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Protein

Sorting nexin-33

Gene

SNX33

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

Functioni

Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes.6 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • phosphatidylinositol binding Source: GO_Central

GO - Biological processi

  • cleavage furrow formation Source: UniProtKB
  • endocytosis Source: UniProtKB
  • endosomal transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • intracellular protein transport Source: InterPro
  • macropinocytosis Source: UniProtKB
  • membrane tubulation Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of endocytosis Source: UniProtKB
  • negative regulation of protein localization to cell surface Source: UniProtKB
  • positive regulation of membrane protein ectodomain proteolysis Source: UniProtKB
  • positive regulation of protein localization to cell surface Source: UniProtKB
  • protein import Source: UniProtKB
  • vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-33
Alternative name(s):
SH3 and PX domain-containing protein 3
Gene namesi
Name:SNX33
Synonyms:SH3PX3, SH3PXD3C, SNX30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:28468. SNX33.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic membrane-bounded vesicle Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • endosome Source: GO_Central
  • extrinsic component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162404345.

Polymorphism and mutation databases

BioMutaiSNX33.
DMDMi74751538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Sorting nexin-33PRO_0000311948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WV41.
PaxDbiQ8WV41.
PRIDEiQ8WV41.

PTM databases

PhosphoSiteiQ8WV41.

Expressioni

Tissue specificityi

Detected in heart and pancreas.1 Publication

Gene expression databases

BgeeiQ8WV41.
CleanExiHS_SNX30.
HS_SNX33.
ExpressionAtlasiQ8WV41. baseline and differential.
GenevisibleiQ8WV41. HS.

Organism-specific databases

HPAiHPA040988.

Interactioni

Subunit structurei

Homodimer (via BAR domain). Interacts with ADAM15. Interacts with FASLG. Interacts (via SH3 domain) with DNM1 and DNM2. Interacts with WASL.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2481535,EBI-2481535
ADAM15Q134442EBI-2481535,EBI-77818
DNM1Q051932EBI-2481535,EBI-713135
FASLGP480232EBI-2481535,EBI-495538
SNX9Q9Y5X12EBI-2481535,EBI-77848
WASP427683EBI-2481535,EBI-346375

Protein-protein interaction databases

BioGridi129214. 5 interactions.
IntActiQ8WV41. 8 interactions.
MINTiMINT-2792452.
STRINGi9606.ENSP00000311427.

Structurei

Secondary structure

1
574
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi213 – 2153Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2653Combined sources
Helixi267 – 28014Combined sources
Beta strandi282 – 2843Combined sources
Turni302 – 3043Combined sources
Helixi305 – 31814Combined sources
Helixi323 – 3253Combined sources
Helixi327 – 3337Combined sources
Helixi339 – 34911Combined sources
Helixi355 – 3606Combined sources
Helixi371 – 40737Combined sources
Helixi409 – 42719Combined sources
Helixi432 – 4343Combined sources
Helixi437 – 45923Combined sources
Helixi460 – 4623Combined sources
Helixi465 – 50440Combined sources
Helixi510 – 56859Combined sources
Helixi569 – 5713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AKVX-ray2.65A/B212-574[»]
ProteinModelPortaliQ8WV41.
SMRiQ8WV41. Positions 1-100, 212-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6161SH3PROSITE-ProRule annotationAdd
BLAST
Domaini230 – 340111PXPROSITE-ProRule annotationAdd
BLAST
Domaini371 – 574204BARAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi112 – 12211Poly-AspAdd
BLAST

Domaini

The PX and BAR domains mediate association with membranes and are required for membrane tubulation.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.
InParanoidiQ8WV41.
KOiK17923.
OMAiLRMYDNL.
OrthoDBiEOG7ZKS9P.
PhylomeDBiQ8WV41.
TreeFamiTF314082.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
IPR028642. SNX33.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERiPTHR10555:SF121. PTHR10555:SF121. 1 hit.
PfamiPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF14604. SH3_9. 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.

