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O15400

- STX7_HUMAN

UniProt

O15400 - STX7_HUMAN

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Protein

Syntaxin-7

Gene

STX7

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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
Complete GO annotation...

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. endosome Source: UniProtKB-KW
  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
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 – 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. 68 interactions.
DIPiDIP-57384N.
IntActiO15400. 8 interactions.
MINTiMINT-5002218.
STRINGi9606.ENSP00000356918.

Structurei

3D structure databases

ProteinModelPortaliO15400.
SMRiO15400. Positions 10-227.
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.
GeneTreeiENSGT00450000040239.
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

        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:
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 10-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114003. 68 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 GC06M132767.
HGNCi HGNC:11442. STX7.
HPAi CAB062564.
HPA001467.
MIMi 603217. gene.
neXtProti NX_O15400.
PharmGKBi PA36239.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5325.
GeneTreei ENSGT00450000040239.
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

« 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(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 29, 2014
This is version 134 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