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Q13596

- SNX1_HUMAN

UniProt

Q13596 - SNX1_HUMAN

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Protein

Sorting nexin-1

Gene

SNX1

Organism
Homo sapiens (Human)
Status
Reviewed - 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:12198132). 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) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity (PubMed:19816406, PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1) and Shiginella dysenteria toxin stxB. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi (PubMed:12198132, PubMed:15498486, PubMed:17550970, PubMed:17101778, PubMed:18088323, PubMed:21040701). Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R (PubMed:16407403, PubMed:20070609). 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). Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (PubMed:23152498).12 Publications1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861Phosphatidylinositol 3-phosphateBy similarity
Binding sitei188 – 1881Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei214 – 2141Phosphatidylinositol 3-phosphateBy similarity
Binding sitei238 – 2381Phosphatidylinositol 3-phosphateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. early endosome to Golgi transport Source: UniProtKB
  2. intracellular protein transport Source: UniProtKB
  3. positive regulation of protein catabolic process Source: Ensembl
  4. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-1
Gene namesi
Name:SNX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11172. SNX1.

Subcellular locationi

Endosome membrane 2 Publications; Peripheral membrane protein; Cytoplasmic side. Golgi apparatustrans-Golgi network membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium 1 Publication
Note: Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (PubMed:15498486). 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 (PubMed:18088323). Colocalizes with DNAJC13 and Shiginella dysenteria toxin stxB on early endosomes (PubMed:19874558). Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner (PubMed:20604901).3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. cytoplasmic membrane-bounded vesicle Source: RefGenome
  3. cytosol Source: Ensembl
  4. early endosome membrane Source: UniProtKB
  5. endosome membrane Source: UniProtKB
  6. Golgi apparatus Source: UniProtKB-SubCell
  7. intracellular membrane-bounded organelle Source: HPA
  8. membrane Source: UniProtKB
  9. protein complex Source: UniProtKB
  10. retromer complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 2 Publications
Mutagenesisi287 – 2882MF → EE: Abolishes membrane remodeling capacity; no effect on dimerization. 1 Publication
Mutagenesisi429 – 4313KKR → EEE: Loss of endosomal location. 1 Publication
Mutagenesisi442 – 4421K → A: No effect on membrane remodeling and membrane binding; when associated with A-445. 1 Publication
Mutagenesisi445 – 4451K → A: No effect on membrane remodeling and membrane binding; when associated with A-442. 1 Publication

Organism-specific databases

PharmGKBiPA36011.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Sorting nexin-1PRO_0000213835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication
Modified residuei188 – 1881Phosphoserine3 Publications
Modified residuei237 – 2371N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13596.
PaxDbiQ13596.
PRIDEiQ13596.

PTM databases

PhosphoSiteiQ13596.

Expressioni

Gene expression databases

BgeeiQ13596.
CleanExiHS_SNX1.
ExpressionAtlasiQ13596. baseline and differential.
GenevestigatoriQ13596.

Organism-specific databases

HPAiHPA047373.
HPA052761.

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 described 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, DRD5, DENND5A, KALRN, RHOG (GDP-bound form) (PubMed:9819414, PubMed:11102511, PubMed:19619496, PubMed:19935774, PubMed:19619496, PubMed:20604901, PubMed:23085988, PubMed:23152498). The interaction with SNX2 is reported controversially (PubMed:9819414, PubMed:11997453, PubMed:19619496, PubMed:23085988). Interacts with DNAJC13; prevented by presence of HGS (PubMed:19874558). Interacts with HGS (By similarity).By similarity12 Publications2 Publications

Protein-protein interaction databases

BioGridi112525. 36 interactions.
DIPiDIP-398N.
IntActiQ13596. 10 interactions.
MINTiMINT-4135098.
STRINGi9606.ENSP00000369638.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi173 – 1764
Helixi187 – 19913
Beta strandi202 – 2054
Beta strandi210 – 2134
Beta strandi216 – 2216
Helixi234 – 25118
Helixi253 – 2564
Helixi259 – 2624
Turni263 – 2664
Helixi307 – 35650
Helixi361 – 38525
Helixi388 – 44053
Helixi443 – 48341
Turni484 – 4874
Helixi489 – 51123

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I4KNMR-A142-269[»]
4FZSX-ray2.80A/B301-522[»]
ProteinModelPortaliQ13596.
SMRiQ13596. Positions 142-269, 305-513.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13596.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 272130PXPROSITE-ProRule annotationAdd
BLAST
Domaini302 – 522221BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni281 – 29818Membrane-binding amphipathic helix1 PublicationAdd
BLAST

Domaini

The BAR domain is able to sense membrane curvature upon dimerization (PubMed:19816406). Membrane remodeling seems to implicate insertion of a N-terminal amphipatric helix (AH) in the membrane (Probable).1 Publication1 Publication

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

eggNOGiCOG5391.
GeneTreeiENSGT00760000119259.
HOVERGENiHBG000618.
InParanoidiQ13596.
KOiK17917.
OMAiEIAEWES.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ13596.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF129. PTHR10555:SF129. 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13596-1) [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
MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA
60 70 80 90 100
AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS
110 120 130 140 150
TQNNQKKVLA KTLISLPPQE ATNSSKPQPT YEELEEEEQE DQFDLTVGIT
160 170 180 190 200
DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ FAVKRRFSDF LGLYEKLSEK
210 220 230 240 250
HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA ALERYLQRIV
260 270 280 290 300
NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI
310 320 330 340 350
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS
360 370 380 390 400
LAMLGSSEDN TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI
410 420 430 440 450
RLLAIVRAAF DQRMKTWQRW QDAQATLQKK REAEARLLWA NKPDKLQQAK
460 470 480 490 500
DEILEWESRV TQYERDFERI STVVRKEVIR FEKEKSKDFK NHVIKYLETL
510 520
LYSQQQLAKY WEAFLPEAKA IS
Length:522
Mass (Da):59,070
Last modified:November 16, 2001 - v3
Checksum:i6AC8AA0A589513E3
GO
Isoform 1A (identifier: Q13596-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     91-155: Missing.

Show »
Length:457
Mass (Da):51,813
Checksum:i3F844B9E84C258C2
GO
Isoform 3 (identifier: Q13596-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     507-522: LAKYWEAFLPEAKAIS → AGEQLGIRSGILLTKKLPRYSKFFSTVHKFCAAASLWKWGFFLSAYLSYLF

Note: No experimental confirmation available.

Show »
Length:557
Mass (Da):63,082
Checksum:iA03926548995DDA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171P → S in AAC17182. (PubMed:9819414)Curated
Sequence conflicti211 – 2111P → S in AAC17182. (PubMed:9819414)Curated
Sequence conflicti211 – 2111P → S in AAC17183. (PubMed:9819414)Curated
Sequence conflicti502 – 5021Y → C in BAC87312. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151S → Y.
Corresponds to variant rs1049501 [ dbSNP | Ensembl ].
VAR_052477
Natural varianti466 – 4661D → N.
Corresponds to variant rs1802376 [ dbSNP | Ensembl ].
VAR_034507

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei91 – 15565Missing in isoform 1A. CuratedVSP_006189Add
BLAST
Alternative sequencei507 – 52216LAKYW…AKAIS → AGEQLGIRSGILLTKKLPRY SKFFSTVHKFCAAASLWKWG FFLSAYLSYLF in isoform 3. 1 PublicationVSP_044823Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53225 mRNA. Translation: AAA98672.1.
AF065483 mRNA. Translation: AAC17182.1.
AF065484 mRNA. Translation: AAC17183.1.
BT006983 mRNA. Translation: AAP35629.1.
AK128179 mRNA. Translation: BAC87312.1.
AK291752 mRNA. Translation: BAF84441.1.
AC021541 Genomic DNA. No translation available.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77663.1.
CH471082 Genomic DNA. Translation: EAW77665.1.
BC000357 mRNA. Translation: AAH00357.1.
CCDSiCCDS32266.1. [Q13596-1]
CCDS32268.1. [Q13596-2]
CCDS58371.1. [Q13596-3]
PIRiG02522.
RefSeqiNP_001229862.1. NM_001242933.1. [Q13596-3]
NP_003090.2. NM_003099.4. [Q13596-1]
NP_683758.1. NM_148955.3. [Q13596-2]
UniGeneiHs.188634.

Genome annotation databases

EnsembliENST00000261889; ENSP00000261889; ENSG00000028528. [Q13596-3]
ENST00000559844; ENSP00000453785; ENSG00000028528. [Q13596-1]
ENST00000561026; ENSP00000453567; ENSG00000028528. [Q13596-2]
GeneIDi6642.
KEGGihsa:6642.
UCSCiuc002amv.3. human. [Q13596-1]
uc002amx.3. human. [Q13596-2]

Polymorphism databases

DMDMi17380569.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53225 mRNA. Translation: AAA98672.1 .
AF065483 mRNA. Translation: AAC17182.1 .
AF065484 mRNA. Translation: AAC17183.1 .
BT006983 mRNA. Translation: AAP35629.1 .
AK128179 mRNA. Translation: BAC87312.1 .
AK291752 mRNA. Translation: BAF84441.1 .
AC021541 Genomic DNA. No translation available.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77663.1 .
CH471082 Genomic DNA. Translation: EAW77665.1 .
BC000357 mRNA. Translation: AAH00357.1 .
CCDSi CCDS32266.1. [Q13596-1 ]
CCDS32268.1. [Q13596-2 ]
CCDS58371.1. [Q13596-3 ]
PIRi G02522.
RefSeqi NP_001229862.1. NM_001242933.1. [Q13596-3 ]
NP_003090.2. NM_003099.4. [Q13596-1 ]
NP_683758.1. NM_148955.3. [Q13596-2 ]
UniGenei Hs.188634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I4K NMR - A 142-269 [» ]
4FZS X-ray 2.80 A/B 301-522 [» ]
ProteinModelPortali Q13596.
SMRi Q13596. Positions 142-269, 305-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112525. 36 interactions.
DIPi DIP-398N.
IntActi Q13596. 10 interactions.
MINTi MINT-4135098.
STRINGi 9606.ENSP00000369638.

PTM databases

PhosphoSitei Q13596.

Polymorphism databases

DMDMi 17380569.

Proteomic databases

MaxQBi Q13596.
PaxDbi Q13596.
PRIDEi Q13596.

Protocols and materials databases

DNASUi 6642.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261889 ; ENSP00000261889 ; ENSG00000028528 . [Q13596-3 ]
ENST00000559844 ; ENSP00000453785 ; ENSG00000028528 . [Q13596-1 ]
ENST00000561026 ; ENSP00000453567 ; ENSG00000028528 . [Q13596-2 ]
GeneIDi 6642.
KEGGi hsa:6642.
UCSCi uc002amv.3. human. [Q13596-1 ]
uc002amx.3. human. [Q13596-2 ]

Organism-specific databases

CTDi 6642.
GeneCardsi GC15P065757.
HGNCi HGNC:11172. SNX1.
HPAi HPA047373.
HPA052761.
MIMi 601272. gene.
neXtProti NX_Q13596.
PharmGKBi PA36011.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5391.
GeneTreei ENSGT00760000119259.
HOVERGENi HBG000618.
InParanoidi Q13596.
KOi K17917.
OMAi EIAEWES.
OrthoDBi EOG7HHWSB.
PhylomeDBi Q13596.
TreeFami TF313698.

Miscellaneous databases

ChiTaRSi SNX1. human.
EvolutionaryTracei Q13596.
GeneWikii SNX1.
GenomeRNAii 6642.
NextBioi 25881.
PROi Q13596.
SOURCEi Search...

