Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y5X3

- SNX5_HUMAN

UniProt

Q9Y5X3 - SNX5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Sorting nexin-5

Gene

SNX5

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 3,4-bisphosphate (PtdIns(3,4)P2) (PubMed:15561769). 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). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde transport of lysosomal enzyme receptor IGF2R (PubMed:17148574, PubMed:18596235). May function as link between endosomal transport vesicles and dynactin (Probable). Plays a role in the internalization of EGFR after EGF stimulation (Probable). Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C isoform 3 and is retromer-independent (PubMed:23602387). Together with PIP5K1C isoform 3 facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation (Probable). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). Plays a role in macropinocytosis (PubMed:18854019, PubMed:21048941).3 Publications3 Publications

GO - Molecular functioni

  1. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: RefGenome
  2. pinocytosis Source: UniProtKB
  3. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, 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-5
Gene namesi
Name:SNX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:14969. SNX5.

Subcellular locationi

Endosome 1 Publication. Early endosome 2 Publications. Early endosome membrane 1 Publication; Peripheral membrane protein; Cytoplasmic side. Cell membrane 1 Publication; Peripheral membrane protein; Cytoplasmic side 1 Publication. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projectionphagocytic cup. Cell projectionruffle
Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (PubMed:15561769). Detected on macropinosomes (PubMed:16968745, PubMed:21048941). Targeted to membrane ruffles in response to EGFR stimulation.3 Publications

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. early endosome membrane Source: UniProtKB-SubCell
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. extrinsic component of endosome membrane Source: UniProtKB
  5. macropinocytic cup Source: UniProtKB
  6. phagocytic cup Source: UniProtKB-SubCell
  7. retromer complex Source: UniProtKB
  8. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1872FF → EE: No effect on dimerization. 1 Publication
Mutagenesisi224 – 2241K → E: Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-235, E-324, E-328 and E-330. 1 Publication
Mutagenesisi235 – 2351R → E: Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-324, E-328 and E-330. 1 Publication
Mutagenesisi280 – 2801E → A: Enables homodimerization; when associated with A-383. 1 Publication
Mutagenesisi324 – 3241K → E: Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-328 and E-330. 1 Publication
Mutagenesisi328 – 3281K → E: Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-324 and E-330. 1 Publication
Mutagenesisi330 – 3301R → E: Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-324 and E-328. 1 Publication
Mutagenesisi383 – 3831E → A: Enables homodimerization; when associated with A-280.

Organism-specific databases

PharmGKBiPA37945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 404403Sorting nexin-5PRO_0000213844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei275 – 2751N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y5X3.
PaxDbiQ9Y5X3.
PRIDEiQ9Y5X3.

PTM databases

PhosphoSiteiQ9Y5X3.

Expressioni

Gene expression databases

BgeeiQ9Y5X3.
CleanExiHS_SNX5.
ExpressionAtlasiQ9Y5X3. baseline and differential.
GenevestigatoriQ9Y5X3.

Organism-specific databases

HPAiCAB020679.

Interactioni

Subunit structurei

Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2; does not homodimerize (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 SNX1, SNX2, VPS26A, VPS29, VPS35, DCTN1, DOCK1, MIB1, PIP5K1C isoform 3. Interacts with HGS; increased by PIP5K1C isoform 3 kinase activity and by PtdIns(3P) and/or PtdIns(3,4)P2 (PubMed:16857196, PubMed:16968745, PubMed:19619496, PubMed:23085988, PubMed:18596235, PubMed:23602387, PubMed:24610942).7 Publications2 Publications

Protein-protein interaction databases

BioGridi118022. 32 interactions.
IntActiQ9Y5X3. 17 interactions.
MINTiMINT-2823978.
STRINGi9606.ENSP00000366988.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYSX-ray2.40C257-265[»]
ProteinModelPortaliQ9Y5X3.
SMRiQ9Y5X3. Positions 20-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5X3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 172148PXPROSITE-ProRule annotationAdd
BLAST
Domaini202 – 404203BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 467Phosphatidylinositol bisphosphate bindingBy similarity
Regioni99 – 1057Phosphatidylinositol bisphosphate bindingBy similarity
Regioni113 – 1164Phosphatidylinositol bisphosphate bindingBy similarity
Regioni169 – 26193Interaction with DOCK11 PublicationAdd
BLAST
Regioni183 – 20018Membrane-binding amphipathic helix1 PublicationAdd
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 (Probable).1 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

eggNOGiNOG255198.
GeneTreeiENSGT00760000119259.
HOVERGENiHBG000716.
InParanoidiQ9Y5X3.
KOiK17920.
OMAiIKDSCAK.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9Y5X3.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF6. PTHR10555:SF6. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5X3-1) [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
MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH
60 70 80 90 100
TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD
110 120 130 140 150
GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV SSHEVFLQRL
160 170 180 190 200
SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFT
210 220 230 240 250
GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV ADDYIHTAAC
260 270 280 290 300
LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML
310 320 330 340 350
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF
360 370 380 390 400
EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL

FKNN
Length:404
Mass (Da):46,816
Last modified:November 1, 1999 - v1
Checksum:i87A85620AF827EC6
GO
Isoform 2 (identifier: Q9Y5X3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-126: LRSVSVDLNV...TKEEFAKMKQ → VRSSQPQTPG...FFLKLSSASW
     127-404: Missing.

Show »
Length:126
Mass (Da):13,349
Checksum:iF04391B429CE2D7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791V → L(PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei18 – 126109LRSVS…AKMKQ → VRSSQPQTPGRAALRAPGSL HSFPCASIGRGCSPPSPARE APVRPGRPLSLVFTEGCPGE SLWMSRILLGQNQRRGTLAP AQAPVPSGLGEMISGDPGMF FLKLSSASW in isoform 2. 2 PublicationsVSP_056386Add
BLAST
Alternative sequencei127 – 404278Missing in isoform 2. 2 PublicationsVSP_056387Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121855 mRNA. Translation: AAD27828.1.
BT007191 mRNA. Translation: AAP35855.1.
AK001793 mRNA. Translation: BAA91914.1.
AK123903 mRNA. Translation: BAG53980.1.
AL121585 Genomic DNA. Translation: CAC00471.1.
BC000100 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10264.1.
CH471133 Genomic DNA. Translation: EAX10265.1.
CH471133 Genomic DNA. Translation: EAX10266.1.
CH471133 Genomic DNA. Translation: EAX10268.1.
BC093623 mRNA. Translation: AAH93623.1.
BC093980 mRNA. Translation: AAH93980.1.
BC143274 mRNA. Translation: AAI43275.1.
CCDSiCCDS13130.1. [Q9Y5X3-1]
RefSeqiNP_055241.1. NM_014426.3. [Q9Y5X3-1]
NP_689413.1. NM_152227.2. [Q9Y5X3-1]
UniGeneiHs.316890.

Genome annotation databases

EnsembliENST00000377759; ENSP00000366988; ENSG00000089006. [Q9Y5X3-1]
ENST00000377768; ENSP00000366998; ENSG00000089006. [Q9Y5X3-1]
ENST00000606557; ENSP00000475510; ENSG00000089006. [Q9Y5X3-2]
GeneIDi27131.
KEGGihsa:27131.
UCSCiuc002wqc.3. human. [Q9Y5X3-1]

Polymorphism databases

DMDMi10720289.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121855 mRNA. Translation: AAD27828.1 .
BT007191 mRNA. Translation: AAP35855.1 .
AK001793 mRNA. Translation: BAA91914.1 .
AK123903 mRNA. Translation: BAG53980.1 .
AL121585 Genomic DNA. Translation: CAC00471.1 .
BC000100 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10264.1 .
CH471133 Genomic DNA. Translation: EAX10265.1 .
CH471133 Genomic DNA. Translation: EAX10266.1 .
CH471133 Genomic DNA. Translation: EAX10268.1 .
BC093623 mRNA. Translation: AAH93623.1 .
BC093980 mRNA. Translation: AAH93980.1 .
BC143274 mRNA. Translation: AAI43275.1 .
CCDSi CCDS13130.1. [Q9Y5X3-1 ]
RefSeqi NP_055241.1. NM_014426.3. [Q9Y5X3-1 ]
NP_689413.1. NM_152227.2. [Q9Y5X3-1 ]
UniGenei Hs.316890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SYS X-ray 2.40 C 257-265 [» ]
ProteinModelPortali Q9Y5X3.
SMRi Q9Y5X3. Positions 20-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118022. 32 interactions.
IntActi Q9Y5X3. 17 interactions.
MINTi MINT-2823978.
STRINGi 9606.ENSP00000366988.

PTM databases

PhosphoSitei Q9Y5X3.

Polymorphism databases

DMDMi 10720289.

Proteomic databases

MaxQBi Q9Y5X3.
PaxDbi Q9Y5X3.
PRIDEi Q9Y5X3.

Protocols and materials databases

DNASUi 27131.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377759 ; ENSP00000366988 ; ENSG00000089006 . [Q9Y5X3-1 ]
ENST00000377768 ; ENSP00000366998 ; ENSG00000089006 . [Q9Y5X3-1 ]
ENST00000606557 ; ENSP00000475510 ; ENSG00000089006 . [Q9Y5X3-2 ]
GeneIDi 27131.
KEGGi hsa:27131.
UCSCi uc002wqc.3. human. [Q9Y5X3-1 ]

Organism-specific databases

CTDi 27131.
GeneCardsi GC20M017870.
HGNCi HGNC:14969. SNX5.
HPAi CAB020679.
MIMi 605937. gene.
neXtProti NX_Q9Y5X3.
PharmGKBi PA37945.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255198.
GeneTreei ENSGT00760000119259.
HOVERGENi HBG000716.
InParanoidi Q9Y5X3.
KOi K17920.
OMAi IKDSCAK.
OrthoDBi EOG7X0VH4.
PhylomeDBi Q9Y5X3.
TreeFami TF313698.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSi SNX5. human.
EvolutionaryTracei Q9Y5X3.
GeneWikii SNX5.
GenomeRNAii 27131.
NextBioi 35540772.
PROi Q9Y5X3.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5X3.
CleanExi HS_SNX5.
ExpressionAtlasi Q9Y5X3. baseline and differential.
Genevestigatori Q9Y5X3.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view ]
PANTHERi PTHR10555:SF6. PTHR10555:SF6. 1 hit.
Pfami PF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view ]
PIRSFi PIRSF036924. Snx5_Snx6. 1 hit.
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. "A large family of endosome-localized proteins related to sorting nexin 1."
    Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.
    Biochem. J. 358:7-16(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "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] (ISOFORM 2).
  3. "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: Ovarian carcinoma.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain and Placenta.
  7. "Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation."
    Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C., Teasdale R.D., Gleeson P.A.
    J. Cell Sci. 117:6413-6424(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE BINDING.
  8. "Snx5, as a Mind bomb-binding protein, is expressed in hematopoietic and endothelial precursor cells in zebrafish."
    Yoo K.W., Kim E.H., Jung S.H., Rhee M., Koo B.K., Yoon K.J., Kong Y.Y., Kim C.H.
    FEBS Lett. 580:4409-4416(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIB1.
  9. "Visualisation of macropinosome maturation by the recruitment of sorting nexins."
    Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F., Parton R.G., Gleeson P.A., Teasdale R.D.
    J. Cell Sci. 119:3967-3980(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX1, SUBCELLULAR LOCATION.
  10. "A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer."
    Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J., Cullen P.J.
    J. Cell Sci. 120:45-54(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "A role for SNX5 in the regulation of macropinocytosis."
    Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.
    BMC Cell Biol. 9:58-58(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "The DHR1 domain of DOCK180 binds to SNX5 and regulates cation-independent mannose 6-phosphate receptor transport."
    Hara S., Kiyokawa E., Iemura S., Natsume T., Wassmer T., Cullen P.J., Hiai H., Matsuda M.
    Mol. Biol. Cell 19:3823-3835(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DOCK1.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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 SNX1; SNX2; VPS26A; VPS29; VPS35 AND DCTN1.
  15. "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.
  16. "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-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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 SNX1 AND SNX2, DOMAIN, MUTAGENESIS OF 186-PHE-PHE-187; GLU-280 AND GLU-383.
  20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Endosomal type Igamma PIP 5-kinase controls EGF receptor lysosomal sorting."
    Sun Y., Hedman A.C., Tan X., Schill N.J., Anderson R.A.
    Dev. Cell 25:144-155(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIP5K1C.
  23. "Isoform 5 of PIPKIgamma regulates the endosomal trafficking and degradation of E-cadherin."
    Schill N.J., Hedman A.C., Choi S., Anderson R.A.
    J. Cell Sci. 127:2189-2203(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHOINOSITIDE BINDING, INTERACTION WITH PIP5K1C AND HGS, MUTAGENESIS OF LYS-224; ARG-235; LYS-324; LYS-328 AND ARG-330.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA CLASS I HISTOCOMPATIBILITY COMPLEX.

Entry informationi

Entry nameiSNX5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X3
Secondary accession number(s): B7ZKN3
, D3DW26, Q52LC4, Q7KZN0, Q9BWP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 127 of the entry and version 1 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

Caution

The selectivity for particular phosphatidylinositol lipids is under debate. According to one report (PubMed:19553671), the rat protein binds exclusively to phosphatidylinositol 4,5-bisphosphate, while the human protein has been reported (PubMed:15561769) to bind to phosphatidylinositol 3,4-bisphosphate and also to phosphatidylinositol 3-phosphate.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.