STML2_HUMAN
ID STML2_HUMAN Reviewed; 356 AA.
AC Q9UJZ1; B4E1K7; D3DRN3; O60376; Q53G29; Q96FY2; Q9P042;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Stomatin-like protein 2, mitochondrial;
DE Short=SLP-2;
DE AltName: Full=EPB72-like protein 2;
DE AltName: Full=Paraprotein target 7;
DE Short=Paratarg-7;
DE Flags: Precursor;
GN Name=STOML2; Synonyms=SLP2; ORFNames=HSPC108;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=10713127; DOI=10.1074/jbc.275.11.8062;
RA Wang Y., Morrow J.S.;
RT "Identification and characterization of human SLP-2, a novel homologue of
RT stomatin (band 7.2b) present in erythrocytes and other tissues.";
RL J. Biol. Chem. 275:8062-8071(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11435687; DOI=10.1159/000056902;
RA Owczarek C.M., Treutlein H.R., Portbury K.J., Gulluyan L.M., Kola I.,
RA Hertzog P.J.;
RT "A novel member of the stomatin/EPB72/mec-2 family, stomatin-like 2
RT (STOML2), is ubiquitously expressed and localizes to HSA chromosome
RT 9p13.1.";
RL Cytogenet. Cell Genet. 92:196-203(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-129.
RC TISSUE=Lung, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-356 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP PROTEIN SEQUENCE OF 188-197; 201-211 AND 234-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16671055; DOI=10.1002/prot.20987;
RA John J.P., Anrather D., Pollak A., Lubec G.;
RT "Mass spectrometrical verification of stomatin-like protein 2 (SLP-2)
RT primary structure.";
RL Proteins 64:543-551(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MFN2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17121834; DOI=10.1074/jbc.m608168200;
RA Hajek P., Chomyn A., Attardi G.;
RT "Identification of a novel mitochondrial complex containing mitofusin 2 and
RT stomatin-like protein 2.";
RL J. Biol. Chem. 282:5670-5681(2007).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PHB1 AND PHB2.
RX PubMed=18339324; DOI=10.1016/j.bbamcr.2008.02.006;
RA Da Cruz S., Parone P.A., Gonzalo P., Bienvenut W.V., Tondera D.,
RA Jourdain A., Quadroni M., Martinou J.C.;
RT "SLP-2 interacts with prohibitins in the mitochondrial inner membrane and
RT contributes to their stability.";
RL Biochim. Biophys. Acta 1783:904-911(2008).
RN [14]
RP FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=18641330; DOI=10.4049/jimmunol.181.3.1927;
RA Kirchhof M.G., Chau L.A., Lemke C.D., Vardhana S., Darlington P.J.,
RA Marquez M.E., Taylor R., Rizkalla K., Blanca I., Dustin M.L., Madrenas J.;
RT "Modulation of T cell activation by stomatin-like protein 2.";
RL J. Immunol. 181:1927-1936(2008).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19597348; DOI=10.4161/cbt.8.17.9283;
RA Wang Y., Cao W., Yu Z., Liu Z.;
RT "Downregulation of a mitochondria associated protein SLP-2 inhibits tumor
RT cell motility, proliferation and enhances cell sensitivity to
RT chemotherapeutic reagents.";
RL Cancer Biol. Ther. 8:1651-1658(2009).
RN [16]
RP IDENTIFICATION AS A COMMON ANTIGEN IN B-CELL NEOPLASMS.
RX PubMed=19405124; DOI=10.1002/ijc.24427;
RA Preuss K.D., Pfreundschuh M., Ahlgrimm M., Fadle N., Regitz E.,
RA Murawski N., Grass S.;
RT "A frequent target of paraproteins in the sera of patients with multiple
RT myeloma and MGUS.";
RL Int. J. Cancer 125:656-661(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP FUNCTION IN CALCIUM HOMEOSTASIS.
RX PubMed=19944461; DOI=10.1016/j.ceca.2009.10.005;
RA Da Cruz S., De Marchi U., Frieden M., Parone P.A., Martinou J.C.,
RA Demaurex N.;
RT "SLP-2 negatively modulates mitochondrial sodium-calcium exchange.";
RL Cell Calcium 47:11-18(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION AT SER-17.
RX PubMed=21791414; DOI=10.1182/blood-2011-04-351668;
RA Preuss K.D., Pfreundschuh M., Fadle N., Regitz E., Raudies S., Murwaski N.,
RA Ahlgrimm M., Bittenbring J., Klotz M., Schafer K.H., Held G., Neumann F.,
RA Grass S.;
RT "Hyperphosphorylation of autoantigenic targets of paraproteins is due to
RT inactivation of PP2A.";
RL Blood 118:3340-3346(2011).
RN [21]
RP FUNCTION IN MITOCHONDRIAL BIOGENESIS, SUBCELLULAR LOCATION, INTERACTION
RP WITH PHB1 AND PHB2, CARDIOLIPIN-BINDING, AND INDUCTION.
RX PubMed=21746876; DOI=10.1128/mcb.05393-11;
RA Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B.,
RA Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.;
RT "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial
RT biogenesis and function.";
RL Mol. Cell. Biol. 31:3845-3856(2011).
RN [22]
RP FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, AND
RP HOMOOLIGOMERIZATION.
RX PubMed=22623988; DOI=10.1371/journal.pone.0037144;
RA Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.;
RT "Mitochondrial and plasma membrane pools of stomatin-like protein 2
RT coalesce at the immunological synapse during T cell activation.";
RL PLoS ONE 7:E37144-E37144(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Mitochondrial protein that probably regulates the biogenesis
CC and the activity of mitochondria. Stimulates cardiolipin biosynthesis,
CC binds cardiolipin-enriched membranes where it recruits and stabilizes
CC some proteins including prohibitin and may therefore act in the
CC organization of functional microdomains in mitochondrial membranes.
CC Through regulation of the mitochondrial function may play a role into
CC several biological processes including cell migration, cell
CC proliferation, T-cell activation, calcium homeostasis and cellular
CC response to stress. May play a role in calcium homeostasis through
CC negative regulation of calcium efflux from mitochondria. Required for
CC mitochondrial hyperfusion a pro-survival cellular response to stress
CC which results in increased ATP production by mitochondria. May also
CC regulate the organization of functional domains at the plasma membrane
CC and play a role in T-cell activation through association with the T-
CC cell receptor signaling complex and its regulation.
CC {ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18641330,
CC ECO:0000269|PubMed:19597348, ECO:0000269|PubMed:19944461,
CC ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with MFN2; may form
CC heterooligomers. Interacts with CACNA2D2 (By similarity). Interacts
CC with PHB1 and PHB2; recruits them to cardiolipin-enriched mitochondrial
CC membranes and stabilizes them. {ECO:0000250,
CC ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18339324,
CC ECO:0000269|PubMed:21746876}.
CC -!- INTERACTION:
CC Q9UJZ1; Q99700-5: ATXN2; NbExp=3; IntAct=EBI-1044428, EBI-25891409;
CC Q9UJZ1; O43933: PEX1; NbExp=3; IntAct=EBI-1044428, EBI-988601;
CC Q9UJZ1; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-1044428, EBI-712367;
CC Q9UJZ1; O76024: WFS1; NbExp=3; IntAct=EBI-1044428, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10713127,
CC ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876,
CC ECO:0000269|PubMed:22623988}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10713127}. Mitochondrion
CC {ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:19597348,
CC ECO:0000269|PubMed:22623988}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18339324,
CC ECO:0000269|PubMed:21746876}; Lipid-anchor
CC {ECO:0000269|PubMed:21746876}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:17121834}. Membrane raft
CC {ECO:0000269|PubMed:18641330}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330}.
CC Note=Behaves as an integral membrane protein of the mitochondrion
CC despite the absence of a detectable transmembrane domain
CC (PubMed:21746876). Also associates with the actin cytoskeleton and
CC membrane rafts in activated T-cells (PubMed:18641330, PubMed:10713127).
CC A minor pool is associated with the plasma membrane and is enriched at
CC the immunological synapse in activated T-cells (PubMed:22623988).
CC {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330,
CC ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJZ1-2; Sequence=VSP_054651;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Expressed in
CC lymphoid tissues (at protein level). {ECO:0000269|PubMed:10713127,
CC ECO:0000269|PubMed:11435687, ECO:0000269|PubMed:18641330}.
CC -!- INDUCTION: Up-regulated in activated B- and T-cells and upon
CC mitochondrial stress by chloramphenicol. {ECO:0000269|PubMed:18641330,
CC ECO:0000269|PubMed:21746876}.
CC -!- PTM: Hyperphosphorylated at Ser-17 in some patients with monoclonal
CC gammopathy of undetermined significance (MGUS), multiple myeloma (MM)
CC and Waldenstrom macroglobulinemia due to impaired dephosphorylation by
CC PP2A.
CC -!- MISCELLANEOUS: Paratarg-7/STOML2 is a frequent autoantigenic target in
CC monoclonal gammopathy of undetermined significance (MGUS), multiple
CC myeloma (MM) and Waldenstrom macroglobulinemia, 3 B-cell neoplasms
CC associated with excessive secretion of a single monoclonal
CC gammaglobulin (also named paraprotein) in the blood.
CC {ECO:0000305|PubMed:19405124}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC07983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF29073.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/STOML2ID44346ch9p13.html";
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DR EMBL; AF190167; AAF09142.1; -; mRNA.
DR EMBL; AF282596; AAF91466.1; -; mRNA.
DR EMBL; AK027405; BAB55091.1; -; mRNA.
DR EMBL; AK303883; BAG64819.1; -; mRNA.
DR EMBL; AK223102; BAD96822.1; -; mRNA.
DR EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004472; AAC07983.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471071; EAW58395.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58396.1; -; Genomic_DNA.
DR EMBL; BC002442; AAH02442.1; -; mRNA.
DR EMBL; BC003025; AAH03025.1; -; mRNA.
DR EMBL; BC010152; AAH10152.1; -; mRNA.
DR EMBL; BC014990; AAH14990.1; -; mRNA.
DR EMBL; AF161458; AAF29073.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6577.1; -. [Q9UJZ1-1]
DR CCDS; CCDS69588.1; -. [Q9UJZ1-2]
DR PIR; T02246; T02246.
DR RefSeq; NP_001273960.1; NM_001287031.1. [Q9UJZ1-2]
DR RefSeq; NP_001273961.1; NM_001287032.1.
DR RefSeq; NP_038470.1; NM_013442.2. [Q9UJZ1-1]
DR AlphaFoldDB; Q9UJZ1; -.
DR SMR; Q9UJZ1; -.
DR BioGRID; 119062; 241.
DR IntAct; Q9UJZ1; 80.
DR MINT; Q9UJZ1; -.
DR STRING; 9606.ENSP00000348886; -.
DR GlyGen; Q9UJZ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJZ1; -.
DR MetOSite; Q9UJZ1; -.
DR PhosphoSitePlus; Q9UJZ1; -.
DR SwissPalm; Q9UJZ1; -.
DR BioMuta; STOML2; -.
DR DMDM; 60415944; -.
DR OGP; Q9UJZ1; -.
DR REPRODUCTION-2DPAGE; IPI00334190; -.
DR CPTAC; CPTAC-595; -.
DR CPTAC; CPTAC-596; -.
DR EPD; Q9UJZ1; -.
DR jPOST; Q9UJZ1; -.
DR MassIVE; Q9UJZ1; -.
DR MaxQB; Q9UJZ1; -.
DR PaxDb; Q9UJZ1; -.
DR PeptideAtlas; Q9UJZ1; -.
DR PRIDE; Q9UJZ1; -.
DR ProteomicsDB; 5767; -.
DR ProteomicsDB; 84697; -. [Q9UJZ1-1]
DR TopDownProteomics; Q9UJZ1-1; -. [Q9UJZ1-1]
DR Antibodypedia; 25758; 277 antibodies from 29 providers.
DR DNASU; 30968; -.
DR Ensembl; ENST00000356493.10; ENSP00000348886.5; ENSG00000165283.16. [Q9UJZ1-1]
DR Ensembl; ENST00000452248.6; ENSP00000395743.2; ENSG00000165283.16. [Q9UJZ1-2]
DR GeneID; 30968; -.
DR KEGG; hsa:30968; -.
DR MANE-Select; ENST00000356493.10; ENSP00000348886.5; NM_013442.3; NP_038470.1.
DR UCSC; uc003zwi.5; human. [Q9UJZ1-1]
DR CTD; 30968; -.
DR DisGeNET; 30968; -.
DR GeneCards; STOML2; -.
DR HGNC; HGNC:14559; STOML2.
DR HPA; ENSG00000165283; Low tissue specificity.
DR MIM; 608292; gene.
DR neXtProt; NX_Q9UJZ1; -.
DR OpenTargets; ENSG00000165283; -.
DR PharmGKB; PA37897; -.
DR VEuPathDB; HostDB:ENSG00000165283; -.
DR eggNOG; KOG2620; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR InParanoid; Q9UJZ1; -.
DR OMA; TQIRAEM; -.
DR OrthoDB; 1237942at2759; -.
DR PhylomeDB; Q9UJZ1; -.
DR TreeFam; TF105750; -.
DR PathwayCommons; Q9UJZ1; -.
DR Reactome; R-HSA-8949664; Processing of SMDT1.
DR SignaLink; Q9UJZ1; -.
DR SIGNOR; Q9UJZ1; -.
DR BioGRID-ORCS; 30968; 47 hits in 1092 CRISPR screens.
DR ChiTaRS; STOML2; human.
DR GeneWiki; STOML2; -.
DR GenomeRNAi; 30968; -.
DR Pharos; Q9UJZ1; Tbio.
DR PRO; PR:Q9UJZ1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UJZ1; protein.
DR Bgee; ENSG00000165283; Expressed in apex of heart and 201 other tissues.
DR ExpressionAtlas; Q9UJZ1; baseline and differential.
DR Genevisible; Q9UJZ1; HS.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010876; P:lipid localization; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:1900210; P:positive regulation of cardiolipin metabolic process; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:UniProtKB.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IMP:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR032435; Band_7_C.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF16200; Band_7_C; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Lipid-binding; Lipoprotein;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 29..356
FT /note="Stomatin-like protein 2, mitochondrial"
FT /id="PRO_0000094031"
FT REGION 321..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..252
FT /evidence="ECO:0000255"
FT COMPBIAS 326..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000269|PubMed:21791414"
FT MOD_RES 124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 145
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 145
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JB2"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 149..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054651"
FT VARIANT 129
FT /note="L -> P (in dbSNP:rs17856326)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026830"
FT CONFLICT 14
FT /note="L -> M (in Ref. 5; AAC07983)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="V -> I (in Ref. 4; BAD96822)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> P (in Ref. 8; AAF29073)"
FT /evidence="ECO:0000305"
SQ 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
