EL021828MO Mouse Smith-Magenis syndrome chromosomal region candidate gene 8 protein(SMCR8) ELISA kit SpeciesMouse 96T
EIAAB38788 Homo sapiens,Human,SMCR8,Smith-Magenis syndrome chromosomal region candidate gene 8 protein
EIAAB38786 Homo sapiens,Human,SMCR5,Smith-Magenis syndrome chromosomal region candidate gene 5 protein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur