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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: 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. identical protein binding Source: MGI
  3. lipid binding Source: UniProtKB
  4. phosphatidic acid binding Source: UniProtKB
  5. phospholipid binding Source: GO_Central

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. cytoskeleton organization Source: GO_Central
  6. membrane tubulation Source: UniProtKB
  7. negative regulation of endocytosis Source: MGI
  8. protein localization to endosome Source: MGI
  9. 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 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1345153. Pacsin2.

Subcellular locationi

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. endosome Source: GO_Central
  9. extracellular vesicular exosome Source: MGI
  10. extrinsic component of membrane Source: UniProtKB
  11. focal adhesion Source: MGI
  12. intracellular membrane-bounded organelle Source: MGI
  13. membrane-bounded vesicle Source: GO_Central
  14. nucleoplasm Source: MGI
  15. recycling endosome membrane Source: MGI
  16. 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. 1 Publication
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 2PRO_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

BgeeiQ9WVE8.
ExpressionAtlasiQ9WVE8. baseline and differential.
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

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni21 – 244Combined sources
Helixi25 – 7147Combined sources
Helixi77 – 10630Combined sources
Helixi108 – 11710Combined sources
Beta strandi124 – 1285Combined sources
Helixi131 – 17444Combined sources
Helixi184 – 1929Combined sources
Turni193 – 1986Combined sources
Helixi199 – 2024Combined sources
Helixi204 – 21613Combined sources
Helixi220 – 25536Combined sources
Helixi261 – 27515Combined sources
Helixi279 – 28911Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9WVE8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 282272F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini426 – 48661SH3PROSITE-ProRule annotationAdd
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.2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9WVE8.
OMAiHHAACKE.
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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WVE8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR
60 70 80 90 100
IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWIAVMSEA ERVSELHLEV
110 120 130 140 150
KASLMNEDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK
160 170 180 190 200
EVEAAKKAHH TACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD
210 220 230 240 250
VLKTKDKYEK SLKELDQTTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE
260 270 280 290 300
VQKHLDLSNV ASYKTIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ
310 320 330 340 350
FEEWSADLNR TLSRREKKKA VDGVTLTGIN QTGDQSGQNK PGSNLSVPSN
360 370 380 390 400
PAQSTQLQSS YNPFEDEDDT GSSISEKEDI KAKNVSSYEK TQTYPTDWSD
410 420 430 440 450
DESNNPFSST DANGDSNPFD EDTTSGTEVR VRALYDYEGQ EHDELSFKAG
460 470 480
DELTKIEDED EQGWCKGRLD SGQVGLYPAN YVEAIQ
Length:486
Mass (Da):55,833
Last modified:November 1, 1999 - v1
Checksum:i66C17ECCC767E0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9WVE8. 3 interactions.
MINTiMINT-1697712.

Chemistry

ChEMBLiCHEMBL2176817.

PTM databases

PhosphoSiteiQ9WVE8.

Proteomic databases

MaxQBiQ9WVE8.
PaxDbiQ9WVE8.
PRIDEiQ9WVE8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11252.
MGIiMGI:1345153. Pacsin2.

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9WVE8.
OMAiHHAACKE.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ9WVE8.
TreeFamiTF313677.

Miscellaneous databases

ChiTaRSiPacsin2. mouse.
EvolutionaryTraceiQ9WVE8.
NextBioi303853.
PROiQ9WVE8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVE8.
ExpressionAtlasiQ9WVE8. baseline and differential.
GenevestigatoriQ9WVE8.

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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: March 4, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.