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 27-MAR-2024, entry version 199. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 179. DR IntAct; Q9UNF0; 58. 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 SwissPalm; 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; 9606-ENSP00000263246; -. DR PeptideAtlas; Q9UNF0; -. DR ProteomicsDB; 85284; -. [Q9UNF0-1] DR ProteomicsDB; 85285; -. [Q9UNF0-2] DR Pumba; Q9UNF0; -. DR ABCD; Q9UNF0; 1 sequenced antibody. DR Antibodypedia; 34964; 265 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 AGR; HGNC:8571; -. 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; FEEWCAD; -. DR OrthoDB; 9421at2759; -. DR PhylomeDB; Q9UNF0; -. DR TreeFam; TF313677; -. DR PathwayCommons; Q9UNF0; -. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; Q9UNF0; -. DR SIGNOR; Q9UNF0; -. DR BioGRID-ORCS; 11252; 11 hits in 1153 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 205 other cell types or tissues. DR ExpressionAtlas; Q9UNF0; baseline and differential. DR GO; GO:0005901; C:caveola; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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: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; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR037453; PACSIN2_F-BAR. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR23065:SF14; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9UNF0; HS. 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 HCVNS5A." FT /evidence="ECO:0000269|PubMed:31801866" FT MUTAGEN 313 FT /note="S->E: Decreased protein interaction with HCVNS5A." 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 //