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Protein

Sorting nexin-2

Gene

SNX2

Organism
Homo sapiens (Human)
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) (PubMed:16179610). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:17101778). 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) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Required for retrograde endosome-to-TGN transport of TGN38 (PubMed:20138391). Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (PubMed:20604901).1 Publication5 Publications

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

  • epidermal growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • leptin receptor binding Source: UniProtKB
  • phosphatidylinositol binding Source: GO_Central
  • transferrin receptor binding Source: UniProtKB

GO - Biological processi

  • early endosome to Golgi transport Source: GO_Central
  • endocytosis Source: GO_Central
  • intracellular protein transport Source: InterPro
  • lamellipodium morphogenesis Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-2
Alternative name(s):
Transformation-related gene 9 protein
Short name:
TRG-9
Gene namesi
Name:SNX2
ORF Names:TRG9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11173. SNX2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • early endosome membrane Source: UniProtKB-SubCell
  • endosome Source: GO_Central
  • endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extrinsic component of membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: HPA
  • lamellipodium Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • protein complex Source: UniProtKB
  • retromer complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1843RRF → AAA: Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN. 1 Publication
Mutagenesisi211 – 2111K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 1 Publication
Mutagenesisi426 – 4261K → A: Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN; when associated with A-428. 1 Publication
Mutagenesisi428 – 4281R → A: Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN; when associated with A-426. 1 Publication

Organism-specific databases

PharmGKBiPA36012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Sorting nexin-2PRO_0000213838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011Phosphothreonine1 Publication
Modified residuei104 – 1041Phosphothreonine1 Publication
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine2 Publications
Modified residuei277 – 2771Phosphoserine3 Publications
Modified residuei469 – 4691N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60749.
PaxDbiO60749.
PeptideAtlasiO60749.
PRIDEiO60749.

PTM databases

PhosphoSiteiO60749.

Expressioni

Gene expression databases

BgeeiO60749.
CleanExiHS_SNX2.
ExpressionAtlasiO60749. baseline and differential.
GenevisibleiO60749. HS.

Organism-specific databases

HPAiHPA037400.

Interactioni

Subunit structurei

Predominantly forms heterodimers with BAR domain-containing sorting nexins SNX5, SNX6 and SNX32; can self-associate to form homodimers (PubMed:23085988). 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 (Probable). Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, FNBP1, KALRN, RHOG (GDP-bound form) (PubMed:11438682, PubMed:14596906, PubMed:17101778, PubMed:19935774., PubMed:19619496, PubMed:20604901, PubMed:23085988).3 Publications7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FNBP1Q96RU34EBI-1046690,EBI-1111248

Protein-protein interaction databases

BioGridi112526. 47 interactions.
IntActiO60749. 20 interactions.
MINTiMINT-5000817.
STRINGi9606.ENSP00000368831.

Structurei

3D structure databases

ProteinModelPortaliO60749.
SMRiO60749. 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 RhoG1 PublicationAdd
BLAST
Regioni278 – 29518Membrane-binding amphipathic helix1 PublicationAdd
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 (Probable).2 Publications

