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Q6PHU5

- SORT_MOUSE

UniProt

Q6PHU5 - SORT_MOUSE

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Protein
Sortilin
Gene
Sort1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi.7 Publications

GO - Molecular functioni

  1. nerve growth factor receptor activity Source: Ensembl
  2. neurotensin receptor activity, non-G-protein coupled Source: Ensembl
  3. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. Golgi to endosome transport Source: Ensembl
  2. endocytosis Source: UniProtKB-KW
  3. endosome to lysosome transport Source: Ensembl
  4. endosome transport via multivesicular body sorting pathway Source: Ensembl
  5. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  6. glucose import Source: BHF-UCL
  7. multicellular organismal development Source: UniProtKB-KW
  8. myotube differentiation Source: BHF-UCL
  9. negative regulation of lipoprotein lipase activity Source: Ensembl
  10. neuropeptide signaling pathway Source: Ensembl
  11. neurotrophin TRK receptor signaling pathway Source: Ensembl
  12. ossification Source: UniProtKB-KW
  13. plasma membrane to endosome transport Source: Ensembl
  14. regulation of gene expression Source: Ensembl
  15. response to insulin Source: BHF-UCL
  16. vesicle organization Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Endocytosis, Osteogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Sortilin
Alternative name(s):
Neurotensin receptor 3
Short name:
NTR3
Short name:
mNTR3
Gene namesi
Name:Sort1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1338015. Sort1.

Subcellular locationi

Membrane; Single-pass type I membrane protein Reviewed prediction. Endoplasmic reticulum membrane; Single-pass type I membrane protein Reviewed prediction. Endosome membrane; Single-pass type I membrane protein Reviewed prediction. Golgi apparatusGolgi stack membrane; Single-pass type I membrane protein Reviewed prediction. Nucleus membrane; Single-pass type I membrane protein Reviewed prediction. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane; Single-pass type I membrane protein Reviewed prediction
Note: Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. Interaction with NRADD promotes localization at the cell membrane in neurons; this promotes interaction with NGFR. Also found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes is enhanced by insulin.5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 754723Extracellular Reviewed prediction
Add
BLAST
Transmembranei755 – 77521Helical; Reviewed prediction
Add
BLAST
Topological domaini776 – 82550Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. cell surface Source: Ensembl
  3. coated pit Source: Ensembl
  4. early endosome Source: Ensembl
  5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  6. endosome membrane Source: UniProtKB-SubCell
  7. integral component of membrane Source: UniProtKB-KW
  8. lysosomal membrane Source: UniProtKB-SubCell
  9. nuclear membrane Source: UniProtKB-SubCell
  10. perinuclear region of cytoplasm Source: Ensembl
  11. plasma membrane Source: BHF-UCL
  12. trans-Golgi network transport vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Propeptidei32 – 7544Removed in mature form By similarity
PRO_0000045155Add
BLAST
Chaini76 – 825750Sortilin
PRO_0000045156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi84 ↔ 554 By similarity
Glycosylationi96 – 961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi160 – 1601N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi255 ↔ 275 By similarity
Glycosylationi272 – 2721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi404 – 4041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi446 ↔ 456 By similarity
Glycosylationi580 – 5801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi610 ↔ 649 By similarity
Disulfide bondi632 ↔ 664 By similarity
Disulfide bondi666 ↔ 721 By similarity
Disulfide bondi673 ↔ 686 By similarity
Glycosylationi682 – 6821N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi700 ↔ 738 By similarity
Modified residuei813 – 8131Phosphoserine By similarity
Modified residuei819 – 8191Phosphoserine1 Publication

Post-translational modificationi

The N-terminal propeptide is cleaved by furin and possibly other homologous proteases By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ6PHU5.
PaxDbiQ6PHU5.
PRIDEiQ6PHU5.

PTM databases

PhosphoSiteiQ6PHU5.

Expressioni

Tissue specificityi

Expressed in the brain, particularly the piriform cortex, the cerebral cortex and the hippocampus.1 Publication

Developmental stagei

Expressed in the ectoderm at E7.5 and within the germ cell layers at E8.5. Expressed within the neural epithelium and the neural tube at E9.5 and subsequently expressed in the nervous system throughout development. Expression in the proliferative zones of the central nervous system declines between E14.5 and E16.5, while expression remains high in the cerebral cortex and the neural retina. Expressed in the pituitary and the sensory epithelia throughout development.1 Publication

Inductioni

During adipocyte differentiation.2 Publications

Gene expression databases

ArrayExpressiQ6PHU5.
BgeeiQ6PHU5.
CleanExiMM_SORT1.
GenevestigatoriQ6PHU5.

Interactioni

Subunit structurei

Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, NTS and GM2A. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate their anterograde axonal transport and signaling By similarity. Interacts with LPL, PSAP and SLC2A4. Interacts with NRADD and NGFR. Interaction with NRADD protects against degradation in the lysosome.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NraddQ8CJ265EBI-6985663,EBI-6985725

Protein-protein interaction databases

BioGridi203393. 1 interaction.
DIPiDIP-46095N.
IntActiQ6PHU5. 4 interactions.
MINTiMINT-4130555.
STRINGi10090.ENSMUSP00000088052.

Structurei

3D structure databases

ProteinModelPortaliQ6PHU5.
SMRiQ6PHU5. Positions 86-747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati143 – 15412BNR 1
Add
BLAST
Repeati196 – 20712BNR 2
Add
BLAST
Repeati238 – 24912BNR 3
Add
BLAST
Repeati285 – 29612BNR 4
Add
BLAST
Repeati326 – 33712BNR 5
Add
BLAST
Repeati375 – 38612BNR 6
Add
BLAST
Repeati426 – 43712BNR 7
Add
BLAST
Repeati504 – 51512BNR 8
Add
BLAST
Repeati546 – 55712BNR 9
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 5912Intrachain binding of the propeptide and the extracellular domain By similarity
Add
BLAST
Regioni610 – 754145Interactions with LRPAP1 and NGFB By similarity
Add
BLAST
Regioni777 – 82549Golgi to endosome transport and interactions with GGA1 and GGA2 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi785 – 7906Endocytosis signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 447Poly-Pro

Domaini

The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding By similarity.
The extracellular domain may be shed following protease cleavage in some cell types By similarity.

Sequence similaritiesi

Contains 9 BNR repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG281049.
GeneTreeiENSGT00510000046443.
HOGENOMiHOG000231347.
HOVERGENiHBG080235.
KOiK12388.
OMAiLTQMMYS.
OrthoDBiEOG7RBZ7S.
PhylomeDBiQ6PHU5.
TreeFamiTF324918.

Family and domain databases

InterProiIPR006581. VPS10.
[Graphical view]
SMARTiSM00602. VPS10. 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: Q6PHU5-1) [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

MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG    50
PVGVSWGLRA AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ 100
HVFDDLSGSV SLSWVGDSTG VILVLTTFQV PLVIVSFGQS KLYRSEDYGK 150
NFKDITNLIN NTFIRTEFGM AIGPENSGKV ILTAEVSGGS RGGRVFRSSD 200
FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS KNFGEKWEEI 250
HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK 300
IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS 350
ILAANEDMVF MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET 400
DFTNVTSLRG VYITSTLSED NSIQSMITFD QGGRWEHLRK PENSKCDATA 450
KNKNECSLHI HASYSISQKL NVPMAPLSEP NAVGIVIAHG SVGDAISVMV 500
PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR PINVIKFSTD 550
EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV 600
DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ 650
NGRDYVVAKQ PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC 700
LYGKEEHLTT NGYRKIPGDK CQGGMNPARE VKDLKKKCTS NFLNPTKQNS 750
KSNSVPIILA IVGLMLVTVV AGVLIVKKYV CGGRFLVHRY SVLQQHAEAD 800
GVEALDSTSH AKSGYHDDSD EDLLE 825
Length:825
Mass (Da):91,200
Last modified:July 5, 2004 - v1
Checksum:i9A7A73C6FE1C8201
GO
Isoform 2 (identifier: Q6PHU5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     748-748: Q → QDSRPQGHSLSQNPAPPPLGYTENTHFLSPTQKQ

Note: No experimental confirmation available.

Show »
Length:858
Mass (Da):94,813
Checksum:iB4AC632F993E8E14
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei748 – 7481Q → QDSRPQGHSLSQNPAPPPLG YTENTHFLSPTQKQ in isoform 2.
VSP_016650

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti315 – 3151V → E in AAF22639. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF175279 mRNA. Translation: AAF22639.1.
AK147442 mRNA. Translation: BAE27915.1.
AL671899 Genomic DNA. Translation: CAM19473.1.
BC034129 mRNA. Translation: AAH34129.1.
BC056343 mRNA. Translation: AAH56343.1.
CCDSiCCDS17756.1. [Q6PHU5-1]
RefSeqiNP_001258528.1. NM_001271599.1. [Q6PHU5-2]
NP_064356.2. NM_019972.3. [Q6PHU5-1]
UniGeneiMm.157119.

Genome annotation databases

EnsembliENSMUST00000102632; ENSMUSP00000099692; ENSMUSG00000068747. [Q6PHU5-1]
GeneIDi20661.
KEGGimmu:20661.
UCSCiuc008qyr.1. mouse. [Q6PHU5-1]
uc008qys.1. mouse. [Q6PHU5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF175279 mRNA. Translation: AAF22639.1 .
AK147442 mRNA. Translation: BAE27915.1 .
AL671899 Genomic DNA. Translation: CAM19473.1 .
BC034129 mRNA. Translation: AAH34129.1 .
BC056343 mRNA. Translation: AAH56343.1 .
CCDSi CCDS17756.1. [Q6PHU5-1 ]
RefSeqi NP_001258528.1. NM_001271599.1. [Q6PHU5-2 ]
NP_064356.2. NM_019972.3. [Q6PHU5-1 ]
UniGenei Mm.157119.

3D structure databases

ProteinModelPortali Q6PHU5.
SMRi Q6PHU5. Positions 86-747.
ModBasei Search...

Protein-protein interaction databases

BioGridi 203393. 1 interaction.
DIPi DIP-46095N.
IntActi Q6PHU5. 4 interactions.
MINTi MINT-4130555.
STRINGi 10090.ENSMUSP00000088052.

PTM databases

PhosphoSitei Q6PHU5.

Proteomic databases

MaxQBi Q6PHU5.
PaxDbi Q6PHU5.
PRIDEi Q6PHU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102632 ; ENSMUSP00000099692 ; ENSMUSG00000068747 . [Q6PHU5-1 ]
GeneIDi 20661.
KEGGi mmu:20661.
UCSCi uc008qyr.1. mouse. [Q6PHU5-1 ]
uc008qys.1. mouse. [Q6PHU5-2 ]

Organism-specific databases

CTDi 6272.
MGIi MGI:1338015. Sort1.

Phylogenomic databases

eggNOGi NOG281049.
GeneTreei ENSGT00510000046443.
HOGENOMi HOG000231347.
HOVERGENi HBG080235.
KOi K12388.
OMAi LTQMMYS.
OrthoDBi EOG7RBZ7S.
PhylomeDBi Q6PHU5.
TreeFami TF324918.

Miscellaneous databases

ChiTaRSi SORT1. mouse.
NextBioi 299105.
PROi Q6PHU5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6PHU5.
Bgeei Q6PHU5.
CleanExi MM_SORT1.
Genevestigatori Q6PHU5.

Family and domain databases

InterProi IPR006581. VPS10.
[Graphical view ]
SMARTi SM00602. VPS10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Pharmacological properties of the mouse neurotensin receptor 3. Maintenance of cell surface receptor during internalization of neurotensin."
    Navarro V., Martin S., Sarret P., Nielsen M.S., Petersen C.M., Vincent J.-P., Mazella J.
    FEBS Lett. 495:100-105(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A NEUROTENSIN RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Strain: BALB/c.
    Tissue: Brain.
  2. "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] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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).
    Strain: C57BL/6.
    Tissue: Brain and Salivary gland.
  5. "Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes."
    Morris N.J., Ross S.A., Lane W.S., Moestrup S.K., Petersen C.M., Keller S.R., Lienhard G.E.
    J. Biol. Chem. 273:3582-3587(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  6. "Expression of the 100-kDa neurotensin receptor sortilin during mouse embryonal development."
    Hermans-Borgmeyer I., Hermey G., Nykjaer A., Schaller C.
    Brain Res. Mol. Brain Res. 65:216-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase."
    Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.
    J. Biol. Chem. 274:8832-8836(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPL.
  8. "Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes."
    Hashiramoto M., James D.E.
    Mol. Cell. Biol. 20:416-427(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Study of the mouse sortilin gene: effects of its transient silencing by RNA interference in TM4 Sertoli cells."
    Zeng J., Hassan A.J., Morales C.R.
    Mol. Reprod. Dev. 68:469-475(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSAP, SUBCELLULAR LOCATION.
  10. "The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins."
    Hassan A.J., Zeng J., Ni X., Morales C.R.
    Mol. Reprod. Dev. 68:476-483(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Neurotensin receptor-3/sortilin mediates neurotensin-induced cytokine/chemokine expression in a murine microglial cell line."
    Dicou E., Vincent J.-P., Mazella J.
    J. Neurosci. Res. 78:92-99(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes."
    Shi J., Kandror K.V.
    Dev. Cell 9:99-108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC2A4, SUBCELLULAR LOCATION, INDUCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death."
    Kim T., Hempstead B.L.
    EMBO J. 28:1612-1623(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NGFR AND NRADD.
  15. "Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling."
    Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S., Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L., Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A.
    Nat. Neurosci. 14:54-61(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NTRK1 SIGNALING.

Entry informationi

Entry nameiSORT_MOUSE
AccessioniPrimary (citable) accession number: Q6PHU5
Secondary accession number(s): A2AEE8
, Q3UHE2, Q8K043, Q9QXW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi