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O60493

- SNX3_HUMAN

UniProt

O60493 - SNX3_HUMAN

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Protein

Sorting nexin-3

Gene

SNX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in protein transport between cellular compartments. Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Phosphatidylinositol 3-phosphateBy similarity
Binding sitei72 – 721Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei95 – 951Phosphatidylinositol 3-phosphateBy similarity
Binding sitei118 – 1181Phosphatidylinositol 3-phosphateBy similarity

GO - Molecular functioni

  1. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  2. protein phosphatase binding Source: UniProtKB

GO - Biological processi

  1. hemoglobin biosynthetic process Source: RefGenome
  2. intracellular protein transport Source: RefGenome
  3. intralumenal vesicle formation Source: UniProtKB
  4. membrane invagination Source: UniProtKB
  5. negative regulation of early endosome to late endosome transport Source: UniProtKB
  6. negative regulation of protein catabolic process Source: UniProtKB
  7. negative regulation of protein transport Source: UniProtKB
  8. negative regulation of viral entry into host cell Source: UniProtKB
  9. regulation of cellular protein metabolic process Source: Ensembl
  10. regulation of intracellular protein transport Source: Ensembl
  11. transferrin transport Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-3
Alternative name(s):
Protein SDP3
Gene namesi
Name:SNX3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11174. SNX3.

Subcellular locationi

Early endosome 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. cytosol Source: UniProtKB
  3. early endosome Source: UniProtKB
  4. early endosome membrane Source: UniProtKB
  5. endosome membrane Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endosome

Pathology & Biotechi

Involvement in diseasei

Microphthalmia, syndromic, 8 (MCOPS8) [MIM:601349]: A very rare congenital syndrome characterized by microcephaly, microphthalmia, ectrodactyly of the lower limbs and prognathism. Intellectual deficit has been reported. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities.1 Publication
Note: The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving SNX3 has been found in patients with syndromic microphthalmia. Translocation t(6;13)(q21;q12).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 713RRY → AAA: Abolishes binding to phosphatidylinositol 3-phosphate. 1 Publication
Mutagenesisi71 – 711Y → A: Abolishes binding to phosphatidylinositol 3-phosphate. 1 Publication

Keywords - Diseasei

Microphthalmia

Organism-specific databases

MIMi601349. phenotype.
Orphaneti3434. MMEP syndrome.
PharmGKBiPA36013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 162161Sorting nexin-3PRO_0000213840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei72 – 721Phosphoserine2 Publications

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO60493.
PaxDbiO60493.
PRIDEiO60493.

2D gel databases

REPRODUCTION-2DPAGEIPI00815770.
UCD-2DPAGEO60493.

PTM databases

PhosphoSiteiO60493.

Expressioni

Gene expression databases

BgeeiO60493.
CleanExiHS_SNX3.
GenevestigatoriO60493.

Organism-specific databases

HPAiHPA028638.

Interactioni

Subunit structurei

Interacts with USP10 and SCNN1A.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CRKP461082EBI-727209,EBI-886

Protein-protein interaction databases

BioGridi114263. 39 interactions.
IntActiO60493. 9 interactions.
MINTiMINT-1421811.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 346
Helixi44 – 463
Beta strandi49 – 557
Beta strandi63 – 697
Helixi71 – 8414
Helixi114 – 13118
Helixi133 – 1364
Helixi139 – 1468

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YPSX-ray2.60A/B/C/D24-155[»]
ProteinModelPortaliO60493.
SMRiO60493. Positions 24-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 151125PXPROSITE-ProRule annotationAdd
BLAST

Domaini

The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)).1 Publication

Sequence similaritiesi

Belongs to the sorting nexin family.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00650000093174.
HOVERGENiHBG055338.
InParanoidiO60493.
KOiK17918.
OMAiEVIDKNY.
OrthoDBiEOG7GJ6G1.
PhylomeDBiO60493.
TreeFamiTF314980.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
[Graphical view]
PfamiPF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60493-1) [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
MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE
60 70 80 90 100
IRVKTNLPIF KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ
110 120 130 140 150
LPFRGDDGIF DDNFIEERKQ GLEQFINKVA GHPLAQNERC LHMFLQDEII
160
DKSYTPSKIR HA
Length:162
Mass (Da):18,762
Last modified:January 23, 2007 - v3
Checksum:i983D422FCA6E07BC
GO
Isoform 2 (identifier: O60493-2) [UniParc]FASTAAdd to Basket

Also known as: SNX 3A

The sequence of this isoform differs from the canonical sequence as follows:
     55-86: Missing.

Show »
Length:130
Mass (Da):14,766
Checksum:i39DD7F3E916554AD
GO
Isoform 3 (identifier: O60493-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-162: VVVPPLPGKA...SYTPSKIRHA → PCLRMTSEARSHGRTWCAQNDEKLFCD

Note: No experimental confirmation available.

Show »
Length:113
Mass (Da):13,172
Checksum:iF8C0774B88153F42
GO
Isoform 4 (identifier: O60493-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-54: Missing.

Note: No experimental confirmation available.

Show »
Length:140
Mass (Da):16,316
Checksum:i01710ACF7D256DCA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1012QL → HF in AAC16018. (PubMed:11433298)Curated
Sequence conflicti151 – 1511D → V in BAF82165. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei33 – 5422Missing in isoform 4. CuratedVSP_014694Add
BLAST
Alternative sequencei55 – 8632Missing in isoform 2. 1 PublicationVSP_006190Add
BLAST
Alternative sequencei87 – 16276VVVPP…KIRHA → PCLRMTSEARSHGRTWCAQN DEKLFCD in isoform 3. 1 PublicationVSP_012928Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF034546 mRNA. Translation: AAC16040.1.
AF062483 mRNA. Translation: AAC16018.1.
AB047360 mRNA. Translation: BAB32649.1.
AK289476 mRNA. Translation: BAF82165.1.
BT007114 mRNA. Translation: AAP35778.1.
CR456898 mRNA. Translation: CAG33179.1.
AL078596, Z98742 Genomic DNA. Translation: CAI20817.1.
AL078596, Z98742 Genomic DNA. Translation: CAI20818.1.
AL078596, Z98742 Genomic DNA. Translation: CAI20819.1.
Z98742, AL078596 Genomic DNA. Translation: CAI95646.1.
Z98742, AL078596 Genomic DNA. Translation: CAI95647.1.
Z98742, AL078596 Genomic DNA. Translation: CAI95648.1.
CH471051 Genomic DNA. Translation: EAW48378.1.
CH471051 Genomic DNA. Translation: EAW48379.1.
CH471051 Genomic DNA. Translation: EAW48381.1.
CH471051 Genomic DNA. Translation: EAW48382.1.
BC008444 mRNA. Translation: AAH08444.1.
BC014580 mRNA. Translation: AAH14580.1.
BC015179 mRNA. Translation: AAH15179.1.
BC016863 mRNA. Translation: AAH16863.1.
CCDSiCCDS5064.1. [O60493-1]
CCDS5065.1. [O60493-2]
CCDS75501.1. [O60493-4]
RefSeqiNP_003786.1. NM_003795.5. [O60493-1]
NP_690040.1. NM_152827.3. [O60493-2]
UniGeneiHs.12102.

Genome annotation databases

EnsembliENST00000230085; ENSP00000230085; ENSG00000112335. [O60493-1]
ENST00000349379; ENSP00000296991; ENSG00000112335. [O60493-4]
ENST00000368979; ENSP00000357975; ENSG00000112335. [O60493-3]
ENST00000426155; ENSP00000401779; ENSG00000112335. [O60493-2]
GeneIDi8724.
KEGGihsa:8724.
UCSCiuc003psh.3. human. [O60493-1]
uc003psi.3. human. [O60493-2]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF034546 mRNA. Translation: AAC16040.1 .
AF062483 mRNA. Translation: AAC16018.1 .
AB047360 mRNA. Translation: BAB32649.1 .
AK289476 mRNA. Translation: BAF82165.1 .
BT007114 mRNA. Translation: AAP35778.1 .
CR456898 mRNA. Translation: CAG33179.1 .
AL078596 , Z98742 Genomic DNA. Translation: CAI20817.1 .
AL078596 , Z98742 Genomic DNA. Translation: CAI20818.1 .
AL078596 , Z98742 Genomic DNA. Translation: CAI20819.1 .
Z98742 , AL078596 Genomic DNA. Translation: CAI95646.1 .
Z98742 , AL078596 Genomic DNA. Translation: CAI95647.1 .
Z98742 , AL078596 Genomic DNA. Translation: CAI95648.1 .
CH471051 Genomic DNA. Translation: EAW48378.1 .
CH471051 Genomic DNA. Translation: EAW48379.1 .
CH471051 Genomic DNA. Translation: EAW48381.1 .
CH471051 Genomic DNA. Translation: EAW48382.1 .
BC008444 mRNA. Translation: AAH08444.1 .
BC014580 mRNA. Translation: AAH14580.1 .
BC015179 mRNA. Translation: AAH15179.1 .
BC016863 mRNA. Translation: AAH16863.1 .
CCDSi CCDS5064.1. [O60493-1 ]
CCDS5065.1. [O60493-2 ]
CCDS75501.1. [O60493-4 ]
RefSeqi NP_003786.1. NM_003795.5. [O60493-1 ]
NP_690040.1. NM_152827.3. [O60493-2 ]
UniGenei Hs.12102.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YPS X-ray 2.60 A/B/C/D 24-155 [» ]
ProteinModelPortali O60493.
SMRi O60493. Positions 24-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114263. 39 interactions.
IntActi O60493. 9 interactions.
MINTi MINT-1421811.

PTM databases

PhosphoSitei O60493.

2D gel databases

REPRODUCTION-2DPAGE IPI00815770.
UCD-2DPAGE O60493.

Proteomic databases

MaxQBi O60493.
PaxDbi O60493.
PRIDEi O60493.

Protocols and materials databases

DNASUi 8724.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230085 ; ENSP00000230085 ; ENSG00000112335 . [O60493-1 ]
ENST00000349379 ; ENSP00000296991 ; ENSG00000112335 . [O60493-4 ]
ENST00000368979 ; ENSP00000357975 ; ENSG00000112335 . [O60493-3 ]
ENST00000426155 ; ENSP00000401779 ; ENSG00000112335 . [O60493-2 ]
GeneIDi 8724.
KEGGi hsa:8724.
UCSCi uc003psh.3. human. [O60493-1 ]
uc003psi.3. human. [O60493-2 ]

Organism-specific databases

CTDi 8724.
GeneCardsi GC06M108578.
H-InvDB HIX0006117.
HGNCi HGNC:11174. SNX3.
HPAi HPA028638.
MIMi 601349. phenotype.
605930. gene.
neXtProti NX_O60493.
Orphaneti 3434. MMEP syndrome.
PharmGKBi PA36013.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5391.
GeneTreei ENSGT00650000093174.
HOVERGENi HBG055338.
InParanoidi O60493.
KOi K17918.
OMAi EVIDKNY.
OrthoDBi EOG7GJ6G1.
PhylomeDBi O60493.
TreeFami TF314980.

Enzyme and pathway databases

Reactomei REACT_163710. WNT ligand biogenesis and trafficking.

Miscellaneous databases

GeneWikii SNX3.
GenomeRNAii 8724.
NextBioi 32723.
PROi O60493.
SOURCEi Search...

Gene expression databases

Bgeei O60493.
CleanExi HS_SNX3.
Genevestigatori O60493.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
[Graphical view ]
Pfami PF00787. PX. 1 hit.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a family of sorting nexin molecules and characterization of their association with receptors."
    Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.
    Mol. Cell. Biol. 18:7278-7287(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P."
    Xu Y., Hortsman H., Seet L., Wong S.H., Hong W.
    Nat. Cell Biol. 3:658-666(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, PHOSPHOINOSITIDE-BINDING, DOMAIN PX, MUTAGENESIS OF 69-ARG--TYR-71 AND TYR-71.
  3. "Homo sapiens sorting nexin 3A (SNX 3A) mRNA."
    Hayama A., Uchida S., Sasaki S., Marumo F.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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 1).
    Tissue: Cerebellum.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain, Colon, Pancreas and Skin.
  10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  11. "Sorting nexin 3 (SNX3) is disrupted in a patient with a translocation t(6;13)(q21;q12) and microcephaly, microphthalmia, ectrodactyly, prognathism (MMEP) phenotype."
    Vervoort V.S., Viljoen D., Smart R., Suthers G., DuPont B.R., Abbott A., Schwartz C.E.
    J. Med. Genet. 39:893-899(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION, INVOLVEMENT IN MCOPS8.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Hrs and SNX3 functions in sorting and membrane invagination within multivesicular bodies."
    Pons V., Luyet P.P., Morel E., Abrami L., van der Goot F.G., Parton R.G., Gruenberg J.
    PLoS Biol. 6:E214-E214(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Crystal structure of the PX domain of human sorting nexin 3."
    Structural genomics consortium (SGC)
    Submitted (MAR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-155.

Entry informationi

Entry nameiSNX3_HUMAN
AccessioniPrimary (citable) accession number: O60493
Secondary accession number(s): A8K0B1
, E1P5E4, E1P5E5, O60718, Q4TT29, Q4TT31, Q5JXJ7, Q5JXJ8, Q96AP9, Q9C0J5, Q9NU45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 136 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3