Skip Header

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

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • cytoskeletal protein binding Source: MGI
  • identical protein binding Source: MGI
  • lipid binding Source: UniProtKB
  • phosphatidic acid binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • caveola assembly Source: UniProtKB
  • caveolin-mediated endocytosis Source: UniProtKB
  • cell projection morphogenesis Source: UniProtKB
  • membrane tubulation Source: UniProtKB
  • negative regulation of endocytosis Source: MGI
  • protein localization to endosome Source: MGI
  • signal transduction Source: MGI
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-8856828. Clathrin-mediated endocytosis.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1345153. Pacsin2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: UniProtKB
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: MGI
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: GO_Central
  • extracellular exosome Source: MGI
  • extrinsic component of membrane Source: UniProtKB
  • focal adhesion Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nucleoplasm Source: MGI
  • recycling endosome membrane Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi40D → K: Slight increase in affinity for membranes. Increases membrane tubulation activity. 1 Publication1
Mutagenesisi50R → D: Slight decrease in affinity for membranes. Nearly abolishes membrane tubulation activity. 1 Publication1
Mutagenesisi124 – 125MM → TT: Nearly abolishes membrane tubulation activity. 1 Publication2
Mutagenesisi189K → E: Decreases affinity for membranes. 1 Publication1
Mutagenesisi478P → L: Loss of DNM1-, SYNJ1- and WASL-binding. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2176817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001617961 – 486Protein kinase C and casein kinase substrate in neurons protein 2Add BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysineCombined sources1
Modified residuei273PhosphoserineBy similarity1
Modified residuei399PhosphoserineCombined sources1
Modified residuei446PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9WVE8.
MaxQBiQ9WVE8.
PaxDbiQ9WVE8.
PRIDEiQ9WVE8.

PTM databases

iPTMnetiQ9WVE8.
PhosphoSitePlusiQ9WVE8.

Expressioni

Tissue specificityi

Widely expressed (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000016664.
ExpressionAtlasiQ9WVE8. baseline and differential.
GenevisibleiQ9WVE8. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9WVE8. 3 interactors.
MINTiMINT-1697712.
STRINGi10090.ENSMUSP00000058320.

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni21 – 24Combined sources4
Helixi25 – 71Combined sources47
Helixi77 – 106Combined sources30
Helixi108 – 117Combined sources10
Beta strandi124 – 128Combined sources5
Helixi131 – 174Combined sources44
Helixi184 – 192Combined sources9
Turni193 – 198Combined sources6
Helixi199 – 202Combined sources4
Helixi204 – 216Combined sources13
Helixi220 – 255Combined sources36
Helixi261 – 275Combined sources15
Helixi279 – 289Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9WVE8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 282F-BARPROSITE-ProRule annotationAdd BLAST272
Domaini426 – 486SH3PROSITE-ProRule annotationAdd BLAST61

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili25 – 274Add BLAST250

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi362 – 364NPF13
Motifi405 – 407NPF23
Motifi417 – 419NPF33

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

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9WVE8.
KOiK20123.
OMAiHHAACKE.
OrthoDBiEOG091G0AS9.
PhylomeDBiQ9WVE8.
TreeFamiTF313677.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF14. PTHR23065:SF14. 2 hits.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LLLX-ray3.30A/B16-302[»]
ProteinModelPortaliQ9WVE8.
SMRiQ9WVE8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVE8. 3 interactors.
MINTiMINT-1697712.
STRINGi10090.ENSMUSP00000058320.

Chemistry databases

ChEMBLiCHEMBL2176817.

PTM databases

iPTMnetiQ9WVE8.
PhosphoSitePlusiQ9WVE8.

Proteomic databases

EPDiQ9WVE8.
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

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9WVE8.
KOiK20123.
OMAiHHAACKE.
OrthoDBiEOG091G0AS9.
PhylomeDBiQ9WVE8.
TreeFamiTF313677.

Enzyme and pathway databases

ReactomeiR-MMU-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000016664.
ExpressionAtlasiQ9WVE8. baseline and differential.
GenevisibleiQ9WVE8. MM.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF14. PTHR23065:SF14. 2 hits.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 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...

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: November 2, 2016
This is version 129 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

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 one 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.