SubmitCancel

Skip Header

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

Q9D8U8

- SNX5_MOUSE

UniProt

Q9D8U8 - SNX5_MOUSE

(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
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation By similarity.1 Publication

GO - Molecular functioni

  1. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: RefGenome
  2. pinocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-5
Gene namesi
Name:Snx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1916428. Snx5.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 404403Sorting nexin-5PRO_0000213845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei275 – 2751N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D8U8.
PaxDbiQ9D8U8.
PRIDEiQ9D8U8.

PTM databases

PhosphoSiteiQ9D8U8.

Expressioni

Tissue specificityi

Detected in macrophages (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ9D8U8.
BgeeiQ9D8U8.
CleanExiMM_SNX5.
GenevestigatoriQ9D8U8.

Interactioni

Subunit structurei

Interacts with SNX1; this promotes location at the endosome membrane By similarity.

Protein-protein interaction databases

IntActiQ9D8U8. 1 interaction.
MINTiMINT-1751142.

Structurei

3D structure databases

ProteinModelPortaliQ9D8U8.
SMRiQ9D8U8. Positions 20-174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 172148PXAdd
BLAST
Domaini202 – 404203BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 467Phosphatidylinositol bisphosphate binding By similarity
Regioni99 – 1057Phosphatidylinositol bisphosphate binding By similarity
Regioni113 – 1164Phosphatidylinositol bisphosphate binding By similarity

Domaini

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate By similarity.

Sequence similaritiesi

Belongs to the sorting nexin family.
Contains 1 BAR domain.

Phylogenomic databases

eggNOGiNOG255198.
GeneTreeiENSGT00740000115413.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ9D8U8.
KOiK17920.
OMAiIKDSCAK.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9D8U8.
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]

Sequencei

Sequence statusi: Complete.

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

Q9D8U8-1 [UniParc]FASTAAdd to Basket

« Hide

MAAVPELLEQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH    50
TKTTLSTFQS PEFSVTRQHE DFVWLHDTLT ETTDYAGLII PPAPTKPDFD 100
GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV STHEVFLQRL 150
SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFS 200
GVKEVDDFFE QEKNFLINYY NRIKDSCAKA DKMTRSHKNV ADDYIHTAAC 250
LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML 300
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE THQQECCQKF 350
EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL 400
FKNN 404
Length:404
Mass (Da):46,797
Last modified:June 1, 2001 - v1
Checksum:iC24D8C78F753FAFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK007676 mRNA. Translation: BAB25180.1.
AK029463 mRNA. Translation: BAC26460.1.
AK031873 mRNA. Translation: BAC27587.1.
AK049129 mRNA. Translation: BAC33558.1.
AK159904 mRNA. Translation: BAE35468.1.
AK169786 mRNA. Translation: BAE41365.1.
BC002242 mRNA. Translation: AAH02242.1.
CCDSiCCDS16815.1.
RefSeqiNP_001186117.1. NM_001199188.1.
NP_077187.1. NM_024225.5.
UniGeneiMm.273379.

Genome annotation databases

EnsembliENSMUST00000028909; ENSMUSP00000028909; ENSMUSG00000027423.
ENSMUST00000110030; ENSMUSP00000105657; ENSMUSG00000027423.
GeneIDi69178.
KEGGimmu:69178.
UCSCiuc008mqq.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK007676 mRNA. Translation: BAB25180.1 .
AK029463 mRNA. Translation: BAC26460.1 .
AK031873 mRNA. Translation: BAC27587.1 .
AK049129 mRNA. Translation: BAC33558.1 .
AK159904 mRNA. Translation: BAE35468.1 .
AK169786 mRNA. Translation: BAE41365.1 .
BC002242 mRNA. Translation: AAH02242.1 .
CCDSi CCDS16815.1.
RefSeqi NP_001186117.1. NM_001199188.1.
NP_077187.1. NM_024225.5.
UniGenei Mm.273379.

3D structure databases

ProteinModelPortali Q9D8U8.
SMRi Q9D8U8. Positions 20-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D8U8. 1 interaction.
MINTi MINT-1751142.

PTM databases

PhosphoSitei Q9D8U8.

Proteomic databases

MaxQBi Q9D8U8.
PaxDbi Q9D8U8.
PRIDEi Q9D8U8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028909 ; ENSMUSP00000028909 ; ENSMUSG00000027423 .
ENSMUST00000110030 ; ENSMUSP00000105657 ; ENSMUSG00000027423 .
GeneIDi 69178.
KEGGi mmu:69178.
UCSCi uc008mqq.3. mouse.

Organism-specific databases

CTDi 27131.
MGIi MGI:1916428. Snx5.

Phylogenomic databases

eggNOGi NOG255198.
GeneTreei ENSGT00740000115413.
HOGENOMi HOG000231691.
HOVERGENi HBG000716.
InParanoidi Q9D8U8.
KOi K17920.
OMAi IKDSCAK.
OrthoDBi EOG7X0VH4.
PhylomeDBi Q9D8U8.
TreeFami TF313698.

Miscellaneous databases

ChiTaRSi SNX5. mouse.
NextBioi 328774.
PROi Q9D8U8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D8U8.
Bgeei Q9D8U8.
CleanExi MM_SNX5.
Genevestigatori Q9D8U8.

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. "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 and NOD.
    Tissue: Head, Medulla oblongata, Pancreas and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSNX5_MOUSE
AccessioniPrimary (citable) accession number: Q9D8U8
Secondary accession number(s): Q543N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.

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