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Q6PHU5 (SORT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sortilin
Alternative name(s):
Neurotensin receptor 3
Short name=NTR3
Short name=mNTR3
Gene names
Name:Sort1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length825 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.11 Ref.12 Ref.14 Ref.15

Subunit structure

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. Ref.7 Ref.9 Ref.12 Ref.14

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Endosome membrane; Single-pass type I membrane protein Potential. Golgi apparatusGolgi stack 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. 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. Ref.1 Ref.5 Ref.9 Ref.12 Ref.14

Tissue specificity

Expressed in the brain, particularly the piriform cortex, the cerebral cortex and the hippocampus. Ref.6

Developmental stage

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. Ref.6

Induction

During adipocyte differentiation. Ref.5 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 By similarity.

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

Post-translational modification

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

Sequence similarities

Belongs to the VPS10-related sortilin family. SORT1 subfamily.

Contains 9 BNR repeats.

Ontologies

Keywords
   Biological processDifferentiation
Endocytosis
Osteogenesis
Transport
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to endosome transport

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

endosome to lysosome transport

Inferred from electronic annotation. Source: Ensembl

endosome transport via multivesicular body sorting pathway

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

glucose import

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

myotube differentiation

Inferred from mutant phenotype PubMed 18258592. Source: BHF-UCL

negative regulation of lipoprotein lipase activity

Inferred from electronic annotation. Source: Ensembl

neuropeptide signaling pathway

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane to endosome transport

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

vesicle organization

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.12. Source: BHF-UCL

trans-Golgi network transport vesicle

Inferred from direct assay PubMed 15078902. Source: MGI

   Molecular_functionnerve growth factor receptor activity

Inferred from electronic annotation. Source: Ensembl

neurotensin receptor activity, non-G-protein coupled

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.14. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NraddQ8CJ265EBI-6985663,EBI-6985725

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PHU5-1)

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.
Isoform 2 (identifier: Q6PHU5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     748-748: Q → QDSRPQGHSLSQNPAPPPLGYTENTHFLSPTQKQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 7544Removed in mature form By similarity
PRO_0000045155
Chain76 – 825750Sortilin
PRO_0000045156

Regions

Topological domain32 – 754723Extracellular Potential
Transmembrane755 – 77521Helical; Potential
Topological domain776 – 82550Cytoplasmic Potential
Repeat143 – 15412BNR 1
Repeat196 – 20712BNR 2
Repeat238 – 24912BNR 3
Repeat285 – 29612BNR 4
Repeat326 – 33712BNR 5
Repeat375 – 38612BNR 6
Repeat426 – 43712BNR 7
Repeat504 – 51512BNR 8
Repeat546 – 55712BNR 9
Region48 – 5912Intrachain binding of the propeptide and the extracellular domain By similarity
Region610 – 754145Interactions with LRPAP1 and NGFB By similarity
Region777 – 82549Golgi to endosome transport and interactions with GGA1 and GGA2 By similarity
Motif785 – 7906Endocytosis signal Potential
Compositional bias38 – 447Poly-Pro

Amino acid modifications

Modified residue8131Phosphoserine By similarity
Modified residue8191Phosphoserine Ref.13
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation6821N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 554 By similarity
Disulfide bond255 ↔ 275 By similarity
Disulfide bond446 ↔ 456 By similarity
Disulfide bond610 ↔ 649 By similarity
Disulfide bond632 ↔ 664 By similarity
Disulfide bond666 ↔ 721 By similarity
Disulfide bond673 ↔ 686 By similarity
Disulfide bond700 ↔ 738 By similarity

Natural variations

Alternative sequence7481Q → QDSRPQGHSLSQNPAPPPLG YTENTHFLSPTQKQ in isoform 2.
VSP_016650

Experimental info

Sequence conflict3151V → E in AAF22639. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9A7A73C6FE1C8201

FASTA82591,200
        10         20         30         40         50         60 
MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG PVGVSWGLRA 

        70         80         90        100        110        120 
AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ HVFDDLSGSV SLSWVGDSTG 

       130        140        150        160        170        180 
VILVLTTFQV PLVIVSFGQS KLYRSEDYGK NFKDITNLIN NTFIRTEFGM AIGPENSGKV 

       190        200        210        220        230        240 
ILTAEVSGGS RGGRVFRSSD FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS 

       250        260        270        280        290        300 
KNFGEKWEEI HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK 

       310        320        330        340        350        360 
IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS ILAANEDMVF 

       370        380        390        400        410        420 
MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET DFTNVTSLRG VYITSTLSED 

       430        440        450        460        470        480 
NSIQSMITFD QGGRWEHLRK PENSKCDATA KNKNECSLHI HASYSISQKL NVPMAPLSEP 

       490        500        510        520        530        540 
NAVGIVIAHG SVGDAISVMV PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR 

       550        560        570        580        590        600 
PINVIKFSTD EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV 

       610        620        630        640        650        660 
DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ NGRDYVVAKQ 

       670        680        690        700        710        720 
PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC LYGKEEHLTT NGYRKIPGDK 

       730        740        750        760        770        780 
CQGGMNPARE VKDLKKKCTS NFLNPTKQNS KSNSVPIILA IVGLMLVTVV AGVLIVKKYV 

       790        800        810        820 
CGGRFLVHRY SVLQQHAEAD GVEALDSTSH AKSGYHDDSD EDLLE 

« Hide

Isoform 2 [UniParc].

Checksum: B4AC632F993E8E14
Show »

FASTA85894,813

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17756.1. [Q6PHU5-1]
RefSeqNP_001258528.1. NM_001271599.1. [Q6PHU5-2]
NP_064356.2. NM_019972.3. [Q6PHU5-1]
UniGeneMm.157119.

3D structure databases

ProteinModelPortalQ6PHU5.
SMRQ6PHU5. Positions 86-747.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203393. 1 interaction.
DIPDIP-46095N.
IntActQ6PHU5. 4 interactions.
MINTMINT-4130555.
STRING10090.ENSMUSP00000088052.

PTM databases

PhosphoSiteQ6PHU5.

Proteomic databases

MaxQBQ6PHU5.
PaxDbQ6PHU5.
PRIDEQ6PHU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102632; ENSMUSP00000099692; ENSMUSG00000068747. [Q6PHU5-1]
GeneID20661.
KEGGmmu:20661.
UCSCuc008qyr.1. mouse. [Q6PHU5-1]
uc008qys.1. mouse. [Q6PHU5-2]

Organism-specific databases

CTD6272.
MGIMGI:1338015. Sort1.

Phylogenomic databases

eggNOGNOG281049.
GeneTreeENSGT00510000046443.
HOGENOMHOG000231347.
HOVERGENHBG080235.
KOK12388.
OMALTQMMYS.
OrthoDBEOG7RBZ7S.
PhylomeDBQ6PHU5.
TreeFamTF324918.

Gene expression databases

ArrayExpressQ6PHU5.
BgeeQ6PHU5.
CleanExMM_SORT1.
GenevestigatorQ6PHU5.

Family and domain databases

InterProIPR006581. VPS10.
[Graphical view]
SMARTSM00602. VPS10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSORT1. mouse.
NextBio299105.
PROQ6PHU5.
SOURCESearch...

Entry information

Entry nameSORT_MOUSE
AccessionPrimary (citable) accession number: Q6PHU5
Secondary accession number(s): A2AEE8 expand/collapse secondary AC list , Q3UHE2, Q8K043, Q9QXW6
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot