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Reviewed, UniProtKB/Swiss-Prot P27105 (STOM_HUMAN)

Last modified November 3, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Erythrocyte band 7 integral membrane protein
Alternative name(s):
    Stomatin
    Protein 7.2b
Gene names
Name: STOM
Synonyms: BND7, EPB72
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Thought to regulate cation conductance. May regulate ACCN1 and ACCN3 gating By similarity.

Subunit structure

Homooligomer containing between 9 and 12 monomers. Interacts with ACCN1, ACCN2 and ACCN3 By similarity. Interacts with LANCL1.

Subcellular location

Cell membrane; Single-pass membrane protein; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Melanosome. 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. Ref.2 Ref.9 Ref.13 Ref.14 Ref.16

Tissue specificity

Widely expressed. Ref.2

Involvement in disease

Stomatin is deficient in overhydrated hereditary stomatocytosis (OHS); also known as cryohydrocytosis or hereditary stomatocytosis. OHS results in red cell anomaly associated with hemolytic anemia. There is increased Na+/K+-permeability and hence a disorder of cell volume control. The nature of the molecular defect underlying OHS is unknown.

Sequence similarities

Belongs to the band 7/mec-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 288287Erythrocyte band 7 integral membrane protein
PRO_0000094027

Regions

Topological domain2 – 2524Cytoplasmic Potential
Transmembrane26 – 5429 Potential
Topological domain55 – 288234Cytoplasmic Potential
Region265 – 2739Required for homooligomerization
Region267 – 2693Required for lipid raft association
Region273 – 28715Interaction with LANCL1

Amino acid modifications

Modified residue101Phosphoserine; by PKA Ref.8
Modified residue1611Phosphoserine By similarity
Modified residue2441Phosphoserine Ref.17
Lipidation301S-palmitoyl cysteine Ref.12
Lipidation871S-palmitoyl cysteine; partial Ref.12

Experimental info

Mutagenesis1821T → A: No effect on oligomerization. Ref.15
Mutagenesis1851W → A: Complete loss of oligomerization. Ref.15
Mutagenesis2521Y → A: Complete loss of oligomerization. Ref.15
Mutagenesis2631K → A: Reduced oligomerization and lipid raft association.
Mutagenesis2641N → A: Reduced oligomerization and lipid raft association.
Mutagenesis2651S → A: Oligomerization reduced to 18%. Reduced lipid raft association.
Mutagenesis2661T → A: Complete loss of oligomerization. Reduced lipid raft association.
Mutagenesis2671I → A: Complete loss of oligomerization and lipid raft association.
Mutagenesis2681V → A: Complete loss of oligomerization and lipid raft association.
Mutagenesis2691F → A: Complete loss of oligomerization and lipid raft association.
Mutagenesis2701P → A: Complete loss of oligomerization. No effect on lipid raft association.
Mutagenesis2711L → A: Complete loss of oligomerization. Reduced lipid raft association.
Mutagenesis2721P → A: Oligomerization reduced to 18%. Reduced lipid raft association.
Mutagenesis2731I → A: Complete loss of oligomerization. Reduced lipid raft association.
Mutagenesis2741D → A: Reduced oligomerization and lipid raft association.
Mutagenesis2751M → A: Reduced oligomerization and lipid raft association.
Mutagenesis2761L → A: Reduced oligomerization and lipid raft association.
Sequence conflict61H → D in AAA58432. Ref.3
Sequence conflict2441S → Y in AAH10703. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P27105-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5FEDA92230D99A24

FASTA28831,731
        10         20         30         40         50         60 
MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY 

        70         80         90        100        110        120 
ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG 

       130        140        150        160        170        180 
VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD 

       190        200        210        220        230        240 
ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV 

       250        260        270        280 
ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG 

« Hide

References

« Hide 'large scale' references
[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: 1883838] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 1547348] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 8825639] [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: 7592848] [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].
[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. expand/collapse author list , 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: 15164053] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[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: 8373790] [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: 9243190] [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: 9512664] [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: 9642292] [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: 10338112] [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: 12130500] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 16766530] [Abstract]
Cited for: MUTAGENESIS OF THR-182; TRP-185; TYR-252 AND 263-LYS--LEU-276.
[16]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY.
[18]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X60067 mRNA. Translation: CAA42671.1.
M81635 mRNA. Translation: AAA58432.1.
X85116, X85117 Genomic DNA. Translation: CAA59436.1.
U33931 expand/collapse EMBL AC list , 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.
AL161784, AL359644 Genomic DNA. Translation: CAH72707.1.
BC010703 mRNA. Translation: AAH10703.1.
IPIIPI00219682.
PIRS17659.
RefSeqNP_004090.4.
NP_937837.1.
UniGeneHs.253903

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP27105. 6 interactions.
STRINGP27105.

Protein family/group databases

TCDB8.A.21.1.1. stomatin/podocin/band 7/nephrosis.2/SPFH (Stomatin) family.

PTM databases

PhosphoSiteP27105.

Proteomic databases

PeptideAtlasP27105.
PRIDEP27105.

Genome annotation databases

EnsemblENST00000286713; ENSP00000286713; ENSG00000148175; Homo sapiens. [Genome view]
ENST00000347359; ENSP00000339607; ENSG00000148175; Homo sapiens. [Genome view]
ENST00000442659; ENSP00000408675; ENSG00000148175; Homo sapiens. [Genome view]
GeneID2040.
KEGGhsa:2040.
UCSCuc004blh.1. human.

Organism-specific databases

CTD2040.
GeneCardsGC09M123141.
H-InvDBHIX0020447.
HIX0058680.
HGNCHGNC:3383. STOM.
HPAHPA010961.
HPA011419.
MIM133090. gene.
PharmGKBPA27816.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP27105.
HOVERGENP27105.
OMATMVRAIA.

Gene expression databases

ArrayExpressP27105.
BgeeP27105.
CleanExHS_STOM.
GenevestigatorP27105.
GermOnlineENSG00000148175. Homo sapiens.

Family and domain databases

InterProIPR001107. Band_7.
IPR018080. Band_7/stomatin-like_CS.
IPR001972. Stomatin.
[Graphical view]
PfamPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSPR00721. STOMATIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
PROSITEPS01270. BAND_7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8285.
SOURCESearch...

Entry information

Entry nameSTOM_HUMAN
AccessionPrimary (citable) accession number: P27105
Secondary accession number(s): Q14087 expand/collapse secondary AC list , Q15609, Q5VX96, Q96FK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents