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UniProtKB/Swiss-Prot entry Q9Y5X1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SNX9_HUMAN
Primary accession number Q9Y5X1
Secondary accession numbers Q9BSI7 Q9BVM1 Q9UJH6 Q9UP20
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Sorting nexin-9
Synonyms SH3 and PX domain-containing protein 1
Protein SDP1
SH3 and PX domain-containing protein 3A
Gene name
Name: SNX9
Synonyms: SH3PX1, SH3PXD3A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1042/0264-6021:3580007; PubMed=11485546 [NCBI, ExPASy, EBI, Israel, Japan]
Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
"A large family of endosome-localized proteins related to sorting nexin 1.";
Biochem. J. 358:7-16(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.274.44.31693; PubMed=10531379 [NCBI, ExPASy, EBI, Israel, Japan]
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1.";
J. Biol. Chem. 274:31693-31699(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang J.S., Smith D.I.;
"Identification of differentially expressed genes in matched prostate cancer and normal epithelial cell lines.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-595.
Ramanathan G., Subramaniam V.N., Hong W.;
"Human SDP1.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF121859; AAD27832.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF131214; AAF04473.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172847; AAL54871.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035634; CAI20465.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139330; CAI20465.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391863; CAI20465.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139330; CAI12979.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035634; CAI12979.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391863; CAI12979.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391863; CAI15180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035634; CAI15180.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139330; CAI15180.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001084; AAH01084.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005022; AAH05022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF076957; AAD43001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057308.1; -.
UniGene Hs.191213
3D structure databases
PDB
2RAI; X-ray; 3.20 A; A/B=204-595.[ExPASy / RCSB / EBI]
2RAJ; X-ray; 2.45 A; A=204-595.[ExPASy / RCSB / EBI]
2RAK; X-ray; 3.00 A; A=204-595.[ExPASy / RCSB / EBI]
3DYT; X-ray; 2.08 A; A=230-595.[ExPASy / RCSB / EBI]
3DYU; X-ray; 4.10 A; A/B/C=230-595.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2RAI; -.
2RAJ; -.
2RAK; -.
ModBase Q9Y5X1.
Protein-protein interaction databases
IntAct Q9Y5X1; -.
PTM databases
PhosphoSite Q9Y5X1; -.
Organism-specific databases
H-InvDB HIX0018165; -.
HGNC HGNC:14973; SNX9.
GenAtlas SNX9.
MIM 605952; gene. [NCBI / EBI]
PharmGKB PA37949; -.
GeneCards Q9Y5X1.
Gene expression databases
ArrayExpress Q9Y5X1; -.
CleanEx HS_SNX9; -.
GermOnline ENSG00000130340; Homo sapiens.
Ontologies
GO
GO:0035091; Molecular function: phosphoinositide binding (inferred from electronic annotation from InterPro).
GO:0005070; Molecular function: SH3/SH2 adaptor activity (traceable author statement from ProtInc).
GO:0007154; Biological process: cell communication (inferred from electronic annotation from InterPro).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001683; PX.
IPR001452; SH3.
IPR014536; Snx9.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1520.10; PX; 1.
Pfam PF00787; PX; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF027744; Snx9; 1.
PRINTS PR00452; SH3DOMAIN.
ProDom PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00312; PX; 1.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS50195; PX; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y5X1.
Proteomic databases
PeptideAtlas Q9Y5X1; -.
Genome annotation databases
Ensembl ENSG00000130340; Homo sapiens. [Contig view]
GeneID 51429; -.
KEGG hsa:51429; -.
Phylogenomic databases
HOGENOM Q9Y5X1; -.
HOVERGEN Q9Y5X1; -.
Other
NextBio 54991; -.
SOURCE SNX9; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Phosphoprotein; Protein transport; SH3 domain; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   595  595     Sorting nexin-9. PRO_0000213852
DOMAIN   1    62  62     SH3. 
DOMAIN   250   361  112     PX. 
MOD_RES   176   176        Phosphoserine (By similarity). 
CONFLICT   89    89        Q -> H (in Ref. 5; AAH05022). 
Sequence information
Length: 595 AA [This is the length of the unprocessed precursor] Molecular weight: 66592 Da [This is the MW of the unprocessed precursor] CRC64: 963892AC1A5A9227 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATKARVMYD FAAEPGNNEL TVNEGEIITI TNPDVGGGWL EGRNIKGERG LVPTDYVEIL 

        70         80         90        100        110        120 
PSDGKDQFSC GNSVADQAFL DSLSASTAQA SSSAASNNHQ VGSGNDPWSA WSASKSGNWE 

       130        140        150        160        170        180 
SSEGWGAQPE GAGAQRNTNT PNNWDTAFGH PQAYQGPATG DDDDWDEDWD GPKSSSYFKD 

       190        200        210        220        230        240 
SESADAGGAQ RGNSRASSSS MKIPLNKFPG FAKPGTEQYL LAKQLAKPKE KIPIIVGDYG 

       250        260        270        280        290        300 
PMWVYPTSTF DCVVADPRKG SKMYGLKSYI EYQLTPTNTN RSVNHRYKHF DWLYERLLVK 

       310        320        330        340        350        360 
FGSAIPIPSL PDKQVTGRFE EEFIKMRMER LQAWMTRMCR HPVISESEVF QQFLNFRDEK 

       370        380        390        400        410        420 
EWKTGKRKAE RDELAGVMIF STMEPEAPDL DLVEIEQKCE AVGKFTKAMD DGVKELLTVG 

       430        440        450        460        470        480 
QEHWKRCTGP LPKEYQKIGK ALQSLATVFS SSGYQGETDL NDAITEAGKT YEEIASLVAE 

       490        500        510        520        530        540 
QPKKDLHFLM ECNHEYKGFL GCFPDIIGTH KGAIEKVKES DKLVATSKIT LQDKQNMVKR 

       550        560        570        580        590 
VSIMSYALQA EMNHFHSNRI YDYNSVIRLY LEQQVQFYET IAEKLRQALS RFPVM 

Q9Y5X1 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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