Sorting nexin-17 - Homo sapiens (Human)

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Q15036 (SNX17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sorting nexin-17

Gene names

Name:	SNX17
Synonyms:	KIAA0064

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in several stages of intracellular protein trafficking. 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. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). Ref.11 Ref.12 Ref.13 Ref.15
Subunit structure	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). Ref.9 Ref.10 Ref.12 Ref.13 Ref.15
Subcellular location	Cytoplasm. Early endosome. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Ref.9 Ref.10 Ref.11 Ref.12 Ref.13.
Domain	The PX domain mediates specific binding to phosphatidylinositol-3-phosphate (PtdIns(P3)). Required for association with endosomes.
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
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. Source: UniProtKB endosome transport Non-traceable author statement. Source: UniProtKB intracellular protein transport Non-traceable author statement. Source: UniProtKB regulation of endocytosis Non-traceable author statement. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: UniProtKB cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.13. Source: UniProtKB early endosome Inferred from direct assay. Source: UniProtKB
Molecular function	low-density lipoprotein particle receptor binding Inferred from direct assay. Source: UniProtKB phosphatidylinositol binding Inferred from direct assay Ref.13. Source: UniProtKB protein C-terminus binding Inferred from physical interaction Ref.9. 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

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

Domain

115 – 206

Ras-associating

Sites

Binding site

Phosphatidylinositol 3-phosphate By similarity

Binding site

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

Binding site

Phosphatidylinositol 3-phosphate By similarity

Binding site

Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue

334

Phosphothreonine By similarity

Modified residue

407

Phosphoserine Ref.16

Modified residue

409

Phosphoserine Ref.14

Modified residue

415

Phosphoserine Ref.14 Ref.16

Modified residue

421

Phosphoserine Ref.14 Ref.16

Modified residue

437

Phosphoserine Ref.14

Modified residue

440

Phosphoserine Ref.14

Experimental info

Mutagenesis

K → A: No association with endosomes. Ref.10

Sequence conflict

429

M → V in BAD96263. Ref.5

Secondary structure

470

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q15036 [UniParc].

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

« Hide

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: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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].
[4]	"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].
[5]	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]. Tissue: Adipose tissue.
[6]	"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. Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph, Muscle, Placenta and Testis.
[8]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11. Tissue: Platelet.
[9]	"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: 11237770] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN.
[10]	"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: 14739284] [Abstract] Cited for: INTERACTION WITH LDLR, MUTAGENESIS OF LYS-62, SUBCELLULAR LOCATION.
[11]	"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: 15121882] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
[12]	"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: 15769472] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH P-SELECTIN; LRP1 AND PTC, FUNCTION.
[13]	"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: 16712798] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KRIT1.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-415; SER-421; SER-437 AND SER-440, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19005208] [Abstract] Cited for: FUNCTION, INTERACTION WITH LRP1.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-415 AND SER-421, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"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.
[19]	"Structure of the SNX17 PX domain." Ghai R., Collins B. Submitted (MAR-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112.
+	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.
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.

RefSeq

NP_055563.1. NM_014748.2.

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	[»]

ProteinModelPortal

Q15036.

SMR

Q15036. Positions 1-109.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15036. 9 interactions.

MINT

MINT-1188067.

STRING

Q15036.

PTM databases

PhosphoSite

Q15036.

Polymorphism databases

DMDM

3123050.

Proteomic databases

PeptideAtlas

Q15036.

PRIDE

Q15036.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233575; ENSP00000233575; ENSG00000115234.

GeneID

9784.

KEGG

hsa:9784.

UCSC

uc002rkg.1. human.

Organism-specific databases

CTD

9784.

GeneCards

GC02P027593.

H-InvDB

HIX0001920.

HGNC

HGNC:14979. SNX17.

HPA

HPA043867.

MIM

605963. gene.

neXtProt

NX_Q15036.

PharmGKB

PA37954.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19026.

GeneTree

ENSGT00530000063147.

HOGENOM

HBG713823.

HOVERGEN

HBG061207.

InParanoid

Q15036.

OMA

DIEHGWI.

OrthoDB

EOG49KFQH.

PhylomeDB

Q15036.

Gene expression databases

ArrayExpress

Q15036.

Bgee

Q15036.

CleanEx

HS_SNX17.

Genevestigator

Q15036.

GermOnline

ENSG00000115234. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.30.1520.10. PX. 1 hit.

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

NextBio

36842.

SOURCE

Search...

Entry information

Entry name

SNX17_HUMAN

Accession

Primary (citable) accession number: Q15036
Secondary accession number(s): Q53HN7, Q6IAS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 116 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.

Relevant documents

Human chromosome 2

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents