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Q91VH2 (SNX9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-9
Gene names
Name:Snx9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

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 By similarity. Interacts with ADAM9 and ADAM15 cytoplasmic tails. Ref.2

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicleclathrin-coated vesicle By similarity. Golgi apparatustrans-Golgi network By similarity. Cell projectionruffle By similarity. Cytoplasm By similarity. 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 By similarity. Colocalizes with the actin cytoskeleton at the cell membrane By similarity.

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 By similarity.

Post-translational modification

Phosphorylated on tyrosine residues by TNK2. Phosphorylation promotes its activity in the degradation of EGFR By similarity.

Ubiquitinated by ITCH By similarity.

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 processCell cycle
Cell division
Endocytosis
Mitosis
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
   DomainSH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcleavage furrow formation

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

endosomal transport

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype PubMed 12917015. Source: MGI

lipid tube assembly

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein oligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

receptor-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentclathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 12917015. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12917015. Source: MGI

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function1-phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay PubMed 12917015. Source: MGI

protein binding

Inferred from physical interaction PubMed 12917015. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595Sorting nexin-9
PRO_0000213853

Regions

Domain1 – 6262SH3
Domain250 – 360111PX
Domain392 – 595204BAR
Region201 – 21313Critical for tubulation activity By similarity

Sites

Binding site2861Phosphatidylinositol 4,5-bisphosphate By similarity
Binding site2881Phosphatidylinositol 4,5-bisphosphate By similarity
Binding site3131Phosphatidylinositol 4,5-bisphosphate By similarity
Binding site3271Phosphatidylinositol 4,5-bisphosphate By similarity

Amino acid modifications

Modified residue2391Phosphotyrosine Ref.3
Modified residue2881N6-acetyllysine By similarity

Secondary structure

............. 595
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q91VH2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 3D5568476F2D816D

FASTA59566,546
        10         20         30         40         50         60 
MATKARVMYD FAAEPGNNEL TVTEGEIITV TNPNVGGGWL EGKNNKGEQG LVPTDYVEIL 

        70         80         90        100        110        120 
PNDGKDPFSC GNSVADQAFL DSLTASTAQT NSSSANSNNQ VGGGNDPWTA WNAPKPGNWD 

       130        140        150        160        170        180 
SSDAWGSRTD GTSAQRNSSA NNWDTGFGHP QAYQGPATGD DDEWDEDWDD PKSSSPYFKD 

       190        200        210        220        230        240 
SEPAEAGGIQ RGNSRAGASS MKLPLNKFPG FAKPGMEQYL LAKQLAKPKE KIAIIVGDYG 

       250        260        270        280        290        300 
PMWVYPTSTF DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK 

       310        320        330        340        350        360 
FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVVSESEVF QQFLNFRDEK 

       370        380        390        400        410        420 
EWKTGKRKAE KDELVGVMIF STMEPEAPDL DLIEIEQKCD AVGKFTKAMD DGVKELLTVG 

       430        440        450        460        470        480 
QEHWKRCTGP LPKEYQKIGK ALQSLAAVFS SSGYQGETDL NDAITEAGKT YEEIASLVAE 

       490        500        510        520        530        540 
QPKKDLHFLM ECNHEYKGFL GCFPDIIGAH KGAIEKVKES DKLVATSKIT PQDKQTMVKR 

       550        560        570        580        590 
VGTMSYALQA EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM 

« Hide

References

« Hide 'large scale' references
[1]"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: Mammary tumor.
[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: INTERACTION WITH ADAM9 AND ADAM15.
[3]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Solution structure of the SH3 domain from mouse sorting nexin-9."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC014814 mRNA. Translation: AAH14814.1.
CCDSCCDS57041.1.
RefSeqNP_079940.2. NM_025664.5.
UniGeneMm.89515.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ENMNMR-A1-70[»]
ProteinModelPortalQ91VH2.
SMRQ91VH2. Positions 1-70, 214-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211598. 2 interactions.
IntActQ91VH2. 1 interaction.
MINTMINT-1866620.

PTM databases

PhosphoSiteQ91VH2.

Proteomic databases

MaxQBQ91VH2.
PaxDbQ91VH2.
PRIDEQ91VH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002436; ENSMUSP00000002436; ENSMUSG00000002365.
GeneID66616.
KEGGmmu:66616.
UCSCuc008afj.1. mouse.

Organism-specific databases

CTD51429.
MGIMGI:1913866. Snx9.

Phylogenomic databases

eggNOGCOG5391.
GeneTreeENSGT00510000046469.
HOGENOMHOG000261633.
HOVERGENHBG009996.
InParanoidQ91VH2.
KOK17923.
OMADPWSAWN.
OrthoDBEOG7GTT36.
PhylomeDBQ91VH2.
TreeFamTF314082.

Gene expression databases

BgeeQ91VH2.
CleanExMM_SNX9.
GenevestigatorQ91VH2.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR001452. SH3_domain.
IPR028644. SNX9.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERPTHR10555:SF14. PTHR10555:SF14. 1 hit.
PfamPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFPIRSF027744. Snx9. 1 hit.
SMARTSM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNX9. mouse.
EvolutionaryTraceQ91VH2.
NextBio322180.
PROQ91VH2.
SOURCESearch...

Entry information

Entry nameSNX9_MOUSE
AccessionPrimary (citable) accession number: Q91VH2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot