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O15400

- STX7_HUMAN

UniProt

O15400 - STX7_HUMAN

Protein

Syntaxin-7

Gene

STX7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.

    GO - Molecular functioni

    1. SNAP receptor activity Source: RefGenome
    2. SNARE binding Source: MGI

    GO - Biological processi

    1. intracellular protein transport Source: RefGenome
    2. post-Golgi vesicle-mediated transport Source: ProtInc
    3. synaptic vesicle exocytosis Source: RefGenome

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Syntaxin-7
    Gene namesi
    Name:STX7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11442. STX7.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. intracellular membrane-bounded organelle Source: HPA
    5. lysosomal membrane Source: UniProtKB
    6. perinuclear region of cytoplasm Source: Ensembl
    7. SNARE complex Source: RefGenome

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36239.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 261260Syntaxin-7PRO_0000210213Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei45 – 451PhosphoserineBy similarity
    Modified residuei79 – 791PhosphothreonineBy similarity
    Modified residuei125 – 1251PhosphoserineBy similarity
    Modified residuei126 – 1261PhosphoserineBy similarity
    Modified residuei129 – 1291Phosphoserine2 Publications
    Modified residuei205 – 2051PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO15400.
    PaxDbiO15400.
    PRIDEiO15400.

    2D gel databases

    OGPiO15400.

    PTM databases

    PhosphoSiteiO15400.

    Miscellaneous databases

    PMAP-CutDBO15400.

    Expressioni

    Tissue specificityi

    Highest expression is found in placenta followed by heart, skeletal muscle, kidney and brain. Low expression is found in pancreas, lung and liver.

    Gene expression databases

    BgeeiO15400.
    CleanExiHS_STX7.
    GenevestigatoriO15400.

    Organism-specific databases

    HPAiCAB062564.
    HPA001467.

    Interactioni

    Subunit structurei

    Forms a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late endosomes with lysosomes By similarity. Interacts with VPS11, VPS16 and VPS18. Interacts with VPS33A.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi114003. 35 interactions.
    DIPiDIP-57384N.
    IntActiO15400. 8 interactions.
    MINTiMINT-5002218.
    STRINGi9606.ENSP00000356918.

    Structurei

    3D structure databases

    ProteinModelPortaliO15400.
    SMRiO15400. Positions 10-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 238237CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini260 – 2612VesicularSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei239 – 25921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 22763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili47 – 6923Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the syntaxin family.Curated
    Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5325.
    HOGENOMiHOG000188453.
    HOVERGENiHBG053083.
    InParanoidiO15400.
    KOiK08488.
    OMAiTHIENAV.
    OrthoDBiEOG7B31PS.
    PhylomeDBiO15400.
    TreeFamiTF315607.

    Family and domain databases

    InterProiIPR006012. Syntaxin/epimorphin_CS.
    IPR006011. Syntaxin_N.
    IPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PfamiPF05739. SNARE. 1 hit.
    [Graphical view]
    SMARTiSM00503. SynN. 1 hit.
    SM00397. t_SNARE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47661. SSF47661. 1 hit.
    PROSITEiPS00914. SYNTAXIN. 1 hit.
    PS50192. T_SNARE. 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: O15400-1) [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

    MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ    50
    QLQQKQQYTN QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS 100
    LTNFQKVQRQ AAEREKEFVA RVRASSRVSG SFPEDSSKER NLVSWESQTQ 150
    PQVQVQDEEI TEDDLRLIHE RESSIRQLEA DIMDINEIFK DLGMMIHEQG 200
    DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI IILILVIGVA 250
    IISLIIWGLN H 261
    Length:261
    Mass (Da):29,816
    Last modified:January 23, 2007 - v4
    Checksum:i42AC173F0233ACDA
    GO
    Isoform 2 (identifier: O15400-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         232-261: RKSRKTLCIIILILVIGVAIISLIIWGLNH → KKDSCMLM

    Note: No experimental confirmation available.

    Show »
    Length:239
    Mass (Da):27,400
    Checksum:i6F35F3042EECF335
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121A → T in AAC51851. (PubMed:9358037)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei232 – 26130RKSRK…WGLNH → KKDSCMLM in isoform 2. CuratedVSP_012938Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77942 mRNA. Translation: AAC51851.1.
    AL357034 Genomic DNA. Translation: CAI15716.1.
    AL357034 Genomic DNA. Translation: CAI15717.1.
    AL589691 Genomic DNA. Translation: CAI16816.1.
    AL589691 Genomic DNA. Translation: CAI16817.1.
    CH471051 Genomic DNA. Translation: EAW48029.1.
    CH471051 Genomic DNA. Translation: EAW48030.1.
    BC011975 mRNA. Translation: AAH11975.1.
    CCDSiCCDS5153.1. [O15400-1]
    RefSeqiNP_003560.2. NM_003569.2. [O15400-1]
    UniGeneiHs.593148.
    Hs.605992.

    Genome annotation databases

    EnsembliENST00000367937; ENSP00000356914; ENSG00000079950. [O15400-2]
    ENST00000367941; ENSP00000356918; ENSG00000079950. [O15400-1]
    GeneIDi8417.
    KEGGihsa:8417.
    UCSCiuc003qdg.2. human. [O15400-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77942 mRNA. Translation: AAC51851.1 .
    AL357034 Genomic DNA. Translation: CAI15716.1 .
    AL357034 Genomic DNA. Translation: CAI15717.1 .
    AL589691 Genomic DNA. Translation: CAI16816.1 .
    AL589691 Genomic DNA. Translation: CAI16817.1 .
    CH471051 Genomic DNA. Translation: EAW48029.1 .
    CH471051 Genomic DNA. Translation: EAW48030.1 .
    BC011975 mRNA. Translation: AAH11975.1 .
    CCDSi CCDS5153.1. [O15400-1 ]
    RefSeqi NP_003560.2. NM_003569.2. [O15400-1 ]
    UniGenei Hs.593148.
    Hs.605992.

    3D structure databases

    ProteinModelPortali O15400.
    SMRi O15400. Positions 10-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114003. 35 interactions.
    DIPi DIP-57384N.
    IntActi O15400. 8 interactions.
    MINTi MINT-5002218.
    STRINGi 9606.ENSP00000356918.

    PTM databases

    PhosphoSitei O15400.

    2D gel databases

    OGPi O15400.

    Proteomic databases

    MaxQBi O15400.
    PaxDbi O15400.
    PRIDEi O15400.

    Protocols and materials databases

    DNASUi 8417.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367937 ; ENSP00000356914 ; ENSG00000079950 . [O15400-2 ]
    ENST00000367941 ; ENSP00000356918 ; ENSG00000079950 . [O15400-1 ]
    GeneIDi 8417.
    KEGGi hsa:8417.
    UCSCi uc003qdg.2. human. [O15400-1 ]

    Organism-specific databases

    CTDi 8417.
    GeneCardsi GC06M132822.
    HGNCi HGNC:11442. STX7.
    HPAi CAB062564.
    HPA001467.
    MIMi 603217. gene.
    neXtProti NX_O15400.
    PharmGKBi PA36239.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5325.
    HOGENOMi HOG000188453.
    HOVERGENi HBG053083.
    InParanoidi O15400.
    KOi K08488.
    OMAi THIENAV.
    OrthoDBi EOG7B31PS.
    PhylomeDBi O15400.
    TreeFami TF315607.

    Miscellaneous databases

    ChiTaRSi STX7. human.
    GeneWikii STX7.
    GenomeRNAii 8417.
    NextBioi 31504.
    PMAP-CutDB O15400.
    PROi O15400.
    SOURCEi Search...

    Gene expression databases

    Bgeei O15400.
    CleanExi HS_STX7.
    Genevestigatori O15400.

    Family and domain databases

    InterProi IPR006012. Syntaxin/epimorphin_CS.
    IPR006011. Syntaxin_N.
    IPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    Pfami PF05739. SNARE. 1 hit.
    [Graphical view ]
    SMARTi SM00503. SynN. 1 hit.
    SM00397. t_SNARE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47661. SSF47661. 1 hit.
    PROSITEi PS00914. SYNTAXIN. 1 hit.
    PS50192. T_SNARE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle trafficking to lysosomes."
      Wang H., Frelin L., Pevsner J.
      Gene 199:39-48(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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).
      Tissue: Ovary.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2.
      Tissue: Platelet.
    6. "Differential roles of syntaxin 7 and syntaxin 8 in endosomal trafficking."
      Prekeris R., Yang B., Oorschot V., Klumperman J., Scheller R.H.
      Mol. Biol. Cell 10:3891-3908(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Syntaxin 7 mediates endocytic trafficking to late endosomes."
      Nakamura N., Yamamoto A., Wada Y., Futai M.
      J. Biol. Chem. 275:6523-6529(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7."
      Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S., Akazawa C.
      J. Biol. Chem. 276:29393-29402(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS11; VPS16; VPS18 AND VPS33A.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTX7_HUMAN
    AccessioniPrimary (citable) accession number: O15400
    Secondary accession number(s): E1P579, Q5SZW2, Q96ES9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 4 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 6
      Human chromosome 6: 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