Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y5X3 (SNX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorting nexin-5
Gene names
Name:SNX5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation. Ref.8 Ref.12

Subunit structure

Interacts with SNX1; this promotes location at the endosome membrane. Ref.7

Subcellular location

Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projectionphagocytic cup. Cell projectionruffle. Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane ruffles in response to EGFR stimulation. Ref.1 Ref.6 Ref.7 Ref.8 Ref.12

Domain

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate By similarity.

Sequence similarities

Belongs to the sorting nexin family.

Contains 1 BAR domain.

Contains 1 PX (phox homology) domain.

Caution

The selectivity for particular phosphatidylinositol lipids is under debate. According to one report (PubMed:19553671), the rat protein binds exclusively to phosphatidylinositol 4,5-bisphosphate, while the human protein has been reported (Ref.6) to bind to phosphatidylinositol 3,4-bisphosphate and also to phosphatidylinositol 3-phosphate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 404403Sorting nexin-5
PRO_0000213844

Regions

Domain25 – 172148PX
Domain202 – 404203BAR
Region40 – 467Phosphatidylinositol bisphosphate binding By similarity
Region99 – 1057Phosphatidylinositol bisphosphate binding By similarity
Region113 – 1164Phosphatidylinositol bisphosphate binding By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.14 Ref.15
Modified residue2751N6-acetyllysine Ref.11

Experimental info

Sequence conflict2791V → L Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y5X3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 87A85620AF827EC6

FASTA40446,816
        10         20         30         40         50         60 
MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS 

        70         80         90        100        110        120 
PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD GPREKMQKLG EGEGSMTKEE 

       130        140        150        160        170        180 
FAKMKQELEA EYLAVFKKTV SSHEVFLQRL SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK 

       190        200        210        220        230        240 
EMFGGFFKSV VKSADEVLFT GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV 

       250        260        270        280        290        300 
ADDYIHTAAC LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML 

       310        320        330        340        350        360 
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF EQLSESAKEE 

       370        380        390        400 
LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL FKNN 

« Hide

References

« Hide 'large scale' references
[1]"A large family of endosome-localized proteins related to sorting nexin 1."
Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.
Biochem. J. 358:7-16(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovarian carcinoma.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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].
[5]"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].
Tissue: Brain and Placenta.
[6]"Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation."
Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C., Teasdale R.D., Gleeson P.A.
J. Cell Sci. 117:6413-6424(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE BINDING.
[7]"Visualisation of macropinosome maturation by the recruitment of sorting nexins."
Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F., Parton R.G., Gleeson P.A., Teasdale R.D.
J. Cell Sci. 119:3967-3980(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX1, SUBCELLULAR LOCATION.
[8]"A role for SNX5 in the regulation of macropinocytosis."
Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.
BMC Cell Biol. 9:58-58(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteins."
Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.
PLoS ONE 5:E13763-E13763(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"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].
[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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion."
Zernich D., Purcell A.W., Macdonald W.A., Kjer-Nielsen L., Ely L.K., Laham N., Crockford T., Mifsud N.A., Bharadwaj M., Chang L., Tait B.D., Holdsworth R., Brooks A.G., Bottomley S.P., Beddoe T., Peh C.A., Rossjohn J., McCluskey J.
J. Exp. Med. 200:13-24(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA CLASS I HISTOCOMPATIBILITY COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121855 mRNA. Translation: AAD27828.1.
AK001793 mRNA. Translation: BAA91914.1.
AL121585 Genomic DNA. Translation: CAC00471.1.
BC000100 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10264.1.
CH471133 Genomic DNA. Translation: EAX10265.1.
CH471133 Genomic DNA. Translation: EAX10266.1.
CH471133 Genomic DNA. Translation: EAX10268.1.
BC093623 mRNA. Translation: AAH93623.1.
BC093980 mRNA. Translation: AAH93980.1.
BC143274 mRNA. Translation: AAI43275.1.
CCDSCCDS13130.1.
RefSeqNP_055241.1. NM_014426.3.
NP_689413.1. NM_152227.2.
UniGeneHs.316890.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYSX-ray2.40C257-265[»]
ProteinModelPortalQ9Y5X3.
SMRQ9Y5X3. Positions 20-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118022. 23 interactions.
IntActQ9Y5X3. 17 interactions.
MINTMINT-2823978.
STRING9606.ENSP00000366988.

PTM databases

PhosphoSiteQ9Y5X3.

Polymorphism databases

DMDM10720289.

Proteomic databases

MaxQBQ9Y5X3.
PaxDbQ9Y5X3.
PRIDEQ9Y5X3.

Protocols and materials databases

DNASU27131.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377759; ENSP00000366988; ENSG00000089006.
ENST00000377768; ENSP00000366998; ENSG00000089006.
GeneID27131.
KEGGhsa:27131.
UCSCuc002wqc.3. human.

Organism-specific databases

CTD27131.
GeneCardsGC20M017870.
HGNCHGNC:14969. SNX5.
HPACAB020679.
MIM605937. gene.
neXtProtNX_Q9Y5X3.
PharmGKBPA37945.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255198.
HOVERGENHBG000716.
InParanoidQ9Y5X3.
KOK17920.
OMAIKDSCAK.
OrthoDBEOG7X0VH4.
PhylomeDBQ9Y5X3.
TreeFamTF313698.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9Y5X3.
BgeeQ9Y5X3.
CleanExHS_SNX5.
GenevestigatorQ9Y5X3.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view]
PANTHERPTHR10555:SF6. PTHR10555:SF6. 1 hit.
PfamPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFPIRSF036924. Snx5_Snx6. 1 hit.
SMARTSM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNX5. human.
EvolutionaryTraceQ9Y5X3.
GeneWikiSNX5.
GenomeRNAi27131.
NextBio49854.
PROQ9Y5X3.
SOURCESearch...

Entry information

Entry nameSNX5_HUMAN
AccessionPrimary (citable) accession number: Q9Y5X3
Secondary accession number(s): B7ZKN3 expand/collapse secondary AC list , D3DW26, Q52LC4, Q9BWP0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM