Skip Header

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

Sorting nexin-6

Gene

SNX6

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

Functioni

Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex (PubMed:19935774). The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Does not have in vitro vesicle-to-membrane remodeling activity (PubMed:23085988). Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptor IGF2R (PubMed:17148574). May function as link between transport vesicles and dynactin (Probable). Negatively regulates retrograde transport of BACE1 from the cell surface to the trans-Golgi network (PubMed:20354142). Involved in E-cadherin sorting and degradation; inhibits PIP5K1C isoform 3-mediated E-cadherin degradation (PubMed:24610942). In association with GIT1 involved in EGFR degradation. Promotes lysosomal degradation of CDKN1B (By similarity). May contribute to transcription regulation (Probable).By similarity5 Publications2 PublicationsCurated

GO - Molecular functioni

  1. dynactin binding Source: UniProtKB
  2. phosphatidylinositol binding Source: GO_Central
  3. protein homodimerization activity Source: HGNC

GO - Biological processi

  1. endocytosis Source: GO_Central
  2. intracellular protein transport Source: UniProtKB
  3. negative regulation of epidermal growth factor-activated receptor activity Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. negative regulation of transforming growth factor beta receptor signaling pathway Source: HGNC
  6. retrograde transport, endosome to Golgi Source: UniProtKB
  7. vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

SignaLinkiQ9UNH7.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-6
Alternative name(s):
TRAF4-associated factor 2
Cleaved into the following chain:
Gene namesi
Name:SNX6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:14970. SNX6.

Subcellular locationi

Early endosome 3 Publications. Early endosome membrane 1 Publication1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side Curated. Cytoplasmic vesicle 1 Publication. Cytoplasm 1 Publication. Nucleus 2 Publications
Note: Interaction with SNX1 or SNX2 promotes location at endosome membranes (PubMed:19935774). Only a minor proportion is seen in the nucleus.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. early endosome membrane Source: UniProtKB
  4. extrinsic component of membrane Source: GO_Central
  5. intracellular Source: UniProtKB
  6. nucleus Source: UniProtKB-SubCell
  7. retromer complex Source: UniProtKB
  8. tubular endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681R → A: Reduces interaction with SNX1. Abolishes location at endosome membranes. 1 Publication
Mutagenesisi69 – 691Q → A: No effect on subcellular location. 1 Publication
Mutagenesisi97 – 971R → A: No effect on subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA37946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Sorting nexin-6PRO_0000423277Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 406405Sorting nexin-6, N-terminally processedPRO_0000213846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei2 – 21N-acetylmethionine; in Sorting nexin-6, N-terminally processed2 Publications

Post-translational modificationi

In vitro phosphorylated by PIM1; not affecting PIM1-dependent nuclear translocation (PubMed:11591366).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UNH7.
PaxDbiQ9UNH7.
PRIDEiQ9UNH7.

2D gel databases

OGPiQ9UNH7.
REPRODUCTION-2DPAGEIPI00298111.

PTM databases

PhosphoSiteiQ9UNH7.

Expressioni

Gene expression databases

BgeeiQ9UNH7.
CleanExiHS_SNX6.
ExpressionAtlasiQ9UNH7. baseline and differential.
GenevestigatoriQ9UNH7.

Organism-specific databases

HPAiHPA049374.

Interactioni

Subunit structurei

Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2 (PubMed:23085988). The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also descibed as vacuolar protein sorting subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity (Probable). Interacts with SNX1, SNX2, VPS26A, VPS29, VPS35, CDKN1B, TGFB receptors, BACE1, BRMS1, PIP5K1C isoform 3. Interacts with DCTN1; the association with DCTN1 is involved in movement of retromer-c ontaining vesicles toward the TGN (PubMed:11279102, PubMed:17148574, PubMed:19935774, PubMed:19619496, PubMed:20354142, PubMed:20830743, PubMed:23085988, PubMed:24610942). Interacts with CDKN1B and GIT1 (By similarity). Interacts with PIM1; translocating SNX6 to the nucleus (PubMed:11591366).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OPTNQ96CV92EBI-949294,EBI-748974

Protein-protein interaction databases

BioGridi121852. 50 interactions.
DIPiDIP-37549N.
IntActiQ9UNH7. 15 interactions.
MINTiMINT-2634416.
STRINGi9606.ENSP00000355217.

Structurei

3D structure databases

ProteinModelPortaliQ9UNH7.
SMRiQ9UNH7. Positions 21-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 173148PXPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 406204BARCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 179179Interaction with PIM11 PublicationAdd
BLAST
Regioni41 – 477Phosphatidylinositol bisphosphate bindingBy similarity
Regioni100 – 1067Phosphatidylinositol bisphosphate bindingBy similarity
Regioni114 – 1174Phosphatidylinositol bisphosphate bindingBy similarity
Regioni182 – 19918Membrane-binding amphipathic helix1 PublicationAdd
BLAST

Domaini

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate.By similarity
The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an amphipatric helix (AH) in the membrane (Probable).1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG255198.
GeneTreeiENSGT00780000121944.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ9UNH7.
KOiK17920.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9UNH7.
TreeFamiTF313698.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR001683. Phox.
IPR014637. SNX5/SNX6/SNX32.
IPR028657. SNX6.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF120. PTHR10555:SF120. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UNH7-1) [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
MMEGLDDGPD FLSEEDRGLK AINVDLQSDA ALQVDISDAL SERDKVKFTV
60 70 80 90 100
HTKSSLPNFK QNEFSVVRQH EEFIWLHDSF VENEDYAGYI IPPAPPRPDF
110 120 130 140 150
DASREKLQKL GEGEGSMTKE EFTKMKQELE AEYLAIFKKT VAMHEVFLCR
160 170 180 190 200
VAAHPILRRD LNFHVFLEYN QDLSVRGKNK KEKLEDFFKN MVKSADGVIV
210 220 230 240 250
SGVKDVDDFF EHERTFLLEY HNRVKDASAK SDRMTRSHKS AADDYNRIGS
260 270 280 290 300
SLYALGTQDS TDICKFFLKV SELFDKTRKI EARVSADEDL KLSDLLKYYL
310 320 330 340 350
RESQAAKDLL YRRSRSLVDY ENANKALDKA RAKNKDVLQA ETSQQLCCQK
360 370 380 390 400
FEKISESAKQ ELIDFKTRRV AAFRKNLVEL AELELKHAKG NLQLLQNCLA

VLNGDT
Length:406
Mass (Da):46,649
Last modified:May 1, 2000 - v1
Checksum:iE3659DB19C59E1BB
GO
Isoform 2 (identifier: Q9UNH7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.

Note: No experimental confirmation available.

Show »
Length:290
Mass (Da):33,570
Checksum:iC12EC83110C71CA8
GO

Sequence cautioni

The sequence AAD24202.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 116116Missing in isoform 2. 1 PublicationVSP_044824Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121856 mRNA. Translation: AAD27829.1.
U83194 mRNA. Translation: AAD24202.1. Different initiation.
AL445363 Genomic DNA. No translation available.
AL445883 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65913.1.
CH471078 Genomic DNA. Translation: EAW65915.1.
BC001798 mRNA. Translation: AAH01798.1.
CCDSiCCDS9648.1. [Q9UNH7-2]
RefSeqiNP_067072.3. NM_021249.3. [Q9UNH7-2]
NP_689419.2. NM_152233.2.
UniGeneiHs.356647.

Genome annotation databases

EnsembliENST00000396526; ENSP00000379779; ENSG00000129515. [Q9UNH7-2]
GeneIDi58533.
KEGGihsa:58533.
UCSCiuc001wse.1. human. [Q9UNH7-1]

Polymorphism databases

DMDMi10720285.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF121856 mRNA. Translation: AAD27829.1.
U83194 mRNA. Translation: AAD24202.1. Different initiation.
AL445363 Genomic DNA. No translation available.
AL445883 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65913.1.
CH471078 Genomic DNA. Translation: EAW65915.1.
BC001798 mRNA. Translation: AAH01798.1.
CCDSiCCDS9648.1. [Q9UNH7-2]
RefSeqiNP_067072.3. NM_021249.3. [Q9UNH7-2]
NP_689419.2. NM_152233.2.
UniGeneiHs.356647.

3D structure databases

ProteinModelPortaliQ9UNH7.
SMRiQ9UNH7. Positions 21-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121852. 50 interactions.
DIPiDIP-37549N.
IntActiQ9UNH7. 15 interactions.
MINTiMINT-2634416.
STRINGi9606.ENSP00000355217.

PTM databases

PhosphoSiteiQ9UNH7.

Polymorphism databases

DMDMi10720285.

2D gel databases

OGPiQ9UNH7.
REPRODUCTION-2DPAGEIPI00298111.

Proteomic databases

MaxQBiQ9UNH7.
PaxDbiQ9UNH7.
PRIDEiQ9UNH7.

Protocols and materials databases

DNASUi58533.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396526; ENSP00000379779; ENSG00000129515. [Q9UNH7-2]
GeneIDi58533.
KEGGihsa:58533.
UCSCiuc001wse.1. human. [Q9UNH7-1]

Organism-specific databases

CTDi58533.
GeneCardsiGC14M035030.
H-InvDBHIX0011592.
HGNCiHGNC:14970. SNX6.
HPAiHPA049374.
MIMi606098. gene.
neXtProtiNX_Q9UNH7.
PharmGKBiPA37946.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255198.
GeneTreeiENSGT00780000121944.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ9UNH7.
KOiK17920.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9UNH7.
TreeFamiTF313698.

Enzyme and pathway databases

SignaLinkiQ9UNH7.

Miscellaneous databases

ChiTaRSiSNX6. human.
GenomeRNAii58533.
NextBioi65116.
PROiQ9UNH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNH7.
CleanExiHS_SNX6.
ExpressionAtlasiQ9UNH7. baseline and differential.
GenevestigatoriQ9UNH7.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR001683. Phox.
IPR014637. SNX5/SNX6/SNX32.
IPR028657. SNX6.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF120. PTHR10555:SF120. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A large family of endosome-localized proteins related to sorting nexin 1."
    Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.
    Biochem. J. 358:7-16(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. Toji S., Yano M., Kobayasi A., Tamai K.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Eye.
  6. "Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from cytoplasm to nucleus."
    Ishibashi Y., Maita H., Yano M., Koike N., Tamai K., Ariga H., Iguchi-Ariga S.M.
    FEBS Lett. 506:33-38(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PIM1, PHOSPHORYLATION BY PIM1.
  7. "Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases."
    Parks W.T., Frank D.B., Huff C., Haft C.R., Martin J., Meng X., de Caestecker M.P., McNally J.G., Reddi A., Taylor S.I., Roberts A.B., Wang T., Lechleider R.J.
    J. Biol. Chem. 276:19332-19339(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBUNIT.
  8. "A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer."
    Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J., Cullen P.J.
    J. Cell Sci. 120:45-54(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNX1, SUBCELLULAR LOCATION.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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: FUNCTION, INTERACTION WITH DCTN1; SNX1 AND SNX2, MUTAGENESIS OF ARG-68; GLN-69 AND ARG-97, SUBCELLULAR LOCATION.
  11. "The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network."
    Wassmer T., Attar N., Harterink M., van Weering J.R., Traer C.J., Oakley J., Goud B., Stephens D.J., Verkade P., Korswagen H.C., Cullen P.J.
    Dev. Cell 17:110-122(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX1; SNX2; VPS26A; VPS29; VPS35 AND DCTN1.
  12. "Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing."
    Okada H., Zhang W., Peterhoff C., Hwang J.C., Nixon R.A., Ryu S.H., Kim T.W.
    FASEB J. 24:2783-2794(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BACE1.
  13. "Sorting nexin 6 interacts with breast cancer metastasis suppressor-1 and promotes transcriptional repression."
    Rivera J., Megias D., Bravo J.
    J. Cell. Biochem. 111:1464-1472(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRMS1.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules."
    van Weering J.R., Sessions R.B., Traer C.J., Kloer D.P., Bhatia V.K., Stamou D., Carlsson S.R., Hurley J.H., Cullen P.J.
    EMBO J. 31:4466-4480(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNX1 AND SNX2, DOMAIN.
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Isoform 5 of PIPKIgamma regulates the endosomal trafficking and degradation of E-cadherin."
    Schill N.J., Hedman A.C., Choi S., Anderson R.A.
    J. Cell Sci. 127:2189-2203(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIP5K1C.

Entry informationi

Entry nameiSNX6_HUMAN
AccessioniPrimary (citable) accession number: Q9UNH7
Secondary accession number(s): C0H5W9, Q9Y449
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.