Q9Y5X1 (SNX9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sorting nexin-9

Alternative name(s):
SH3 and PX domain-containing protein 1
Short name=Protein SDP1
SH3 and PX domain-containing protein 3A

Gene names

Name:	SNX9
Synonyms:	SH3PX1, SH3PXD3A

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	595 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 endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate. Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.17 Ref.18 Ref.20
Subunit structure	Homodimer, and homooligomer. Heterodimer with SNX18. Interacts with ITCH. Interacts (via SH3 domain) with TNK2, WASL and ARP3. Identified in a complex with TNK2 and clathrin heavy chains. Identified in a complex with the AP-2 complex, clathrin and DNM2. Interacts (via SH3 domain) with DNM1 and DNM2. Identified in an oligomeric complex containing DNM1 and SNX9. Interacts with ADAM9 and ADAM15 cytoplasmic tails. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21
Subcellular location	Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle › clathrin-coated vesicle. Golgi apparatus › trans-Golgi network. Cell projection › ruffle. Cytoplasm. Note: Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation. Colocalizes with the actin cytoskeleton at the cell membrane. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.20
Tissue specificity	Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes. Ref.2
Domain	The PX domain mediates interaction with membranes enriched in phosphatidylinositol phosphate. Has high affinity for phosphatidylinositol 4,5-bisphosphate, but can also bind to membranes enriched in other phosphatidylinositol phosphates. Ref.20
Post-translational modification	Ubiquitinated by ITCH. Ref.16 Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR. Ref.7 Ref.11
Sequence similarities	Belongs to the sorting nexin family. Contains 1 BAR domain. Contains 1 PX (phox homology) domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Endocytosis Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane
Domain	SH3 domain
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro intracellular protein transport Inferred from mutant phenotype Ref.10. Source: UniProtKB lipid tube assembly Inferred from direct assay Ref.20. Source: UniProtKB positive regulation of GTPase activity Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of protein oligomerization Inferred from direct assay Ref.10. Source: UniProtKB receptor-mediated endocytosis Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell clathrin-coated vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle membrane Inferred from direct assay Ref.20. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from direct assay Ref.10. Source: UniProtKB ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	1-phosphatidylinositol binding Inferred from direct assay Ref.20. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FASLG	P48023	2	EBI-77848,EBI-495538
SOS1	Q07889	2	EBI-77848,EBI-297487
SOS2	Q07890	2	EBI-77848,EBI-298181
TNK2	Q17R13	5	EBI-77848,EBI-457220	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 595

595

Sorting nexin-9

PRO_0000213852

Regions

Domain

1 – 62

62

SH3

Domain

250 – 361

112

PX

Domain

392 – 595

204

BAR

Region

201 – 213

13

Critical for tubulation activity

Sites

Binding site

286

1

Phosphatidylinositol 4,5-bisphosphate

Binding site

288

1

Phosphatidylinositol 4,5-bisphosphate

Binding site

313

1

Phosphatidylinositol 4,5-bisphosphate

Binding site

327

1

Phosphatidylinositol 4,5-bisphosphate

Amino acid modifications

Modified residue

176

1

Phosphoserine By similarity

Modified residue

288

1

N6-acetyllysine Ref.15

Experimental info

Mutagenesis

287

1

Y → A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. Ref.20

Mutagenesis

313

1

K → A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. Ref.20

Mutagenesis

363

1

K → E: Strongly reduced membrane binding. Ref.20

Mutagenesis

366 – 367

2

KR → EE: Loss of membrane binding.

Mutagenesis

522

1

K → E: Abolishes membrane tubulation activity; when associated with E-528. Ref.20

Mutagenesis

528

1

K → E: Abolishes membrane tubulation activity; when associated with E-522. Ref.20

Sequence conflict

89

1

Q → H in AAH05022. Ref.5

Secondary structure

1

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595

Helix Strand Turn

Details...

