PACN2_HUMAN
ID PACN2_HUMAN Reviewed; 486 AA.
AC Q9UNF0; O95921; Q96HV9; Q9H0D3; Q9NPN1; Q9Y4V2;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
DE AltName: Full=Syndapin-2;
DE AltName: Full=Syndapin-II;
DE Short=SdpII;
GN Name=PACSIN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Retina;
RX PubMed=10431838; DOI=10.1016/s0014-5793(99)00830-3;
RA Ritter B., Modregger J., Paulsson M., Plomann M.;
RT "PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter
RT proteins.";
RL FEBS Lett. 454:356-362(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-486 (ISOFORM 2).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11082044; DOI=10.1242/jcs.113.24.4511;
RA Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT endocytosis.";
RL J. Cell Sci. 113:4511-4521(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11179684; DOI=10.1016/s0378-1119(00)00531-x;
RA Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.;
RT "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-
RT syndapin-FAP52 gene family.";
RL Gene 262:199-205(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC1.
RX PubMed=21693584; DOI=10.1242/jcs.080630;
RA de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J.,
RA Deelder A.M., Plomann M., Hordijk P.L.;
RT "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell
RT spreading and migration.";
RL J. Cell Sci. 124:2375-2388(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23129763; DOI=10.1074/jbc.m112.391078;
RA de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.;
RT "The F-BAR protein PACSIN2 regulates epidermal growth factor receptor
RT internalization.";
RL J. Biol. Chem. 287:43438-43453(2012).
RN [15]
RP FUNCTION, AND DOMAIN.
RX PubMed=23236520; DOI=10.1371/journal.pone.0051628;
RA Goh S.L., Wang Q., Byrnes L.J., Sondermann H.;
RT "Versatile membrane deformation potential of activated pacsin.";
RL PLoS ONE 7:E51628-E51628(2012).
RN [16]
RP INTERACTION WITH EHD2, AND SUBCELLULAR LOCATION.
RX PubMed=22323287; DOI=10.1091/mbc.e11-09-0787;
RA Moren B., Shah C., Howes M.T., Schieber N.L., McMahon H.T., Parton R.G.,
RA Daumke O., Lundmark R.;
RT "EHD2 regulates caveolar dynamics via ATP-driven targeting and
RT oligomerization.";
RL Mol. Biol. Cell 23:1316-1329(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-446, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH EHD1; EHD3 AND MICALL1.
RX PubMed=23596323; DOI=10.1091/mbc.e13-01-0026;
RA Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.;
RT "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular
RT recycling endosome biogenesis.";
RL Mol. Biol. Cell 24:1776-1790(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH UBIQUITINATED HIV-1 GAG
RP (MICROBIAL INFECTION), DOMAIN (MICROBIAL INFECTION), AND INTERACTION WITH
RP ROUS SARCOMA VIRUS P2B.
RX PubMed=29891700; DOI=10.1073/pnas.1801849115;
RA Popov S., Popova E., Inoue M., Wu Y., Goettlinger H.;
RT "HIV-1 gag recruits PACSIN2 to promote virus spreading.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:7093-7098(2018).
RN [21]
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=31242077; DOI=10.1091/mbc.e19-04-0197;
RA Sanderlin A.G., Vondrak C., Scricco A.J., Fedrigo I., Ahyong V.,
RA Lamason R.L.;
RT "RNAi screen reveals a role for PACSIN2 and caveolins during bacterial
RT cell-to-cell spread.";
RL Mol. Biol. Cell 30:2124-2133(2019).
RN [22]
RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION),
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF SER-313.
RX PubMed=31801866; DOI=10.1128/jvi.01531-19;
RA Nguyen L.P., Tran S.C., Suetsugu S., Lim Y.S., Hwang S.B.;
RT "PACSIN2 Interacts with Nonstructural Protein 5A and Regulates Hepatitis C
RT Virus Assembly.";
RL J. Virol. 94:0-0(2020).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS), AND DOMAIN.
RX PubMed=19549836; DOI=10.1073/pnas.0902974106;
RA Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L.,
RA Rajashankar K.R., Sondermann H.;
RT "Molecular mechanism of membrane constriction and tubulation mediated by
RT the F-BAR protein Pacsin/Syndapin.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-305, AND DOMAIN.
RX PubMed=20188097; DOI=10.1016/j.febslet.2010.02.058;
RA Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T.,
RA Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.;
RT "Mapping of the basic amino-acid residues responsible for tubulation and
RT cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.";
RL FEBS Lett. 584:1111-1118(2010).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 16-304.
RX PubMed=22573331; DOI=10.1074/jbc.m112.358960;
RA Bai X., Meng G., Luo M., Zheng X.;
RT "Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating
RT diameters of tubules.";
RL J. Biol. Chem. 287:22387-22396(2012).
CC -!- FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By
CC similarity). Lipid-binding protein that is able to promote the
CC tubulation of the phosphatidic acid-containing membranes it
CC preferentially binds. Plays a role in intracellular vesicle-mediated
CC transport. Involved in the endocytosis of cell-surface receptors like
CC the EGF receptor, contributing to its internalization in the absence of
CC EGF stimulus. {ECO:0000250|UniProtKB:Q9WVE8,
CC ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23129763,
CC ECO:0000269|PubMed:23236520, ECO:0000269|PubMed:23596323}.
CC -!- FUNCTION: (Microbial infection) Specifically enhances the efficiency of
CC HIV-1 virion spread by cell-to-cell transfer (PubMed:29891700). Also
CC promotes the protrusion engulfment during cell-to-cell spread of
CC bacterial pathogens like Listeria monocytogenes (PubMed:31242077).
CC Involved in lipid droplet formation, which is important for HCV virion
CC assembly (PubMed:31801866). {ECO:0000269|PubMed:29891700,
CC ECO:0000269|PubMed:31242077, ECO:0000269|PubMed:31801866}.
CC -!- SUBUNIT: Homodimer (By similarity). May form heterooligomers with other
CC PACSINs (By similarity). Interacts (via NPF motifs) with EHD1 (via EH
CC domain) (PubMed:23596323). Interacts (via NPF motifs) with EHD2 (via EH
CC domain); this interaction probably stabilizes the caveolae
CC (PubMed:22323287). Interacts with EHD3 (PubMed:23596323). Interacts
CC (via the SH3 domain) with MICALL1 (PubMed:23596323). Interacts with
CC RAC1 (PubMed:21693584). Interacts (via SH3 domain) with DNM1, SYN1,
CC SYNJ1 and WASL (By similarity). Interacts (via F-BAR domain) with CAV1
CC (By similarity). Interacts with TRPV4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QY17, ECO:0000250|UniProtKB:Q9WVE8,
CC ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:22323287,
CC ECO:0000269|PubMed:23596323}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ubiquitinated HIV-1 gag
CC (via p6-gag domain); this interaction allows PACSIN2 recruitment to
CC viral assembly sites and its subsequent incorporation into virions.
CC {ECO:0000269|PubMed:29891700}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via F-BAR domain) with Rous
CC sarcoma virus p2B; this interaction allows PACSIN2 recruitment to viral
CC assembly sites. {ECO:0000269|PubMed:29891700}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with
CC Hepatatis C virus (HCV) non-structural protein 5A (via N-terminus);
CC this interaction attenuates protein kinase C alpha (PRKCA)-mediated
CC phosphorylation of PACSIN2 at Ser-313 by disrupting the interaction
CC between PACSIN2 and PRKCA. {ECO:0000269|PubMed:31801866}.
CC -!- INTERACTION:
CC Q9UNF0; O14672: ADAM10; NbExp=2; IntAct=EBI-742503, EBI-1536151;
CC Q9UNF0; O75128: COBL; NbExp=3; IntAct=EBI-742503, EBI-3446582;
CC Q9UNF0; P50570: DNM2; NbExp=4; IntAct=EBI-742503, EBI-346547;
CC Q9UNF0; P48023: FASLG; NbExp=4; IntAct=EBI-742503, EBI-495538;
CC Q9UNF0; O15499: GSC2; NbExp=3; IntAct=EBI-742503, EBI-19954058;
CC Q9UNF0; P50222: MEOX2; NbExp=3; IntAct=EBI-742503, EBI-748397;
CC Q9UNF0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-742503, EBI-16439278;
CC Q9UNF0; Q9BY11: PACSIN1; NbExp=10; IntAct=EBI-742503, EBI-721769;
CC Q9UNF0; Q9UNF0: PACSIN2; NbExp=7; IntAct=EBI-742503, EBI-742503;
CC Q9UNF0; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-742503, EBI-77926;
CC Q9UNF0; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-742503, EBI-10302990;
CC Q9UNF0; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-742503, EBI-9091816;
CC Q9UNF0; P54274: TERF1; NbExp=2; IntAct=EBI-742503, EBI-710997;
CC Q9UNF0; O00401: WASL; NbExp=3; IntAct=EBI-742503, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Early endosome. Recycling endosome membrane.
CC Cell projection, ruffle membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cell projection {ECO:0000269|PubMed:31242077}.
CC Membrane, caveola {ECO:0000269|PubMed:22323287}. Note=Detected at the
CC neck of flask-shaped caveolae. Localization to tubular recycling
CC endosomes probably requires interaction with MICALL1 and EHD1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNF0-2; Sequence=VSP_004517;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11082044,
CC ECO:0000269|PubMed:11179684}.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation (PubMed:19549836). Autoinhibition of
CC these functions is mediated by an interaction between the SH3 and F-BAR
CC domains (PubMed:20188097, PubMed:23236520). The F-Bar domain also
CC mediates the binding to the cell actin cytoskeleton through the
CC interaction with CAV-1 (By similarity). {ECO:0000250|UniProtKB:Q9WVE8,
CC ECO:0000269|PubMed:19549836, ECO:0000269|PubMed:20188097,
CC ECO:0000269|PubMed:23236520}.
CC -!- DOMAIN: (Microbial infection) The SH3 domain is required for the cell-
CC to-cell spreading of HIV-1 virions. {ECO:0000269|PubMed:29891700}.
CC -!- PTM: Phosphorylated by casein kinase 2 (CK2). Phosphorylation by PKC
CC probably decreases the membrane binding and tubulation capacities of
CC PACSIN2, thereby modulating the lifetime of caveolae (By similarity).
CC {ECO:0000250|UniProtKB:Q9WVE8}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; AF128536; AAD41781.1; -; mRNA.
DR EMBL; AL136845; CAB66779.1; -; mRNA.
DR EMBL; CR456536; CAG30422.1; -; mRNA.
DR EMBL; AL022476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008037; AAH08037.1; -; mRNA.
DR EMBL; AL389984; CAB97538.1; -; mRNA.
DR CCDS; CCDS43023.1; -. [Q9UNF0-1]
DR CCDS; CCDS54536.1; -. [Q9UNF0-2]
DR RefSeq; NP_001171899.1; NM_001184970.1. [Q9UNF0-1]
DR RefSeq; NP_001171900.1; NM_001184971.1. [Q9UNF0-2]
DR RefSeq; NP_009160.2; NM_007229.3. [Q9UNF0-1]
DR RefSeq; XP_005261376.1; XM_005261319.3.
DR RefSeq; XP_016884053.1; XM_017028564.1.
DR PDB; 3ABH; X-ray; 2.00 A; A/B=1-305.
DR PDB; 3ACO; X-ray; 2.70 A; A/B=1-343.
DR PDB; 3HAJ; X-ray; 2.78 A; A/B=1-486.
DR PDB; 3Q0K; X-ray; 2.60 A; A/B/C/D=16-304.
DR PDBsum; 3ABH; -.
DR PDBsum; 3ACO; -.
DR PDBsum; 3HAJ; -.
DR PDBsum; 3Q0K; -.
DR AlphaFoldDB; Q9UNF0; -.
DR SMR; Q9UNF0; -.
DR BioGRID; 116413; 140.
DR IntAct; Q9UNF0; 44.
DR MINT; Q9UNF0; -.
DR STRING; 9606.ENSP00000263246; -.
DR GlyGen; Q9UNF0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UNF0; -.
DR MetOSite; Q9UNF0; -.
DR PhosphoSitePlus; Q9UNF0; -.
DR BioMuta; PACSIN2; -.
DR DMDM; 22256968; -.
DR CPTAC; CPTAC-1627; -.
DR EPD; Q9UNF0; -.
DR jPOST; Q9UNF0; -.
DR MassIVE; Q9UNF0; -.
DR MaxQB; Q9UNF0; -.
DR PaxDb; Q9UNF0; -.
DR PeptideAtlas; Q9UNF0; -.
DR PRIDE; Q9UNF0; -.
DR ProteomicsDB; 85284; -. [Q9UNF0-1]
DR ProteomicsDB; 85285; -. [Q9UNF0-2]
DR ABCD; Q9UNF0; 1 sequenced antibody.
DR Antibodypedia; 34964; 232 antibodies from 31 providers.
DR DNASU; 11252; -.
DR Ensembl; ENST00000263246.8; ENSP00000263246.3; ENSG00000100266.19. [Q9UNF0-1]
DR Ensembl; ENST00000337959.8; ENSP00000338379.4; ENSG00000100266.19. [Q9UNF0-2]
DR Ensembl; ENST00000402229.5; ENSP00000385040.1; ENSG00000100266.19. [Q9UNF0-1]
DR Ensembl; ENST00000403744.7; ENSP00000385372.3; ENSG00000100266.19. [Q9UNF0-1]
DR Ensembl; ENST00000407585.5; ENSP00000385952.1; ENSG00000100266.19. [Q9UNF0-2]
DR GeneID; 11252; -.
DR KEGG; hsa:11252; -.
DR MANE-Select; ENST00000263246.8; ENSP00000263246.3; NM_001184970.3; NP_001171899.1.
DR UCSC; uc003bdf.5; human. [Q9UNF0-1]
DR CTD; 11252; -.
DR DisGeNET; 11252; -.
DR GeneCards; PACSIN2; -.
DR HGNC; HGNC:8571; PACSIN2.
DR HPA; ENSG00000100266; Low tissue specificity.
DR MIM; 604960; gene.
DR neXtProt; NX_Q9UNF0; -.
DR OpenTargets; ENSG00000100266; -.
DR PharmGKB; PA32897; -.
DR VEuPathDB; HostDB:ENSG00000100266; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_0_0_1; -.
DR InParanoid; Q9UNF0; -.
DR OMA; ECLANIH; -.
DR PhylomeDB; Q9UNF0; -.
DR TreeFam; TF313677; -.
DR PathwayCommons; Q9UNF0; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9UNF0; -.
DR BioGRID-ORCS; 11252; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; PACSIN2; human.
DR EvolutionaryTrace; Q9UNF0; -.
DR GeneWiki; PACSIN2; -.
DR GenomeRNAi; 11252; -.
DR Pharos; Q9UNF0; Tbio.
DR PRO; PR:Q9UNF0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UNF0; protein.
DR Bgee; ENSG00000100266; Expressed in parotid gland and 203 other tissues.
DR ExpressionAtlas; Q9UNF0; baseline and differential.
DR Genevisible; Q9UNF0; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0070836; P:caveola assembly; IMP:UniProtKB.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0048858; P:cell projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR CDD; cd07679; F-BAR_PACSIN2; 1.
DR CDD; cd11998; SH3_PACSIN1-2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
DR InterPro; IPR028521; PACSIN2.
DR InterPro; IPR037453; PACSIN2_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF14; PTHR23065:SF14; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..486
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 2"
FT /id="PRO_0000161795"
FT DOMAIN 11..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 426..486
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..362
FT /note="(Microbial infection) Interaction with HCV NS5A"
FT /evidence="ECO:0000269|PubMed:31801866"
FT REGION 314..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..274
FT MOTIF 362..364
FT /note="NPF1"
FT MOTIF 405..407
FT /note="NPF2"
FT MOTIF 417..419
FT /note="NPF3"
FT COMPBIAS 324..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 344..384
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.6"
FT /id="VSP_004517"
FT VARIANT 175
FT /note="N -> S (in dbSNP:rs35383004)"
FT /id="VAR_053555"
FT VARIANT 294
FT /note="M -> I (in dbSNP:rs2746984)"
FT /id="VAR_013711"
FT VARIANT 324
FT /note="V -> F (in dbSNP:rs1062913)"
FT /id="VAR_013712"
FT MUTAGEN 313
FT /note="S->A: Increased protein interaction with HCV NS5A."
FT /evidence="ECO:0000269|PubMed:31801866"
FT MUTAGEN 313
FT /note="S->E: Decreased protein interaction with HCV NS5A."
FT /evidence="ECO:0000269|PubMed:31801866"
FT CONFLICT 182
FT /note="L -> F (in Ref. 1; AAD41781)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="D -> N (in Ref. 1; AAD41781)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="N -> I (in Ref. 1; AAD41781)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="S -> F (in Ref. 1; AAD41781)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..380
FT /note="DDT -> EDI (in Ref. 1; AAD41781)"
FT /evidence="ECO:0000305"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 25..72
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 77..106
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:3ABH"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 129..169
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3ABH"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 197..255
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:3ABH"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:3ABH"
SQ 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
