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Protein kinase C and casein kinase substrate in neurons protein 2 (Syndapin-2) (Syndapin-II)

 PACN2_HUMAN             Reviewed;         486 AA.
Q9UNF0; O95921; Q96HV9; Q9H0D3; Q9NPN1; Q9Y4V2;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
30-AUG-2017, entry version 155.
RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
AltName: Full=Syndapin-2;
AltName: Full=Syndapin-II;
Name=PACSIN2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Retina;
PubMed=10431838; DOI=10.1016/S0014-5793(99)00830-3;
Ritter B., Modregger J., Paulsson M., Plomann M.;
"PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter
proteins.";
FEBS Lett. 454:356-362(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-486 (ISOFORM 2).
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY.
PubMed=11082044;
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
"All three PACSIN isoforms bind to endocytic proteins and inhibit
endocytosis.";
J. Cell Sci. 113:4511-4521(2000).
[8]
TISSUE SPECIFICITY.
PubMed=11179684; DOI=10.1016/S0378-1119(00)00531-X;
Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.;
"PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
pacsin-syndapin-FAP52 gene family.";
Gene 262:199-205(2001).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=21610094; DOI=10.1242/jcs.086264;
Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.;
"Essential role of PACSIN2/syndapin-II in caveolae membrane
sculpting.";
J. Cell Sci. 124:2032-2040(2011).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC1.
PubMed=21693584; DOI=10.1242/jcs.080630;
de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C.,
Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.;
"The F-BAR domain protein PACSIN2 associates with Rac1 and regulates
cell spreading and migration.";
J. Cell Sci. 124:2375-2388(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23129763; DOI=10.1074/jbc.M112.391078;
de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.;
"The F-BAR protein PACSIN2 regulates epidermal growth factor receptor
internalization.";
J. Biol. Chem. 287:43438-43453(2012).
[16]
FUNCTION, AND DOMAIN.
PubMed=23236520; DOI=10.1371/journal.pone.0051628;
Goh S.L., Wang Q., Byrnes L.J., Sondermann H.;
"Versatile membrane deformation potential of activated pacsin.";
PLoS ONE 7:E51628-E51628(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-446, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, SUBCELLULAR LOCATION,
AND INTERACTION WITH EHD1; EHD3 AND MICALL1.
PubMed=23596323; DOI=10.1091/mbc.E13-01-0026;
Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.;
"Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular
recycling endosome biogenesis.";
Mol. Biol. Cell 24:1776-1790(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS), AND DOMAIN.
PubMed=19549836; DOI=10.1073/pnas.0902974106;
Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L.,
Rajashankar K.R., Sondermann H.;
"Molecular mechanism of membrane constriction and tubulation mediated
by the F-BAR protein Pacsin/Syndapin.";
Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-305, AND DOMAIN.
PubMed=20188097; DOI=10.1016/j.febslet.2010.02.058;
Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T.,
Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.;
"Mapping of the basic amino-acid residues responsible for tubulation
and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin
II.";
FEBS Lett. 584:1111-1118(2010).
[22]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 16-304.
PubMed=22573331; DOI=10.1074/jbc.M112.358960;
Bai X., Meng G., Luo M., Zheng X.;
"Rigidity of wedge loop in PACSIN 3 protein is a key factor in
dictating diameters of tubules.";
J. Biol. Chem. 287:22387-22396(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:21610094,
ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23129763,
ECO:0000269|PubMed:23236520, ECO:0000269|PubMed:23596323}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23596323}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-742503, EBI-742503;
P50570:DNM2; NbExp=4; IntAct=EBI-742503, EBI-346547;
P48023:FASLG; NbExp=4; IntAct=EBI-742503, EBI-495538;
P50222:MEOX2; NbExp=5; IntAct=EBI-742503, EBI-748397;
Q9BY11:PACSIN1; NbExp=7; IntAct=EBI-742503, EBI-721769;
P54274:TERF1; NbExp=2; IntAct=EBI-742503, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane;
Peripheral membrane protein; Cytoplasmic side. Early endosome.
Recycling endosome membrane. Cell projection, ruffle membrane;
Peripheral membrane protein; Cytoplasmic side. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Cell projection
{ECO:0000250}. Membrane, caveola. Note=Detected at the neck of
flask-shaped caveolae. Localization to tubular recycling endosomes
probably requires interaction with MICALL1 and EHD1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UNF0-1; Sequence=Displayed;
Name=2;
IsoId=Q9UNF0-2; Sequence=VSP_004517;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11082044, ECO:0000269|PubMed:11179684}.
-!- DOMAIN: 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.
{ECO:0000269|PubMed:19549836, ECO:0000269|PubMed:20188097,
ECO:0000269|PubMed:21610094, ECO:0000269|PubMed:23236520}.
-!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
(PKC). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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EMBL; AF128536; AAD41781.1; -; mRNA.
EMBL; AL136845; CAB66779.1; -; mRNA.
EMBL; CR456536; CAG30422.1; -; mRNA.
EMBL; AL022476; CAI20163.1; -; Genomic_DNA.
EMBL; AL049758; CAI20163.1; JOINED; Genomic_DNA.
EMBL; AL049758; CAI20948.1; -; Genomic_DNA.
EMBL; AL022476; CAI20948.1; JOINED; Genomic_DNA.
EMBL; BC008037; AAH08037.1; -; mRNA.
EMBL; AL389984; CAB97538.1; -; mRNA.
CCDS; CCDS43023.1; -. [Q9UNF0-1]
CCDS; CCDS54536.1; -. [Q9UNF0-2]
RefSeq; NP_001171899.1; NM_001184970.1. [Q9UNF0-1]
RefSeq; NP_001171900.1; NM_001184971.1. [Q9UNF0-2]
RefSeq; NP_009160.2; NM_007229.3. [Q9UNF0-1]
RefSeq; XP_005261376.1; XM_005261319.3. [Q9UNF0-2]
RefSeq; XP_016884053.1; XM_017028564.1. [Q9UNF0-1]
UniGene; Hs.162877; -.
PDB; 3ABH; X-ray; 2.00 A; A/B=1-305.
PDB; 3ACO; X-ray; 2.70 A; A/B=1-343.
PDB; 3HAJ; X-ray; 2.78 A; A/B=1-486.
PDB; 3Q0K; X-ray; 2.60 A; A/B/C/D=16-304.
PDBsum; 3ABH; -.
PDBsum; 3ACO; -.
PDBsum; 3HAJ; -.
PDBsum; 3Q0K; -.
ProteinModelPortal; Q9UNF0; -.
SMR; Q9UNF0; -.
BioGrid; 116413; 50.
IntAct; Q9UNF0; 18.
MINT; MINT-5005738; -.
STRING; 9606.ENSP00000263246; -.
iPTMnet; Q9UNF0; -.
PhosphoSitePlus; Q9UNF0; -.
BioMuta; PACSIN2; -.
DMDM; 22256968; -.
EPD; Q9UNF0; -.
PaxDb; Q9UNF0; -.
PeptideAtlas; Q9UNF0; -.
PRIDE; Q9UNF0; -.
DNASU; 11252; -.
Ensembl; ENST00000263246; ENSP00000263246; ENSG00000100266. [Q9UNF0-1]
Ensembl; ENST00000337959; ENSP00000338379; ENSG00000100266. [Q9UNF0-2]
Ensembl; ENST00000402229; ENSP00000385040; ENSG00000100266. [Q9UNF0-1]
Ensembl; ENST00000403744; ENSP00000385372; ENSG00000100266. [Q9UNF0-1]
Ensembl; ENST00000407585; ENSP00000385952; ENSG00000100266. [Q9UNF0-2]
GeneID; 11252; -.
KEGG; hsa:11252; -.
UCSC; uc003bdf.5; human. [Q9UNF0-1]
CTD; 11252; -.
DisGeNET; 11252; -.
GeneCards; PACSIN2; -.
HGNC; HGNC:8571; PACSIN2.
HPA; HPA049854; -.
HPA; HPA056520; -.
MIM; 604960; gene.
neXtProt; NX_Q9UNF0; -.
OpenTargets; ENSG00000100266; -.
PharmGKB; PA32897; -.
eggNOG; KOG2856; Eukaryota.
eggNOG; ENOG410XRX2; LUCA.
GeneTree; ENSGT00510000046376; -.
HOGENOM; HOG000007245; -.
HOVERGEN; HBG053486; -.
InParanoid; Q9UNF0; -.
KO; K20123; -.
OMA; CKGRMNG; -.
OrthoDB; EOG091G0AS9; -.
PhylomeDB; Q9UNF0; -.
TreeFam; TF313677; -.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
ChiTaRS; PACSIN2; human.
EvolutionaryTrace; Q9UNF0; -.
GeneWiki; PACSIN2; -.
GenomeRNAi; 11252; -.
PRO; PR:Q9UNF0; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100266; -.
ExpressionAtlas; Q9UNF0; baseline and differential.
Genevisible; Q9UNF0; HS.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
GO; GO:0070836; P:caveola assembly; IMP:UniProtKB.
GO; GO:0072584; P:caveolin-mediated endocytosis; IMP:UniProtKB.
GO; GO:0048858; P:cell projection morphogenesis; ISS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR028521; PACSIN2.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR23065:SF28; PTHR23065:SF28; 1.
Pfam; PF00611; FCH; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00055; FCH; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51741; F_BAR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome;
Lipid-binding; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; SH3 domain.
CHAIN 1 486 Protein kinase C and casein kinase
substrate in neurons protein 2.
/FTId=PRO_0000161795.
DOMAIN 11 282 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 426 486 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 25 274
MOTIF 362 364 NPF1.
MOTIF 405 407 NPF2.
MOTIF 417 419 NPF3.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WVE8}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WVE8}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 344 384 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|Ref.6}.
/FTId=VSP_004517.
VARIANT 175 175 N -> S (in dbSNP:rs35383004).
/FTId=VAR_053555.
VARIANT 294 294 M -> I (in dbSNP:rs2746984).
/FTId=VAR_013711.
VARIANT 324 324 V -> F (in dbSNP:rs1062913).
/FTId=VAR_013712.
CONFLICT 182 182 L -> F (in Ref. 1; AAD41781).
{ECO:0000305}.
CONFLICT 256 256 D -> N (in Ref. 1; AAD41781).
{ECO:0000305}.
CONFLICT 309 309 N -> I (in Ref. 1; AAD41781).
{ECO:0000305}.
CONFLICT 336 336 S -> F (in Ref. 1; AAD41781).
{ECO:0000305}.
CONFLICT 378 380 DDT -> EDI (in Ref. 1; AAD41781).
{ECO:0000305}.
TURN 21 24 {ECO:0000244|PDB:3ABH}.
HELIX 25 72 {ECO:0000244|PDB:3ABH}.
HELIX 77 106 {ECO:0000244|PDB:3ABH}.
HELIX 108 119 {ECO:0000244|PDB:3ABH}.
STRAND 126 128 {ECO:0000244|PDB:3ABH}.
HELIX 129 169 {ECO:0000244|PDB:3ABH}.
HELIX 172 177 {ECO:0000244|PDB:3ABH}.
HELIX 185 188 {ECO:0000244|PDB:3ABH}.
HELIX 189 191 {ECO:0000244|PDB:3ABH}.
TURN 192 195 {ECO:0000244|PDB:3ABH}.
HELIX 197 255 {ECO:0000244|PDB:3ABH}.
HELIX 257 259 {ECO:0000244|PDB:3ABH}.
HELIX 263 275 {ECO:0000244|PDB:3ABH}.
HELIX 279 290 {ECO:0000244|PDB:3ABH}.
SEQUENCE 486 AA; 55739 MW; 821DBEF65DAD1AA8 CRC64;
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR IEKAYAQQLT
EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV KASLMNDDFE KIKNWQKEAF
HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH AACKEEKLAI SREANSKADP
SLNPEQLKKL QDKIEKCKQD VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR
LRFFREVLLE VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ
FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN PAQSAQSQSS
YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD DESNNPFSST DANGDSNPFD
DDATSGTEVR VRALYDYEGQ EHDELSFKAG DELTKMEDED EQGWCKGRLD NGQVGLYPAN
YVEAIQ


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