Turn

167 – 169

3

Helix

215 – 221

7

Beta strand

232 – 237

6

Beta strand

240 – 243

4

Beta strand

252 – 255

4

Helix

257 – 259

3

Beta strand

260 – 262

3

Beta strand

263 – 266

4

Beta strand

271 – 276

6

Turn

277 – 279

3

Beta strand

283 – 286

4

Helix

287 – 301

15

Turn

302 – 304

3

Helix

324 – 339

16

Helix

344 – 346

3

Helix

348 – 355

8

Helix

359 – 370

12

Helix

376 – 382

7

Beta strand

383 – 387

5

Helix

392 – 428

37

Helix

430 – 450

21

Helix

455 – 457

3

Helix

458 – 480

23

Helix

482 – 484

3

Helix

486 – 500

15

Helix

503 – 518

16

Helix

520 – 525

6

Helix

531 – 590

60

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5X1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 963892AC1A5A9227	FASTA	595	66,592
	10 20 30 40 50 60 MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG LVPTDYVEIL 70 80 90 100 110 120 PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ VGSGNDPWSA WSASKSGNWE 130 140 150 160 170 180 SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH PQAYQGPATG DDDDWDEDWD GPKSSSYFKD 190 200 210 220 230 240 SESADAGGAQ RGNSRASSSS MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG 250 260 270 280 290 300 PMWVYPTSTF DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK 310 320 330 340 350 360 FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF QQFLNFRDEK 370 380 390 400 410 420 EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE AVGKFTKAMD DGVKELLTVG 430 440 450 460 470 480 QEHWKRCTGP LPKEYQKIGK ALQSLATVFS SSGYQGETDL NDAITEAGKT YEEIASLVAE 490 500 510 520 530 540 QPKKDLHFLM ECNHEYKGFL GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR 550 560 570 580 590 VSIMSYALQA EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM

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].
[2]	"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1." Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P. J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9 AND ADAM15, TISSUE SPECIFICITY.
[3]	"Identification of differentially expressed genes in matched prostate cancer and normal epithelial cell lines." Zhang J.S., Smith D.I. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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].
[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: Kidney and Skin.
[6]	"Human SDP1." Ramanathan G., Subramaniam V.N., Hong W. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-595.
[7]	"The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation." Lin Q., Lo C.G., Cerione R.A., Yang W. J. Biol. Chem. 277:10134-10138(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TNK2, IDENTIFICATION IN A COMPLEX WITH TNK2 AND CLATHRIN HEAVY CHAIN, TYROSINE PHOSPHORYLATION.
[8]	"Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components." Lundmark R., Carlsson S.R. J. Biol. Chem. 278:46772-46781(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DNM2 AND THE AP-2 COMPLEX, IDENTIFICATION IN A COMPLEX WITH THE AP-2 COMPLEX; CLATHRIN AND DNM2, SUBCELLULAR LOCATION.
[9]	"SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1." Yeow-Fong L., Lim L., Manser E. FEBS Lett. 579:5040-5048(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TNK2, SUBCELLULAR LOCATION.
[10]	"SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis." Soulet F., Yarar D., Leonard M., Schmid S.L. Mol. Biol. Cell 16:2058-2067(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, INTERACTION WITH DNM1 AND DNM2.
[11]	"Dimerization is required for SH3PX1 tyrosine phosphorylation in response to epidermal growth factor signalling and interaction with ACK2." Childress C., Lin Q., Yang W. Biochem. J. 394:693-698(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, TYROSINE PHOSPHORYLATION.
[12]	"SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis." Yarar D., Waterman-Storer C.M., Schmid S.L. Dev. Cell 13:43-56(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH WASL, SUBCELLULAR LOCATION, SUBUNIT, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPATE BINDING.
[13]	"SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2." Shin N., Ahn N., Chang-Ileto B., Park J., Takei K., Ahn S.G., Kim S.A., Di Paolo G., Chang S. J. Cell Sci. 121:1252-1263(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARP3; WASL AND DNM2.
[14]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FASLG.
[15]	"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-288, MASS SPECTROMETRY.
[16]	"The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an unconventional substrate recognition domain." Baumann C., Lindholm C.K., Rimoldi D., Levy F. FEBS J. 277:2803-2814(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITCH, UBIQUITINATION BY ITCH.
[17]	"SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane." Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., Kim H., Chang S. J. Cell Sci. 123:1742-1750(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[18]	"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.
[19]	"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].
[20]	"The PX-BAR membrane-remodeling unit of sorting nexin 9." Pylypenko O., Lundmark R., Rasmuson E., Carlsson S.R., Rak A. EMBO J. 26:4788-4800(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 204-595 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, FUNCTION, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-287; LYS-313; LYS-363; 366-LYS-ARG-367; LYS-522 AND LYS-528.
[21]	"Structure and plasticity of Endophilin and Sorting Nexin 9." Wang Q., Kaan H.Y., Hooda R.N., Goh S.L., Sondermann H. Structure 16:1574-1587(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 230-595, SUBUNIT.
[22]	"Mechanism of aldolase control of sorting nexin 9 function in endocytosis." Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T. J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 152-182 IN COMPLEX WITH ALDOA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF121859 mRNA. Translation: AAD27832.1.
AF131214 mRNA. Translation: AAF04473.1.
AF172847 mRNA. Translation: AAL54871.1.
AL035634, AL139330, AL391863 Genomic DNA. Translation: CAI20465.1.
AL139330, AL035634, AL391863 Genomic DNA. Translation: CAI12979.1.
AL391863, AL035634, AL139330 Genomic DNA. Translation: CAI15180.1.
BC001084 mRNA. Translation: AAH01084.3.
BC005022 mRNA. Translation: AAH05022.1.
AF076957 mRNA. Translation: AAD43001.1.

IPI

IPI00001883.

RefSeq

NP_057308.1. NM_016224.3.

UniGene

Hs.191213.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RAI	X-ray	3.20	A/B	204-595	[»]
2RAJ	X-ray	2.45	A	204-595	[»]
2RAK	X-ray	3.00	A	204-595	[»]
3DYT	X-ray	2.08	A	230-595	[»]
3DYU	X-ray	4.10	A/B/C	230-595	[»]
3LGE	X-ray	2.20	E/F/G/H	152-182	[»]

ProteinModelPortal

Q9Y5X1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30997N.

IntAct

Q9Y5X1. 8 interactions.

MINT

MINT-108846.

STRING

9606.ENSP00000376024.

PTM databases

PhosphoSite

Q9Y5X1.

Polymorphism databases

DMDM

12643956.

Proteomic databases

PaxDb

Q9Y5X1.

PeptideAtlas

Q9Y5X1.

PRIDE

Q9Y5X1.

Protocols and materials databases

DNASU

51429.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000392185; ENSP00000376024; ENSG00000130340.
ENST00000539592; ENSP00000446165; ENSG00000130340.

GeneID

51429.

KEGG

hsa:51429.

UCSC

uc003qqv.1. human.

Organism-specific databases

CTD

51429.

GeneCards

GC06P158153.

HGNC

HGNC:14973. SNX9.

HPA

HPA031410.

MIM

605952. gene.

neXtProt

NX_Q9Y5X1.

PharmGKB

PA37949.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5391.

HOGENOM

HOG000261633.

HOVERGEN

HBG009996.

InParanoid

Q9Y5X1.

OMA

DPWSAWN.

OrthoDB

EOG48GW34.

PhylomeDB

Q9Y5X1.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpress

Q9Y5X1.

Bgee

Q9Y5X1.

CleanEx

HS_SNX9.

Genevestigator

Q9Y5X1.

GermOnline

ENSG00000130340. Homo sapiens.

Family and domain databases

Gene3D

3.30.1520.10. 1 hit.

InterPro

IPR001683. Phox.
IPR001452. SH3_domain.
IPR014536. Snx9.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]

Pfam

PF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PIRSF

PIRSF027744. Snx9. 1 hit.

SMART

SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS51021. BAR. False negative.
PS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SNX9. human.

EvolutionaryTrace

Q9Y5X1.

GenomeRNAi

51429.

NextBio

54991.

SOURCE

Search...

Entry information

Entry name

SNX9_HUMAN

Accession

Primary (citable) accession number: Q9Y5X1
Secondary accession number(s): Q9BSI7 , Q9BVM1, Q9UJH6, Q9UP20

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 116 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.