Reviewed, UniProtKB/Swiss-Prot Q99523 (SORT_HUMAN)

Names and origin

Protein names

Recommended name:
    Sortilin
Alternative name(s):
    Neurotensin receptor 3
      Short name=NTR3
      Short name=NT3
    Glycoprotein 95
      Short name=Gp95
    100 kDa NT receptor

Gene names

Name:

SORT1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21
Subunit structure	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 and PSAP. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF).
Subcellular location	Membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Endosome membrane; Single-pass type I membrane protein Potential. Golgi apparatus › Golgi stack membrane; Single-pass type I membrane protein Potential. Lysosome membrane; Single-pass type I membrane protein Potential. Nucleus membrane; Single-pass type I membrane protein Potential. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane; Single-pass type I membrane protein Potential. 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.
Tissue specificity	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. Ref.1
Induction	During osteoblast differentiation. Ref.12
Domain	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. Ref.11 The extracellular domain may be shed following protease cleavage in some cell types. Ref.11
Post-translational modification	The N-terminal propeptide is cleaved by furin and possibly other homologous proteases. Ref.11 Ref.6 Contains 8 intrachain disulfide bonds. N-glycosylated. Ref.1 Ref.6 Ref.22
Sequence similarities	Contains 9 BNR repeats.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Osteogenesis Transport
Cellular component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane
Molecular function	Developmental protein Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	Golgi to endosome transport Ref.9 Inferred from direct assay. Source: UniProtKB endocytosis Ref.9 Inferred from direct assay. Source: UniProtKB endosome to lysosome transport Ref.9 Inferred from direct assay. Source: UniProtKB endosome transport via multivesicular body sorting pathway Ref.9 Inferred from direct assay. Source: UniProtKB glucose import Inferred from mutant phenotype. Source: UniProtKB induction of apoptosis by extracellular signals Ref.19 Inferred from mutant phenotype. Source: UniProtKB myotube differentiation Inferred from mutant phenotype. Source: UniProtKB negative regulation of apoptosis Ref.19 Inferred from direct assay. Source: UniProtKB negative regulation of lipoprotein lipase activity Ref.8 Inferred from direct assay. Source: UniProtKB nerve growth factor receptor signaling pathway Ref.19 Inferred from mutant phenotype. Source: UniProtKB neuropeptide signaling pathway Ref.5 Inferred from direct assay. Source: UniProtKB ossification Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane to endosome transport Ref.9 Inferred from direct assay. Source: UniProtKB regulation of gene expression Inferred from mutant phenotype. Source: UniProtKB response to insulin stimulus Inferred from mutant phenotype. Source: UniProtKB vesicle organization Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Ref.8 Inferred from direct assay. Source: UniProtKB clathrin-coated vesicle Ref.9 Inferred from direct assay. Source: UniProtKB coated pit Ref.9 Inferred from direct assay. Source: UniProtKB early endosome Ref.9 Inferred from direct assay. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from direct assay. Source: UniProtKB lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: UniProtKB nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Ref.9 Inferred from direct assay. Source: UniProtKB
Molecular function	enzyme binding Ref.8 Inferred from physical interaction. Source: UniProtKB nerve growth factor binding Ref.19 Inferred from physical interaction. Source: UniProtKB nerve growth factor receptor activity Ref.19 Inferred from direct assay. Source: UniProtKB neurotensin receptor activity, non-G-protein coupled Ref.5 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK2	P24941	1	EBI-1057058,EBI-375096

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 33	33	Potential
	Propeptide	34 – 77	44	Removed in mature form Ref.5		PRO_0000033162
	Chain	78 – 831	754	Sortilin		PRO_0000033163
Regions
	Topological domain	78 – 755	678	Extracellular Potential
	Transmembrane	756 – 778	23	Potential
	Topological domain	779 – 831	53	Cytoplasmic Potential
	Repeat	145 – 156	12	BNR 1
	Repeat	198 – 209	12	BNR 2
	Repeat	240 – 251	12	BNR 3
	Repeat	287 – 298	12	BNR 4
	Repeat	328 – 339	12	BNR 5
	Repeat	377 – 388	12	BNR 6
	Repeat	428 – 439	12	BNR 7
	Repeat	506 – 517	12	BNR 8
	Repeat	548 – 559	12	BNR 9
	Region	50 – 61	12	Intrachain binding of the propeptide and the extracellular domain
	Region	612 – 756	145	Interactions with LRPAP1 and NGFB
	Region	779 – 831	53	Golgi to endosome transport and interactions with GGA1 and GGA2
	Motif	787 – 792	6	Endocytosis signal Probable
Amino acid modifications
	Modified residue	825	1	Phosphoserine Ref.23
	Glycosylation	98	1	N-linked (GlcNAc...) Probable
	Glycosylation	162	1	N-linked (GlcNAc...) Ref.22
	Glycosylation	163	1	N-linked (GlcNAc...)
	Glycosylation	274	1	N-linked (GlcNAc...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	582	1	N-linked (GlcNAc...) Potential
	Glycosylation	684	1	N-linked (GlcNAc...) Potential
	Disulfide bond	86 ↔ 556		Ref.18
	Disulfide bond	257 ↔ 277		Ref.18
	Disulfide bond	448 ↔ 458		Ref.18
	Disulfide bond	612 ↔ 651		Ref.18
	Disulfide bond	634 ↔ 666		Ref.18
	Disulfide bond	668 ↔ 723		Ref.18
	Disulfide bond	675 ↔ 688		Ref.18
	Disulfide bond	702 ↔ 740		Ref.18
Natural variations
	Natural variant	358	1	D → Y: dbSNP rs2228605.		VAR_053681
Experimental info
	Mutagenesis	74 – 77	4	RWRR → GWRA: Abrogates propeptide cleavage. Ref.6
	Mutagenesis	76 – 77	2	RR → GG: Abrogates propeptide cleavage.
	Mutagenesis	792	1	Y → A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-795. Ref.9
	Mutagenesis	795	1	L → A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-792. Ref.9
	Mutagenesis	823 – 824	2	DD → NN: Reduces interaction with GGA1.
	Mutagenesis	825	1	S → A: Reduces interaction with GGA1. Ref.10
	Mutagenesis	826 – 828	3	DED → NQN: Abrogates interaction with GGA1 and impairs localization to the Golgi. Ref.10
	Mutagenesis	829 – 830	2	LL → AA: Abrogates interaction with GGA1 and impairs localization to the Golgi.
	Mutagenesis	829 – 830	2	Missing: Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795.
	Sequence conflict	650	1	V → M in CAA66904. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99523-1 [UniParc]. Last modified December 20, 2005. Version 3. Checksum: 91F96A3035A4B43A	FASTA	831	92,068
	10 20 30 40 50 60 MERPWGAADG LSRWPHGLGL LLLLQLLPPS TLSQDRLDAP PPPAAPLPRW SGPIGVSWGL 70 80 90 100 110 120 RAAAAGGAFP RGGRWRRSAP GEDEECGRVR DFVAKLANNT HQHVFDDLRG SVSLSWVGDS 130 140 150 160 170 180 TGVILVLTTF HVPLVIMTFG QSKLYRSEDY GKNFKDITDL INNTFIRTEF GMAIGPENSG 190 200 210 220 230 240 KVVLTAEVSG GSRGGRIFRS SDFAKNFVQT DLPFHPLTQM MYSPQNSDYL LALSTENGLW 250 260 270 280 290 300 VSKNFGGKWE EIHKAVCLAK WGSDNTIFFT TYANGSCKAD LGALELWRTS DLGKSFKTIG 310 320 330 340 350 360 VKIYSFGLGG RFLFASVMAD KDTTRRIHVS TDQGDTWSMA QLPSVGQEQF YSILAANDDM 370 380 390 400 410 420 VFMHVDEPGD TGFGTIFTSD DRGIVYSKSL DRHLYTTTGG ETDFTNVTSL RGVYITSVLS 430 440 450 460 470 480 EDNSIQTMIT FDQGGRWTHL RKPENSECDA TAKNKNECSL HIHASYSISQ KLNVPMAPLS 490 500 510 520 530 540 EPNAVGIVIA HGSVGDAISV MVPDVYISDD GGYSWTKMLE GPHYYTILDS GGIIVAIEHS 550 560 570 580 590 600 SRPINVIKFS TDEGQCWQTY TFTRDPIYFT GLASEPGARS MNISIWGFTE SFLTSQWVSY 610 620 630 640 650 660 TIDFKDILER NCEEKDYTIW LAHSTDPEDY EDGCILGYKE QFLRLRKSSV CQNGRDYVVT 670 680 690 700 710 720 KQPSICLCSL EDFLCDFGYY RPENDSKCVE QPELKGHDLE FCLYGREEHL TTNGYRKIPG 730 740 750 760 770 780 DKCQGGVNPV REVKDLKKKC TSNFLSPEKQ NSKSNSVPII LAIVGLMLVT VVAGVLIVKK 790 800 810 820 830 YVCGGRFLVH RYSVLQQHAE ANGVDGVDAL DTASHTNKSG YHDDSDEDLL E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9013611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[5]	"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: 9756851] [Abstract] Cited for: PROTEIN SEQUENCE OF 78-100, IDENTIFICATION AS A NEUROTENSIN RECEPTOR. Tissue: Brain.
[6]	"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: 9927419] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, MUTAGENESIS OF 74-ARG--ARG-77 AND 76-ARG-ARG-77, CLEAVAGE BY FURIN, GLYCOSYLATION.
[7]	"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: 9657377] [Abstract] Cited for: INTERACTION WITH LRPAP1.
[8]	"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: 10085125] [Abstract] Cited for: FUNCTION.
[9]	"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: 11331584] [Abstract] Cited for: FUNCTION, INTERACTION WITH GGA2, MUTAGENESIS OF TYR-792; LEU-795 AND 829-LEU-LEU-830.
[10]	"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: 11390366] [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.
[11]	"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: 12419319] [Abstract] Cited for: CLEAVAGE OF THE EXTRACELLULAR DOMAIN.
[12]	"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: 12209882] [Abstract] Cited for: FUNCTION, INDUCTION.
[13]	"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: 11859376] [Abstract] Cited for: INTERACTION WITH GGA1.
[14]	"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: 14657016] [Abstract] Cited for: FUNCTION, INTERACTION WITH GM2A AND PSAP, SUBCELLULAR LOCATION.
[15]	Erratum Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R. EMBO J. 23:1680-1680(2004)
[16]	"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: 12598608] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]	"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: 15313463] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]	"Functional organization of the sortilin Vps10p domain." Westergaard U.B., Soerensen E.S., Hermey G., Nielsen M.S., Nykjaer A., Kirkegaard K., Jacobsen C., Gliemann J., Madsen P., Petersen C.M. J. Biol. Chem. 279:50221-50229(2004) [PubMed: 15364913] [Abstract] Cited for: INTERACTION WITH LRPAP1 AND NGFB, SUBCELLULAR LOCATION, MASS SPECTROMETRY, DISULFIDE BONDS.
[19]	"Sortilin is essential for proNGF-induced neuronal cell death." Nykjaer A., Lee R., Teng K.K., Jansen P., Madsen P., Nielsen M.S., Jacobsen C., Kliemannel M., Schwarz E., Willnow T.E., Hempstead B.L., Petersen C.M. Nature 427:843-848(2004) [PubMed: 14985763] [Abstract] Cited for: FUNCTION, INTERACTION WITH NGFB AND NGFR.
[20]	"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: 15930396] [Abstract] Cited for: FUNCTION.
[21]	"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: 15987945] [Abstract] Cited for: FUNCTION, INTERACTION WITH BDNF.
[22]	"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: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, MASS SPECTROMETRY. Tissue: Platelet.
[23]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, MASS SPECTROMETRY. Tissue: Platelet.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-163, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X98248 mRNA. Translation: CAA66904.2.
AL390252 Genomic DNA. Translation: CAI13180.1.
BC023542 mRNA. Translation: AAH23542.1.

IPI

IPI00217882.

RefSeq

NP_002950.3.

UniGene

Hs.485195
Hs.703487

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F6K	X-ray	2.00	A	78-756	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99523. 1 interaction.

PTM databases

PhosphoSite

Q99523.

Proteomic databases

PRIDE

Q99523.

Genome annotation databases

Ensembl

ENSG00000134243. Homo sapiens. [Contig view]

GeneID

6272.

KEGG

hsa:6272.

NMPDR

fig|9606.3.peg.1632.

UCSC

uc001dxm.1. human.

Organism-specific databases

GeneCards

GC01M109653.

H-InvDB

HIX0000847.

HGNC

HGNC:11186. SORT1.

HPA

HPA006889.

MIM

602458. gene.

PharmGKB

PA36023.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q99523.

HOVERGEN

Q99523.

OMA

Q99523. LTQMMYS.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Gene expression databases

ArrayExpress

Q99523.

Bgee

Q99523.

CleanEx

HS_SORT1.

GermOnline

ENSG00000134243. Homo sapiens.

Family and domain databases

InterPro

IPR006581. VPS10.
[Graphical view]

SMART

SM00602. VPS10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

24343.

SOURCE

Search...

Entry information

Entry name

SORT_HUMAN

Accession

Primary (citable) accession number: Q99523
Secondary accession number(s): Q8IZ49

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 20, 2005
Last modified:	July 7, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)