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Stomatin-like protein 2, mitochondrial (SLP-2) (EPB72-like protein 2) (Paraprotein target 7) (Paratarg-7)

 STML2_HUMAN             Reviewed;         356 AA.
Q9UJZ1; B4E1K7; D3DRN3; O60376; Q53G29; Q96FY2; Q9P042;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 143.
RecName: Full=Stomatin-like protein 2, mitochondrial;
Short=SLP-2;
AltName: Full=EPB72-like protein 2;
AltName: Full=Paraprotein target 7;
Short=Paratarg-7;
Flags: Precursor;
Name=STOML2; Synonyms=SLP2; ORFNames=HSPC108;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Heart muscle;
PubMed=10713127; DOI=10.1074/jbc.275.11.8062;
Wang Y., Morrow J.S.;
"Identification and characterization of human SLP-2, a novel homologue
of stomatin (band 7.2b) present in erythrocytes and other tissues.";
J. Biol. Chem. 275:8062-8071(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11435687;
Owczarek C.M., Treutlein H.R., Portbury K.J., Gulluyan L.M., Kola I.,
Hertzog P.J.;
"A novel member of the stomatin/EPB72/mec-2 family, stomatin-like 2
(STOML2), is ubiquitously expressed and localizes to HSA chromosome
9p13.1.";
Cytogenet. Cell Genet. 92:196-203(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-129.
TISSUE=Lung, Pancreas, and Skin;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-356 (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[9]
PROTEIN SEQUENCE OF 188-197; 201-211 AND 234-250, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[10]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16671055; DOI=10.1002/prot.20987;
John J.P., Anrather D., Pollak A., Lubec G.;
"Mass spectrometrical verification of stomatin-like protein 2 (SLP-2)
primary structure.";
Proteins 64:543-551(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MFN2,
AND SUBCELLULAR LOCATION.
PubMed=17121834; DOI=10.1074/jbc.M608168200;
Hajek P., Chomyn A., Attardi G.;
"Identification of a novel mitochondrial complex containing mitofusin
2 and stomatin-like protein 2.";
J. Biol. Chem. 282:5670-5681(2007).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH PHB AND PHB2.
PubMed=18339324; DOI=10.1016/j.bbamcr.2008.02.006;
Da Cruz S., Parone P.A., Gonzalo P., Bienvenut W.V., Tondera D.,
Jourdain A., Quadroni M., Martinou J.C.;
"SLP-2 interacts with prohibitins in the mitochondrial inner membrane
and contributes to their stability.";
Biochim. Biophys. Acta 1783:904-911(2008).
[14]
FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=18641330; DOI=10.4049/jimmunol.181.3.1927;
Kirchhof M.G., Chau L.A., Lemke C.D., Vardhana S., Darlington P.J.,
Marquez M.E., Taylor R., Rizkalla K., Blanca I., Dustin M.L.,
Madrenas J.;
"Modulation of T cell activation by stomatin-like protein 2.";
J. Immunol. 181:1927-1936(2008).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19597348; DOI=10.4161/cbt.8.17.9283;
Wang Y., Cao W., Yu Z., Liu Z.;
"Downregulation of a mitochondria associated protein SLP-2 inhibits
tumor cell motility, proliferation and enhances cell sensitivity to
chemotherapeutic reagents.";
Cancer Biol. Ther. 8:1651-1658(2009).
[16]
IDENTIFICATION AS A COMMON ANTIGEN IN B-CELL NEOPLASMS.
PubMed=19405124; DOI=10.1002/ijc.24427;
Preuss K.D., Pfreundschuh M., Ahlgrimm M., Fadle N., Regitz E.,
Murawski N., Grass S.;
"A frequent target of paraproteins in the sera of patients with
multiple myeloma and MGUS.";
Int. J. Cancer 125:656-661(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-233, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
FUNCTION IN CALCIUM HOMEOSTASIS.
PubMed=19944461; DOI=10.1016/j.ceca.2009.10.005;
Da Cruz S., De Marchi U., Frieden M., Parone P.A., Martinou J.C.,
Demaurex N.;
"SLP-2 negatively modulates mitochondrial sodium-calcium exchange.";
Cell Calcium 47:11-18(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION AT SER-17.
PubMed=21791414; DOI=10.1182/blood-2011-04-351668;
Preuss K.D., Pfreundschuh M., Fadle N., Regitz E., Raudies S.,
Murwaski N., Ahlgrimm M., Bittenbring J., Klotz M., Schafer K.H.,
Held G., Neumann F., Grass S.;
"Hyperphosphorylation of autoantigenic targets of paraproteins is due
to inactivation of PP2A.";
Blood 118:3340-3346(2011).
[21]
FUNCTION IN MITOCHONDRIAL BIOGENESIS, SUBCELLULAR LOCATION,
INTERACTION WITH PHB AND PHB2, CARDIOLIPIN-BINDING, AND INDUCTION.
PubMed=21746876; DOI=10.1128/MCB.05393-11;
Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G.,
Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.;
"Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial
biogenesis and function.";
Mol. Cell. Biol. 31:3845-3856(2011).
[22]
FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, AND
HOMOOLIGOMERIZATION.
PubMed=22623988; DOI=10.1371/journal.pone.0037144;
Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.;
"Mitochondrial and plasma membrane pools of stomatin-like protein 2
coalesce at the immunological synapse during T cell activation.";
PLoS ONE 7:E37144-E37144(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-330, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-330, AND
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).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Mitochondrial protein that probably regulates the
biogenesis and the activity of mitochondria. Stimulates
cardiolipin biosynthesis, binds cardiolipin-enriched membranes
where it recruits and stabilizes some proteins including
prohibitin and may therefore act in the organization of functional
microdomains in mitochondrial membranes. Through regulation of the
mitochondrial function may play a role into several biological
processes including cell migration, cell proliferation, T-cell
activation, calcium homeostasis and cellular response to stress.
May play a role in calcium homeostasis through negative regulation
of calcium efflux from mitochondria. Required for mitochondrial
hyperfusion a pro-survival cellular response to stress which
results in increased ATP production by mitochondria. May also
regulate the organization of functional domains at the plasma
membrane and play a role in T-cell activation through association
with the T-cell receptor signaling complex and its regulation.
{ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18641330,
ECO:0000269|PubMed:19597348, ECO:0000269|PubMed:19944461,
ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.
-!- SUBUNIT: Forms homooligomers. Interacts with MFN2; may form
heterooligomers. Interacts with CACNA2D2 (By similarity).
Interacts with PHB and PHB2; recruits them to cardiolipin-enriched
mitochondrial membranes and stabilizes them. {ECO:0000250,
ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18339324,
ECO:0000269|PubMed:21746876}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10713127,
ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876,
ECO:0000269|PubMed:22623988}; Peripheral membrane protein
{ECO:0000269|PubMed:10713127}. Mitochondrion
{ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:19597348,
ECO:0000269|PubMed:22623988}. Mitochondrion inner membrane
{ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18339324,
ECO:0000269|PubMed:21746876}; Lipid-anchor
{ECO:0000269|PubMed:21746876}. Mitochondrion intermembrane space
{ECO:0000269|PubMed:17121834}. Membrane raft
{ECO:0000269|PubMed:18641330}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330}.
Note=Behaves as an integral membrane protein of the mitochondrion
despite the absence of a detectable transmembrane domain
(PubMed:21746876). Also associates with the actin cytoskeleton and
membrane rafts in activated T-cells (PubMed:18641330,
PubMed:10713127). A minor pool is associated with the plasma
membrane and is enriched at the immunological synapse in activated
T-cells (PubMed:22623988). {ECO:0000269|PubMed:10713127,
ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876,
ECO:0000269|PubMed:22623988}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UJZ1-1; Sequence=Displayed;
Name=2;
IsoId=Q9UJZ1-2; Sequence=VSP_054651;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels.
Expressed in lymphoid tissues (at protein level).
{ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:11435687,
ECO:0000269|PubMed:18641330}.
-!- INDUCTION: Up-regulated in activated B- and T-cells and upon
mitochondrial stress by chloramphenicol.
{ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876}.
-!- PTM: Hyperphosphorylated at Ser-17 in some patients with
monoclonal gammopathy of undetermined significance (MGUS),
multiple myeloma (MM) and Waldenstrom macroglobulinemia due to
impaired dephosphorylation by PP2A.
-!- MISCELLANEOUS: Paratarg-7/STOML2 is a frequent autoantigenic
target in monoclonal gammopathy of undetermined significance
(MGUS), multiple myeloma (MM) and Waldenstrom macroglobulinemia, 3
B-cell neoplasms associated with excessive secretion of a single
monoclonal gammaglobulin (also named paraprotein) in the blood.
{ECO:0000305|PubMed:19405124}.
-!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC07983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAF29073.1; Type=Frameshift; Positions=14, 26; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STOML2ID44346ch9p13.html";
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EMBL; AF190167; AAF09142.1; -; mRNA.
EMBL; AF282596; AAF91466.1; -; mRNA.
EMBL; AK027405; BAB55091.1; -; mRNA.
EMBL; AK303883; BAG64819.1; -; mRNA.
EMBL; AK223102; BAD96822.1; -; mRNA.
EMBL; AL353795; CAH70998.1; -; Genomic_DNA.
EMBL; AC004472; AAC07983.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471071; EAW58395.1; -; Genomic_DNA.
EMBL; CH471071; EAW58396.1; -; Genomic_DNA.
EMBL; BC002442; AAH02442.1; -; mRNA.
EMBL; BC003025; AAH03025.1; -; mRNA.
EMBL; BC010152; AAH10152.1; -; mRNA.
EMBL; BC014990; AAH14990.1; -; mRNA.
EMBL; AF161458; AAF29073.1; ALT_FRAME; mRNA.
CCDS; CCDS6577.1; -. [Q9UJZ1-1]
CCDS; CCDS69588.1; -. [Q9UJZ1-2]
PIR; T02246; T02246.
RefSeq; NP_001273960.1; NM_001287031.1. [Q9UJZ1-2]
RefSeq; NP_001273961.1; NM_001287032.1.
RefSeq; NP_038470.1; NM_013442.2. [Q9UJZ1-1]
UniGene; Hs.3439; -.
ProteinModelPortal; Q9UJZ1; -.
SMR; Q9UJZ1; -.
BioGrid; 119062; 85.
IntAct; Q9UJZ1; 35.
MINT; MINT-2999996; -.
STRING; 9606.ENSP00000348886; -.
iPTMnet; Q9UJZ1; -.
PhosphoSitePlus; Q9UJZ1; -.
SwissPalm; Q9UJZ1; -.
DMDM; 60415944; -.
OGP; Q9UJZ1; -.
REPRODUCTION-2DPAGE; IPI00334190; -.
EPD; Q9UJZ1; -.
PaxDb; Q9UJZ1; -.
PeptideAtlas; Q9UJZ1; -.
PRIDE; Q9UJZ1; -.
TopDownProteomics; Q9UJZ1-1; -. [Q9UJZ1-1]
DNASU; 30968; -.
Ensembl; ENST00000356493; ENSP00000348886; ENSG00000165283. [Q9UJZ1-1]
Ensembl; ENST00000452248; ENSP00000395743; ENSG00000165283. [Q9UJZ1-2]
GeneID; 30968; -.
KEGG; hsa:30968; -.
UCSC; uc003zwi.5; human. [Q9UJZ1-1]
CTD; 30968; -.
DisGeNET; 30968; -.
EuPathDB; HostDB:ENSG00000165283.15; -.
GeneCards; STOML2; -.
HGNC; HGNC:14559; STOML2.
HPA; CAB015944; -.
HPA; HPA062016; -.
MIM; 608292; gene.
neXtProt; NX_Q9UJZ1; -.
OpenTargets; ENSG00000165283; -.
PharmGKB; PA37897; -.
eggNOG; KOG2620; Eukaryota.
eggNOG; COG0330; LUCA.
GeneTree; ENSGT00550000074454; -.
HOGENOM; HOG000217038; -.
HOVERGEN; HBG061488; -.
InParanoid; Q9UJZ1; -.
OMA; RDQINGQ; -.
OrthoDB; EOG091G0MSB; -.
PhylomeDB; Q9UJZ1; -.
TreeFam; TF105750; -.
Reactome; R-HSA-8949664; Processing of SMDT1.
ChiTaRS; STOML2; human.
GeneWiki; STOML2; -.
GenomeRNAi; 30968; -.
PRO; PR:Q9UJZ1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165283; -.
CleanEx; HS_STOML2; -.
ExpressionAtlas; Q9UJZ1; baseline and differential.
Genevisible; Q9UJZ1; HS.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0032623; P:interleukin-2 production; ISS:UniProtKB.
GO; GO:0010876; P:lipid localization; ISS:UniProtKB.
GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0034982; P:mitochondrial protein processing; ISS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
GO; GO:1900210; P:positive regulation of cardiolipin metabolic process; IMP:UniProtKB.
GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:UniProtKB.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:1990046; P:stress-induced mitochondrial fusion; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
InterPro; IPR001107; Band_7.
InterPro; IPR032435; Band_7_C.
InterPro; IPR001972; Stomatin_fam.
Pfam; PF01145; Band_7; 1.
Pfam; PF16200; Band_7_C; 1.
PRINTS; PR00721; STOMATIN.
SMART; SM00244; PHB; 1.
SUPFAM; SSF117892; SSF117892; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Lipid-binding; Lipoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 28 Mitochondrion. {ECO:0000305}.
CHAIN 29 356 Stomatin-like protein 2, mitochondrial.
/FTId=PRO_0000094031.
COILED 215 252 {ECO:0000255}.
MOD_RES 17 17 Phosphoserine; by PKC/PRKCZ.
{ECO:0000269|PubMed:21791414}.
MOD_RES 124 124 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 145 145 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 145 145 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99JB2}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 327 327 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 149 193 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054651.
VARIANT 129 129 L -> P (in dbSNP:rs17856326).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_026830.
CONFLICT 14 14 L -> M (in Ref. 5; AAC07983).
{ECO:0000305}.
CONFLICT 83 83 V -> I (in Ref. 4; BAD96822).
{ECO:0000305}.
CONFLICT 202 202 A -> P (in Ref. 8; AAF29073).
{ECO:0000305}.
SEQUENCE 356 AA; 38534 MW; 672331B57C82654E CRC64;
MLARAARGTG ALLLRGSLLA SGRAPRRASS GLPRNTVVLF VPQQEAWVVE RMGRFHRILE
PGLNILIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ IDGVLYLRIM DPYKASYGVE
DPEYAVTQLA QTTMRSELGK LSLDKVFRER ESLNASIVDA INQAADCWGI RCLRYEIKDI
HVPPRVKESM QMQVEAERRK RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA
AGEASAVLAK AKAKAEAIRI LAAALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTILLPS
NPGDVTSMVA QAMGVYGALT KAPVPGTPDS LSSGSSRDVQ GTDASLDEEL DRVKMS


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