Gene expression databases

Bgeei Q13596.
CleanExi HS_SNX1.
ExpressionAtlasi Q13596. baseline and differential.
Genevestigatori Q13596.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view ]
PANTHERi PTHR10555:SF129. PTHR10555:SF129. 1 hit.
Pfami PF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Enhanced degradation of EGF receptors by a sorting nexin, SNX1."
    Kurten R.C., Cadena D.L., Gill G.N.
    Science 272:1008-1010(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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], ALTERNATIVE SPLICING, INTERACTION WITH VPS26A; VPS29; VPS35 AND SNX2.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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 3).
    Tissue: Placenta and Testis.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Muscle.
  8. "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: INTERACTION WITH VPS26A, SUBUNIT.
  9. "The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation."
    Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D., Mellor H., Cullen P.J.
    J. Biol. Chem. 277:48730-48736(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214, INTERACTION WITH PHOSPHATIDYLINOSITIDES.
  10. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX2.
  11. "Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides."
    Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T., Cullen P.J.
    Curr. Biol. 14:1791-1800(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214 AND 429-LYS--ARG-431.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins."
    Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T., Trejo J.
    Mol. Biol. Cell 17:1228-1238(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The retromer component sorting nexin-1 is required for efficient retrograde transport of Shiga toxin from early endosome to the trans Golgi network."
    Bujny M.V., Popoff V., Johannes L., Cullen P.J.
    J. Cell Sci. 120:2010-2021(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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: FUNCTION, SUBCELLULAR LOCATION.
  18. "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.
  19. "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: SUBUNIT, INTERACTION WITH SNX5; SNX6; VPS26A; VPS29; VPS35 AND DENND5A.
  20. "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: FUNCTION, DOMAIN.
  21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "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-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Analysis of articulation between clathrin and retromer in retrograde sorting on early endosomes."
    Popoff V., Mardones G.A., Bai S.K., Chambon V., Tenza D., Burgos P.V., Shi A., Benaroch P., Urbe S., Lamaze C., Grant B.D., Raposo G., Johannes L.
    Traffic 10:1868-1880(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJC13, SUBCELLULAR LOCATION.
  24. "Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking."
    Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R., Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.
    Biochem. Biophys. Res. Commun. 403:167-171(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  25. "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-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "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.
  27. "Regulation of P2Y1 receptor traffic by sorting Nexin 1 is retromer independent."
    Nisar S., Kelly E., Cullen P.J., Mundell S.J.
    Traffic 11:508-519(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Sorting nexin 1 loss results in D5 dopamine receptor dysfunction in human renal proximal tubule cells and hypertension in mice."
    Villar V.A., Jones J.E., Armando I., Asico L.D., Escano C.S. Jr., Lee H., Wang X., Yang Y., Pascua-Crusan A.M., Palmes-Saloma C.P., Felder R.A., Jose P.A.
    J. Biol. Chem. 288:152-163(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DRD5.
  30. "Determinants of the endosomal localization of sorting nexin 1."
    Zhong Q., Watson M.J., Lazar C.S., Hounslow A.M., Waltho J.P., Gill G.N.
    Mol. Biol. Cell 16:2049-2057(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 142-269, SUBCELLULAR LOCATION.
  31. "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: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 301-522, FUNCTION, INTERACTION WITH SNX5; SNX6 AND SNX32, SELF-ASSOCIATION, SUBUNIT, DOMAIN, MUTAGENESIS OF 287-MET-PHE-288; LYS-442 AND LYS-445.

Entry informationi

Entry nameiSNX1_HUMAN
AccessioniPrimary (citable) accession number: Q13596
Secondary accession number(s): A6NM19
, A8K6T7, H0Y2M5, O60750, O60751, Q6ZRJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 16, 2001
Last modified: January 7, 2015
This is version 138 of the entry and version 3 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

Miscellaneous

Binds phosphatidylinositol 3-phosphate (PtdIns-3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays, but not in liposome-based assays.

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.