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Q9UNF0

- PACN2_HUMAN

UniProt

Q9UNF0 - PACN2_HUMAN

Protein

Protein kinase C and casein kinase substrate in neurons protein 2

Gene

PACSIN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (13 Aug 2002)
      Previous versions | rss
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    Functioni

    Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis.5 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. phosphatidic acid binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transporter activity Source: ProtInc

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. caveola assembly Source: UniProtKB
    3. caveolin-mediated endocytosis Source: UniProtKB
    4. cell projection morphogenesis Source: UniProtKB
    5. membrane tubulation Source: UniProtKB
    6. negative regulation of endocytosis Source: Ensembl
    7. protein localization to endosome 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 2
    Alternative name(s):
    Syndapin-2
    Syndapin-II
    Gene namesi
    Name:PACSIN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:8571. PACSIN2.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection By similarity. Membranecaveola
    Note: Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1.

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. cytosol Source: Ensembl
    6. early endosome Source: UniProtKB-SubCell
    7. extracellular vesicular exosome Source: UniProt
    8. extrinsic component of membrane Source: UniProtKB
    9. intracellular membrane-bounded organelle Source: HPA
    10. nucleus Source: HPA
    11. recycling endosome membrane Source: UniProtKB
    12. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32897.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2PRO_0000161795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UNF0.
    PaxDbiQ9UNF0.
    PRIDEiQ9UNF0.

    PTM databases

    PhosphoSiteiQ9UNF0.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9UNF0.
    BgeeiQ9UNF0.
    GenevestigatoriQ9UNF0.

    Organism-specific databases

    HPAiCAB009929.
    HPA028852.
    HPA049854.

    Interactioni

    Subunit structurei

    Homodimer. May form heterooligomers with other PACSINs. Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL. Interacts with CAV1. Interacts with TRPV4.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-742503,EBI-742503
    DNM2P505704EBI-742503,EBI-346547
    FASLGP480234EBI-742503,EBI-495538

    Protein-protein interaction databases

    BioGridi116413. 33 interactions.
    IntActiQ9UNF0. 8 interactions.
    MINTiMINT-5005738.
    STRINGi9606.ENSP00000263246.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni21 – 244
    Helixi25 – 7248
    Helixi77 – 10630
    Helixi108 – 11912
    Beta strandi126 – 1283
    Helixi129 – 16941
    Helixi172 – 1776
    Helixi185 – 1884
    Helixi189 – 1913
    Turni192 – 1954
    Helixi197 – 25559
    Helixi257 – 2593
    Helixi263 – 27513
    Helixi279 – 29012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ABHX-ray2.00A/B1-305[»]
    3ACOX-ray2.70A/B1-343[»]
    3HAJX-ray2.78A/B1-486[»]
    3Q0KX-ray2.60A/B/C/D16-304[»]
    ProteinModelPortaliQ9UNF0.
    SMRiQ9UNF0. Positions 16-303, 429-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNF0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 7565FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 48661SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 306306F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili25 – 274250Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi362 – 3643NPF1
    Motifi405 – 4073NPF2
    Motifi417 – 4193NPF3

    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.4 Publications

    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.
    InParanoidiQ9UNF0.
    OMAiCKQDVLK.
    PhylomeDBiQ9UNF0.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028521. PACSIN2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10959:SF2. PTHR10959:SF2. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNF0-1) [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

    MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR    50
    IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV 100
    KASLMNDDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK 150
    EVEAAKKAHH AACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD 200
    VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE 250
    VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ 300
    FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN 350
    PAQSAQSQSS YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD 400
    DESNNPFSST DANGDSNPFD DDATSGTEVR VRALYDYEGQ EHDELSFKAG 450
    DELTKMEDED EQGWCKGRLD NGQVGLYPAN YVEAIQ 486
    Length:486
    Mass (Da):55,739
    Last modified:August 13, 2002 - v2
    Checksum:i821DBEF65DAD1AA8
    GO
    Isoform 2 (identifier: Q9UNF0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         344-384: Missing.

    Show »
    Length:445
    Mass (Da):51,353
    Checksum:i1DA87A2D42B5D5F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1821L → F in AAD41781. (PubMed:10431838)Curated
    Sequence conflicti256 – 2561D → N in AAD41781. (PubMed:10431838)Curated
    Sequence conflicti309 – 3091N → I in AAD41781. (PubMed:10431838)Curated
    Sequence conflicti336 – 3361S → F in AAD41781. (PubMed:10431838)Curated
    Sequence conflicti378 – 3803DDT → EDI in AAD41781. (PubMed:10431838)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751N → S.
    Corresponds to variant rs35383004 [ dbSNP | Ensembl ].
    VAR_053555
    Natural varianti294 – 2941M → I.
    Corresponds to variant rs2746984 [ dbSNP | Ensembl ].
    VAR_013711
    Natural varianti324 – 3241V → F.
    Corresponds to variant rs1062913 [ dbSNP | Ensembl ].
    VAR_013712

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei344 – 38441Missing in isoform 2. 2 PublicationsVSP_004517Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128536 mRNA. Translation: AAD41781.1.
    AL136845 mRNA. Translation: CAB66779.1.
    CR456536 mRNA. Translation: CAG30422.1.
    AL022476, AL049758 Genomic DNA. Translation: CAI20163.1.
    AL049758, AL022476 Genomic DNA. Translation: CAI20948.1.
    BC008037 mRNA. Translation: AAH08037.1.
    AL389984 mRNA. Translation: CAB97538.1.
    CCDSiCCDS43023.1. [Q9UNF0-1]
    CCDS54536.1. [Q9UNF0-2]
    RefSeqiNP_001171899.1. NM_001184970.1. [Q9UNF0-1]
    NP_001171900.1. NM_001184971.1. [Q9UNF0-2]
    NP_009160.2. NM_007229.3. [Q9UNF0-1]
    XP_005261376.1. XM_005261319.2. [Q9UNF0-2]
    XP_006724180.1. XM_006724117.1. [Q9UNF0-1]
    XP_006724181.1. XM_006724118.1. [Q9UNF0-1]
    XP_006724182.1. XM_006724119.1. [Q9UNF0-1]
    UniGeneiHs.162877.

    Genome annotation databases

    EnsembliENST00000263246; ENSP00000263246; ENSG00000100266. [Q9UNF0-1]
    ENST00000337959; ENSP00000338379; ENSG00000100266. [Q9UNF0-2]
    ENST00000402229; ENSP00000385040; ENSG00000100266. [Q9UNF0-1]
    ENST00000403744; ENSP00000385372; ENSG00000100266. [Q9UNF0-1]
    ENST00000407585; ENSP00000385952; ENSG00000100266. [Q9UNF0-2]
    GeneIDi11252.
    KEGGihsa:11252.
    UCSCiuc003bdg.4. human. [Q9UNF0-1]

    Polymorphism databases

    DMDMi22256968.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128536 mRNA. Translation: AAD41781.1 .
    AL136845 mRNA. Translation: CAB66779.1 .
    CR456536 mRNA. Translation: CAG30422.1 .
    AL022476 , AL049758 Genomic DNA. Translation: CAI20163.1 .
    AL049758 , AL022476 Genomic DNA. Translation: CAI20948.1 .
    BC008037 mRNA. Translation: AAH08037.1 .
    AL389984 mRNA. Translation: CAB97538.1 .
    CCDSi CCDS43023.1. [Q9UNF0-1 ]
    CCDS54536.1. [Q9UNF0-2 ]
    RefSeqi NP_001171899.1. NM_001184970.1. [Q9UNF0-1 ]
    NP_001171900.1. NM_001184971.1. [Q9UNF0-2 ]
    NP_009160.2. NM_007229.3. [Q9UNF0-1 ]
    XP_005261376.1. XM_005261319.2. [Q9UNF0-2 ]
    XP_006724180.1. XM_006724117.1. [Q9UNF0-1 ]
    XP_006724181.1. XM_006724118.1. [Q9UNF0-1 ]
    XP_006724182.1. XM_006724119.1. [Q9UNF0-1 ]
    UniGenei Hs.162877.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ABH X-ray 2.00 A/B 1-305 [» ]
    3ACO X-ray 2.70 A/B 1-343 [» ]
    3HAJ X-ray 2.78 A/B 1-486 [» ]
    3Q0K X-ray 2.60 A/B/C/D 16-304 [» ]
    ProteinModelPortali Q9UNF0.
    SMRi Q9UNF0. Positions 16-303, 429-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116413. 33 interactions.
    IntActi Q9UNF0. 8 interactions.
    MINTi MINT-5005738.
    STRINGi 9606.ENSP00000263246.

    PTM databases

    PhosphoSitei Q9UNF0.

    Polymorphism databases

    DMDMi 22256968.

    Proteomic databases

    MaxQBi Q9UNF0.
    PaxDbi Q9UNF0.
    PRIDEi Q9UNF0.

    Protocols and materials databases

    DNASUi 11252.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263246 ; ENSP00000263246 ; ENSG00000100266 . [Q9UNF0-1 ]
    ENST00000337959 ; ENSP00000338379 ; ENSG00000100266 . [Q9UNF0-2 ]
    ENST00000402229 ; ENSP00000385040 ; ENSG00000100266 . [Q9UNF0-1 ]
    ENST00000403744 ; ENSP00000385372 ; ENSG00000100266 . [Q9UNF0-1 ]
    ENST00000407585 ; ENSP00000385952 ; ENSG00000100266 . [Q9UNF0-2 ]
    GeneIDi 11252.
    KEGGi hsa:11252.
    UCSCi uc003bdg.4. human. [Q9UNF0-1 ]

    Organism-specific databases

    CTDi 11252.
    GeneCardsi GC22M043243.
    HGNCi HGNC:8571. PACSIN2.
    HPAi CAB009929.
    HPA028852.
    HPA049854.
    MIMi 604960. gene.
    neXtProti NX_Q9UNF0.
    PharmGKBi PA32897.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283356.
    HOGENOMi HOG000007245.
    HOVERGENi HBG053486.
    InParanoidi Q9UNF0.
    OMAi CKQDVLK.
    PhylomeDBi Q9UNF0.
    TreeFami TF313677.

    Miscellaneous databases

    ChiTaRSi PACSIN2. human.
    EvolutionaryTracei Q9UNF0.
    GeneWikii PACSIN2.
    GenomeRNAii 11252.
    NextBioi 42818.
    PROi Q9UNF0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNF0.
    Bgeei Q9UNF0.
    Genevestigatori Q9UNF0.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028521. PACSIN2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10959:SF2. PTHR10959:SF2. 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 2, a novel member of the PACSIN family of cytoplasmic adapter proteins."
      Ritter B., Modregger J., Paulsson M., Plomann M.
      FEBS Lett. 454:356-362(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Retina.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      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. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-486 (ISOFORM 2).
    7. "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: TISSUE SPECIFICITY.
    8. "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: TISSUE SPECIFICITY.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."
      Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.
      J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
    13. "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration."
      de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.
      J. Cell Sci. 124:2375-2388(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization."
      de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.
      J. Biol. Chem. 287:43438-43453(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "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, DOMAIN.
    17. "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis."
      Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.
      Mol. Biol. Cell 24:1776-1790(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH EHD1; EHD3 AND MICALL1.
    18. "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 (2.78 ANGSTROMS), DOMAIN.
    19. "Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II."
      Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T., Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.
      FEBS Lett. 584:1111-1118(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-305, DOMAIN.
    20. "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 (2.6 ANGSTROMS) OF 16-304.

    Entry informationi

    Entry nameiPACN2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNF0
    Secondary accession number(s): O95921
    , Q96HV9, Q9H0D3, Q9NPN1, Q9Y4V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 126 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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