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Q9Y5X1

- SNX9_HUMAN

UniProt

Q9Y5X1 - SNX9_HUMAN

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Protein

Sorting nexin-9

Gene

SNX9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. 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.9 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei286 – 2861Phosphatidylinositol 4,5-bisphosphate
Binding sitei288 – 2881Phosphatidylinositol 4,5-bisphosphate
Binding sitei313 – 3131Phosphatidylinositol 4,5-bisphosphate
Binding sitei327 – 3271Phosphatidylinositol 4,5-bisphosphate

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cleavage furrow formation Source: UniProtKB
  2. endocytosis Source: UniProtKB
  3. endosomal transport Source: UniProtKB
  4. intracellular protein transport Source: UniProtKB
  5. lipid tube assembly Source: UniProtKB
  6. mitotic cytokinesis Source: UniProtKB
  7. mitotic nuclear division Source: UniProtKB-KW
  8. positive regulation of GTPase activity Source: UniProtKB
  9. positive regulation of membrane protein ectodomain proteolysis Source: UniProtKB
  10. positive regulation of protein oligomerization Source: UniProtKB
  11. receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Endocytosis, Mitosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiQ9Y5X1.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SNX9
Synonyms:SH3PX1, SH3PXD3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14973. SNX9.

Subcellular locationi

Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleclathrin-coated vesicle. Golgi apparatustrans-Golgi network. Cell projectionruffle. 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.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: HPA
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  4. cytoplasmic vesicle membrane Source: UniProtKB
  5. endosome Source: RefGenome
  6. extracellular vesicular exosome Source: UniProt
  7. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  8. plasma membrane Source: HPA
  9. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi287 – 2871Y → A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. 1 Publication
Mutagenesisi313 – 3131K → A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. 1 Publication
Mutagenesisi363 – 3631K → E: Strongly reduced membrane binding. 1 Publication
Mutagenesisi366 – 3672KR → EE: Loss of membrane binding. 1 Publication
Mutagenesisi522 – 5221K → E: Abolishes membrane tubulation activity; when associated with E-528. 1 Publication
Mutagenesisi528 – 5281K → E: Abolishes membrane tubulation activity; when associated with E-522. 1 Publication

Organism-specific databases

PharmGKBiPA37949.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Sorting nexin-9PRO_0000213852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391PhosphotyrosineBy similarity
Modified residuei288 – 2881N6-acetyllysine1 Publication

Post-translational modificationi

Ubiquitinated by ITCH.1 Publication
Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y5X1.
PaxDbiQ9Y5X1.
PeptideAtlasiQ9Y5X1.
PRIDEiQ9Y5X1.

PTM databases

PhosphoSiteiQ9Y5X1.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiQ9Y5X1.
CleanExiHS_SNX9.
ExpressionAtlasiQ9Y5X1. baseline and differential.
GenevestigatoriQ9Y5X1.

Organism-specific databases

HPAiHPA031410.

Interactioni

Subunit structurei

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.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM15Q134442EBI-77848,EBI-77818
ATRAIDQ6UW562EBI-77848,EBI-723802
DNM2P505702EBI-77848,EBI-346547
espFB7UM884EBI-77848,EBI-2529480From a different organism.
FASLGP480232EBI-77848,EBI-495538
ITCHQ96J027EBI-77848,EBI-1564678
SNX33Q8WV412EBI-77848,EBI-2481535
SOS1Q078892EBI-77848,EBI-297487
SOS2Q078902EBI-77848,EBI-298181
TNK2Q17R135EBI-77848,EBI-457220From a different organism.
UBCP0CG482EBI-77848,EBI-3390054
WASLO004012EBI-77848,EBI-957615

Protein-protein interaction databases

BioGridi119535. 22 interactions.
DIPiDIP-30997N.
IntActiQ9Y5X1. 24 interactions.
MINTiMINT-108846.
STRINGi9606.ENSP00000376024.

Structurei

Secondary structure

1
595
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni167 – 1693Combined sources
Helixi215 – 2217Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi252 – 2554Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi271 – 2766Combined sources
Turni277 – 2793Combined sources
Beta strandi283 – 2864Combined sources
Helixi287 – 30115Combined sources
Turni302 – 3043Combined sources
Helixi324 – 33916Combined sources
Helixi344 – 3463Combined sources
Helixi348 – 3558Combined sources
Helixi359 – 37012Combined sources
Helixi376 – 3827Combined sources
Beta strandi383 – 3875Combined sources
Helixi392 – 42837Combined sources
Helixi430 – 45021Combined sources
Helixi455 – 4573Combined sources
Helixi458 – 48023Combined sources
Helixi482 – 4843Combined sources
Helixi486 – 50015Combined sources
Helixi503 – 51816Combined sources
Helixi520 – 5256Combined sources
Helixi531 – 59060Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RAIX-ray3.20A/B204-595[»]
2RAJX-ray2.45A204-595[»]
2RAKX-ray3.00A204-595[»]
3DYTX-ray2.08A230-595[»]
3DYUX-ray4.10A/B/C230-595[»]
3LGEX-ray2.20E/F/G/H152-182[»]
ProteinModelPortaliQ9Y5X1.
SMRiQ9Y5X1. Positions 1-70, 214-595.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5X1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6262SH3PROSITE-ProRule annotationAdd
BLAST
Domaini250 – 361112PXPROSITE-ProRule annotationAdd
BLAST
Domaini392 – 595204BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 21313Critical for tubulation activityAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the sorting nexin family.Curated
Contains 1 BAR domain.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00510000046469.
HOGENOMiHOG000261633.
HOVERGENiHBG009996.
InParanoidiQ9Y5X1.
KOiK17923.
OMAiDPWSAWN.
OrthoDBiEOG7GTT36.
PhylomeDBiQ9Y5X1.
TreeFamiTF314082.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
IPR028644. SNX9.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERiPTHR10555:SF14. PTHR10555:SF14. 1 hit.
PfamiPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF027744. Snx9. 1 hit.
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5X1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG
60 70 80 90 100
LVPTDYVEIL PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ
110 120 130 140 150
VGSGNDPWSA WSASKSGNWE SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH
160 170 180 190 200
PQAYQGPATG DDDDWDEDWD GPKSSSYFKD SESADAGGAQ RGNSRASSSS
210 220 230 240 250
MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG PMWVYPTSTF
260 270 280 290 300
DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK
310 320 330 340 350
FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF
360 370 380 390 400
QQFLNFRDEK EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE
410 420 430 440 450
AVGKFTKAMD DGVKELLTVG QEHWKRCTGP LPKEYQKIGK ALQSLATVFS
460 470 480 490 500
SSGYQGETDL NDAITEAGKT YEEIASLVAE QPKKDLHFLM ECNHEYKGFL
510 520 530 540 550
GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR VSIMSYALQA
560 570 580 590
EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM
Length:595
Mass (Da):66,592
Last modified:November 1, 1999 - v1
Checksum:i963892AC1A5A9227
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891Q → H in AAH05022. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5253.1.
RefSeqiNP_057308.1. NM_016224.4.
UniGeneiHs.191213.

Genome annotation databases

EnsembliENST00000392185; ENSP00000376024; ENSG00000130340.
GeneIDi51429.
KEGGihsa:51429.
UCSCiuc003qqv.1. human.

Polymorphism databases

DMDMi12643956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS5253.1.
RefSeqi NP_057308.1. NM_016224.4.
UniGenei Hs.191213.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9Y5X1.
SMRi Q9Y5X1. Positions 1-70, 214-595.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119535. 22 interactions.
DIPi DIP-30997N.
IntActi Q9Y5X1. 24 interactions.
MINTi MINT-108846.
STRINGi 9606.ENSP00000376024.

PTM databases

PhosphoSitei Q9Y5X1.

Polymorphism databases

DMDMi 12643956.

Proteomic databases

MaxQBi Q9Y5X1.
PaxDbi Q9Y5X1.
PeptideAtlasi Q9Y5X1.
PRIDEi Q9Y5X1.

Protocols and materials databases

DNASUi 51429.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392185 ; ENSP00000376024 ; ENSG00000130340 .
GeneIDi 51429.
KEGGi hsa:51429.
UCSCi uc003qqv.1. human.

Organism-specific databases

CTDi 51429.
GeneCardsi GC06P158153.
HGNCi HGNC:14973. SNX9.
HPAi HPA031410.
MIMi 605952. gene.
neXtProti NX_Q9Y5X1.
PharmGKBi PA37949.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5391.
GeneTreei ENSGT00510000046469.
HOGENOMi HOG000261633.
HOVERGENi HBG009996.
InParanoidi Q9Y5X1.
KOi K17923.
OMAi DPWSAWN.
OrthoDBi EOG7GTT36.
PhylomeDBi Q9Y5X1.
TreeFami TF314082.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinki Q9Y5X1.

Miscellaneous databases

ChiTaRSi SNX9. human.
EvolutionaryTracei Q9Y5X1.
GeneWikii SNX9.
GenomeRNAii 51429.
NextBioi 54991.
PROi Q9Y5X1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5X1.
CleanExi HS_SNX9.
ExpressionAtlasi Q9Y5X1. baseline and differential.
Genevestigatori Q9Y5X1.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR001452. SH3_domain.
IPR028644. SNX9.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view ]
PANTHERi PTHR10555:SF14. PTHR10555:SF14. 1 hit.
Pfami PF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF027744. Snx9. 1 hit.
SMARTi SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "SNX9, SNX18 and SNX33 are required for progression through and completion of mitosis."
    Ma M.P., Chircop M.
    J. Cell Sci. 125:4372-4382(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiSNX9_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X1
Secondary accession number(s): Q9BSI7
, Q9BVM1, Q9UJH6, Q9UP20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 132 of the entry and version 1 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

3D-structure, Complete proteome, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3