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.
InParanoidiO60749.
KOiK17917.
OMAiCEEHTGL.
OrthoDBiEOG7HHWSB.
PhylomeDBiO60749.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60749-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAEREPPPL GDGKPTDFED LEDGEDLFTS TVSTLESSPS SPEPASLPAE
60 70 80 90 100
DISANSNGPK PTEVVLDDDR EDLFAEATEE VSLDSPEREP ILSSEPSPAV
110 120 130 140 150
TPVTPTTLIA PRIESKSMSA PVIFDRSREE 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 RKLHVSVEAL VCHRKELSAN TAAFAKSAAM
360 370 380 390 400
LGNSEDHTAL SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI
410 420 430 440 450
AAVKGVFDHR MKCWQKWEDA QITLLKKREA EAKMMVANKP DKIQQAKNEI
460 470 480 490 500
REWEAKVQQG ERDFEQISKT IRKEVGRFEK ERVKDFKTVI IKYLESLVQT
510
QQQLIKYWEA FLPEAKAIA
Length:519
Mass (Da):58,471
Last modified:May 30, 2006 - v2
Checksum:i7DC07DFA523312B5
GO
Isoform 2 (identifier: O60749-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Show »
Length:402
Mass (Da):46,098
Checksum:i4CF80EFD3B9C160D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871E → A in AAQ02693 (Ref. 3) Curated
Sequence conflicti146 – 1461V → I in BAH12394 (PubMed:14702039).Curated
Sequence conflicti331 – 3311V → F (Ref. 1) Curated
Sequence conflicti331 – 3311V → F (PubMed:9819414).Curated
Sequence conflicti384 – 3841A → S (Ref. 1) Curated
Sequence conflicti384 – 3841A → S (PubMed:9819414).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 117117Missing in isoform 2. 1 PublicationVSP_054785Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065482 mRNA. Translation: AAC17181.1.
AF043453 mRNA. Translation: AAB99852.1.
AY272044 mRNA. Translation: AAQ02693.1.
BT009841 mRNA. Translation: AAP88843.1.
AK023581 mRNA. Translation: BAG51206.1.
AK293671 mRNA. Translation: BAG57115.1.
AK296596 mRNA. Translation: BAH12394.1.
AC008669 Genomic DNA. No translation available.
AC093267 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48884.1.
BC003382 mRNA. Translation: AAH03382.1.
CCDSiCCDS34217.1. [O60749-1]
CCDS64234.1. [O60749-2]
RefSeqiNP_001265128.1. NM_001278199.1. [O60749-2]
NP_003091.2. NM_003100.3. [O60749-1]
UniGeneiHs.125352.
Hs.713554.

Genome annotation databases

EnsembliENST00000379516; ENSP00000368831; ENSG00000205302.
ENST00000514949; ENSP00000421663; ENSG00000205302. [O60749-2]
GeneIDi6643.
KEGGihsa:6643.
UCSCiuc003kte.4. human. [O60749-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065482 mRNA. Translation: AAC17181.1.
AF043453 mRNA. Translation: AAB99852.1.
AY272044 mRNA. Translation: AAQ02693.1.
BT009841 mRNA. Translation: AAP88843.1.
AK023581 mRNA. Translation: BAG51206.1.
AK293671 mRNA. Translation: BAG57115.1.
AK296596 mRNA. Translation: BAH12394.1.
AC008669 Genomic DNA. No translation available.
AC093267 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48884.1.
BC003382 mRNA. Translation: AAH03382.1.
CCDSiCCDS34217.1. [O60749-1]
CCDS64234.1. [O60749-2]
RefSeqiNP_001265128.1. NM_001278199.1. [O60749-2]
NP_003091.2. NM_003100.3. [O60749-1]
UniGeneiHs.125352.
Hs.713554.

3D structure databases

ProteinModelPortaliO60749.
SMRiO60749. Positions 140-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112526. 47 interactions.
IntActiO60749. 20 interactions.
MINTiMINT-5000817.
STRINGi9606.ENSP00000368831.

PTM databases

PhosphoSiteiO60749.

Proteomic databases

MaxQBiO60749.
PaxDbiO60749.
PeptideAtlasiO60749.
PRIDEiO60749.

Protocols and materials databases

DNASUi6643.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379516; ENSP00000368831; ENSG00000205302.
ENST00000514949; ENSP00000421663; ENSG00000205302. [O60749-2]
GeneIDi6643.
KEGGihsa:6643.
UCSCiuc003kte.4. human. [O60749-1]

Organism-specific databases

CTDi6643.
GeneCardsiGC05P122110.
HGNCiHGNC:11173. SNX2.
HPAiHPA037400.
MIMi605929. gene.
neXtProtiNX_O60749.
PharmGKBiPA36012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00780000121895.
HOGENOMiHOG000293327.
HOVERGENiHBG000618.
InParanoidiO60749.
KOiK17917.
OMAiCEEHTGL.
OrthoDBiEOG7HHWSB.
PhylomeDBiO60749.
TreeFamiTF313698.

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiSNX2. human.
GeneWikiiSNX2.
GenomeRNAii6643.
NextBioi25889.
PROiO60749.
SOURCEiSearch...

Gene expression databases

BgeeiO60749.
CleanExiHS_SNX2.
ExpressionAtlasiO60749. baseline and differential.
GenevisibleiO60749. HS.

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. Kurten R.C., Leychkis Y., Wiley H.S., Gill G.N.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Identification of a family of sorting nexin molecules and characterization of their association with receptors."
    Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.
    Mol. Cell. Biol. 18:7278-7287(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
  3. "Identification of a human transforming gene."
    Kim J.W.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum, Colon and Placenta.
  6. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes."
    Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A., Barr V.A., Taylor S.I.
    Mol. Biol. Cell 11:4105-4116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia."
    Fuchs U., Rehkamp G.F., Haas O.A., Slany R., Koenig M., Bojesen S., Bohle R.M., Damm-Welk C., Ludwig W.-D., Harbott J., Borkhardt A.
    Proc. Natl. Acad. Sci. U.S.A. 98:8756-8761(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FNBP1.
  11. "The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance."
    Fuchs U., Rehkamp G.F., Slany R., Follo M., Borkhardt A.
    FEBS Lett. 554:10-16(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FNBP1.
  12. "Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport."
    Carlton J.G., Bujny M.V., Peter B.J., Oorschot V.M., Rutherford A., Arkell R.S., Klumperman J., McMahon H.T., Cullen P.J.
    J. Cell Sci. 118:4527-4539(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-211, SUBCELLULAR LOCATION.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors."
    Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.
    Mol. Cell. Biol. 27:1112-1124(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-phosphate receptors."
    Mari M., Bujny M.V., Zeuschner D., Geerts W.J., Griffith J., Petersen C.M., Cullen P.J., Klumperman J., Geuze H.J.
    Traffic 9:380-393(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport."
    Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.
    Cell Res. 19:1334-1349(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX6.
  18. "The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network."
    Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J., Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.
    Dev. Cell 17:110-122(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX5; SNX6; VPS26A; VPS29 AND VPS35.
  19. "Amphipathic motifs in BAR domains are essential for membrane curvature sensing."
    Bhatia V.K., Madsen K.L., Bolinger P.Y., Kunding A., Hedegaard P., Gether U., Stamou D.
    EMBO J. 28:3303-3314(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Identification of different itineraries and retromer components for endosome-to-Golgi transport of TGN38 and Shiga toxin."
    Lieu Z.Z., Gleeson P.A.
    Eur. J. Cell Biol. 89:379-393(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "A novel, retromer-independent role for sorting nexins 1 and 2 in RhoG-dependent membrane remodeling."
    Prosser D.C., Tran D., Schooley A., Wendland B., Ngsee J.K.
    Traffic 11:1347-1362(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KALRN AND RHOG, SUBCELLULAR LOCATION, MUTAGENESIS OF 182-ARG--PHE-184; LYS-426 AND ARG-428.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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].
  27. "Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules."
    van Weering J.R., Sessions R.B., Traer C.J., Kloer D.P., Bhatia V.K., Stamou D., Carlsson S.R., Hurley J.H., Cullen P.J.
    EMBO J. 31:4466-4480(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNX5; SNX6 AND SNX32, SELF-ASSOCIATION, DOMAIN.
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; THR-104; SER-185 AND SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSNX2_HUMAN
AccessioniPrimary (citable) accession number: O60749
Secondary accession number(s): B3KN44
, B4DEK4, B7Z408, O43650, P82862, Q53XK8, Q597H6, Q9BTS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 30, 2006
Last modified: July 22, 2015
This is version 136 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. 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.