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Q9UKS6

- PACN3_HUMAN

UniProt

Q9UKS6 - PACN3_HUMAN

Protein

Protein kinase C and casein kinase substrate in neurons protein 3

Gene

PACSIN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (13 Aug 2002)
      Previous versions | rss
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    Functioni

    Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity By similarity.By similarity

    GO - Molecular functioni

    1. calcium channel inhibitor activity Source: UniProtKB
    2. cytoskeletal protein binding Source: UniProtKB
    3. lipid binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. membrane tubulation Source: UniProtKB
    3. negative regulation of calcium ion transport Source: UniProtKB
    4. negative regulation of endocytosis Source: UniProtKB
    5. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C and casein kinase substrate in neurons protein 3
    Alternative name(s):
    SH3 domain-containing protein 6511
    Gene namesi
    Name:PACSIN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8572. PACSIN3.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Detected at the inner aspect of the plasma membrane in myotubes.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32898.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Protein kinase C and casein kinase substrate in neurons protein 3PRO_0000161800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei276 – 2761Phosphoserine1 Publication
    Modified residuei319 – 3191Phosphoserine4 Publications
    Modified residuei324 – 3241Phosphothreonine1 Publication
    Modified residuei327 – 3271Phosphoserine1 Publication
    Modified residuei354 – 3541Phosphoserine3 Publications
    Modified residuei383 – 3831Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKS6.
    PaxDbiQ9UKS6.
    PRIDEiQ9UKS6.

    PTM databases

    PhosphoSiteiQ9UKS6.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in heart and skeletal muscle, intermediate levels in placenta, liver and pancreas, and very low levels in brain, lung and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKS6.
    BgeeiQ9UKS6.
    CleanExiHS_PACSIN3.
    GenevestigatoriQ9UKS6.

    Organism-specific databases

    HPAiHPA039480.
    HPA043904.

    Interactioni

    Subunit structurei

    Homodimer. May form heterooligomers with other PACSINs. Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with TRPV4 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM15Q134443EBI-77926,EBI-77818
    ADAM9Q134432EBI-77926,EBI-77903
    FASLGP480234EBI-77926,EBI-495538
    SOS1Q078892EBI-77926,EBI-297487
    SOS2Q078902EBI-77926,EBI-298181

    Protein-protein interaction databases

    BioGridi118896. 30 interactions.
    IntActiQ9UKS6. 6 interactions.
    MINTiMINT-5002056.
    STRINGi9606.ENSP00000298838.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKS6.
    SMRiQ9UKS6. Positions 12-302, 324-420.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 7364FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini363 – 42462SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 304304F-BAR domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili23 – 272250By similarityAdd
    BLAST

    Domaini

    The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation.1 Publication

    Sequence similaritiesi

    Belongs to the PACSIN family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG283356.
    HOVERGENiHBG053486.
    InParanoidiQ9UKS6.
    OMAiEQAFESC.
    OrthoDBiEOG75TMBJ.
    PhylomeDBiQ9UKS6.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028523. PACSIN3.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10959:SF1. PTHR10959:SF1. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UKS6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPEEDAGGE ALGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE    50
    KAYAQQLADW ARKWRGTVEK GPQYGTLEKA WHAFFTAAER LSALHLEVRE 100
    KLQGQDSERV RAWQRGAFHR PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV 150
    EASKKSYHAA RKDEKTAQTR ESHAKADSAV SQEQLRKLQE RVERCAKEAE 200
    KTKAQYEQTL AELHRYTPRY MEDMEQAFET CQAAERQRLL FFKDMLLTLH 250
    QHLDLSSSEK FHELHRDLHQ GIEAASDEED LRWWRSTHGP GMAMNWPQFE 300
    EWSLDTQRTI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPGSPGTGQD 350
    EEWSDEESPR KAATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG 400
    WCQGQLQSGR IGLYPANYVE CVGA 424
    Length:424
    Mass (Da):48,487
    Last modified:August 13, 2002 - v2
    Checksum:i6DBD940AE6D1F352
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611A → V.1 Publication
    Corresponds to variant rs7106654 [ dbSNP | Ensembl ].
    VAR_053556

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130979 mRNA. Translation: AAF04472.1.
    AF149825 mRNA. Translation: AAG31023.1.
    AF242530 mRNA. Translation: AAK29207.1.
    AC090589 Genomic DNA. No translation available.
    BC007914 mRNA. Translation: AAH07914.1.
    BC011889 mRNA. Translation: AAH11889.1.
    AK000577 mRNA. Translation: BAA91267.1.
    CCDSiCCDS31481.1.
    RefSeqiNP_001171903.1. NM_001184974.1.
    NP_001171904.1. NM_001184975.1.
    NP_057307.2. NM_016223.4.
    UniGeneiHs.334639.

    Genome annotation databases

    EnsembliENST00000298838; ENSP00000298838; ENSG00000165912.
    ENST00000528462; ENSP00000437252; ENSG00000165912.
    ENST00000539589; ENSP00000440945; ENSG00000165912.
    GeneIDi29763.
    KEGGihsa:29763.
    UCSCiuc001ndw.3. human.

    Polymorphism databases

    DMDMi22256967.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF130979 mRNA. Translation: AAF04472.1 .
    AF149825 mRNA. Translation: AAG31023.1 .
    AF242530 mRNA. Translation: AAK29207.1 .
    AC090589 Genomic DNA. No translation available.
    BC007914 mRNA. Translation: AAH07914.1 .
    BC011889 mRNA. Translation: AAH11889.1 .
    AK000577 mRNA. Translation: BAA91267.1 .
    CCDSi CCDS31481.1.
    RefSeqi NP_001171903.1. NM_001184974.1.
    NP_001171904.1. NM_001184975.1.
    NP_057307.2. NM_016223.4.
    UniGenei Hs.334639.

    3D structure databases

    ProteinModelPortali Q9UKS6.
    SMRi Q9UKS6. Positions 12-302, 324-420.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118896. 30 interactions.
    IntActi Q9UKS6. 6 interactions.
    MINTi MINT-5002056.
    STRINGi 9606.ENSP00000298838.

    PTM databases

    PhosphoSitei Q9UKS6.

    Polymorphism databases

    DMDMi 22256967.

    Proteomic databases

    MaxQBi Q9UKS6.
    PaxDbi Q9UKS6.
    PRIDEi Q9UKS6.

    Protocols and materials databases

    DNASUi 29763.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298838 ; ENSP00000298838 ; ENSG00000165912 .
    ENST00000528462 ; ENSP00000437252 ; ENSG00000165912 .
    ENST00000539589 ; ENSP00000440945 ; ENSG00000165912 .
    GeneIDi 29763.
    KEGGi hsa:29763.
    UCSCi uc001ndw.3. human.

    Organism-specific databases

    CTDi 29763.
    GeneCardsi GC11M047199.
    HGNCi HGNC:8572. PACSIN3.
    HPAi HPA039480.
    HPA043904.
    MIMi 606513. gene.
    neXtProti NX_Q9UKS6.
    PharmGKBi PA32898.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283356.
    HOVERGENi HBG053486.
    InParanoidi Q9UKS6.
    OMAi EQAFESC.
    OrthoDBi EOG75TMBJ.
    PhylomeDBi Q9UKS6.
    TreeFami TF313677.

    Miscellaneous databases

    GeneWikii PACSIN3.
    GenomeRNAii 29763.
    NextBioi 52258.
    PROi Q9UKS6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKS6.
    Bgeei Q9UKS6.
    CleanExi HS_PACSIN3.
    Genevestigatori Q9UKS6.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028523. PACSIN3.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10959:SF1. PTHR10959:SF1. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
      Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
      J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-61.
      Tissue: Mammary carcinoma.
    2. "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."
      Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.
      J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    3. "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family."
      Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.
      Gene 262:199-205(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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].
      Tissue: Skin and Uterus.
    6. "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] OF 1-405.
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; THR-324; SER-327; SER-354 AND SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-276; SER-319; SER-354 AND SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Versatile membrane deformation potential of activated pacsin."
      Goh S.L., Wang Q., Byrnes L.J., Sondermann H.
      PLoS ONE 7:E51628-E51628(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.

    Entry informationi

    Entry nameiPACN3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKS6
    Secondary accession number(s): A6NH84, Q9H331, Q9NWV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 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 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3