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Protein

Sorting nexin-6

Gene

Snx6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity (By similarity). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R. May function as link between transport vesicles and dynactin. Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity). In association with GIT1 involved in EGFR degradation (PubMed:18523162). Promotes lysosomal degradation of CDKN1B (PubMed:20228253). May contribute to transcription regulation (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-6
Cleaved into the following chain:
Gene namesi
Name:Snx6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1919433. Snx6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Sorting nexin-6PRO_0000236198Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 406405Sorting nexin-6, N-terminally processedPRO_0000423278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylmethionine; in Sorting nexin-6, N-terminally processedBy similarity
Modified residuei194 – 1941PhosphoserineBy similarity

Post-translational modificationi

In vitro phosphorylated by PIM1; not affecting PIM1-dependent nuclear translocation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6P8X1.
MaxQBiQ6P8X1.
PaxDbiQ6P8X1.
PRIDEiQ6P8X1.

2D gel databases

REPRODUCTION-2DPAGEQ6P8X1.

PTM databases

iPTMnetiQ6P8X1.

Expressioni

Gene expression databases

BgeeiQ6P8X1.
CleanExiMM_SNX6.
GenevisibleiQ6P8X1. MM.

Interactioni

Subunit structurei

Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity (By similarity). Interacts with SNX1, SNX2, VPS26A, VPS29, VPS35, TGFB receptors, BACE1, BRMS1, PIP5K1C. Interacts with DCTN1; the association with DCTN1 is involved in movement of retromer-c ontaining vesicles toward the TGN. Interacts with PIM1; translocating SNX6 to the nucleus (By similarity). Interacts with CDKN1B and GIT1 (PubMed:18523162, PubMed:20228253).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi215205. 2 interactions.
IntActiQ6P8X1. 2 interactions.
MINTiMINT-2634295.
STRINGi10090.ENSMUSP00000005798.

Structurei

3D structure databases

ProteinModelPortaliQ6P8X1.
SMRiQ6P8X1. Positions 21-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 173148PXPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 406204BARCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 179179Interaction with PIM1By similarityAdd
BLAST
Regioni41 – 477Phosphatidylinositol bisphosphate bindingBy similarity
Regioni100 – 1067Phosphatidylinositol bisphosphate bindingBy similarity
Regioni114 – 1174Phosphatidylinositol bisphosphate bindingBy similarity
Regioni182 – 19918Membrane-binding amphipathic helixBy similarityAdd
BLAST

Domaini

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate.By similarity
The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an amphipatric helix (AH) in the membrane (By similarity).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1660. Eukaryota.
ENOG410XPZY. LUCA.
GeneTreeiENSGT00840000129756.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ6P8X1.
KOiK17920.
OMAiKTFLLEY.
OrthoDBiEOG7X0VH4.
TreeFamiTF313698.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR001683. Phox.
IPR014637. SNX5/SNX6/SNX32.
IPR028657. SNX6.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF120. PTHR10555:SF120. 2 hits.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P8X1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMEGLDDGPD FLSEEDRGLK AINVDLQSDA ALQVDISDAL SERDRVKFTV
60 70 80 90 100
HTKSSLPNFK QNEFSVVRQH EEFIWLHDSF VENEDYAGYI IPPAPPRPDF
110 120 130 140 150
DASREKLQKL GEGEGSMTKE EFTKMKQELE AEYLAIFKKT VAMHEVFLCR
160 170 180 190 200
VAAHPILRKD LNFHVFLEYN QDLSVRGKNK KEKLEDFFKN MVKSADGVIV
210 220 230 240 250
SGVKDVDDFF EHERTFLLEY HNRVKDASAK SDRMTRSHKS AADDYNRIGS
260 270 280 290 300
SLYALGTQDS TDICKFFLKV SELFDKTRKI EARVSADEDL KLSDLLKYYL
310 320 330 340 350
RESQAAKDLL YRRSRSLVDY ENANKALDKA RAKNKDVLQA ETSQQLCCQK
360 370 380 390 400
FEKISESAKQ ELIDFKTRRV AAFRKNLVEL AELELKHAKG NLQLLQNCLA

VLNGDT
Length:406
Mass (Da):46,649
Last modified:July 27, 2011 - v2
Checksum:i7B33A7325B814DAF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471K → N in AAH61028 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013158 mRNA. Translation: BAB28684.1.
BC061028 mRNA. Translation: AAH61028.1.
CCDSiCCDS36447.1.
RefSeqiNP_081274.2. NM_026998.3.
UniGeneiMm.28240.
Mm.424023.

Genome annotation databases

EnsembliENSMUST00000005798; ENSMUSP00000005798; ENSMUSG00000005656.
GeneIDi72183.
KEGGimmu:72183.
UCSCiuc007nnv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013158 mRNA. Translation: BAB28684.1.
BC061028 mRNA. Translation: AAH61028.1.
CCDSiCCDS36447.1.
RefSeqiNP_081274.2. NM_026998.3.
UniGeneiMm.28240.
Mm.424023.

3D structure databases

ProteinModelPortaliQ6P8X1.
SMRiQ6P8X1. Positions 21-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215205. 2 interactions.
IntActiQ6P8X1. 2 interactions.
MINTiMINT-2634295.
STRINGi10090.ENSMUSP00000005798.

PTM databases

iPTMnetiQ6P8X1.

2D gel databases

REPRODUCTION-2DPAGEQ6P8X1.

Proteomic databases

EPDiQ6P8X1.
MaxQBiQ6P8X1.
PaxDbiQ6P8X1.
PRIDEiQ6P8X1.

Protocols and materials databases

DNASUi72183.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005798; ENSMUSP00000005798; ENSMUSG00000005656.
GeneIDi72183.
KEGGimmu:72183.
UCSCiuc007nnv.1. mouse.

Organism-specific databases

CTDi58533.
MGIiMGI:1919433. Snx6.

Phylogenomic databases

eggNOGiKOG1660. Eukaryota.
ENOG410XPZY. LUCA.
GeneTreeiENSGT00840000129756.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ6P8X1.
KOiK17920.
OMAiKTFLLEY.
OrthoDBiEOG7X0VH4.
TreeFamiTF313698.

Miscellaneous databases

PROiQ6P8X1.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P8X1.
CleanExiMM_SNX6.
GenevisibleiQ6P8X1. MM.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR001683. Phox.
IPR014637. SNX5/SNX6/SNX32.
IPR028657. SNX6.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF120. PTHR10555:SF120. 2 hits.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. "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: Brain.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 376-386, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "An epidermal growth factor (EGF) -dependent interaction between GIT1 and sorting nexin 6 promotes degradation of the EGF receptor."
    Cavet M.E., Pang J., Yin G., Berk B.C.
    FASEB J. 22:3607-3616(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GIT1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Tumor suppressor p27(Kip1) undergoes endolysosomal degradation through its interaction with sorting nexin 6."
    Fuster J.J., Gonzalez J.M., Edo M.D., Viana R., Boya P., Cervera J., Verges M., Rivera J., Andres V.
    FASEB J. 24:2998-3009(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN1B.

Entry informationi

Entry nameiSNX6_MOUSE
AccessioniPrimary (citable) accession number: Q6P8X1
Secondary accession number(s): Q9CZ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.