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P27105 (STOM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.10 Ref.11 Ref.19

Subcellular location

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. Ref.2 Ref.9 Ref.13 Ref.14 Ref.16 Ref.19

Tissue specificity

Detected in erythrocytes (at protein level). Widely expressed. Ref.2 Ref.19

Sequence similarities

Belongs to the band 7/mec-2 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P27105-1)

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.
Isoform 2 (identifier: P27105-2)

The sequence of this isoform differs from the canonical sequence as follows:
     55-219: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Erythrocyte band 7 integral membrane protein
PRO_0000094027

Regions

Topological domain1 – 2525Cytoplasmic Potential
Intramembrane26 – 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

Natural variations

Alternative sequence55 – 219165Missing in isoform 2.
VSP_044669

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
Isoform 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

Isoform 2 [UniParc].

Checksum: 794017BC3ABB59EF
Show »

FASTA12313,475

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] [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. 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] [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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
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.
CCDSCCDS6830.1. [P27105-1]
CCDS6831.1. [P27105-2]
PIRS17659.
RefSeqNP_004090.4. NM_004099.5. [P27105-1]
NP_937837.1. NM_198194.2. [P27105-2]
UniGeneHs.253903.

3D structure databases

ProteinModelPortalP27105.
SMRP27105. Positions 94-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108354. 36 interactions.
IntActP27105. 11 interactions.
MINTMINT-5004156.
STRING9606.ENSP00000286713.

Protein family/group databases

TCDB8.A.21.1.1. the stomatin/podocin/band 7/nephrosis.2/spfh (stomatin) family.

PTM databases

PhosphoSiteP27105.

Polymorphism databases

DMDM114823.

Proteomic databases

MaxQBP27105.
PaxDbP27105.
PeptideAtlasP27105.
PRIDEP27105.

Protocols and materials databases

DNASU2040.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286713; ENSP00000286713; ENSG00000148175. [P27105-1]
ENST00000347359; ENSP00000339607; ENSG00000148175. [P27105-2]
GeneID2040.
KEGGhsa:2040.
UCSCuc004blh.4. human. [P27105-1]
uc004bli.4. human.

Organism-specific databases

CTD2040.
GeneCardsGC09M124102.
HGNCHGNC:3383. STOM.
HPAHPA010961.
HPA011419.
MIM133090. gene.
neXtProtNX_P27105.
PharmGKBPA27816.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0330.
HOGENOMHOG000217040.
HOVERGENHBG004815.
InParanoidP27105.
KOK17286.
OMAVEDFMMA.
OrthoDBEOG78D7KJ.
PhylomeDBP27105.
TreeFamTF105750.

Gene expression databases

ArrayExpressP27105.
BgeeP27105.
CleanExHS_STOM.
GenevestigatorP27105.

Family and domain databases

InterProIPR001107. Band_7.
IPR018080. Band_7/stomatin-like_CS.
IPR028515. Stomatin.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERPTHR10264. PTHR10264. 1 hit.
PTHR10264:SF49. PTHR10264:SF49. 1 hit.
PfamPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSPR00721. STOMATIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
PROSITEPS01270. BAND_7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTOM. human.
GeneWikiStomatin.
GenomeRNAi2040.
NextBio8285.
PROP27105.
SOURCESearch...

Entry information

Entry nameSTOM_HUMAN
AccessionPrimary (citable) accession number: P27105
Secondary accession number(s): B1AM77 expand/collapse secondary AC list , Q14087, Q15609, Q5VX96, Q96FK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 9

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