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Protein

Sorting nexin-2

Gene

Snx2

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 containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). 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). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Required for retrograde endosome-to-TGN transport of TGN38. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831Phosphatidylinositol 3-phosphateBy similarity
Binding sitei185 – 1851Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei211 – 2111Phosphatidylinositol 3-phosphateBy similarity
Binding sitei235 – 2351Phosphatidylinositol 3-phosphateBy similarity

GO - Molecular functioni

  1. epidermal growth factor receptor binding Source: MGI
  2. insulin receptor binding Source: MGI
  3. leptin receptor binding Source: MGI
  4. phosphatidylinositol binding Source: GO_Central
  5. transferrin receptor binding Source: MGI

GO - Biological processi

  1. early endosome to Golgi transport Source: GO_Central
  2. endocytosis Source: GO_Central
  3. intracellular protein transport Source: InterPro
  4. lamellipodium morphogenesis Source: UniProtKB
  5. protein oligomerization Source: MGI
  6. retrograde transport, endosome to Golgi Source: UniProtKB
  7. vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_232671. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-2
Gene namesi
Name:Snx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1915054. Snx2.

Subcellular locationi

Early endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionlamellipodium
Note: Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in cells in a KALRN-dependent manner (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. early endosome membrane Source: UniProtKB-SubCell
  3. endosome membrane Source: UniProtKB
  4. extracellular vesicular exosome Source: MGI
  5. extrinsic component of membrane Source: GO_Central
  6. intracellular membrane-bounded organelle Source: MGI
  7. lamellipodium Source: UniProtKB-SubCell
  8. membrane Source: UniProtKB
  9. protein complex Source: MGI
  10. retromer complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are born at the expected Mendelian ratio and are fertile. Mice lacking both Snx1 and Snx2 die during embryonic development, around 9.5 and 11.5 dpc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Sorting nexin-2PRO_0000213839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011PhosphothreonineBy similarity
Modified residuei104 – 1041PhosphothreonineBy similarity
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei469 – 4691N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CWK8.
PaxDbiQ9CWK8.
PRIDEiQ9CWK8.

PTM databases

PhosphoSiteiQ9CWK8.

Expressioni

Gene expression databases

BgeeiQ9CWK8.
CleanExiMM_SNX2.
GenevestigatoriQ9CWK8.

Interactioni

Subunit structurei

Predominantly forms heterodimers with BAR domain-containing sorting nexins SNX5, SNX6 and SNX32; can self-associate to form homodimers. 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. Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, FNBP1, KALRN, RHOG (GDP-bound form) (By similarity).By similarity

Protein-protein interaction databases

BioGridi212452. 1 interaction.
MINTiMINT-1864976.

Structurei

3D structure databases

ProteinModelPortaliQ9CWK8.
SMRiQ9CWK8. Positions 140-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 269130PXPROSITE-ProRule annotationAdd
BLAST
Domaini299 – 519221BARBy similarityAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 519260Interaction with RhoGBy similarityAdd
BLAST
Regioni278 – 29518Membrane-binding amphipathic helixBy similarityAdd
BLAST

Domaini

The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of a N-terminal amphipatric helix (AH) in the membrane (By similarity).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00780000121895.
HOGENOMiHOG000293327.
HOVERGENiHBG000618.
InParanoidiQ9CWK8.
KOiK17917.
OMAiQQFDDIS.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ9CWK8.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028653. SNX2.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF31. PTHR10555:SF31. 1 hit.
PfamiPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CWK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEREPPPL GDVKPTDFEE LEDGEDLFTS TVSTLESSPS SPEPASLPAE
60 70 80 90 100
DISANSNGSK PVEVVLDDDR EDLFAEATEE VSLDSPEREL ILSSEPSPAV
110 120 130 140 150
TPVTPTTLIA PRIESKSISA PVIFDRSRDE IEEEANGDIF DIEIGVSDPE
160 170 180 190 200
KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV KRRFSDFLGL HSKLASKYLH
210 220 230 240 250
VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE RYLQRTVKHP
260 270 280 290 300
TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN
310 320 330 340 350
ESDAWFEEKQ QQFENLDQQL RKLHASVEAL VCHRKELSAN TAAFAKSAAM
360 370 380 390 400
LGNSEDHTAL SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI
410 420 430 440 450
AAVKGVFDHR MKCWQKWEDA QITLLKKRET EAKMMVANKP DKIQQAKNEI
460 470 480 490 500
REWEAKVQQG ERDFEQISKT IRKEVGRFEK ERVKDFKAVI IKYLESLVQT
510
QQQLIKYWEA FLPEAKAIA
Length:519
Mass (Da):58,471
Last modified:March 27, 2002 - v2
Checksum:i55DD0BB74E82CD82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451R → I in BAB27035 (PubMed:16141072).Curated
Sequence conflicti428 – 4281R → P in BAB27035 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002692 mRNA. Translation: BAB22287.1.
AK005470 mRNA. Translation: BAB24060.1.
AK010572 mRNA. Translation: BAB27035.1.
AK075929 mRNA. Translation: BAC36060.1.
AK145840 mRNA. Translation: BAE26688.1.
CCDSiCCDS37821.1.
RefSeqiNP_080662.1. NM_026386.1.
UniGeneiMm.252171.

Genome annotation databases

EnsembliENSMUST00000037850; ENSMUSP00000039243; ENSMUSG00000034484.
GeneIDi67804.
KEGGimmu:67804.
UCSCiuc008exr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002692 mRNA. Translation: BAB22287.1.
AK005470 mRNA. Translation: BAB24060.1.
AK010572 mRNA. Translation: BAB27035.1.
AK075929 mRNA. Translation: BAC36060.1.
AK145840 mRNA. Translation: BAE26688.1.
CCDSiCCDS37821.1.
RefSeqiNP_080662.1. NM_026386.1.
UniGeneiMm.252171.

3D structure databases

ProteinModelPortaliQ9CWK8.
SMRiQ9CWK8. Positions 140-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212452. 1 interaction.
MINTiMINT-1864976.

PTM databases

PhosphoSiteiQ9CWK8.

Proteomic databases

MaxQBiQ9CWK8.
PaxDbiQ9CWK8.
PRIDEiQ9CWK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037850; ENSMUSP00000039243; ENSMUSG00000034484.
GeneIDi67804.
KEGGimmu:67804.
UCSCiuc008exr.1. mouse.

Organism-specific databases

CTDi6643.
MGIiMGI:1915054. Snx2.

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00780000121895.
HOGENOMiHOG000293327.
HOVERGENiHBG000618.
InParanoidiQ9CWK8.
KOiK17917.
OMAiQQFDDIS.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ9CWK8.
TreeFamiTF313698.

Enzyme and pathway databases

ReactomeiREACT_232671. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiSnx2. mouse.
NextBioi325603.
PROiQ9CWK8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CWK8.
CleanExiMM_SNX2.
GenevestigatoriQ9CWK8.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028653. SNX2.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF31. PTHR10555:SF31. 1 hit.
PfamiPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
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.
    Tissue: Embryonic stem cell, Kidney and Placenta.
  2. "Genetic analysis of sorting nexins 1 and 2 reveals a redundant and essential function in mice."
    Schwarz D.G., Griffin C.T., Schneider E.A., Yee D., Magnuson T.
    Mol. Biol. Cell 13:3588-3600(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSNX2_MOUSE
AccessioniPrimary (citable) accession number: Q9CWK8
Secondary accession number(s): Q3UKW3, Q9CQV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: March 27, 2002
Last modified: March 4, 2015
This is version 100 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, 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

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.