Q15036 (SNX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sorting nexin-17

Gene names

Name:	SNX17
Synonyms:	KIAA0064

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.
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 process	Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Endosome Membrane
Coding sequence diversity	Alternative splicing
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol 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: Compara regulation of endocytosis Non-traceable author statement PubMed 12169628. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 10942595. Source: UniProtKB 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 membrane Non-traceable author statement PubMed 12169628. Source: UniProtKB
Molecular_function	low-density lipoprotein particle receptor binding Inferred from direct assay PubMed 12169628. Source: UniProtKB phosphatidylinositol binding Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	3	EBI-1752620,EBI-389883
PLCG1	P19174	2	EBI-1752620,EBI-79387

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 470

470

Sorting nexin-17

PRO_0000213865

Regions

Domain

1 – 109

109

PX

Domain

115 – 206

92

Ras-associating

Region

115 – 432

318

FERM-like

Region

270 – 432

163

PTB-like F3 module

Sites

Binding site

36

1

Phosphatidylinositol 3-phosphate By similarity

Binding site

38

1

Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity

Binding site

62

1

Phosphatidylinositol 3-phosphate By similarity

Binding site

75

1

Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue

334

1

Phosphothreonine By similarity

Modified residue

407

1

Phosphoserine Ref.17

Modified residue

409

1

Phosphoserine By similarity

Modified residue

415

1

Phosphoserine Ref.15 Ref.17

Modified residue

421

1

Phosphoserine Ref.15 Ref.17

Modified residue

437

1

Phosphoserine Ref.15 Ref.20

Modified residue

440

1

Phosphoserine Ref.15 Ref.20

Natural variations

Alternative sequence

22 – 46

25

Missing in isoform 2.

VSP_044935

Experimental info

Mutagenesis

62

1

K → A: No association with endosomes. Ref.11

Sequence conflict

429

1

M → V in BAD96263. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

470

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

20 – 27

8

Beta strand

30 – 36

7

Helix

37 – 51

15

Turn

53 – 55

3

Helix

69 – 88

20

Helix

90 – 94

5

Helix

96 – 109

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B1C8650CB8AFB5EE	FASTA	470	52,901
	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
	Isoform 2 [UniParc]. Checksum: A2D07008B80114CE	FASTA	445	49,999
	10 20 30 40 50 60 MHFSIPETES RSGDSGGSAY VLRKEYGANV LPAFPPKKLF SLTPAEVEQR REQLEKYMQA 70 80 90 100 110 120 VRQDPLLGSS ETFNSFLRRA QQETQQVPTE EVSLEVLLSN GQKVLVNVLT SDQTEDVLEA 130 140 150 160 170 180 VAAKLDLPDD LIGYFSLFLV REKEDGAFSF VRKLQEFELP YVSVTSLRSQ EYKIVLRKSY 190 200 210 220 230 240 WDSAYDDDVM ENRVGLNLLY AQTVSDIERG WILVTKEQHR QLKSLQEKVS KKEFLRLAQT 250 260 270 280 290 300 LRHYGYLRFD ACVADFPEKD CPVVVSAGNS ELSLQLRLPG QQLREGSFRV TRMRCWRVTS 310 320 330 340 350 360 SVPLPSGSTS SPGRGRGEVR LELAFEYLMS KDRLQWVTIT SPQAIMMSIC LQSMVDELMV 370 380 390 400 410 420 KKSGGSIRKM LRRRVGGTLR RSDSQQAVKS PPLLESPDAT RESMVKLSSK LSAVSLRGIG 430 440 SPSTDASASD VHGNFAFEGI GDEDL

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, 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.

IPI

IPI00014219.
IPI01010742.

RefSeq

NP_001253989.1. NM_001267060.1.
NP_055563.1. NM_014748.3.

UniGene

Hs.278569.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15036.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15036. 9 interactions.

MINT

MINT-1188067.

STRING

9606.ENSP00000233575.

PTM databases

PhosphoSite

Q15036.

Polymorphism databases

DMDM

3123050.

Proteomic databases

PaxDb

Q15036.

PeptideAtlas

Q15036.

PRIDE

Q15036.

Protocols and materials databases

DNASU

9784.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233575; ENSP00000233575; ENSG00000115234.
ENST00000537606; ENSP00000439208; ENSG00000115234.

GeneID

9784.

KEGG

hsa:9784.

UCSC

uc002rkg.1. human.

Organism-specific databases

CTD

9784.

GeneCards

GC02P027593.

HGNC

HGNC:14979. SNX17.

HPA

HPA043867.

MIM

605963. gene.

neXtProt

NX_Q15036.

PharmGKB

PA37954.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290558.

HOGENOM

HOG000007722.

HOVERGEN

HBG061207.

InParanoid

Q15036.

OMA

SDIEHGW.

OrthoDB

EOG49KFQH.

PhylomeDB

Q15036.

Gene expression databases

ArrayExpress

Q15036.

Bgee

Q15036.

CleanEx

HS_SNX17.

Genevestigator

Q15036.

GermOnline

ENSG00000115234. Homo sapiens.

Family and domain databases

Gene3D

3.30.1520.10. 1 hit.

InterPro

IPR001683. Phox.
IPR000159. Ras-assoc.
[Graphical view]

Pfam

PF00787. PX. 1 hit.
[Graphical view]

SMART

SM00312. PX. 1 hit.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.

PROSITE

PS50195. PX. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SNX17. human.

EvolutionaryTrace

Q15036.

GenomeRNAi

9784.

NextBio

36842.

SOURCE

Search...

Entry information

Entry name

SNX17_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.