Q8WV41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKGRALYD FHSENKEEIS IQQDEDLVIF SETSLDGWLQ GQNSRGETGL
60 70 80 90 100
FPASYVEIVR SGISTNHADY SSSPAGSPGA QVSLYNSPSV ASPARSGGGS
110 120 130 140 150
GFLSNQGSFE EDDDDDWDDW DDGCTVVEEP RAGGLGTNGH PPLNLSYPGA
160 170 180 190 200
YPSQHMAFRP KPPLERQDSL ASAKRGSVVG RNLNRFSCFV RSGVEAFILG
210 220 230 240 250
DVPMMAKIAE TYSIEMGPRG PQWKANPHPF ACSVEDPTKQ TKFKGIKSYI
260 270 280 290 300
SYKLTPTHAA SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE
310 320 330 340 350
DFIEKRKRRL ILWMDHMTSH PVLSQYEGFQ HFLSCLDDKQ WKMGKRRAEK
360 370 380 390 400
DEMVGASFLL TFQIPTEHQD LQDVEDRVDT FKAFSKKMDD SVLQLSTVAS
410 420 430 440 450
ELVRKHVGGF RKEFQKLGSA FQAISHSFQM DPPFCSEALN SAISHTGRTY
460 470 480 490 500
EAIGEMFAEQ PKNDLFQMLD TLSLYQGLLS NFPDIIHLQK GAFAKVKESQ
510 520 530 540 550
RMSDEGRMVQ DEADGIRRRC RVVGFALQAE MNHFHQRREL DFKHMMQNYL
560 570
RQQILFYQRV GQQLEKTLRM YDNL
Length:574
Mass (Da):65,265
Last modified:March 1, 2002 - v1
Checksum:i7CE51C0F35DDBC3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF219141 mRNA. Translation: ABN09670.1.
EF653821 mRNA. Translation: ABV26009.1.
AL833039 mRNA. Translation: CAH56299.1.
CH471136 Genomic DNA. Translation: EAW99243.1.
BC018775 mRNA. Translation: AAH18775.1.
CCDSiCCDS10283.1.
RefSeqiNP_695003.1. NM_153271.1.
UniGeneiHs.8705.

Genome annotation databases

EnsembliENST00000308527; ENSP00000311427; ENSG00000173548.
GeneIDi257364.
KEGGihsa:257364.
UCSCiuc002bau.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF219141 mRNA. Translation: ABN09670.1.
EF653821 mRNA. Translation: ABV26009.1.
AL833039 mRNA. Translation: CAH56299.1.
CH471136 Genomic DNA. Translation: EAW99243.1.
BC018775 mRNA. Translation: AAH18775.1.
CCDSiCCDS10283.1.
RefSeqiNP_695003.1. NM_153271.1.
UniGeneiHs.8705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AKVX-ray2.65A/B212-574[»]
ProteinModelPortaliQ8WV41.
SMRiQ8WV41. Positions 1-100, 212-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129214. 5 interactions.
IntActiQ8WV41. 8 interactions.
MINTiMINT-2792452.
STRINGi9606.ENSP00000311427.

PTM databases

PhosphoSiteiQ8WV41.

Polymorphism and mutation databases

BioMutaiSNX33.
DMDMi74751538.

Proteomic databases

MaxQBiQ8WV41.
PaxDbiQ8WV41.
PRIDEiQ8WV41.

Protocols and materials databases

DNASUi257364.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308527; ENSP00000311427; ENSG00000173548.
GeneIDi257364.
KEGGihsa:257364.
UCSCiuc002bau.3. human.

Organism-specific databases

CTDi257364.
GeneCardsiGC15P075940.
H-InvDBHIX0012446.
HGNCiHGNC:28468. SNX33.
HPAiHPA040988.
neXtProtiNX_Q8WV41.
PharmGKBiPA162404345.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00510000046469.
HOGENOMiHOG000261633.
HOVERGENiHBG009996.
InParanoidiQ8WV41.
KOiK17923.
OMAiLRMYDNL.
OrthoDBiEOG7ZKS9P.
PhylomeDBiQ8WV41.
TreeFamiTF314082.

Miscellaneous databases

ChiTaRSiSNX33. human.
GenomeRNAii257364.
NextBioi92998.
PROiQ8WV41.

Gene expression databases

BgeeiQ8WV41.
CleanExiHS_SNX30.
HS_SNX33.
ExpressionAtlasiQ8WV41. baseline and differential.
GenevisibleiQ8WV41. HS.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR001452. SH3_domain.
IPR028642. SNX33.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERiPTHR10555:SF121. PTHR10555:SF121. 1 hit.
PfamiPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF14604. SH3_9. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome."
    Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I., Vaehae-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K.
    EMBO Rep. 7:186-191(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM15.
  2. "A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein."
    Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E., Seed B., Baumeister R., Haass C., Lichtenthaler S.F.
    J. Biol. Chem. 283:14257-14268(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DNM1 AND DNM2, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Stomach.
  4. 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: Skin.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP shedding."
    Heiseke A., Schobel S., Lichtenthaler S.F., Vorberg I., Groschup M.H., Kretzschmar H., Schatzl H.M., Nunziante M.
    Traffic 9:1116-1129(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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.
  9. "Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein."
    Zhang J., Zhang X., Guo Y., Xu L., Pei D.
    J. Biol. Chem. 284:21659-21669(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
  10. "Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
    Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
    J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM15.
  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. "Specific amino acids in the BAR domain allow homodimerization and prevent heterodimerization of sorting nexin 33."
    Dislich B., Than M.E., Lichtenthaler S.F.
    Biochem. J. 433:75-83(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION, SUBUNIT.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.
  15. "Structure of human sorting nexin 33."
    Structural genomics consortium (SGC)
    Submitted (DEC-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 212-574.

Entry informationi

Entry nameiSNX33_HUMAN
AccessioniPrimary (citable) accession number: Q8WV41
Secondary accession number(s): B1NM17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 117 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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.