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Protein

Sorting nexin-9

Gene

SNX9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei286Phosphatidylinositol 4,5-bisphosphate1
Binding sitei288Phosphatidylinositol 4,5-bisphosphate1
Binding sitei313Phosphatidylinositol 4,5-bisphosphate1
Binding sitei327Phosphatidylinositol 4,5-bisphosphate1

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: UniProtKB
  • Arp2/3 complex binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • phosphatidylinositol binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cleavage furrow formation Source: UniProtKB
  • endocytosis Source: UniProtKB
  • endosomal transport Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • lipid tube assembly Source: UniProtKB
  • membrane organization Source: Reactome
  • mitotic cytokinesis Source: UniProtKB
  • plasma membrane tubulation Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of membrane protein ectodomain proteolysis Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of protein oligomerization Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB

Keywordsi

Biological processCell cycle, Cell division, Endocytosis, Mitosis, Protein transport, Transport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-8856828 Clathrin-mediated endocytosis
SignaLinkiQ9Y5X1
SIGNORiQ9Y5X1

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000130340.14
HGNCiHGNC:14973 SNX9
MIMi605952 gene
neXtProtiNX_Q9Y5X1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi287Y → A: Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313. 1 Publication1
Mutagenesisi313K → A: Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287. 1 Publication1
Mutagenesisi363K → E: Strongly reduced membrane binding. 1 Publication1
Mutagenesisi366 – 367KR → EE: Loss of membrane binding. 1 Publication2
Mutagenesisi522K → E: Abolishes membrane tubulation activity; when associated with E-528. 1 Publication1
Mutagenesisi528K → E: Abolishes membrane tubulation activity; when associated with E-522. 1 Publication1

Organism-specific databases

DisGeNETi51429
OpenTargetsiENSG00000130340
PharmGKBiPA37949

Polymorphism and mutation databases

DMDMi12643956

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002138521 – 595Sorting nexin-9Add BLAST595

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116PhosphoserineCombined sources1
Modified residuei121PhosphoserineCombined sources1
Modified residuei197PhosphoserineCombined sources1
Modified residuei200PhosphoserineCombined sources1
Modified residuei216PhosphothreonineCombined sources1
Modified residuei239PhosphotyrosineBy similarity1
Modified residuei288N6-acetyllysineCombined sources1

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

EPDiQ9Y5X1
MaxQBiQ9Y5X1
PaxDbiQ9Y5X1
PeptideAtlasiQ9Y5X1
PRIDEiQ9Y5X1
ProteomicsDBi86526

PTM databases

iPTMnetiQ9Y5X1
PhosphoSitePlusiQ9Y5X1

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

BgeeiENSG00000130340
CleanExiHS_SNX9
ExpressionAtlasiQ9Y5X1 baseline and differential
GenevisibleiQ9Y5X1 HS

Organism-specific databases

HPAiHPA031410
HPA057203

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

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119535, 54 interactors
DIPiDIP-30997N
IntActiQ9Y5X1, 40 interactors
MINTiQ9Y5X1
STRINGi9606.ENSP00000376024

Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni167 – 169Combined sources3
Helixi175 – 180Combined sources6
Helixi215 – 221Combined sources7
Beta strandi232 – 237Combined sources6
Beta strandi240 – 243Combined sources4
Beta strandi252 – 255Combined sources4
Helixi257 – 259Combined sources3
Beta strandi260 – 262Combined sources3
Beta strandi263 – 266Combined sources4
Beta strandi271 – 276Combined sources6
Turni277 – 279Combined sources3
Beta strandi283 – 286Combined sources4
Helixi287 – 301Combined sources15
Turni302 – 304Combined sources3
Helixi324 – 339Combined sources16
Helixi344 – 346Combined sources3
Helixi348 – 355Combined sources8
Helixi359 – 370Combined sources12
Helixi376 – 382Combined sources7
Beta strandi383 – 387Combined sources5
Helixi392 – 428Combined sources37
Helixi430 – 450Combined sources21
Helixi455 – 457Combined sources3
Helixi458 – 480Combined sources23
Helixi482 – 484Combined sources3
Helixi486 – 500Combined sources15
Helixi503 – 518Combined sources16
Helixi520 – 525Combined sources6
Helixi531 – 590Combined sources60

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5X1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 62SH3PROSITE-ProRule annotationAdd BLAST62
Domaini250 – 361PXPROSITE-ProRule annotationAdd BLAST112
Domaini392 – 595BARAdd BLAST204

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 213Critical for tubulation activityAdd BLAST13

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

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG2528 Eukaryota
ENOG410XPHZ LUCA
GeneTreeiENSGT00510000046469
HOGENOMiHOG000261633
HOVERGENiHBG009996
InParanoidiQ9Y5X1
KOiK17923
OMAiFAKPGME
OrthoDBiEOG091G03D8
PhylomeDBiQ9Y5X1
TreeFamiTF314082

Family and domain databases

CDDicd07668 BAR_SNX9, 1 hit
cd07285 PX_SNX9, 1 hit
cd11898 SH3_SNX9, 1 hit
Gene3Di1.20.1270.60, 1 hit
3.30.1520.10, 1 hit
InterProiView protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR001683 Phox
IPR036871 PX_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR028644 SNX9
IPR037425 SNX9_BAR
IPR014536 Snx9_fam
IPR037426 SNX9_PX
IPR035558 SNX9_SH3
IPR019497 Sorting_nexin_WASP-bd-dom
PANTHERiPTHR10555:SF14 PTHR10555:SF14, 1 hit
PfamiView protein in Pfam
PF10456 BAR_3_WASP_bdg, 1 hit
PF00787 PX, 1 hit
PF00018 SH3_1, 1 hit
PIRSFiPIRSF027744 Snx9, 1 hit
SMARTiView protein in SMART
SM00312 PX, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF64268 SSF64268, 1 hit
PROSITEiView protein in PROSITE
PS50195 PX, 1 hit
PS50002 SH3, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti89Q → H in AAH05022 (PubMed:15489334).Curated1

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 Genomic DNA No translation available.
AL139330 Genomic DNA No translation available.
AL391863 Genomic DNA No translation available.
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.3 human

Similar proteinsi

Entry informationi

Entry nameiSNX9_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X1
Secondary accession number(s): Q9BSI7
, Q9BVM1, Q9UJH6, Q9UP20
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: June 20, 2018
This is version 171 of the entry and version 1 of the sequence. See 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

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