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Protein

Syntaxin-7

Gene

STX7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. chloride channel inhibitor activity Source: UniProtKB
  2. SNAP receptor activity Source: GO_Central
  3. SNARE binding Source: MGI
  4. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: GO_Central
  2. organelle assembly Source: UniProtKB
  3. organelle localization Source: UniProtKB
  4. positive regulation of receptor localization to synapse Source: UniProtKB
  5. positive regulation of T cell mediated cytotoxicity Source: UniProtKB
  6. regulation of protein localization to plasma membrane Source: UniProtKB
  7. vesicle docking Source: GO_Central
  8. vesicle fusion Source: GO_Central
Complete GO annotation...

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:11442. STX7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 238237CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei239 – 25921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini260 – 2612VesicularSequence Analysis

GO - Cellular componenti

  1. azurophil granule Source: UniProtKB
  2. early endosome Source: UniProtKB
  3. early endosome membrane Source: UniProtKB-SubCell
  4. endocytic vesicle Source: UniProtKB
  5. endomembrane system Source: GO_Central
  6. endosome Source: UniProtKB
  7. extracellular vesicular exosome Source: UniProtKB
  8. immunological synapse Source: UniProtKB
  9. integral component of membrane Source: GO_Central
  10. intracellular membrane-bounded organelle Source: HPA
  11. late endosome Source: UniProtKB
  12. lysosomal membrane Source: UniProtKB
  13. lysosome Source: UniProtKB
  14. perinuclear region of cytoplasm Source: UniProtKB
  15. plasma membrane Source: UniProtKB
  16. recycling endosome Source: UniProtKB
  17. SNARE complex Source: GO_Central
  18. tertiary granule Source: UniProtKB
  19. vesicle Source: UniProtKB
Complete GO annotation...

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 – 2051Phosphoserine1 Publication

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

Structurei

3D structure databases

ProteinModelPortaliO15400.
SMRiO15400. Positions 10-227.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiO15400.
KOiK08488.
OMAiKNLVSWE.
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. AlignAdd to basket

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

        10         20         30         40         50
MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ
60 70 80 90 100
QLQQKQQYTN QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS
110 120 130 140 150
LTNFQKVQRQ AAEREKEFVA RVRASSRVSG SFPEDSSKER NLVSWESQTQ
160 170 180 190 200
PQVQVQDEEI TEDDLRLIHE RESSIRQLEA DIMDINEIFK DLGMMIHEQG
210 220 230 240 250
DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI IILILVIGVA
260
IISLIIWGLN H
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliO15400.
SMRiO15400. Positions 10-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114003. 68 interactions.
DIPiDIP-57384N.
IntActiO15400. 8 interactions.
MINTiMINT-5002218.
STRINGi9606.ENSP00000356918.

PTM databases

PhosphoSiteiO15400.

2D gel databases

OGPiO15400.

Proteomic databases

MaxQBiO15400.
PaxDbiO15400.
PRIDEiO15400.

Protocols and materials databases

DNASUi8417.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8417.
GeneCardsiGC06M132767.
HGNCiHGNC:11442. STX7.
HPAiCAB062564.
HPA001467.
MIMi603217. gene.
neXtProtiNX_O15400.
PharmGKBiPA36239.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5325.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiO15400.
KOiK08488.
OMAiKNLVSWE.
OrthoDBiEOG7B31PS.
PhylomeDBiO15400.
TreeFamiTF315607.

Miscellaneous databases

ChiTaRSiSTX7. human.
GeneWikiiSTX7.
GenomeRNAii8417.
NextBioi31504.
PMAP-CutDBO15400.
PROiO15400.
SOURCEiSearch...

Gene expression databases

BgeeiO15400.
CleanExiHS_STX7.
GenevestigatoriO15400.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle trafficking to lysosomes."
    Wang H., Frelin L., Pevsner J.
    Gene 199:39-48(1996) [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(2002) [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(2003) [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(2002) [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(1998) [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(1999) [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(2000) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2008) [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(2010) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.