Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15036 (SNX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Sorting nexin-17
Gene names
Name:SNX17
Synonyms:KIAA0064
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). Ref.12 Ref.13 Ref.14 Ref.16 Ref.21 Ref.23

Subunit structure

Monomer. Interacts with APP (via cytoplasmic YXNPXY motif). Interacts with KIF1B By similarity. Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8. Interacts with KRIT1 (via N-terminus). Interacts with HRAS. Interacts with ITGB1 and ITGB5 (via NPxY motif). Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.21 Ref.23

Subcellular location

Cytoplasm. Early endosome. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.23.

Domain

The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes. Ref.23

The PTB-like F3 module within the FERM-like domain mediates cargo recognition via their NPxY sequences, while the F1 module (Ras-associating) is responsible for interaction with membrane-bound HRAS. Ref.23

Sequence similarities

Belongs to the sorting nexin family.

Contains 1 PX (phox homology) domain.

Contains 1 Ras-associating domain.

Sequence caution

The sequence BAA06542.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol catabolic process

Inferred by curator PubMed 12169628. Source: UniProtKB

endosomal transport

Non-traceable author statement PubMed 12169628. Source: UniProtKB

intracellular protein transport

Non-traceable author statement PubMed 12169628. Source: UniProtKB

receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

regulation of endocytosis

Non-traceable author statement PubMed 12169628. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 10942595. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.14. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 12169628. Source: UniProtKB

endosome

Inferred from direct assay PubMed 23382219. Source: MGI

endosome membrane

Inferred from direct assay PubMed 23382219. Source: MGI

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Non-traceable author statement PubMed 12169628. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionlow-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 12169628. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay Ref.14. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

receptor binding

Non-traceable author statement PubMed 12169628. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15036-1)

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: Q15036-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-46: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Sorting nexin-17
PRO_0000213865

Regions

Domain1 – 109109PX
Domain115 – 20692Ras-associating
Region115 – 432318FERM-like
Region270 – 432163PTB-like F3 module

Sites

Binding site361Phosphatidylinositol 3-phosphate By similarity
Binding site381Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site621Phosphatidylinositol 3-phosphate By similarity
Binding site751Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue4071Phosphoserine Ref.17
Modified residue4091Phosphoserine By similarity
Modified residue4151Phosphoserine Ref.15 Ref.17
Modified residue4211Phosphoserine Ref.15 Ref.17
Modified residue4371Phosphoserine Ref.15 Ref.20
Modified residue4401Phosphoserine Ref.15 Ref.20

Natural variations

Alternative sequence22 – 4625Missing in isoform 2.
VSP_044935

Experimental info

Mutagenesis621K → A: No association with endosomes. Ref.11
Sequence conflict4291M → V in BAD96263. Ref.6

Secondary structure

............................................................ 470
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: B1C8650CB8AFB5EE

FASTA47052,901
        10         20         30         40         50         60 
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVLPAFP 

        70         80         90        100        110        120 
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE 

       130        140        150        160        170        180 
VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ 

       190        200        210        220        230        240 
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT 

       250        260        270        280        290        300 
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ 

       310        320        330        340        350        360 
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF EYLMSKDRLQ 

       370        380        390        400        410        420 
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE 

       430        440        450        460        470 
SPDATRESMV KLSSKLSAVS LRGIGSPSTD ASASDVHGNF AFEGIGDEDL 

« Hide

Isoform 2 [UniParc].

Checksum: A2D07008B80114CE
Show »

FASTA44549,999

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[2]"Genomic structure of the KIAA064 gene."
Wightman P.J., Bonthron D.T.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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).
[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. expand/collapse author list , 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).
[5]"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).
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adipose tissue.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Lymph, Muscle, Placenta and Testis.
[9]"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 1-11.
Tissue: Platelet.
[10]"A new member of the sorting nexin family interacts with the C-terminus of P-selectin."
Florian V., Schlueter T., Bohnensack R.
Biochem. Biophys. Res. Commun. 281:1045-1050(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN.
[11]"Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17."
Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.
J. Biol. Chem. 279:16237-16245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LDLR, MUTAGENESIS OF LYS-62, SUBCELLULAR LOCATION.
[12]"Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin."
Williams R., Schlueter T., Roberts M.S., Knauth P., Bohnensack R., Cutler D.F.
Mol. Biol. Cell 15:3095-3105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[13]"Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking."
Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.
J. Mol. Biol. 347:813-825(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN; LRP1 AND PTC, FUNCTION.
[14]"Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1."
Czubayko M., Knauth P., Schluter T., Florian V., Bohnensack R.
Biochem. Biophys. Res. Commun. 345:1264-1272(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KRIT1.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-421; SER-437 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways."
Donoso M., Cancino J., Lee J., van Kerkhof P., Retamal C., Bu G., Gonzalez A., Caceres A., Marzolo M.P.
Mol. Biol. Cell 20:481-497(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LRP1.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-415 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-437 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways."
Steinberg F., Heesom K.J., Bass M.D., Cullen P.J.
J. Cell Biol. 197:219-230(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1 AND ITGB5.
[22]"Crystal structure of the PX domain of sorting nexin-17 (SNX17)."
Structural genomics consortium (SGC)
Submitted (JAN-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-108.
[23]"Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases."
Ghai R., Mobli M., Norwood S.J., Bugarcic A., Teasdale R.D., King G.F., Collins B.M.
Proc. Natl. Acad. Sci. U.S.A. 108:7763-7768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112, FUNCTION, SUBCELLULAR LOCATION, DOMAIN FERM-LIKE REGION, SUBUNIT, INTERACTION WITH HRAS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31764 mRNA. Translation: BAA06542.2. Different initiation.
AJ404855, AJ404856 Genomic DNA. Translation: CAC12897.1.
BT007167 mRNA. Translation: AAP35831.1.
AK298869 mRNA. Translation: BAG60989.1.
CR457081 mRNA. Translation: CAG33362.1.
AK222543 mRNA. Translation: BAD96263.1.
AC074117 Genomic DNA. Translation: AAY14844.1.
BC002524 mRNA. Translation: AAH02524.1.
BC002610 mRNA. Translation: AAH02610.1.
BC014620 mRNA. Translation: AAH14620.1.
BC050590 mRNA. Translation: AAH50590.1.
CCDSCCDS1750.1. [Q15036-1]
CCDS58704.1. [Q15036-2]
RefSeqNP_001253989.1. NM_001267060.1. [Q15036-2]
NP_055563.1. NM_014748.3. [Q15036-1]
UniGeneHs.278569.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FOGX-ray2.80A1-108[»]
3LUIX-ray1.80A/B/C1-112[»]
4GXBX-ray1.80A111-388[»]
ProteinModelPortalQ15036.
SMRQ15036. Positions 1-109, 112-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115128. 9 interactions.
DIPDIP-52265N.
IntActQ15036. 10 interactions.
MINTMINT-1188067.
STRING9606.ENSP00000233575.

PTM databases

PhosphoSiteQ15036.

Polymorphism databases

DMDM3123050.

Proteomic databases

MaxQBQ15036.
PaxDbQ15036.
PeptideAtlasQ15036.
PRIDEQ15036.

Protocols and materials databases

DNASU9784.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233575; ENSP00000233575; ENSG00000115234. [Q15036-1]
ENST00000537606; ENSP00000439208; ENSG00000115234. [Q15036-2]
GeneID9784.
KEGGhsa:9784.
UCSCuc002rkg.2. human. [Q15036-1]
uc010ylp.2. human.

Organism-specific databases

CTD9784.
GeneCardsGC02P027593.
HGNCHGNC:14979. SNX17.
HPAHPA043867.
MIM605963. gene.
neXtProtNX_Q15036.
PharmGKBPA37954.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290558.
HOGENOMHOG000007722.
HOVERGENHBG061207.
InParanoidQ15036.
KOK17929.
OMAKKIFTLT.
OrthoDBEOG70CR71.
PhylomeDBQ15036.
TreeFamTF318398.

Enzyme and pathway databases

SignaLinkQ15036.

Gene expression databases

ArrayExpressQ15036.
BgeeQ15036.
CleanExHS_SNX17.
GenevestigatorQ15036.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR000159. Ras-assoc.
IPR028666. SNX17.
[Graphical view]
PANTHERPTHR12431:SF16. PTHR12431:SF16. 1 hit.
PfamPF00787. PX. 1 hit.
[Graphical view]
SMARTSM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNX17. human.
EvolutionaryTraceQ15036.
GeneWikiSNX17.
GenomeRNAi9784.
NextBio36842.
PROQ15036.
SOURCESearch...

Entry information

Entry nameSNX17_HUMAN
AccessionPrimary (citable) accession number: Q15036
Secondary accession number(s): B4DQM7, Q53HN7, Q6IAS3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM