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P27105

- STOM_HUMAN

UniProt

P27105 - STOM_HUMAN

Protein

Erythrocyte band 7 integral membrane protein

Gene

STOM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.

    GO - Biological processi

    1. protein homooligomerization Source: UniProtKB

    Protein family/group databases

    TCDBi8.A.21.1.1. the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythrocyte band 7 integral membrane protein
    Alternative name(s):
    Protein 7.2b
    Stomatin
    Gene namesi
    Name:STOM
    Synonyms:BND7, EPB72
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:3383. STOM.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Melanosome. Cytoplasmic vesicle By similarity
    Note: Exposed on the cytoplasmic surface of the membrane. Associated with lipid rafts. Concentrates preferentially in plasma membrane protrusions and in a juxta-nuclear region which may represent Golgi-derived vesicles. Colocalizes with actin. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoplasm Source: HPA
    3. cytoskeleton Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProtKB
    6. integral component of plasma membrane Source: UniProtKB
    7. melanosome Source: UniProtKB-SubCell
    8. membrane Source: UniProtKB
    9. membrane raft Source: UniProtKB
    10. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821T → A: No effect on oligomerization. 1 Publication
    Mutagenesisi185 – 1851W → A: Complete loss of oligomerization. 1 Publication
    Mutagenesisi252 – 2521Y → A: Complete loss of oligomerization. 1 Publication
    Mutagenesisi263 – 2631K → A: Reduced oligomerization and lipid raft association.
    Mutagenesisi264 – 2641N → A: Reduced oligomerization and lipid raft association.
    Mutagenesisi265 – 2651S → A: Oligomerization reduced to 18%. Reduced lipid raft association.
    Mutagenesisi266 – 2661T → A: Complete loss of oligomerization. Reduced lipid raft association.
    Mutagenesisi267 – 2671I → A: Complete loss of oligomerization and lipid raft association.
    Mutagenesisi268 – 2681V → A: Complete loss of oligomerization and lipid raft association.
    Mutagenesisi269 – 2691F → A: Complete loss of oligomerization and lipid raft association.
    Mutagenesisi270 – 2701P → A: Complete loss of oligomerization. No effect on lipid raft association.
    Mutagenesisi271 – 2711L → A: Complete loss of oligomerization. Reduced lipid raft association.
    Mutagenesisi272 – 2721P → A: Oligomerization reduced to 18%. Reduced lipid raft association.
    Mutagenesisi273 – 2731I → A: Complete loss of oligomerization. Reduced lipid raft association.
    Mutagenesisi274 – 2741D → A: Reduced oligomerization and lipid raft association.
    Mutagenesisi275 – 2751M → A: Reduced oligomerization and lipid raft association.
    Mutagenesisi276 – 2761L → A: Reduced oligomerization and lipid raft association.

    Organism-specific databases

    PharmGKBiPA27816.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Erythrocyte band 7 integral membrane proteinPRO_0000094027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine; by PKA1 Publication
    Lipidationi30 – 301S-palmitoyl cysteine1 Publication
    Lipidationi87 – 871S-palmitoyl cysteine; partial1 Publication
    Modified residuei161 – 1611PhosphoserineBy similarity
    Modified residuei244 – 2441Phosphoserine1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP27105.
    PaxDbiP27105.
    PeptideAtlasiP27105.
    PRIDEiP27105.

    PTM databases

    PhosphoSiteiP27105.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level). Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiP27105.
    BgeeiP27105.
    CleanExiHS_STOM.
    GenevestigatoriP27105.

    Organism-specific databases

    HPAiHPA010961.
    HPA011419.

    Interactioni

    Subunit structurei

    Homodimer and higher order homooligomer. The homodimer is banana-shaped. Interacts with ASIC1, ASIC2 and ASIC3 By similarity. Interacts with LANCL1. Interacts with SLC2A1 and SLC4A1. Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi108354. 36 interactions.
    IntActiP27105. 11 interactions.
    MINTiMINT-5004156.
    STRINGi9606.ENSP00000286713.

    Structurei

    3D structure databases

    ProteinModelPortaliP27105.
    SMRiP27105. Positions 94-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini55 – 288234CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei26 – 5429Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 2739Required for homooligomerization
    Regioni267 – 2693Required for lipid raft association
    Regioni273 – 28715Interaction with LANCL1Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0330.
    HOGENOMiHOG000217040.
    HOVERGENiHBG004815.
    InParanoidiP27105.
    KOiK17286.
    OMAiVEDFMMA.
    OrthoDBiEOG78D7KJ.
    PhylomeDBiP27105.
    TreeFamiTF105750.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR018080. Band_7/stomatin-like_CS.
    IPR028515. Stomatin.
    IPR001972. Stomatin_fam.
    [Graphical view]
    PANTHERiPTHR10264. PTHR10264. 1 hit.
    PTHR10264:SF49. PTHR10264:SF49. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    [Graphical view]
    PRINTSiPR00721. STOMATIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]
    PROSITEiPS01270. BAND_7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P27105-1) [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

    MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI    50
    WMCIKIIKEY ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS 100
    FDIPPQEILT KDSVTISVDG VVYYRVQNAT LAVANITNAD SATRLLAQTT 150
    LRNVLGTKNL SQILSDREEI AHNMQSTLDD ATDAWGIKVE RVEIKDVKLP 200
    VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV ITESPAALQL 250
    RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG 288
    Length:288
    Mass (Da):31,731
    Last modified:January 23, 2007 - v3
    Checksum:i5FEDA92230D99A24
    GO
    Isoform 2 (identifier: P27105-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         55-219: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:123
    Mass (Da):13,475
    Checksum:i794017BC3ABB59EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61H → D in AAA58432. (PubMed:8825639)Curated
    Sequence conflicti244 – 2441S → Y in AAH10703. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei55 – 219165Missing in isoform 2. 1 PublicationVSP_044669Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60067 mRNA. Translation: CAA42671.1.
    M81635 mRNA. Translation: AAA58432.1.
    X85116, X85117 Genomic DNA. Translation: CAA59436.1.
    U33931
    , U33925, U33926, U33927, U33928, U33929, U33930 Genomic DNA. Translation: AAC50296.1. Sequence problems.
    CR542100 mRNA. Translation: CAG46897.1.
    AL359644, AL161784 Genomic DNA. Translation: CAH70728.1.
    AL359644, AL161784 Genomic DNA. Translation: CAH70729.1.
    AL161784, AL359644 Genomic DNA. Translation: CAH72706.1.
    AL161784, AL359644 Genomic DNA. Translation: CAH72707.1.
    BC010703 mRNA. Translation: AAH10703.1.
    BI603242 mRNA. No translation available.
    CCDSiCCDS6830.1. [P27105-1]
    CCDS6831.1. [P27105-2]
    PIRiS17659.
    RefSeqiNP_004090.4. NM_004099.5. [P27105-1]
    NP_937837.1. NM_198194.2. [P27105-2]
    UniGeneiHs.253903.

    Genome annotation databases

    EnsembliENST00000286713; ENSP00000286713; ENSG00000148175. [P27105-1]
    ENST00000347359; ENSP00000339607; ENSG00000148175. [P27105-2]
    GeneIDi2040.
    KEGGihsa:2040.
    UCSCiuc004blh.4. human. [P27105-1]
    uc004bli.4. human.

    Polymorphism databases

    DMDMi114823.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60067 mRNA. Translation: CAA42671.1 .
    M81635 mRNA. Translation: AAA58432.1 .
    X85116 , X85117 Genomic DNA. Translation: CAA59436.1 .
    U33931
    , U33925 , U33926 , U33927 , U33928 , U33929 , U33930 Genomic DNA. Translation: AAC50296.1 . Sequence problems.
    CR542100 mRNA. Translation: CAG46897.1 .
    AL359644 , AL161784 Genomic DNA. Translation: CAH70728.1 .
    AL359644 , AL161784 Genomic DNA. Translation: CAH70729.1 .
    AL161784 , AL359644 Genomic DNA. Translation: CAH72706.1 .
    AL161784 , AL359644 Genomic DNA. Translation: CAH72707.1 .
    BC010703 mRNA. Translation: AAH10703.1 .
    BI603242 mRNA. No translation available.
    CCDSi CCDS6830.1. [P27105-1 ]
    CCDS6831.1. [P27105-2 ]
    PIRi S17659.
    RefSeqi NP_004090.4. NM_004099.5. [P27105-1 ]
    NP_937837.1. NM_198194.2. [P27105-2 ]
    UniGenei Hs.253903.

    3D structure databases

    ProteinModelPortali P27105.
    SMRi P27105. Positions 94-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108354. 36 interactions.
    IntActi P27105. 11 interactions.
    MINTi MINT-5004156.
    STRINGi 9606.ENSP00000286713.

    Protein family/group databases

    TCDBi 8.A.21.1.1. the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.

    PTM databases

    PhosphoSitei P27105.

    Polymorphism databases

    DMDMi 114823.

    Proteomic databases

    MaxQBi P27105.
    PaxDbi P27105.
    PeptideAtlasi P27105.
    PRIDEi P27105.

    Protocols and materials databases

    DNASUi 2040.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286713 ; ENSP00000286713 ; ENSG00000148175 . [P27105-1 ]
    ENST00000347359 ; ENSP00000339607 ; ENSG00000148175 . [P27105-2 ]
    GeneIDi 2040.
    KEGGi hsa:2040.
    UCSCi uc004blh.4. human. [P27105-1 ]
    uc004bli.4. human.

    Organism-specific databases

    CTDi 2040.
    GeneCardsi GC09M124102.
    HGNCi HGNC:3383. STOM.
    HPAi HPA010961.
    HPA011419.
    MIMi 133090. gene.
    neXtProti NX_P27105.
    PharmGKBi PA27816.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0330.
    HOGENOMi HOG000217040.
    HOVERGENi HBG004815.
    InParanoidi P27105.
    KOi K17286.
    OMAi VEDFMMA.
    OrthoDBi EOG78D7KJ.
    PhylomeDBi P27105.
    TreeFami TF105750.

    Miscellaneous databases

    ChiTaRSi STOM. human.
    GeneWikii Stomatin.
    GenomeRNAii 2040.
    NextBioi 8285.
    PROi P27105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27105.
    Bgeei P27105.
    CleanExi HS_STOM.
    Genevestigatori P27105.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR018080. Band_7/stomatin-like_CS.
    IPR028515. Stomatin.
    IPR001972. Stomatin_fam.
    [Graphical view ]
    PANTHERi PTHR10264. PTHR10264. 1 hit.
    PTHR10264:SF49. PTHR10264:SF49. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00721. STOMATIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    PROSITEi PS01270. BAND_7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of cDNA encoding human erythrocyte band 7 integral membrane protein."
      Hiebl-Dirschmied C.M., Entler B., Glotzmann C., Maurer-Fogy I., Stratowa C., Prohaska R.
      Biochim. Biophys. Acta 1090:123-124(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Isolation of cDNA coding for an ubiquitous membrane protein deficient in high Na+, low K+ stomatocytic erythrocytes."
      Stewart G.W., Hepworth-Jones B.E., Keen J.N., Dash B.C.J., Argent A.C., Casimir C.M.
      Blood 79:1593-1601(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 187-232, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    3. "The organization of the gene (EPB72) encoding the human erythrocyte band 7 integral membrane protein (protein 7.2b)."
      Unfried I., Entler B., Prohaska R.
      Genomics 30:521-528(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structure, organization, and expression of the human band 7.2b gene, a candidate gene for hereditary hydrocytosis."
      Gallagher P.G., Forget B.G.
      J. Biol. Chem. 270:26358-26363(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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].
    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] (ISOFORMS 1 AND 2).
      Tissue: Eye and Hypothalamus.
    8. "Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure."
      Salzer U., Ahorn H., Prohaska R.
      Biochim. Biophys. Acta 1151:149-152(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-25, PHOSPHORYLATION AT SER-10.
    9. "Colocalization of stomatin (band 7.2b) and actin microfilaments in UAC epithelial cells."
      Snyers L., Thines-Sempoux D., Prohaska R.
      Eur. J. Cell Biol. 73:281-285(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor."
      Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A., Prohaska R.
      Biochim. Biophys. Acta 1395:301-308(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LANCL1.
      Tissue: Bone marrow, Erythrocyte and Fetal brain.
    11. "Oligomeric nature of the integral membrane protein stomatin."
      Snyers L., Umlauf E., Prohaska R.
      J. Biol. Chem. 273:17221-17226(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    12. "Cysteine 29 is the major palmitoylation site on stomatin."
      Snyers L., Umlauf E., Prohaska R.
      FEBS Lett. 449:101-104(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-30 AND CYS-87.
    13. "Stomatin is a major lipid-raft component of platelet alpha granules."
      Mairhofer M., Steiner M., Mosgoeller W., Prohaska R., Salzer U.
      Blood 100:897-904(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    15. "Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association."
      Umlauf E., Mairhofer M., Prohaska R.
      J. Biol. Chem. 281:23349-23356(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-182; TRP-185; TYR-252 AND 263-LYS--LEU-276.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
      Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
      Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SLC2A1 AND SLC4A1, SUBUNIT.

    Entry informationi

    Entry nameiSTOM_HUMAN
    AccessioniPrimary (citable) accession number: P27105
    Secondary accession number(s): B1AM77
    , Q14087, Q15609, Q5VX96, Q96FK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3