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Q9WVE8

- PACN2_MOUSE

UniProt

Q9WVE8 - PACN2_MOUSE

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Protein
Protein kinase C and casein kinase substrate in neurons protein 2
Gene
Pacsin2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.7 Publications

GO - Molecular functioni

  1. cytoskeletal protein binding Source: MGI
  2. lipid binding Source: UniProtKB
  3. phosphatidic acid binding Source: UniProtKB
  4. protein binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  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: MGI
  7. protein localization to endosome Source: Ensembl
  8. signal transduction Source: MGI
Complete GO annotation...

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1345153. Pacsin2.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Membranecaveola
Note: Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1.7 Publications

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cell-cell junction Source: MGI
  3. cytoplasm Source: MGI
  4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  5. cytoskeleton Source: UniProtKB-SubCell
  6. cytosol Source: MGI
  7. early endosome Source: UniProtKB-SubCell
  8. extrinsic component of membrane Source: UniProtKB
  9. recycling endosome membrane Source: UniProtKB-SubCell
  10. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401D → K: Slight increase in affinity for membranes. Increases membrane tubulation activity. 1 Publication
Mutagenesisi50 – 501R → D: Slight decrease in affinity for membranes. Nearly abolishes membrane tubulation activity. 1 Publication
Mutagenesisi124 – 1252MM → TT: Nearly abolishes membrane tubulation activity.
Mutagenesisi189 – 1891K → E: Decreases affinity for membranes. 1 Publication
Mutagenesisi478 – 4781P → L: Loss of DNM1-, SYNJ1- and WASL-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2
PRO_0000161796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WVE8.
PaxDbiQ9WVE8.
PRIDEiQ9WVE8.

PTM databases

PhosphoSiteiQ9WVE8.

Expressioni

Tissue specificityi

Widely expressed (at protein level).2 Publications

Gene expression databases

ArrayExpressiQ9WVE8.
BgeeiQ9WVE8.
GenevestigatoriQ9WVE8.

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 TRPV4.6 Publications

Protein-protein interaction databases

IntActiQ9WVE8. 3 interactions.
MINTiMINT-1697712.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 244
Helixi25 – 7147
Helixi77 – 10630
Helixi108 – 11710
Beta strandi124 – 1285
Helixi131 – 17444
Helixi184 – 1929
Turni193 – 1986
Helixi199 – 2024
Helixi204 – 21613
Helixi220 – 25536
Helixi261 – 27515
Helixi279 – 28911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLLX-ray3.30A/B16-302[»]
ProteinModelPortaliQ9WVE8.
SMRiQ9WVE8. Positions 16-302, 429-484.

Miscellaneous databases

EvolutionaryTraceiQ9WVE8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7565FCH
Add
BLAST
Domaini426 – 48661SH3
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 274250
Add
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.2 Publications

Sequence similaritiesi

Belongs to the PACSIN family.
Contains 1 FCH domain.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9WVE8.
OMAiCKQDVLK.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ9WVE8.
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]

Sequencei

Sequence statusi: Complete.

Q9WVE8-1 [UniParc]FASTAAdd to Basket

« Hide

MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR    50
IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWIAVMSEA ERVSELHLEV 100
KASLMNEDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK 150
EVEAAKKAHH TACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD 200
VLKTKDKYEK SLKELDQTTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE 250
VQKHLDLSNV ASYKTIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ 300
FEEWSADLNR TLSRREKKKA VDGVTLTGIN QTGDQSGQNK PGSNLSVPSN 350
PAQSTQLQSS YNPFEDEDDT GSSISEKEDI KAKNVSSYEK TQTYPTDWSD 400
DESNNPFSST DANGDSNPFD EDTTSGTEVR VRALYDYEGQ EHDELSFKAG 450
DELTKIEDED EQGWCKGRLD SGQVGLYPAN YVEAIQ 486
Length:486
Mass (Da):55,833
Last modified:November 1, 1999 - v1
Checksum:i66C17ECCC767E0E7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF128535 mRNA. Translation: AAD41780.1.
BC023502 mRNA. Translation: AAH23502.1.
CCDSiCCDS27701.1.
RefSeqiNP_001152981.1. NM_001159509.1.
NP_001152982.1. NM_001159510.1.
NP_035992.1. NM_011862.3.
UniGeneiMm.23978.

Genome annotation databases

EnsembliENSMUST00000056177; ENSMUSP00000058320; ENSMUSG00000016664.
ENSMUST00000165095; ENSMUSP00000130098; ENSMUSG00000016664.
ENSMUST00000171436; ENSMUSP00000131504; ENSMUSG00000016664.
GeneIDi23970.
KEGGimmu:23970.
UCSCiuc007xba.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF128535 mRNA. Translation: AAD41780.1 .
BC023502 mRNA. Translation: AAH23502.1 .
CCDSi CCDS27701.1.
RefSeqi NP_001152981.1. NM_001159509.1.
NP_001152982.1. NM_001159510.1.
NP_035992.1. NM_011862.3.
UniGenei Mm.23978.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LLL X-ray 3.30 A/B 16-302 [» ]
ProteinModelPortali Q9WVE8.
SMRi Q9WVE8. Positions 16-302, 429-484.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9WVE8. 3 interactions.
MINTi MINT-1697712.

Chemistry

ChEMBLi CHEMBL2176817.

PTM databases

PhosphoSitei Q9WVE8.

Proteomic databases

MaxQBi Q9WVE8.
PaxDbi Q9WVE8.
PRIDEi Q9WVE8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000056177 ; ENSMUSP00000058320 ; ENSMUSG00000016664 .
ENSMUST00000165095 ; ENSMUSP00000130098 ; ENSMUSG00000016664 .
ENSMUST00000171436 ; ENSMUSP00000131504 ; ENSMUSG00000016664 .
GeneIDi 23970.
KEGGi mmu:23970.
UCSCi uc007xba.2. mouse.

Organism-specific databases

CTDi 11252.
MGIi MGI:1345153. Pacsin2.

Phylogenomic databases

eggNOGi NOG283356.
GeneTreei ENSGT00510000046376.
HOGENOMi HOG000007245.
HOVERGENi HBG053486.
InParanoidi Q9WVE8.
OMAi CKQDVLK.
OrthoDBi EOG75TMBJ.
PhylomeDBi Q9WVE8.
TreeFami TF313677.

Miscellaneous databases

ChiTaRSi PACSIN2. mouse.
EvolutionaryTracei Q9WVE8.
NextBioi 303853.
PROi Q9WVE8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WVE8.
Bgeei Q9WVE8.
Genevestigatori Q9WVE8.

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

« Hide 'large scale' publications
  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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6 X DBA.
  2. "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: Mammary gland.
  3. "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: FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION, HETEROOLIGOMERIZATION WITH PACSIN1 AND PACSIN3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-478.
  4. "EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling."
    Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., Kessels M.M., Qualmann B.
    Mol. Biol. Cell 16:3642-3658(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EHD1 AND EHD3, SUBCELLULAR LOCATION.
  5. "PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4."
    Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.
    J. Biol. Chem. 281:18753-18762(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPV4.
  6. "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: FUNCTION, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-40; ARG-50; 124-MET-MET-125 AND LYS-189.
  7. "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, INTERACTION WITH CAV1, SUBCELLULAR LOCATION.
  8. "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.
  9. "Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis."
    Hansen C.G., Howard G., Nichols B.J.
    J. Cell Sci. 124:2777-2785(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing."
    Plomann M., Wittmann J.G., Rudolph M.G.
    J. Mol. Biol. 400:129-136(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 16-302, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiPACN2_MOUSE
AccessioniPrimary (citable) accession number: Q9WVE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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