O15400 (STX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Syntaxin-7

Gene names

Name:

STX7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Forms a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Interacts with VPS33A. Found in a complex with VAMP8 and VTI1B in the liver. Part of the SNARE core complex containing VAMP8, STX8 and VTI1B By similarity. Interacts with VPS11, VPS16 and VPS18.
Subcellular location	Early endosome membrane; Single-pass type IV membrane protein By similarity.
Tissue specificity	Highest expression is found in placenta followed by heart, skeletal muscle, kidney and brain. Low expression is found in pancreas, lung and liver.
Sequence similarities	Belongs to the syntaxin family. Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
Cellular component	Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Inferred from Biological aspect of Ancestor. Source: RefGenome post-Golgi vesicle-mediated transport Traceable author statement Ref.1. Source: ProtInc synaptic vesicle exocytosis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	SNARE complex Inferred from Biological aspect of Ancestor. Source: RefGenome early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	SNAP receptor activity Inferred from Biological aspect of Ancestor. Source: RefGenome SNARE binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15400-1)

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: O15400-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 261	260	Syntaxin-7		PRO_0000210213
Regions
	Topological domain	2 – 238	237	Cytoplasmic Potential
	Transmembrane	239 – 259	21	Helical; Anchor for type IV membrane protein; Potential
	Topological domain	260 – 261	2	Vesicular Potential
	Domain	165 – 227	63	t-SNARE coiled-coil homology
	Coiled coil	47 – 69	23	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	45	1	Phosphoserine By similarity
	Modified residue	79	1	Phosphothreonine By similarity
	Modified residue	125	1	Phosphoserine By similarity
	Modified residue	126	1	Phosphoserine By similarity
	Modified residue	129	1	Phosphoserine Ref.8 Ref.11
	Modified residue	205	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	232 – 261	30	RKSRK…WGLNH → KKDSCMLM in isoform 2.		VSP_012938
Experimental info
	Sequence conflict	12	1	A → T in AAC51851. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 42AC173F0233ACDA	FASTA	261	29,816
	10 20 30 40 50 60 MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN 70 80 90 100 110 120 QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKVQRQ AAEREKEFVA 130 140 150 160 170 180 RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA 190 200 210 220 230 240 DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI 250 260 IILILVIGVA IISLIIWGLN H
	Isoform 2 [UniParc]. Checksum: 6F35F3042EECF335	FASTA	239	27,400
	10 20 30 40 50 60 MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN 70 80 90 100 110 120 QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKVQRQ AAEREKEFVA 130 140 150 160 170 180 RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA 190 200 210 220 230 DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QKKDSCMLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"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-129, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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.
[10]	"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].
[11]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00289876. IPI00552913.
RefSeq	NP_003560.2. NM_003569.2.
UniGene	Hs.593148. Hs.605992.
3D structure databases
ProteinModelPortal	O15400.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15400. 1 interaction.
STRING	9606.ENSP00000356918.
PTM databases
PhosphoSite	O15400.
2D gel databases
OGP	O15400.
Proteomic databases
PaxDb	O15400.
PRIDE	O15400.
Protocols and materials databases
DNASU	8417.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367937; ENSP00000356914; ENSG00000079950. ENST00000367941; ENSP00000356918; ENSG00000079950. ENST00000448348; ENSP00000412202; ENSG00000079950.
GeneID	8417.
KEGG	hsa:8417.
UCSC	uc003qdg.2. human.
Organism-specific databases
CTD	8417.
GeneCards	GC06M132822.
HGNC	HGNC:11442. STX7.
HPA	HPA001467.
MIM	603217. gene.
neXtProt	NX_O15400.
PharmGKB	PA36239.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5325.
HOGENOM	HOG000188453.
HOVERGEN	HBG053083.
InParanoid	O15400.
KO	K08488.
OMA	VEQTSIF.
OrthoDB	EOG41NTN3.
PhylomeDB	O15400.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_13685. Neuronal System.
Gene expression databases
Bgee	O15400.
CleanEx	HS_STX7.
Genevestigator	O15400.
GermOnline	ENSG00000079950. Homo sapiens.
Family and domain databases
InterPro	IPR006012. Syntaxin/epimorphin_CS. IPR006011. Syntaxin_N. IPR010989. t-SNARE. IPR000727. T_SNARE_dom. [Graphical view]
Pfam	PF05739. SNARE. 1 hit. PF00804. Syntaxin. 1 hit. [Graphical view]
SMART	SM00503. SynN. 1 hit. SM00397. t_SNARE. 1 hit. [Graphical view]
SUPFAM	SSF47661. t-snare. 1 hit.
PROSITE	PS00914. SYNTAXIN. 1 hit. PS50192. T_SNARE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	STX7. human.
GenomeRNAi	8417.
NextBio	31504.
PMAP-CutDB	O15400.
SOURCE	Search...

Entry information

Entry name

STX7_HUMAN

Accession

Primary (citable) accession number: O15400
Secondary accession number(s): E1P579, Q5SZW2, Q96ES9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.