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P27105

- STOM_HUMAN

UniProt

P27105 - STOM_HUMAN

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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

Functioni

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

GO - Biological processi

  1. protein homooligomerization Source: UniProtKB
  2. regulation of acid-sensing ion channel activity Source: Ensembl
Complete GO annotation...

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. cytoplasmic vesicle Source: UniProtKB-KW
  4. cytoskeleton Source: UniProtKB
  5. extracellular space Source: UniProt
  6. extracellular vesicular exosome Source: UniProtKB
  7. integral component of plasma membrane Source: UniProtKB
  8. membrane Source: UniProtKB
  9. membrane raft Source: UniProtKB
  10. vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiP27105.
CleanExiHS_STOM.
ExpressionAtlasiP27105. baseline and differential.
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. 42 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.
GeneTreeiENSGT00550000074454.
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

        10         20         30         40         50
MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI
60 70 80 90 100
WMCIKIIKEY ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS
110 120 130 140 150
FDIPPQEILT KDSVTISVDG VVYYRVQNAT LAVANITNAD SATRLLAQTT
160 170 180 190 200
LRNVLGTKNL SQILSDREEI AHNMQSTLDD ATDAWGIKVE RVEIKDVKLP
210 220 230 240 250
VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV ITESPAALQL
260 270 280
RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG
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. 42 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.
GeneTreei ENSGT00550000074454.
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

Bgeei P27105.
CleanExi HS_STOM.
ExpressionAtlasi P27105. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 146 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