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Q8WV41 (SNX33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorting nexin-33
Alternative name(s):
SH3 and PX domain-containing protein 3
Gene names
Name:SNX33
Synonyms:SH3PX3, SH3PXD3C, SNX30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.7 Ref.9 Ref.11 Ref.12 Ref.14

Subunit structure

Homodimer (via BAR domain). Interacts with ADAM15. Interacts with FASLG. Interacts (via SH3 domain) with DNM1 and DNM2. Interacts with WASL. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Cytoplasmcytosol. Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Primarily cytosolic, but a minor proportion is membrane-bound (Ref.2). Not associated with membranes (Ref.11). Ref.2 Ref.9 Ref.11 Ref.12 Ref.14

Tissue specificity

Detected in heart and pancreas. Ref.2

Domain

The PX and BAR domains mediate association with membranes and are required for membrane tubulation. Ref.12

Post-translational modification

Phosphorylated. Ref.2

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 componentCytoplasm
Cytoplasmic vesicle
Membrane
   DomainSH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcleavage furrow formation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.14. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.14. Source: UniProtKB

endosome organization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

intracellular protein transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

macropinocytosis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

membrane tubulation

Inferred from direct assay Ref.12. Source: UniProtKB

mitotic cytokinesis

Inferred from mutant phenotype Ref.14. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

extrinsic component of membrane

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.9PubMed 23085988. Source: IntAct

phosphatidylinositol binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.1Ref.9Ref.8PubMed 23085988. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Sorting nexin-33
PRO_0000311948

Regions

Domain1 – 6161SH3
Domain230 – 340111PX
Domain371 – 574204BAR
Compositional bias112 – 12211Poly-Asp

Amino acid modifications

Modified residue771Phosphoserine Ref.6

Secondary structure

.......................................... 574
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WV41 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7CE51C0F35DDBC3C

FASTA57465,265
        10         20         30         40         50         60 
MALKGRALYD FHSENKEEIS IQQDEDLVIF SETSLDGWLQ GQNSRGETGL FPASYVEIVR 

        70         80         90        100        110        120 
SGISTNHADY SSSPAGSPGA QVSLYNSPSV ASPARSGGGS GFLSNQGSFE EDDDDDWDDW 

       130        140        150        160        170        180 
DDGCTVVEEP RAGGLGTNGH PPLNLSYPGA YPSQHMAFRP KPPLERQDSL ASAKRGSVVG 

       190        200        210        220        230        240 
RNLNRFSCFV RSGVEAFILG DVPMMAKIAE TYSIEMGPRG PQWKANPHPF ACSVEDPTKQ 

       250        260        270        280        290        300 
TKFKGIKSYI SYKLTPTHAA SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE 

       310        320        330        340        350        360 
DFIEKRKRRL ILWMDHMTSH PVLSQYEGFQ HFLSCLDDKQ WKMGKRRAEK DEMVGASFLL 

       370        380        390        400        410        420 
TFQIPTEHQD LQDVEDRVDT FKAFSKKMDD SVLQLSTVAS ELVRKHVGGF RKEFQKLGSA 

       430        440        450        460        470        480 
FQAISHSFQM DPPFCSEALN SAISHTGRTY EAIGEMFAEQ PKNDLFQMLD TLSLYQGLLS 

       490        500        510        520        530        540 
NFPDIIHLQK GAFAKVKESQ RMSDEGRMVQ DEADGIRRRC RVVGFALQAE MNHFHQRREL 

       550        560        570 
DFKHMMQNYL RQQILFYQRV GQQLEKTLRM YDNL 

« Hide

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Stomach.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10283.1.
RefSeqNP_695003.1. NM_153271.1.
UniGeneHs.8705.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AKVX-ray2.65A/B212-574[»]
ProteinModelPortalQ8WV41.
SMRQ8WV41. Positions 1-100, 212-573.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129214. 3 interactions.
IntActQ8WV41. 5 interactions.
MINTMINT-2792452.
STRING9606.ENSP00000311427.

PTM databases

PhosphoSiteQ8WV41.

Polymorphism databases

DMDM74751538.

Proteomic databases

MaxQBQ8WV41.
PaxDbQ8WV41.
PRIDEQ8WV41.

Protocols and materials databases

DNASU257364.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308527; ENSP00000311427; ENSG00000173548.
GeneID257364.
KEGGhsa:257364.
UCSCuc002bau.3. human.

Organism-specific databases

CTD257364.
GeneCardsGC15P075940.
H-InvDBHIX0012446.
HGNCHGNC:28468. SNX33.
HPAHPA040988.
neXtProtNX_Q8WV41.
PharmGKBPA162404345.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5391.
HOGENOMHOG000261633.
HOVERGENHBG009996.
InParanoidQ8WV41.
KOK17923.
OMAQGSFEDD.
OrthoDBEOG7ZKS9P.
PhylomeDBQ8WV41.
TreeFamTF314082.

Gene expression databases

ArrayExpressQ8WV41.
BgeeQ8WV41.
CleanExHS_SNX30.
HS_SNX33.
GenevestigatorQ8WV41.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR001452. SH3_domain.
IPR028642. SNX33.
IPR014536. Snx9_subfam.
IPR019497. Sorting_nexin_WASP-bd-dom.
[Graphical view]
PANTHERPTHR10555:SF121. PTHR10555:SF121. 1 hit.
PfamPF10456. BAR_3_WASP_bdg. 1 hit.
PF00787. PX. 1 hit.
PF14604. SH3_9. 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

GenomeRNAi257364.
NextBio92998.
PROQ8WV41.

Entry information

Entry nameSNX33_HUMAN
AccessionPrimary (citable) accession number: Q8WV41
Secondary accession number(s): B1NM17
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM