Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q9BY11

- PACN1_HUMAN

UniProt

Q9BY11 - PACN1_HUMAN

Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

PACSIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission By similarity. Binds to membranes via its F-BAR domain and mediates membrane tubulation.By similarity3 Publications

    GO - Molecular functioni

    1. phospholipid binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament organization Source: InterPro
    2. establishment of protein localization to plasma membrane Source: BHF-UCL
    3. membrane tubulation Source: UniProtKB
    4. negative regulation of endocytosis Source: Ensembl
    5. neuron projection morphogenesis Source: UniProtKB
    6. positive regulation of dendrite development Source: BHF-UCL
    7. protein localization to membrane Source: UniProtKB
    8. synaptic vesicle endocytosis Source: UniProtKB

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C and casein kinase substrate in neurons protein 1
    Alternative name(s):
    Syndapin-1
    Gene namesi
    Name:PACSIN1
    Synonyms:KIAA1379
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8570. PACSIN1.

    Subcellular locationi

    Cytoplasm By similarity. Cell projection By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectionruffle membrane By similarity. Membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity. Cell junctionsynapse By similarity. Cytoplasmcytosol By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Colocalizes with MAPT in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites By similarity. Associates with membranes via its F-BAR domain.By similarity

    GO - Cellular componenti

    1. axon terminus Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. COPI-coated vesicle Source: Ensembl
    4. cytoplasm Source: LIFEdb
    5. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    6. cytosol Source: UniProtKB-SubCell
    7. perinuclear region of cytoplasm Source: BHF-UCL
    8. plasma membrane Source: BHF-UCL
    9. ruffle membrane Source: UniProtKB
    10. synapse Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251I → E: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication
    Mutagenesisi126 – 1261M → E: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication

    Organism-specific databases

    PharmGKBiPA32896.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Protein kinase C and casein kinase substrate in neurons protein 1PRO_0000161792Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei184 – 1841PhosphothreonineBy similarity
    Modified residuei394 – 3941PhosphotyrosineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BY11.
    PaxDbiQ9BY11.
    PRIDEiQ9BY11.

    PTM databases

    PhosphoSiteiQ9BY11.

    Expressioni

    Tissue specificityi

    Highly expressed in brain and, at much lower levels, in heart and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9BY11.
    BgeeiQ9BY11.
    CleanExiHS_PACSIN1.
    GenevestigatoriQ9BY11.

    Organism-specific databases

    HPAiCAB009929.
    HPA028852.
    HPA055491.

    Interactioni

    Subunit structurei

    May form heterooligomers with other PACSINs. Interacts with MAPT. Interacts with TRPV4 By similarity. Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts with DNM2 and DNM3. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3 By similarity. Homodimer. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FASLGP480234EBI-721769,EBI-495538
    HTTP428583EBI-721769,EBI-466029

    Protein-protein interaction databases

    BioGridi119018. 34 interactions.
    IntActiQ9BY11. 18 interactions.
    MINTiMINT-4538742.
    STRINGi9606.ENSP00000244458.

    Structurei

    Secondary structure

    1
    444
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni22 – 254
    Helixi26 – 7348
    Helixi78 – 10730
    Helixi109 – 12012
    Beta strandi127 – 1293
    Helixi130 – 17041
    Turni176 – 1794
    Helixi193 – 25664
    Helixi258 – 2603
    Turni262 – 2643
    Helixi265 – 27511
    Helixi280 – 29112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HAHX-ray2.77A/B1-325[»]
    3HAIX-ray2.88A/B/C/D1-308[»]
    3Q84X-ray2.80A/B/G/H/M/N14-308[»]
    3QNIX-ray2.80A/B1-307[»]
    ProteinModelPortaliQ9BY11.
    SMRiQ9BY11. Positions 15-308, 388-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BY11.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 7664FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini385 – 44460SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 307307F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili26 – 275250Add
    BLAST

    Domaini

    The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition By similarity.By similarity

    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.
    HOGENOMiHOG000007245.
    HOVERGENiHBG053486.
    InParanoidiQ9BY11.
    OMAiAMTREAN.
    OrthoDBiEOG75TMBJ.
    PhylomeDBiQ9BY11.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028518. PACSIN1.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10959:SF7. PTHR10959:SF7. 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.

    Q9BY11-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSYDEASL APEETTDSFW EVGNYKRTVK RIDDGHRLCN DLMNCVQERA    50
    KIEKAYGQQL TDWAKRWRQL IEKGPQYGSL ERAWGAIMTE ADKVSELHQE 100
    VKNNLLNEDL EKVKNWQKDA YHKQIMGGFK ETKEAEDGFR KAQKPWAKKM 150
    KELEAAKKAY HLACKEEKLA MTREMNSKTE QSVTPEQQKK LQDKVDKCKQ 200
    DVQKTQEKYE KVLEDVGKTT PQYMENMEQV FEQCQQFEEK RLVFLKEVLL 250
    DIKRHLNLAE NSSYIHVYRE LEQAIRGADA QEDLRWFRST SGPGMPMNWP 300
    QFEEWNPDLP HTTTKKEKQP KKAEGVALTN ATGAVESTSQ AGDRGSVSSY 350
    DRGQPYATEW SDDESGNPFG GSETNGGANP FEDDSKGVRV RALYDYDGQE 400
    QDELSFKAGD ELTKLGEEDE QGWCRGRLDS GQLGLYPANY VEAI 444
    Length:444
    Mass (Da):50,966
    Last modified:June 1, 2001 - v1
    Checksum:i6AAF801873770975
    GO

    Sequence cautioni

    The sequence BAA92617.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti334 – 3341A → V.
    Corresponds to variant rs41312309 [ dbSNP | Ensembl ].
    VAR_053554

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF242529 mRNA. Translation: AAK29206.1.
    AB037800 mRNA. Translation: BAA92617.2. Different initiation.
    AL834211 mRNA. Translation: CAD38895.1.
    BC040228 mRNA. Translation: AAH40228.1.
    CCDSiCCDS4793.1.
    RefSeqiNP_001186512.1. NM_001199583.2.
    NP_065855.1. NM_020804.4.
    UniGeneiHs.520087.

    Genome annotation databases

    EnsembliENST00000244458; ENSP00000244458; ENSG00000124507.
    ENST00000538621; ENSP00000439639; ENSG00000124507.
    GeneIDi29993.
    KEGGihsa:29993.
    UCSCiuc003ojo.4. human.

    Polymorphism databases

    DMDMi22256962.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF242529 mRNA. Translation: AAK29206.1 .
    AB037800 mRNA. Translation: BAA92617.2 . Different initiation.
    AL834211 mRNA. Translation: CAD38895.1 .
    BC040228 mRNA. Translation: AAH40228.1 .
    CCDSi CCDS4793.1.
    RefSeqi NP_001186512.1. NM_001199583.2.
    NP_065855.1. NM_020804.4.
    UniGenei Hs.520087.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HAH X-ray 2.77 A/B 1-325 [» ]
    3HAI X-ray 2.88 A/B/C/D 1-308 [» ]
    3Q84 X-ray 2.80 A/B/G/H/M/N 14-308 [» ]
    3QNI X-ray 2.80 A/B 1-307 [» ]
    ProteinModelPortali Q9BY11.
    SMRi Q9BY11. Positions 15-308, 388-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119018. 34 interactions.
    IntActi Q9BY11. 18 interactions.
    MINTi MINT-4538742.
    STRINGi 9606.ENSP00000244458.

    PTM databases

    PhosphoSitei Q9BY11.

    Polymorphism databases

    DMDMi 22256962.

    Proteomic databases

    MaxQBi Q9BY11.
    PaxDbi Q9BY11.
    PRIDEi Q9BY11.

    Protocols and materials databases

    DNASUi 29993.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244458 ; ENSP00000244458 ; ENSG00000124507 .
    ENST00000538621 ; ENSP00000439639 ; ENSG00000124507 .
    GeneIDi 29993.
    KEGGi hsa:29993.
    UCSCi uc003ojo.4. human.

    Organism-specific databases

    CTDi 29993.
    GeneCardsi GC06P036299.
    HGNCi HGNC:8570. PACSIN1.
    HPAi CAB009929.
    HPA028852.
    HPA055491.
    MIMi 606512. gene.
    neXtProti NX_Q9BY11.
    PharmGKBi PA32896.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283356.
    HOGENOMi HOG000007245.
    HOVERGENi HBG053486.
    InParanoidi Q9BY11.
    OMAi AMTREAN.
    OrthoDBi EOG75TMBJ.
    PhylomeDBi Q9BY11.
    TreeFami TF313677.

    Miscellaneous databases

    EvolutionaryTracei Q9BY11.
    GeneWikii PACSIN1.
    GenomeRNAii 29993.
    NextBioi 52788.
    PROi Q9BY11.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BY11.
    Bgeei Q9BY11.
    CleanExi HS_PACSIN1.
    Genevestigatori Q9BY11.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028518. PACSIN1.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10959:SF7. PTHR10959:SF7. 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. "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], TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala.
    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: Brain.
    6. "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: FUNCTION, INTERACTION WITH DNM1, SUBCELLULAR LOCATION, DOMAIN.
    7. "Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin."
      Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L., Rajashankar K.R., Sondermann H.
      Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 1-325, FUNCTION, LIPID-BINDING, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-125 AND MET-126, DOMAIN.
    8. "Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules."
      Bai X., Meng G., Luo M., Zheng X.
      J. Biol. Chem. 287:22387-22396(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-308, FUNCTION, DOMAIN.

    Entry informationi

    Entry nameiPACN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BY11
    Secondary accession number(s): Q9P2G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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