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Q15036

- SNX17_HUMAN

UniProt

Q15036 - SNX17_HUMAN

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Protein

Sorting nexin-17

Gene

SNX17

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

Functioni

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)).6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Phosphatidylinositol 3-phosphateBy similarity
Binding sitei38 – 381Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei62 – 621Phosphatidylinositol 3-phosphateBy similarity
Binding sitei75 – 751Phosphatidylinositol 3-phosphateBy similarity

GO - Molecular functioni

  1. low-density lipoprotein particle receptor binding Source: UniProtKB
  2. phosphatidylinositol binding Source: UniProtKB
  3. protein C-terminus binding Source: UniProtKB
  4. receptor binding Source: UniProtKB

GO - Biological processi

  1. cholesterol catabolic process Source: UniProtKB
  2. endosomal transport Source: UniProtKB
  3. intracellular protein transport Source: UniProtKB
  4. receptor-mediated endocytosis Source: Ensembl
  5. regulation of endocytosis Source: UniProtKB
  6. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

SignaLinkiQ15036.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-17
Gene namesi
Name:SNX17
Synonyms:KIAA0064
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14979. SNX17.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. early endosome Source: UniProtKB
  5. endosome Source: MGI
  6. endosome membrane Source: MGI
  7. Golgi apparatus Source: UniProtKB
  8. intracellular membrane-bounded organelle Source: HPA
  9. membrane Source: UniProtKB
  10. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621K → A: No association with endosomes. 1 Publication

Organism-specific databases

PharmGKBiPA37954.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Sorting nexin-17PRO_0000213865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei415 – 4151Phosphoserine2 Publications
Modified residuei421 – 4211Phosphoserine2 Publications
Modified residuei437 – 4371Phosphoserine2 Publications
Modified residuei440 – 4401Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15036.
PaxDbiQ15036.
PeptideAtlasiQ15036.
PRIDEiQ15036.

PTM databases

PhosphoSiteiQ15036.

Expressioni

Gene expression databases

BgeeiQ15036.
CleanExiHS_SNX17.
ExpressionAtlasiQ15036. baseline and differential.
GenevestigatoriQ15036.

Organism-specific databases

HPAiHPA043867.

Interactioni

Subunit structurei

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).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-1752620,EBI-389883
PLCG1P191742EBI-1752620,EBI-79387

Protein-protein interaction databases

BioGridi115128. 14 interactions.
DIPiDIP-52265N.
IntActiQ15036. 10 interactions.
MINTiMINT-1188067.
STRINGi9606.ENSP00000233575.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi20 – 278Combined sources
Beta strandi30 – 367Combined sources
Helixi37 – 5115Combined sources
Turni53 – 553Combined sources
Helixi69 – 8820Combined sources
Helixi90 – 945Combined sources
Helixi96 – 10914Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi128 – 1347Combined sources
Helixi139 – 15012Combined sources
Helixi154 – 1596Combined sources
Beta strandi160 – 1678Combined sources
Beta strandi173 – 1786Combined sources
Helixi185 – 1906Combined sources
Turni191 – 1933Combined sources
Beta strandi197 – 2037Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 2144Combined sources
Helixi218 – 23316Combined sources
Beta strandi236 – 2383Combined sources
Helixi241 – 25313Combined sources
Helixi256 – 2638Combined sources
Turni268 – 2703Combined sources
Beta strandi277 – 2837Combined sources
Beta strandi286 – 2938Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi310 – 3145Combined sources
Helixi315 – 3173Combined sources
Beta strandi318 – 3258Combined sources
Beta strandi346 – 35510Combined sources
Beta strandi358 – 3658Combined sources
Helixi369 – 38719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FOGX-ray2.80A1-108[»]
3LUIX-ray1.80A/B/C1-112[»]
4GXBX-ray1.80A111-388[»]
4TKNX-ray3.00A/B/C108-391[»]
ProteinModelPortaliQ15036.
SMRiQ15036. Positions 1-109, 112-388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15036.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 109109PXPROSITE-ProRule annotationAdd
BLAST
Domaini115 – 20692Ras-associatingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 432318FERM-likeAdd
BLAST
Regioni270 – 432163PTB-like F3 moduleAdd
BLAST

Domaini

The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes.1 Publication
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.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG290558.
GeneTreeiENSGT00530000063147.
HOGENOMiHOG000007722.
HOVERGENiHBG061207.
InParanoidiQ15036.
KOiK17929.
OMAiKKIFTLT.
OrthoDBiEOG70CR71.
PhylomeDBiQ15036.
TreeFamiTF318398.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR000159. Ras-assoc.
IPR028666. SNX17.
[Graphical view]
PANTHERiPTHR12431:SF16. PTHR12431:SF16. 1 hit.
PfamiPF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15036-1) [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
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE
60 70 80 90 100
YGANVLPAFP PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS
110 120 130 140 150
FLRRAQQETQ QVPTEEVSLE VLLSNGQKVL VNVLTSDQTE DVLEAVAAKL
160 170 180 190 200
DLPDDLIGYF SLFLVREKED GAFSFVRKLQ EFELPYVSVT SLRSQEYKIV
210 220 230 240 250
LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIERGWILVT KEQHRQLKSL
260 270 280 290 300
QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ
310 320 330 340 350
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGSTSSPGRG RGEVRLELAF
360 370 380 390 400
EYLMSKDRLQ WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV
410 420 430 440 450
GGTLRRSDSQ QAVKSPPLLE SPDATRESMV KLSSKLSAVS LRGIGSPSTD
460 470
ASASDVHGNF AFEGIGDEDL
Length:470
Mass (Da):52,901
Last modified:November 1, 1996 - v1
Checksum:iB1C8650CB8AFB5EE
GO
Isoform 2 (identifier: Q15036-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-46: Missing.

Note: No experimental confirmation available.

Show »
Length:445
Mass (Da):49,999
Checksum:iA2D07008B80114CE
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti429 – 4291M → V in BAD96263. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 4625Missing in isoform 2. 1 PublicationVSP_044935Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1750.1. [Q15036-1]
CCDS58704.1. [Q15036-2]
RefSeqiNP_001253989.1. NM_001267060.1. [Q15036-2]
NP_055563.1. NM_014748.3. [Q15036-1]
UniGeneiHs.278569.

Genome annotation databases

EnsembliENST00000233575; ENSP00000233575; ENSG00000115234. [Q15036-1]
ENST00000537606; ENSP00000439208; ENSG00000115234. [Q15036-2]
GeneIDi9784.
KEGGihsa:9784.
UCSCiuc002rkg.2. human. [Q15036-1]
uc010ylp.2. human.

Polymorphism databases

DMDMi3123050.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS1750.1. [Q15036-1 ]
CCDS58704.1. [Q15036-2 ]
RefSeqi NP_001253989.1. NM_001267060.1. [Q15036-2 ]
NP_055563.1. NM_014748.3. [Q15036-1 ]
UniGenei Hs.278569.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FOG X-ray 2.80 A 1-108 [» ]
3LUI X-ray 1.80 A/B/C 1-112 [» ]
4GXB X-ray 1.80 A 111-388 [» ]
4TKN X-ray 3.00 A/B/C 108-391 [» ]
ProteinModelPortali Q15036.
SMRi Q15036. Positions 1-109, 112-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115128. 14 interactions.
DIPi DIP-52265N.
IntActi Q15036. 10 interactions.
MINTi MINT-1188067.
STRINGi 9606.ENSP00000233575.

PTM databases

PhosphoSitei Q15036.

Polymorphism databases

DMDMi 3123050.

Proteomic databases

MaxQBi Q15036.
PaxDbi Q15036.
PeptideAtlasi Q15036.
PRIDEi Q15036.

Protocols and materials databases

DNASUi 9784.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233575 ; ENSP00000233575 ; ENSG00000115234 . [Q15036-1 ]
ENST00000537606 ; ENSP00000439208 ; ENSG00000115234 . [Q15036-2 ]
GeneIDi 9784.
KEGGi hsa:9784.
UCSCi uc002rkg.2. human. [Q15036-1 ]
uc010ylp.2. human.

Organism-specific databases

CTDi 9784.
GeneCardsi GC02P027593.
HGNCi HGNC:14979. SNX17.
HPAi HPA043867.
MIMi 605963. gene.
neXtProti NX_Q15036.
PharmGKBi PA37954.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290558.
GeneTreei ENSGT00530000063147.
HOGENOMi HOG000007722.
HOVERGENi HBG061207.
InParanoidi Q15036.
KOi K17929.
OMAi KKIFTLT.
OrthoDBi EOG70CR71.
PhylomeDBi Q15036.
TreeFami TF318398.

Enzyme and pathway databases

SignaLinki Q15036.

Miscellaneous databases

ChiTaRSi SNX17. human.
EvolutionaryTracei Q15036.
GeneWikii SNX17.
GenomeRNAii 9784.
NextBioi 36842.
PROi Q15036.
SOURCEi Search...

Gene expression databases

Bgeei Q15036.
CleanExi HS_SNX17.
ExpressionAtlasi Q15036. baseline and differential.
Genevestigatori Q15036.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR000159. Ras-assoc.
IPR028666. SNX17.
[Graphical view ]
PANTHERi PTHR12431:SF16. PTHR12431:SF16. 1 hit.
Pfami PF00787. PX. 1 hit.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
PS50200. RA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiSNX17_HUMAN
AccessioniPrimary (citable) accession number: Q15036
Secondary accession number(s): B4DQM7, Q53HN7, Q6IAS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 147 of the entry and version 1 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 2
    Human chromosome 2: 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