SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13596

- SNX1_HUMAN

UniProt

Q13596 - SNX1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Sorting nexin-1
Gene
SNX1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861Phosphatidylinositol 3-phosphate By similarity
Binding sitei188 – 1881Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei214 – 2141Phosphatidylinositol 3-phosphate By similarity
Binding sitei238 – 2381Phosphatidylinositol 3-phosphate By similarity

GO - Molecular functioni

  1. phosphatidylinositol binding Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. early endosome to Golgi transport Source: UniProtKB
  2. endocytosis Source: ProtInc
  3. intracellular protein transport Source: UniProtKB
  4. positive regulation of protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-1
Gene namesi
Name:SNX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11172. SNX1.

Subcellular locationi

Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side
Note: Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).5 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. cytoplasm Source: HGNC
  3. cytoplasmic membrane-bounded vesicle Source: RefGenome
  4. cytosol Source: Ensembl
  5. early endosome membrane Source: UniProtKB
  6. endosome membrane Source: UniProtKB
  7. intracellular membrane-bounded organelle Source: HPA
  8. retromer complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 2 Publications
Mutagenesisi429 – 4313KKR → EEE: Loss of endosomal location. 1 Publication

Organism-specific databases

PharmGKBiPA36011.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Sorting nexin-1
PRO_0000213835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication
Modified residuei188 – 1881Phosphoserine3 Publications
Modified residuei237 – 2371N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13596.
PaxDbiQ13596.
PRIDEiQ13596.

PTM databases

PhosphoSiteiQ13596.

Expressioni

Gene expression databases

ArrayExpressiQ13596.
BgeeiQ13596.
CleanExiHS_SNX1.
GenevestigatoriQ13596.

Organism-specific databases

HPAiHPA047373.
HPA052761.

Interactioni

Subunit structurei

Homodimer. Self-assembles into a complex of approximately 300 kDa By similarity. Interacts with HGS By similarity. Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with SNX6.6 Publications

Protein-protein interaction databases

BioGridi112525. 30 interactions.
DIPiDIP-398N.
IntActiQ13596. 10 interactions.
MINTiMINT-4135098.
STRINGi9606.ENSP00000369638.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi173 – 1764
Helixi187 – 19913
Beta strandi202 – 2054
Beta strandi210 – 2134
Beta strandi216 – 2216
Helixi234 – 25118
Helixi253 – 2564
Helixi259 – 2624
Turni263 – 2664
Helixi307 – 35650
Helixi361 – 38525
Helixi388 – 44053
Helixi443 – 48341
Turni484 – 4874
Helixi489 – 51123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I4KNMR-A142-269[»]
4FZSX-ray2.80A/B301-522[»]
ProteinModelPortaliQ13596.
SMRiQ13596. Positions 142-269, 305-513.

Miscellaneous databases

EvolutionaryTraceiQ13596.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 272130PX
Add
BLAST
Domaini302 – 522221BAR
Add
BLAST

Sequence similaritiesi

Belongs to the sorting nexin family.
Contains 1 BAR domain.

Phylogenomic databases

eggNOGiCOG5391.
HOVERGENiHBG000618.
InParanoidiQ13596.
KOiK17917.
OMAiEIAEWES.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ13596.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF129. PTHR10555:SF129. 1 hit.
PfamiPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13596-1) [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

MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA    50
AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS 100
TQNNQKKVLA KTLISLPPQE ATNSSKPQPT YEELEEEEQE DQFDLTVGIT 150
DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ FAVKRRFSDF LGLYEKLSEK 200
HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA ALERYLQRIV 250
NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI 300
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS 350
LAMLGSSEDN TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI 400
RLLAIVRAAF DQRMKTWQRW QDAQATLQKK REAEARLLWA NKPDKLQQAK 450
DEILEWESRV TQYERDFERI STVVRKEVIR FEKEKSKDFK NHVIKYLETL 500
LYSQQQLAKY WEAFLPEAKA IS 522
Length:522
Mass (Da):59,070
Last modified:November 16, 2001 - v3
Checksum:i6AC8AA0A589513E3
GO
Isoform 1A (identifier: Q13596-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     91-155: Missing.

Show »
Length:457
Mass (Da):51,813
Checksum:i3F844B9E84C258C2
GO
Isoform 3 (identifier: Q13596-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     507-522: LAKYWEAFLPEAKAIS → AGEQLGIRSGILLTKKLPRYSKFFSTVHKFCAAASLWKWGFFLSAYLSYLF

Note: No experimental confirmation available.

Show »
Length:557
Mass (Da):63,082
Checksum:iA03926548995DDA2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151S → Y.
Corresponds to variant rs1049501 [ dbSNP | Ensembl ].
VAR_052477
Natural varianti466 – 4661D → N.
Corresponds to variant rs1802376 [ dbSNP | Ensembl ].
VAR_034507

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei91 – 15565Missing in isoform 1A.
VSP_006189Add
BLAST
Alternative sequencei507 – 52216LAKYW…AKAIS → AGEQLGIRSGILLTKKLPRY SKFFSTVHKFCAAASLWKWG FFLSAYLSYLF in isoform 3.
VSP_044823Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171P → S in AAC17182. 1 Publication
Sequence conflicti211 – 2111P → S in AAC17182. 1 Publication
Sequence conflicti211 – 2111P → S in AAC17183. 1 Publication
Sequence conflicti502 – 5021Y → C in BAC87312. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53225 mRNA. Translation: AAA98672.1.
AF065483 mRNA. Translation: AAC17182.1.
AF065484 mRNA. Translation: AAC17183.1.
BT006983 mRNA. Translation: AAP35629.1.
AK128179 mRNA. Translation: BAC87312.1.
AK291752 mRNA. Translation: BAF84441.1.
AC021541 Genomic DNA. No translation available.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77663.1.
CH471082 Genomic DNA. Translation: EAW77665.1.
BC000357 mRNA. Translation: AAH00357.1.
CCDSiCCDS32266.1. [Q13596-1]
CCDS32268.1. [Q13596-2]
CCDS58371.1. [Q13596-3]
PIRiG02522.
RefSeqiNP_001229862.1. NM_001242933.1. [Q13596-3]
NP_003090.2. NM_003099.4. [Q13596-1]
NP_683758.1. NM_148955.3. [Q13596-2]
UniGeneiHs.188634.

Genome annotation databases

EnsembliENST00000261889; ENSP00000261889; ENSG00000028528. [Q13596-3]
ENST00000559844; ENSP00000453785; ENSG00000028528. [Q13596-1]
ENST00000561026; ENSP00000453567; ENSG00000028528. [Q13596-2]
GeneIDi6642.
KEGGihsa:6642.
UCSCiuc002amv.3. human. [Q13596-1]
uc002amx.3. human. [Q13596-2]

Polymorphism databases

DMDMi17380569.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53225 mRNA. Translation: AAA98672.1 .
AF065483 mRNA. Translation: AAC17182.1 .
AF065484 mRNA. Translation: AAC17183.1 .
BT006983 mRNA. Translation: AAP35629.1 .
AK128179 mRNA. Translation: BAC87312.1 .
AK291752 mRNA. Translation: BAF84441.1 .
AC021541 Genomic DNA. No translation available.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77663.1 .
CH471082 Genomic DNA. Translation: EAW77665.1 .
BC000357 mRNA. Translation: AAH00357.1 .
CCDSi CCDS32266.1. [Q13596-1 ]
CCDS32268.1. [Q13596-2 ]
CCDS58371.1. [Q13596-3 ]
PIRi G02522.
RefSeqi NP_001229862.1. NM_001242933.1. [Q13596-3 ]
NP_003090.2. NM_003099.4. [Q13596-1 ]
NP_683758.1. NM_148955.3. [Q13596-2 ]
UniGenei Hs.188634.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I4K NMR - A 142-269 [» ]
4FZS X-ray 2.80 A/B 301-522 [» ]
ProteinModelPortali Q13596.
SMRi Q13596. Positions 142-269, 305-513.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112525. 30 interactions.
DIPi DIP-398N.
IntActi Q13596. 10 interactions.
MINTi MINT-4135098.
STRINGi 9606.ENSP00000369638.

PTM databases

PhosphoSitei Q13596.

Polymorphism databases

DMDMi 17380569.

Proteomic databases

MaxQBi Q13596.
PaxDbi Q13596.
PRIDEi Q13596.

Protocols and materials databases

DNASUi 6642.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261889 ; ENSP00000261889 ; ENSG00000028528 . [Q13596-3 ]
ENST00000559844 ; ENSP00000453785 ; ENSG00000028528 . [Q13596-1 ]
ENST00000561026 ; ENSP00000453567 ; ENSG00000028528 . [Q13596-2 ]
GeneIDi 6642.
KEGGi hsa:6642.
UCSCi uc002amv.3. human. [Q13596-1 ]
uc002amx.3. human. [Q13596-2 ]

Organism-specific databases

CTDi 6642.
GeneCardsi GC15P064875.
HGNCi HGNC:11172. SNX1.
HPAi HPA047373.
HPA052761.
MIMi 601272. gene.
neXtProti NX_Q13596.
PharmGKBi PA36011.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5391.
HOVERGENi HBG000618.
InParanoidi Q13596.
KOi K17917.
OMAi EIAEWES.
OrthoDBi EOG7HHWSB.
PhylomeDBi Q13596.
TreeFami TF313698.

Miscellaneous databases

ChiTaRSi SNX1. human.
EvolutionaryTracei Q13596.
GeneWikii SNX1.
GenomeRNAii 6642.
NextBioi 25881.
PROi Q13596.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13596.
Bgeei Q13596.
CleanExi HS_SNX1.
Genevestigatori Q13596.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view ]
PANTHERi PTHR10555:SF129. PTHR10555:SF129. 1 hit.
Pfami PF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Enhanced degradation of EGF receptors by a sorting nexin, SNX1."
    Kurten R.C., Cadena D.L., Gill G.N.
    Science 272:1008-1010(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of a family of sorting nexin molecules and characterization of their association with receptors."
    Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.
    Mol. Cell. Biol. 18:7278-7287(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, INTERACTION WITH VPS26A; VPS29; VPS35 AND SNX2.
  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. "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] (ISOFORMS 1 AND 3).
    Tissue: Placenta and Testis.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  8. "The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation."
    Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D., Mellor H., Cullen P.J.
    J. Biol. Chem. 277:48730-48736(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214, INTERACTION WITH PHOSPHATIDYLINOSITIDES.
  9. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX2.
  10. "Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides."
    Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T., Cullen P.J.
    Curr. Biol. 14:1791-1800(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214 AND 429-LYS--ARG-431.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors."
    Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.
    Mol. Cell. Biol. 27:1112-1124(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport."
    Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.
    Cell Res. 19:1334-1349(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX6.
  15. "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-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Determinants of the endosomal localization of sorting nexin 1."
    Zhong Q., Watson M.J., Lazar C.S., Hounslow A.M., Waltho J.P., Gill G.N.
    Mol. Biol. Cell 16:2049-2057(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 142-269, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSNX1_HUMAN
AccessioniPrimary (citable) accession number: Q13596
Secondary accession number(s): A6NM19
, A8K6T7, H0Y2M5, O60750, O60751, Q6ZRJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 16, 2001
Last modified: September 3, 2014
This is version 134 of the entry and version 3 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

Miscellaneous

Binds phosphatidylinositol 3-phosphate (PtdIns-3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays, but not in liposome-based assays.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi