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Q9UJZ1

- STML2_HUMAN

UniProt

Q9UJZ1 - STML2_HUMAN

Protein

Stomatin-like protein 2, mitochondrial

Gene

STOML2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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.6 Publications

    GO - Molecular functioni

    1. cardiolipin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. receptor binding Source: ProtInc

    GO - Biological processi

    1. CD4-positive, alpha-beta T cell activation Source: UniProtKB
    2. cellular calcium ion homeostasis Source: UniProtKB
    3. interleukin-2 production Source: UniProtKB
    4. lipid localization Source: UniProtKB
    5. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    6. mitochondrial calcium ion transport Source: UniProtKB
    7. mitochondrial protein processing Source: UniProtKB
    8. mitochondrion organization Source: UniProtKB
    9. positive regulation of cardiolipin metabolic process Source: UniProtKB
    10. positive regulation of mitochondrial DNA replication Source: UniProtKB
    11. positive regulation of mitochondrial membrane potential Source: UniProtKB
    12. protein oligomerization Source: UniProtKB
    13. stress-induced mitochondrial fusion Source: UniProtKB
    14. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stomatin-like protein 2, mitochondrial
    Short name:
    SLP-2
    Alternative name(s):
    EPB72-like protein 2
    Paraprotein target 7
    Short name:
    Paratarg-7
    Gene namesi
    Name:STOML2
    Synonyms:SLP2
    ORF Names:HSPC108
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:14559. STOML2.

    Subcellular locationi

    Mitochondrion inner membrane. Mitochondrion intermembrane space. Cell membrane; Peripheral membrane protein. Membrane raft; Peripheral membrane protein
    Note: Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells.

    GO - Cellular componenti

    1. cytoskeleton Source: ProtInc
    2. extrinsic component of plasma membrane Source: UniProtKB
    3. membrane raft Source: UniProtKB
    4. mitochondrial inner membrane Source: UniProtKB
    5. mitochondrial intermembrane space Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37897.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionCuratedAdd
    BLAST
    Chaini29 – 356328Stomatin-like protein 2, mitochondrialPRO_0000094031Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine; by PKC/PRKCZ1 Publication
    Modified residuei124 – 1241Phosphotyrosine1 Publication
    Modified residuei145 – 1451N6-acetyllysine; alternate1 Publication
    Modified residuei145 – 1451N6-succinyllysine; alternateBy similarity
    Modified residuei233 – 2331N6-acetyllysine1 Publication

    Post-translational modificationi

    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.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJZ1.
    PaxDbiQ9UJZ1.
    PeptideAtlasiQ9UJZ1.
    PRIDEiQ9UJZ1.

    2D gel databases

    OGPiQ9UJZ1.
    REPRODUCTION-2DPAGEIPI00334190.

    PTM databases

    PhosphoSiteiQ9UJZ1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed at low levels. Expressed in lymphoid tissues (at protein level).3 Publications

    Inductioni

    Up-regulated in activated B- and T-cells and upon mitochondrial stress by chloramphenicol.2 Publications

    Gene expression databases

    ArrayExpressiQ9UJZ1.
    BgeeiQ9UJZ1.
    CleanExiHS_STOML2.
    GenevestigatoriQ9UJZ1.

    Organism-specific databases

    HPAiCAB015944.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi119062. 25 interactions.
    IntActiQ9UJZ1. 8 interactions.
    MINTiMINT-2999996.
    STRINGi9606.ENSP00000348886.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJZ1.
    SMRiQ9UJZ1. Positions 76-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili215 – 25238Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the band 7/mec-2 family.Curated

    Keywords - Domaini

    Coiled coil, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0330.
    HOGENOMiHOG000217038.
    HOVERGENiHBG061488.
    InParanoidiQ9UJZ1.
    OMAiDYWGIRC.
    OrthoDBiEOG77M8NR.
    PhylomeDBiQ9UJZ1.
    TreeFamiTF105750.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR001972. Stomatin_fam.
    [Graphical view]
    PANTHERiPTHR10264. PTHR10264. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    [Graphical view]
    PRINTSiPR00721. STOMATIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJZ1-1) [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

    MLARAARGTG ALLLRGSLLA SGRAPRRASS GLPRNTVVLF VPQQEAWVVE    50
    RMGRFHRILE PGLNILIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ 100
    IDGVLYLRIM DPYKASYGVE DPEYAVTQLA QTTMRSELGK LSLDKVFRER 150
    ESLNASIVDA INQAADCWGI RCLRYEIKDI HVPPRVKESM QMQVEAERRK 200
    RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA AGEASAVLAK 250
    AKAKAEAIRI LAAALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTILLPS 300
    NPGDVTSMVA QAMGVYGALT KAPVPGTPDS LSSGSSRDVQ GTDASLDEEL 350
    DRVKMS 356
    Length:356
    Mass (Da):38,534
    Last modified:May 1, 2000 - v1
    Checksum:i672331B57C82654E
    GO
    Isoform 2 (identifier: Q9UJZ1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         149-193: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:311
    Mass (Da):33,337
    Checksum:i3C391E1AFC830705
    GO

    Sequence cautioni

    The sequence AAF29073.1 differs from that shown. Reason: Frameshift at positions 14 and 26.
    The sequence AAC07983.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141L → M in AAC07983. (PubMed:15164053)Curated
    Sequence conflicti83 – 831V → I in BAD96822. 1 PublicationCurated
    Sequence conflicti202 – 2021A → P in AAF29073. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291L → P.1 Publication
    Corresponds to variant rs17856326 [ dbSNP | Ensembl ].
    VAR_026830

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei149 – 19345Missing in isoform 2. 1 PublicationVSP_054651Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190167 mRNA. Translation: AAF09142.1.
    AF282596 mRNA. Translation: AAF91466.1.
    AK027405 mRNA. Translation: BAB55091.1.
    AK303883 mRNA. Translation: BAG64819.1.
    AK223102 mRNA. Translation: BAD96822.1.
    AL353795 Genomic DNA. Translation: CAH70998.1.
    AC004472 Genomic DNA. Translation: AAC07983.1. Sequence problems.
    CH471071 Genomic DNA. Translation: EAW58395.1.
    CH471071 Genomic DNA. Translation: EAW58396.1.
    BC002442 mRNA. Translation: AAH02442.1.
    BC003025 mRNA. Translation: AAH03025.1.
    BC010152 mRNA. Translation: AAH10152.1.
    BC014990 mRNA. Translation: AAH14990.1.
    AF161458 mRNA. Translation: AAF29073.1. Frameshift.
    CCDSiCCDS6577.1. [Q9UJZ1-1]
    CCDS69588.1. [Q9UJZ1-2]
    PIRiT02246.
    RefSeqiNP_001273960.1. NM_001287031.1. [Q9UJZ1-2]
    NP_001273961.1. NM_001287032.1.
    NP_038470.1. NM_013442.2. [Q9UJZ1-1]
    UniGeneiHs.3439.

    Genome annotation databases

    EnsembliENST00000356493; ENSP00000348886; ENSG00000165283. [Q9UJZ1-1]
    ENST00000452248; ENSP00000395743; ENSG00000165283. [Q9UJZ1-2]
    GeneIDi30968.
    KEGGihsa:30968.
    UCSCiuc003zwi.3. human. [Q9UJZ1-1]

    Polymorphism databases

    DMDMi60415944.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190167 mRNA. Translation: AAF09142.1 .
    AF282596 mRNA. Translation: AAF91466.1 .
    AK027405 mRNA. Translation: BAB55091.1 .
    AK303883 mRNA. Translation: BAG64819.1 .
    AK223102 mRNA. Translation: BAD96822.1 .
    AL353795 Genomic DNA. Translation: CAH70998.1 .
    AC004472 Genomic DNA. Translation: AAC07983.1 . Sequence problems.
    CH471071 Genomic DNA. Translation: EAW58395.1 .
    CH471071 Genomic DNA. Translation: EAW58396.1 .
    BC002442 mRNA. Translation: AAH02442.1 .
    BC003025 mRNA. Translation: AAH03025.1 .
    BC010152 mRNA. Translation: AAH10152.1 .
    BC014990 mRNA. Translation: AAH14990.1 .
    AF161458 mRNA. Translation: AAF29073.1 . Frameshift.
    CCDSi CCDS6577.1. [Q9UJZ1-1 ]
    CCDS69588.1. [Q9UJZ1-2 ]
    PIRi T02246.
    RefSeqi NP_001273960.1. NM_001287031.1. [Q9UJZ1-2 ]
    NP_001273961.1. NM_001287032.1.
    NP_038470.1. NM_013442.2. [Q9UJZ1-1 ]
    UniGenei Hs.3439.

    3D structure databases

    ProteinModelPortali Q9UJZ1.
    SMRi Q9UJZ1. Positions 76-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119062. 25 interactions.
    IntActi Q9UJZ1. 8 interactions.
    MINTi MINT-2999996.
    STRINGi 9606.ENSP00000348886.

    PTM databases

    PhosphoSitei Q9UJZ1.

    Polymorphism databases

    DMDMi 60415944.

    2D gel databases

    OGPi Q9UJZ1.
    REPRODUCTION-2DPAGE IPI00334190.

    Proteomic databases

    MaxQBi Q9UJZ1.
    PaxDbi Q9UJZ1.
    PeptideAtlasi Q9UJZ1.
    PRIDEi Q9UJZ1.

    Protocols and materials databases

    DNASUi 30968.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356493 ; ENSP00000348886 ; ENSG00000165283 . [Q9UJZ1-1 ]
    ENST00000452248 ; ENSP00000395743 ; ENSG00000165283 . [Q9UJZ1-2 ]
    GeneIDi 30968.
    KEGGi hsa:30968.
    UCSCi uc003zwi.3. human. [Q9UJZ1-1 ]

    Organism-specific databases

    CTDi 30968.
    GeneCardsi GC09M035099.
    HGNCi HGNC:14559. STOML2.
    HPAi CAB015944.
    MIMi 608292. gene.
    neXtProti NX_Q9UJZ1.
    PharmGKBi PA37897.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0330.
    HOGENOMi HOG000217038.
    HOVERGENi HBG061488.
    InParanoidi Q9UJZ1.
    OMAi DYWGIRC.
    OrthoDBi EOG77M8NR.
    PhylomeDBi Q9UJZ1.
    TreeFami TF105750.

    Miscellaneous databases

    ChiTaRSi STOML2. human.
    GeneWikii STOML2.
    GenomeRNAii 30968.
    NextBioi 35477056.
    PROi Q9UJZ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJZ1.
    Bgeei Q9UJZ1.
    CleanExi HS_STOML2.
    Genevestigatori Q9UJZ1.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR001972. Stomatin_fam.
    [Graphical view ]
    PANTHERi PTHR10264. PTHR10264. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00721. STOMATIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues."
      Wang Y., Morrow J.S.
      J. Biol. Chem. 275:8062-8071(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Heart muscle.
    2. "A novel member of the stomatin/EPB72/mec-2 family, stomatin-like 2 (STOML2), is ubiquitously expressed and localizes to HSA chromosome 9p13.1."
      Owczarek C.M., Treutlein H.R., Portbury K.J., Gulluyan L.M., Kola I., Hertzog P.J.
      Cytogenet. Cell Genet. 92:196-203(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Trachea.
    4. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "DNA sequence and analysis of human chromosome 9."
      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.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1), VARIANT PRO-129.
      Tissue: Lung, Pancreas and Skin.
    8. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      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.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-356 (ISOFORM 1).
      Tissue: Umbilical cord blood.
    9. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 188-197; 201-211 AND 234-250, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    10. "Mass spectrometrical verification of stomatin-like protein 2 (SLP-2) primary structure."
      John J.P., Anrather D., Pollak A., Lubec G.
      Proteins 64:543-551(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      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.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Identification of a novel mitochondrial complex containing mitofusin 2 and stomatin-like protein 2."
      Hajek P., Chomyn A., Attardi G.
      J. Biol. Chem. 282:5670-5681(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MFN2, SUBCELLULAR LOCATION.
    13. "SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability."
      Da Cruz S., Parone P.A., Gonzalo P., Bienvenut W.V., Tondera D., Jourdain A., Quadroni M., Martinou J.C.
      Biochim. Biophys. Acta 1783:904-911(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PHB AND PHB2.
    14. Cited for: FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    15. "Downregulation of a mitochondria associated protein SLP-2 inhibits tumor cell motility, proliferation and enhances cell sensitivity to chemotherapeutic reagents."
      Wang Y., Cao W., Yu Z., Liu Z.
      Cancer Biol. Ther. 8:1651-1658(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "A frequent target of paraproteins in the sera of patients with multiple myeloma and MGUS."
      Preuss K.D., Pfreundschuh M., Ahlgrimm M., Fadle N., Regitz E., Murawski N., Grass S.
      Int. J. Cancer 125:656-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A COMMON ANTIGEN IN B-CELL NEOPLASMS.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "SLP-2 negatively modulates mitochondrial sodium-calcium exchange."
      Da Cruz S., De Marchi U., Frieden M., Parone P.A., Martinou J.C., Demaurex N.
      Cell Calcium 47:11-18(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CALCIUM HOMEOSTASIS.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Hyperphosphorylation of autoantigenic targets of paraproteins is due to inactivation of PP2A."
      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.
      Blood 118:3340-3346(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-17.
    21. "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
      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.
      Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL BIOGENESIS, SUBCELLULAR LOCATION, INTERACTION WITH PHB AND PHB2, CARDIOLIPIN-BINDING, INDUCTION.
    22. "Mitochondrial and plasma membrane pools of stomatin-like protein 2 coalesce at the immunological synapse during T cell activation."
      Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.
      PLoS ONE 7:E37144-E37144(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION.

    Entry informationi

    Entry nameiSTML2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJZ1
    Secondary accession number(s): B4E1K7
    , D3DRN3, O60376, Q53G29, Q96FY2, Q9P042
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 117 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

    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.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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