Q9Y5X3 (SNX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sorting nexin-5

Gene names

Name:

SNX5

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	404 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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 projection › phagocytic cup. Cell projection › ruffle. 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.11
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.

Ontologies

Keywords
Biological process	Endocytosis Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Endosome Membrane
Ligand	Lipid-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro pinocytosis Inferred from direct assay Ref.8. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to endosome membrane Inferred from direct assay Ref.6. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from direct assay Ref.6Ref.8. Source: UniProtKB macropinocytic cup Inferred from direct assay Ref.8. Source: UniProtKB phagocytic cup Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidylinositol binding Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 404	404	Sorting nexin-5		PRO_0000213844
Regions
	Domain	25 – 172	148	PX
	Domain	202 – 404	203	BAR
	Region	40 – 46	7	Phosphatidylinositol bisphosphate binding By similarity
	Region	99 – 105	7	Phosphatidylinositol bisphosphate binding By similarity
	Region	113 – 116	4	Phosphatidylinositol bisphosphate binding By similarity
Amino acid modifications
	Modified residue	275	1	N6-acetyllysine Ref.10
Experimental info
	Sequence conflict	279	1	V → L Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5X3 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 87A85620AF827EC6	FASTA	404	46,816
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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]	"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, MASS SPECTROMETRY.
[11]	"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.
[12]	"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].
[13]	"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.

IPI

IPI00295209.

RefSeq

NP_055241.1. NM_014426.2.
NP_689413.1. NM_152227.1.

UniGene

Hs.316890.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SYS	X-ray	2.40	C	257-265	[»]

ProteinModelPortal

Q9Y5X3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y5X3. 8 interactions.

MINT

MINT-2823978.

STRING

9606.ENSP00000366988.

PTM databases

PhosphoSite

Q9Y5X3.

Polymorphism databases

DMDM

10720289.

Proteomic databases

PaxDb

Q9Y5X3.

PRIDE

Q9Y5X3.

Protocols and materials databases

DNASU

27131.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377759; ENSP00000366988; ENSG00000089006.
ENST00000377768; ENSP00000366998; ENSG00000089006.

GeneID

27131.

KEGG

hsa:27131.

UCSC

uc002wqc.3. human.

Organism-specific databases

CTD

27131.

GeneCards

GC20M017870.

HGNC

HGNC:14969. SNX5.

HPA

CAB020679.

MIM

605937. gene.

neXtProt

NX_Q9Y5X3.

PharmGKB

PA37945.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG255198.

HOVERGEN

HBG000716.

InParanoid

Q9Y5X3.

OMA

IKDSCAK.

OrthoDB

EOG4CNQR4.

PhylomeDB

Q9Y5X3.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpress

Q9Y5X3.

Bgee

Q9Y5X3.

CleanEx

HS_SNX5.

Genevestigator

Q9Y5X3.

GermOnline

ENSG00000089006. Homo sapiens.

Family and domain databases

Gene3D

3.30.1520.10. 1 hit.

InterPro

IPR001683. Phox.
IPR014637. Snx5_Snx6.
IPR015404. Vps5_C.
[Graphical view]

Pfam

PF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]

PIRSF

PIRSF036924. Snx5_Snx6. 1 hit.

SMART

SM00312. PX. 1 hit.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.

PROSITE

PS51021. BAR. False negative.
PS50195. PX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SNX5. human.

EvolutionaryTrace

Q9Y5X3.

GenomeRNAi

27131.

NextBio

49854.

SOURCE

Search...

Entry information

Entry name

SNX5_HUMAN

Accession

Primary (citable) accession number: Q9Y5X3
Secondary accession number(s): B7ZKN3 , D3DW26, Q52LC4, Q9BWP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 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.