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O95219

- SNX4_HUMAN

UniProt

O95219 - SNX4_HUMAN

Protein

Sorting nexin-4

Gene

SNX4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei108 – 1081Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei132 – 1321Phosphatidylinositol 3-phosphateBy similarity
    Binding sitei154 – 1541Phosphatidylinositol 3-phosphateBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. endocytic recycling Source: UniProtKB
    2. endocytosis Source: ProtInc
    3. intracellular protein transport Source: RefGenome
    4. protein transport Source: UniProtKB

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorting nexin-4
    Gene namesi
    Name:SNX4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11175. SNX4.

    Subcellular locationi

    Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    Note: Also detected on a juxtanuclear endocytic recycling compartment (ERC).

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytoplasmic dynein complex Source: UniProtKB
    3. early endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. 1 Publication

    Organism-specific databases

    PharmGKBiPA36014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Sorting nexin-4PRO_0000213842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei22 – 221Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95219.
    PaxDbiO95219.
    PRIDEiO95219.

    2D gel databases

    DOSAC-COBS-2DPAGEO95219.

    PTM databases

    PhosphoSiteiO95219.

    Expressioni

    Gene expression databases

    ArrayExpressiO95219.
    BgeeiO95219.
    CleanExiHS_SNX4.
    GenevestigatoriO95219.

    Organism-specific databases

    HPAiHPA005709.

    Interactioni

    Subunit structurei

    Interacts with WWC1/KIBRA. Identified in a complex with WWC1/KIBRA and dynein components DYNLL1 and DYNC1I2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BIN1O004993EBI-724909,EBI-719094
    SNX30Q5VWJ92EBI-724909,EBI-8099676
    SNX7Q9UNH62EBI-724909,EBI-751422

    Protein-protein interaction databases

    BioGridi114262. 17 interactions.
    DIPiDIP-36719N.
    IntActiO95219. 12 interactions.
    MINTiMINT-263255.
    STRINGi9606.ENSP00000251775.

    Structurei

    3D structure databases

    ProteinModelPortaliO95219.
    SMRiO95219. Positions 55-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 187127PXPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5391.
    HOGENOMiHOG000007933.
    HOVERGENiHBG017826.
    InParanoidiO95219.
    KOiK17919.
    OMAiMDVYAAS.
    OrthoDBiEOG76HQ1H.
    PhylomeDBiO95219.
    TreeFamiTF328543.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    [Graphical view]
    PfamiPF00787. PX. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95219-1) [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

    MEQAPPDPER QLQPAPLEPL GSPDAGLGAA VGKEAEGAGE ESSGVDTMTH    50
    NNFWLKKIEI SVSEAEKRTG RNAMNMQETY TAYLIETRSV EHTDGQSVLT 100
    DSLWRRYSEF ELLRSYLLVY YPHIVVPPLP EKRAEFVWHK LSADNMDPDF 150
    VERRRIGLEN FLLRIASHPI LCRDKIFYLF LTQEGNWKET VNETGFQLKA 200
    DSRLKALNAT FRVKNPDKRF TDLKHYSDEL QSVISHLLRV RARVADRLYG 250
    VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY 300
    ADQLKEYLFY AEALRAVCRK HELMQYDLEM AAQDLASKKQ QCEELVTGTV 350
    RTFSLKGMTT KLFGQETPEQ REARIKVLEE QINEGEQQLK SKNLEGREFV 400
    KNAWADIERF KEQKNRDLKE ALISYAVMQI SMCKKGIQVW TNAKECFSKM 450
    Length:450
    Mass (Da):51,909
    Last modified:May 1, 1999 - v1
    Checksum:i3D5B52AC52A07686
    GO
    Isoform 2 (identifier: O95219-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-145: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:305
    Mass (Da):35,611
    Checksum:i2A82E353F65B99BB
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 145145Missing in isoform 2. 1 PublicationVSP_056665Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF065485 mRNA. Translation: AAC83149.1.
    AK001835 mRNA. Translation: BAG50982.1.
    AK298972 mRNA. Translation: BAG61066.1.
    AC080096 Genomic DNA. No translation available.
    AC117487 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79390.1.
    CH471052 Genomic DNA. Translation: EAW79391.1.
    CH471052 Genomic DNA. Translation: EAW79393.1.
    BC018762 mRNA. Translation: AAH18762.1.
    CCDSiCCDS3032.1.
    RefSeqiNP_003785.1. NM_003794.3.
    UniGeneiHs.507243.

    Genome annotation databases

    EnsembliENST00000251775; ENSP00000251775; ENSG00000114520.
    ENST00000536067; ENSP00000440824; ENSG00000114520.
    GeneIDi8723.
    KEGGihsa:8723.
    UCSCiuc003eib.4. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF065485 mRNA. Translation: AAC83149.1 .
    AK001835 mRNA. Translation: BAG50982.1 .
    AK298972 mRNA. Translation: BAG61066.1 .
    AC080096 Genomic DNA. No translation available.
    AC117487 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79390.1 .
    CH471052 Genomic DNA. Translation: EAW79391.1 .
    CH471052 Genomic DNA. Translation: EAW79393.1 .
    BC018762 mRNA. Translation: AAH18762.1 .
    CCDSi CCDS3032.1.
    RefSeqi NP_003785.1. NM_003794.3.
    UniGenei Hs.507243.

    3D structure databases

    ProteinModelPortali O95219.
    SMRi O95219. Positions 55-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114262. 17 interactions.
    DIPi DIP-36719N.
    IntActi O95219. 12 interactions.
    MINTi MINT-263255.
    STRINGi 9606.ENSP00000251775.

    PTM databases

    PhosphoSitei O95219.

    2D gel databases

    DOSAC-COBS-2DPAGE O95219.

    Proteomic databases

    MaxQBi O95219.
    PaxDbi O95219.
    PRIDEi O95219.

    Protocols and materials databases

    DNASUi 8723.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251775 ; ENSP00000251775 ; ENSG00000114520 .
    ENST00000536067 ; ENSP00000440824 ; ENSG00000114520 .
    GeneIDi 8723.
    KEGGi hsa:8723.
    UCSCi uc003eib.4. human.

    Organism-specific databases

    CTDi 8723.
    GeneCardsi GC03M125196.
    HGNCi HGNC:11175. SNX4.
    HPAi HPA005709.
    MIMi 605931. gene.
    neXtProti NX_O95219.
    PharmGKBi PA36014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5391.
    HOGENOMi HOG000007933.
    HOVERGENi HBG017826.
    InParanoidi O95219.
    KOi K17919.
    OMAi MDVYAAS.
    OrthoDBi EOG76HQ1H.
    PhylomeDBi O95219.
    TreeFami TF328543.

    Miscellaneous databases

    ChiTaRSi SNX4. human.
    GeneWikii SNX4.
    GenomeRNAii 8723.
    NextBioi 32719.
    PROi O95219.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95219.
    Bgeei O95219.
    CleanExi HS_SNX4.
    Genevestigatori O95219.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    [Graphical view ]
    Pfami PF00787. PX. 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

    1. "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] (ISOFORM 1).
    2. "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 2).
      Tissue: Placenta.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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 1).
      Tissue: Skin.
    6. "SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment."
      Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N., Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.
      Nat. Cell Biol. 9:1370-1380(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WWC1/KIBRA, MUTAGENESIS OF LYS-132, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNX4_HUMAN
    AccessioniPrimary (citable) accession number: O95219
    Secondary accession number(s): B3KMH0, B4DQV4, D3DNA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 112 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 3
      Human chromosome 3: 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