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Q99523

- SORT_HUMAN

UniProt

Q99523 - SORT_HUMAN

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Protein

Sortilin

Gene

SORT1

Organism
Homo sapiens (Human)
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.10 Publications

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. nerve growth factor binding Source: BHF-UCL
  3. nerve growth factor receptor activity Source: BHF-UCL
  4. neurotensin receptor activity, non-G-protein coupled Source: BHF-UCL

GO - Biological processi

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

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Endocytosis, Osteogenesis, Transport

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sortilin
Alternative name(s):
100 kDa NT receptor
Glycoprotein 95
Short name:
Gp95
Neurotensin receptor 3
Short name:
NT3
Short name:
NTR3
Gene namesi
Name:SORT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:11186. SORT1.

Subcellular locationi

Membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated. Endosome membrane Curated; Single-pass type I membrane protein Curated. Golgi apparatusGolgi stack membrane Curated; Single-pass type I membrane protein Curated. Nucleus membrane Curated; Single-pass type I membrane protein Curated. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane Curated; Single-pass type I membrane protein Curated
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. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini78 – 755678ExtracellularSequence AnalysisAdd
BLAST
Transmembranei756 – 77823HelicalSequence AnalysisAdd
BLAST
Topological domaini779 – 83153CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. clathrin-coated vesicle Source: BHF-UCL
  3. coated pit Source: BHF-UCL
  4. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
  5. early endosome Source: BHF-UCL
  6. endoplasmic reticulum Source: UniProtKB-KW
  7. Golgi apparatus Source: BHF-UCL
  8. integral component of membrane Source: BHF-UCL
  9. lysosome Source: UniProtKB-KW
  10. nucleus Source: UniProtKB-KW
  11. perinuclear region of cytoplasm Source: BHF-UCL
  12. plasma membrane Source: BHF-UCL
  13. trans-Golgi network transport vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

A common polymorphism located in a non-coding region between CELSR2 and PSRC1 alters a CEBP transcription factor binding site and is responsible for changes in hepatic expression of SORT1. Altered SORT1 expression in liver affects low density lipoprotein cholesterol levels in plasma and is associated with susceptibility to myocardial infarction.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 774RWRR → GWRA: Abrogates propeptide cleavage. 1 Publication
Mutagenesisi76 – 772RR → GG: Abrogates propeptide cleavage. 1 Publication
Mutagenesisi792 – 7921Y → A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-795. 1 Publication
Mutagenesisi795 – 7951L → A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-792. 1 Publication
Mutagenesisi823 – 8242DD → NN: Reduces interaction with GGA1. 1 Publication
Mutagenesisi825 – 8251S → A: Reduces interaction with GGA1. 1 Publication
Mutagenesisi826 – 8283DED → NQN: Abrogates interaction with GGA1 and impairs localization to the Golgi. 1 Publication
Mutagenesisi829 – 8302LL → AA: Abrogates interaction with GGA1 and impairs localization to the Golgi. 2 Publications
Mutagenesisi829 – 8302Missing: Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795. 2 Publications

Organism-specific databases

MIMi613589. phenotype.
PharmGKBiPA36023.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Propeptidei34 – 7744Removed in mature form1 PublicationPRO_0000033162Add
BLAST
Chaini78 – 831754SortilinPRO_0000033163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 ↔ 556
Glycosylationi98 – 981N-linked (GlcNAc...)Curated
Glycosylationi162 – 1621N-linked (GlcNAc...)2 Publications
Glycosylationi163 – 1631N-linked (GlcNAc...); atypical1 Publication
Disulfide bondi257 ↔ 277
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)1 Publication
Disulfide bondi448 ↔ 458
Glycosylationi582 – 5821N-linked (GlcNAc...)1 Publication
Disulfide bondi612 ↔ 651
Disulfide bondi634 ↔ 666
Disulfide bondi668 ↔ 723
Disulfide bondi675 ↔ 688
Glycosylationi684 – 6841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi702 ↔ 740
Modified residuei819 – 8191Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine2 Publications

Post-translational modificationi

The N-terminal propeptide is cleaved by furin and possibly other homologous proteases.2 Publications

Keywords - PTMi

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

Proteomic databases

MaxQBiQ99523.
PaxDbiQ99523.
PRIDEiQ99523.

PTM databases

PhosphoSiteiQ99523.

Expressioni

Tissue specificityi

Expressed in brain and prostate (at protein level). Expressed at high levels in brain, spinal cord, heart, skeletal muscle, thyroid, placenta and testis. Expressed at lower levels in lymphoid organs, kidney, colon and liver.2 Publications

Inductioni

During osteoblast differentiation.1 Publication

Gene expression databases

BgeeiQ99523.
CleanExiHS_SORT1.
GenevestigatoriQ99523.

Organism-specific databases

HPAiCAB011498.
HPA006889.

Interactioni

Subunit structurei

Interacts with LPL and SLC2A4 (By similarity). Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, GM2A, NTS and PSAP. 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 similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GGA1Q9UJY52EBI-1057058,EBI-447141
LPLP111516EBI-1057058,EBI-8794090From a different organism.
NGFP011384EBI-1057058,EBI-1028250

Protein-protein interaction databases

BioGridi112180. 11 interactions.
DIPiDIP-41798N.
IntActiQ99523. 10 interactions.
MINTiMINT-197682.
STRINGi9606.ENSP00000256637.

Structurei

Secondary structure

1
831
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi92 – 976Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi141 – 1499Combined sources
Helixi158 – 1614Combined sources
Helixi168 – 1703Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi226 – 2349Combined sources
Beta strandi239 – 2446Combined sources
Beta strandi247 – 26115Combined sources
Helixi263 – 2653Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi273 – 2753Combined sources
Turni277 – 2826Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi297 – 30913Combined sources
Beta strandi312 – 3187Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi325 – 3328Combined sources
Beta strandi351 – 3566Combined sources
Beta strandi361 – 3666Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi372 – 3798Combined sources
Beta strandi385 – 39511Combined sources
Turni397 – 3993Combined sources
Beta strandi414 – 4196Combined sources
Beta strandi421 – 4233Combined sources
Beta strandi425 – 4328Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi453 – 4564Combined sources
Beta strandi459 – 4624Combined sources
Helixi465 – 4695Combined sources
Beta strandi488 – 49710Combined sources
Beta strandi504 – 5107Combined sources
Beta strandi516 – 5216Combined sources
Beta strandi523 – 5286Combined sources
Helixi529 – 5313Combined sources
Beta strandi533 – 5386Combined sources
Beta strandi546 – 5527Combined sources
Beta strandi558 – 5614Combined sources
Beta strandi567 – 5737Combined sources
Beta strandi581 – 59010Combined sources
Beta strandi595 – 6039Combined sources
Helixi604 – 6063Combined sources
Helixi614 – 6163Combined sources
Beta strandi617 – 6215Combined sources
Turni630 – 6334Combined sources
Beta strandi638 – 6458Combined sources
Beta strandi661 – 6655Combined sources
Helixi670 – 6723Combined sources
Beta strandi673 – 6753Combined sources
Beta strandi683 – 6853Combined sources
Helixi696 – 7049Combined sources
Helixi707 – 7104Combined sources
Beta strandi714 – 7174Combined sources
Beta strandi724 – 7263Combined sources
Beta strandi734 – 7363Combined sources
Helixi737 – 7404Combined sources
Helixi741 – 7433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F6KX-ray2.00A78-756[»]
3G2UX-ray2.30C/D819-831[»]
3G2VX-ray2.10C/D819-831[»]
4MSLX-ray2.70A78-756[»]
4N7EX-ray2.70A78-756[»]
4PO7X-ray2.66A78-756[»]
ProteinModelPortaliQ99523.
SMRiQ99523. Positions 88-749.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati145 – 15612BNR 1Add
BLAST
Repeati198 – 20912BNR 2Add
BLAST
Repeati240 – 25112BNR 3Add
BLAST
Repeati287 – 29812BNR 4Add
BLAST
Repeati328 – 33912BNR 5Add
BLAST
Repeati377 – 38812BNR 6Add
BLAST
Repeati428 – 43912BNR 7Add
BLAST
Repeati506 – 51712BNR 8Add
BLAST
Repeati548 – 55912BNR 9Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 6112Intrachain binding of the propeptide and the extracellular domainAdd
BLAST
Regioni612 – 756145Interactions with LRPAP1 and NGFBAdd
BLAST
Regioni779 – 83153Golgi to endosome transport and interactions with GGA1 and GGA2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi787 – 7926Endocytosis signalCurated

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.
The extracellular domain may be shed following protease cleavage in some cell types.

Sequence similaritiesi

Contains 9 BNR repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG281049.
GeneTreeiENSGT00510000046443.
HOGENOMiHOG000231347.
HOVERGENiHBG080235.
InParanoidiQ99523.
KOiK12388.
OMAiLTQMMYS.
OrthoDBiEOG7RBZ7S.
PhylomeDBiQ99523.
TreeFamiTF324918.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR006581. VPS10.
IPR015943. WD40/YVTN_repeat-like_dom.
[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: Q99523-1) [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
MERPWGAADG LSRWPHGLGL LLLLQLLPPS TLSQDRLDAP PPPAAPLPRW
60 70 80 90 100
SGPIGVSWGL RAAAAGGAFP RGGRWRRSAP GEDEECGRVR DFVAKLANNT
110 120 130 140 150
HQHVFDDLRG SVSLSWVGDS TGVILVLTTF HVPLVIMTFG QSKLYRSEDY
160 170 180 190 200
GKNFKDITDL INNTFIRTEF GMAIGPENSG KVVLTAEVSG GSRGGRIFRS
210 220 230 240 250
SDFAKNFVQT DLPFHPLTQM MYSPQNSDYL LALSTENGLW VSKNFGGKWE
260 270 280 290 300
EIHKAVCLAK WGSDNTIFFT TYANGSCKAD LGALELWRTS DLGKSFKTIG
310 320 330 340 350
VKIYSFGLGG RFLFASVMAD KDTTRRIHVS TDQGDTWSMA QLPSVGQEQF
360 370 380 390 400
YSILAANDDM VFMHVDEPGD TGFGTIFTSD DRGIVYSKSL DRHLYTTTGG
410 420 430 440 450
ETDFTNVTSL RGVYITSVLS EDNSIQTMIT FDQGGRWTHL RKPENSECDA
460 470 480 490 500
TAKNKNECSL HIHASYSISQ KLNVPMAPLS EPNAVGIVIA HGSVGDAISV
510 520 530 540 550
MVPDVYISDD GGYSWTKMLE GPHYYTILDS GGIIVAIEHS SRPINVIKFS
560 570 580 590 600
TDEGQCWQTY TFTRDPIYFT GLASEPGARS MNISIWGFTE SFLTSQWVSY
610 620 630 640 650
TIDFKDILER NCEEKDYTIW LAHSTDPEDY EDGCILGYKE QFLRLRKSSV
660 670 680 690 700
CQNGRDYVVT KQPSICLCSL EDFLCDFGYY RPENDSKCVE QPELKGHDLE
710 720 730 740 750
FCLYGREEHL TTNGYRKIPG DKCQGGVNPV REVKDLKKKC TSNFLSPEKQ
760 770 780 790 800
NSKSNSVPII LAIVGLMLVT VVAGVLIVKK YVCGGRFLVH RYSVLQQHAE
810 820 830
ANGVDGVDAL DTASHTNKSG YHDDSDEDLL E
Length:831
Mass (Da):92,068
Last modified:December 20, 2005 - v3
Checksum:i91F96A3035A4B43A
GO
Isoform 2 (identifier: Q99523-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.
     278-279: KA → T

Note: No experimental confirmation available.

Show »
Length:694
Mass (Da):77,375
Checksum:i4F80EC724C360750
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti650 – 6501V → M in CAA66904. (PubMed:9013611)Curated

Polymorphismi

Genetic variations in SORT1 influence low density lipoprotein cholesterol (LDL-C) variability and contribute to the low density lipoprotein cholesterol level quantitative trait locus 6 (LDLCQ6) [MIMi:613589].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581D → Y.
Corresponds to variant rs2228605 [ dbSNP | Ensembl ].
VAR_053681

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_046239Add
BLAST
Alternative sequencei278 – 2792KA → T in isoform 2. 1 PublicationVSP_046240

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98248 mRNA. Translation: CAA66904.2.
FJ525881 Genomic DNA. Translation: ACN81319.1.
AK301548 mRNA. Translation: BAG63045.1.
AL390252 Genomic DNA. Translation: CAI13180.1.
BC023542 mRNA. Translation: AAH23542.1.
CCDSiCCDS55618.1. [Q99523-2]
CCDS798.1. [Q99523-1]
RefSeqiNP_001192157.1. NM_001205228.1. [Q99523-2]
NP_002950.3. NM_002959.5. [Q99523-1]
UniGeneiHs.485195.
Hs.703487.

Genome annotation databases

EnsembliENST00000256637; ENSP00000256637; ENSG00000134243. [Q99523-1]
ENST00000538502; ENSP00000438597; ENSG00000134243. [Q99523-2]
GeneIDi6272.
KEGGihsa:6272.
UCSCiuc001dxm.2. human. [Q99523-1]
uc010ovi.2. human.

Polymorphism databases

DMDMi84028263.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98248 mRNA. Translation: CAA66904.2 .
FJ525881 Genomic DNA. Translation: ACN81319.1 .
AK301548 mRNA. Translation: BAG63045.1 .
AL390252 Genomic DNA. Translation: CAI13180.1 .
BC023542 mRNA. Translation: AAH23542.1 .
CCDSi CCDS55618.1. [Q99523-2 ]
CCDS798.1. [Q99523-1 ]
RefSeqi NP_001192157.1. NM_001205228.1. [Q99523-2 ]
NP_002950.3. NM_002959.5. [Q99523-1 ]
UniGenei Hs.485195.
Hs.703487.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3F6K X-ray 2.00 A 78-756 [» ]
3G2U X-ray 2.30 C/D 819-831 [» ]
3G2V X-ray 2.10 C/D 819-831 [» ]
4MSL X-ray 2.70 A 78-756 [» ]
4N7E X-ray 2.70 A 78-756 [» ]
4PO7 X-ray 2.66 A 78-756 [» ]
ProteinModelPortali Q99523.
SMRi Q99523. Positions 88-749.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112180. 11 interactions.
DIPi DIP-41798N.
IntActi Q99523. 10 interactions.
MINTi MINT-197682.
STRINGi 9606.ENSP00000256637.

Chemistry

BindingDBi Q99523.
ChEMBLi CHEMBL3091.

PTM databases

PhosphoSitei Q99523.

Polymorphism databases

DMDMi 84028263.

Proteomic databases

MaxQBi Q99523.
PaxDbi Q99523.
PRIDEi Q99523.

Protocols and materials databases

DNASUi 6272.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256637 ; ENSP00000256637 ; ENSG00000134243 . [Q99523-1 ]
ENST00000538502 ; ENSP00000438597 ; ENSG00000134243 . [Q99523-2 ]
GeneIDi 6272.
KEGGi hsa:6272.
UCSCi uc001dxm.2. human. [Q99523-1 ]
uc010ovi.2. human.

Organism-specific databases

CTDi 6272.
GeneCardsi GC01M109852.
HGNCi HGNC:11186. SORT1.
HPAi CAB011498.
HPA006889.
MIMi 602458. gene.
613589. phenotype.
neXtProti NX_Q99523.
PharmGKBi PA36023.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281049.
GeneTreei ENSGT00510000046443.
HOGENOMi HOG000231347.
HOVERGENi HBG080235.
InParanoidi Q99523.
KOi K12388.
OMAi LTQMMYS.
OrthoDBi EOG7RBZ7S.
PhylomeDBi Q99523.
TreeFami TF324918.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSi SORT1. human.
EvolutionaryTracei Q99523.
GeneWikii Sortilin_1.
GenomeRNAii 6272.
NextBioi 24343.
PROi Q99523.
SOURCEi Search...

Gene expression databases

Bgeei Q99523.
CleanExi HS_SORT1.
Genevestigatori Q99523.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR006581. VPS10.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
SMARTi SM00602. VPS10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography."
    Petersen C.M., Nielsen M.S., Nykjaer A., Jacobsen L., Tommerup N., Rasmussen H.H., Roeigaard H., Gliemann J., Madsen P., Moestrup S.K.
    J. Biol. Chem. 272:3599-3605(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: T-cell.
  2. Madsen P.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Mammary gland.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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: Muscle.
  7. "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor."
    Mazella J., Zsurger N., Navarro V., Chabry J., Kaghad M., Caput D., Ferrara P., Vita M., Gully D., Maffrand J.-P., Vincent J.-P.
    J. Biol. Chem. 273:26273-26276(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 78-100, IDENTIFICATION AS A NEUROTENSIN RECEPTOR.
    Tissue: Brain.
  8. "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding."
    Petersen C.M., Nielsen M.S., Jacobsen C., Tauris J., Jacobsen L., Gliemann J., Moestrup S.K., Madsen P.
    EMBO J. 18:595-604(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, MUTAGENESIS OF 74-ARG--ARG-77 AND 76-ARG-ARG-77, CLEAVAGE BY FURIN, GLYCOSYLATION.
  9. "The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin."
    Tauris J., Ellgaard L., Jacobsen C., Nielsen M.S., Madsen P., Thoegersen H.C., Gliemann J., Petersen C.M., Moestrup S.K.
    FEBS Lett. 429:27-30(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRPAP1.
  10. "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: FUNCTION.
  11. "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein."
    Nielsen M.S., Madsen P., Christensen E.I., Nykjaer A., Gliemann J., Kasper D., Pohlmann R., Petersen C.M.
    EMBO J. 20:2180-2190(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GGA2, MUTAGENESIS OF TYR-792; LEU-795 AND 829-LEU-LEU-830.
  12. "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains."
    Takatsu H., Katoh Y., Shiba Y., Nakayama K.
    J. Biol. Chem. 276:28541-28545(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GGA1 AND GGA2, MUTAGENESIS OF 823-ASP-ASP-824; SER-825; 826-ASP--ASP-828 AND 829-LEU-LEU-830.
  13. "Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line."
    Navarro V., Vincent J.-P., Mazella J.
    Biochem. Biophys. Res. Commun. 298:760-764(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF THE EXTRACELLULAR DOMAIN.
  14. "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization."
    Maeda S., Nobukuni T., Shimo-Onoda K., Hayashi K., Yone K., Komiya S., Inoue I.
    J. Cell. Physiol. 193:73-79(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  15. "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1."
    Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N., Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.
    Nature 415:937-941(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GGA1.
  16. "The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin."
    Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.
    EMBO J. 22:6430-6437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GM2A AND PSAP, SUBCELLULAR LOCATION.
  17. Erratum
    Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.
    EMBO J. 23:1680-1680(2004)
  18. "Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia."
    Martin S., Vincent J.-P., Mazella J.
    J. Neurosci. 23:1198-1205(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. "Internalization and trafficking of neurotensin via NTS3 receptors in HT29 cells."
    Morinville A., Martin S., Lavallee M., Vincent J.-P., Beaudet A., Mazella J.
    Int. J. Biochem. Cell Biol. 36:2153-2168(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. Cited for: INTERACTION WITH LRPAP1 AND NGFB, SUBCELLULAR LOCATION, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
  21. Cited for: FUNCTION, INTERACTION WITH NGFB AND NGFR.
  22. "ProBDNF induces neuronal apoptosis via activation of a receptor complex of p75NTR and sortilin."
    Teng H.K., Teng K.K., Lee R., Wright S., Tevar S., Almeida R.D., Kermani P., Torkin R., Chen Z.-Y., Lee F.S., Kraemer R.T., Nykjaer A., Hempstead B.L.
    J. Neurosci. 25:5455-5463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway."
    Chen Z.-Y., Ieraci A., Teng H., Dall H., Meng C.-X., Herrera D.G., Nykjaer A., Hempstead B.L., Lee F.S.
    J. Neurosci. 25:6156-6166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BDNF.
  24. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162.
    Tissue: Platelet.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-163.
    Tissue: Leukemic T-cell.
  28. "Altered expression of neurotensin receptors is associated with the differentiation state of prostate cancer."
    Swift S.L., Burns J.E., Maitland N.J.
    Cancer Res. 70:347-356(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  29. "Biological, clinical and population relevance of 95 loci for blood lipids."
    Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S.
    , Thorleifsson G., Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M., Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D., Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A., Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D., Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C., Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M., Kathiresan S.
    Nature 466:707-713(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LDLCQ6.
  30. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MYOCARDIAL INFARCTION.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "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: INTERACTION WITH NTRK1.
  33. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain."
    Quistgaard E.M., Madsen P., Groftehauge M.K., Nissen P., Petersen C.M., Thirup S.S.
    Nat. Struct. Mol. Biol. 16:96-98(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-756 IN COMPLEX WITH NTS, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-406 AND ASN-582.

Entry informationi

Entry nameiSORT_HUMAN
AccessioniPrimary (citable) accession number: Q99523
Secondary accession number(s): B4DWI3, C0JYZ0, Q8IZ49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 20, 2005
Last modified: November 26, 2014
This is version 145 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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