EPN2_MOUSE
ID EPN2_MOUSE Reviewed; 595 AA.
AC Q8CHU3; O70447; Q5NCM4; Q8BZ85;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Epsin-2;
DE AltName: Full=EPS-15-interacting protein 2;
DE AltName: Full=Intersectin-EH-binding protein 2;
DE Short=Ibp2;
GN Name=Epn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-595 (ISOFORM 2), AND INTERACTION WITH
RP ITSN1.
RX PubMed=9813051; DOI=10.1074/jbc.273.47.31401;
RA Yamabhai M., Hoffman N.G., Hardison N.L., McPherson P.S., Castagnoli L.,
RA Cesareni G., Kay B.K.;
RT "Intersectin, a novel adaptor protein with two eps15 homology and five src
RT homology 3 domains.";
RL J. Biol. Chem. 273:31401-31407(1998).
RN [5]
RP PROTEIN SEQUENCE OF 77-86, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-170, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays a role in the formation of clathrin-coated
CC invaginations and endocytosis. {ECO:0000250}.
CC -!- SUBUNIT: Binds EPS15, AP-2 and clathrin (By similarity). Interacts with
CC UBQLN2 (By similarity). Interacts with ITSN1.
CC {ECO:0000250|UniProtKB:O95208, ECO:0000250|UniProtKB:Q9Z1Z3,
CC ECO:0000269|PubMed:9813051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In punctate
CC structures throughout the cell and particularly concentrated in the
CC region of the Golgi complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHU3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHU3-2; Sequence=VSP_009157;
CC -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding.
CC -!- DOMAIN: The DPW repeat domain is involved in AP-2 and clathrin binding.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC97476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK036331; BAC29387.1; -; mRNA.
DR EMBL; AL604029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039138; AAH39138.1; -; mRNA.
DR EMBL; AF057286; AAC97476.1; ALT_INIT; mRNA.
DR CCDS; CCDS24816.1; -. [Q8CHU3-1]
DR CCDS; CCDS56779.1; -. [Q8CHU3-2]
DR RefSeq; NP_001239118.1; NM_001252189.1. [Q8CHU3-2]
DR RefSeq; NP_034278.1; NM_010148.3. [Q8CHU3-1]
DR RefSeq; XP_017169742.1; XM_017314253.1.
DR AlphaFoldDB; Q8CHU3; -.
DR SMR; Q8CHU3; -.
DR BioGRID; 199486; 8.
DR ELM; Q8CHU3; -.
DR IntAct; Q8CHU3; 1.
DR MINT; Q8CHU3; -.
DR STRING; 10090.ENSMUSP00000001063; -.
DR iPTMnet; Q8CHU3; -.
DR PhosphoSitePlus; Q8CHU3; -.
DR jPOST; Q8CHU3; -.
DR MaxQB; Q8CHU3; -.
DR PeptideAtlas; Q8CHU3; -.
DR PRIDE; Q8CHU3; -.
DR ProteomicsDB; 275634; -. [Q8CHU3-1]
DR ProteomicsDB; 275635; -. [Q8CHU3-2]
DR Antibodypedia; 25881; 348 antibodies from 27 providers.
DR DNASU; 13855; -.
DR Ensembl; ENSMUST00000001063; ENSMUSP00000001063; ENSMUSG00000001036. [Q8CHU3-1]
DR Ensembl; ENSMUST00000108713; ENSMUSP00000104353; ENSMUSG00000001036. [Q8CHU3-2]
DR Ensembl; ENSMUST00000178202; ENSMUSP00000136553; ENSMUSG00000001036. [Q8CHU3-1]
DR GeneID; 13855; -.
DR KEGG; mmu:13855; -.
DR UCSC; uc007jhv.2; mouse. [Q8CHU3-1]
DR CTD; 22905; -.
DR MGI; MGI:1333766; Epn2.
DR VEuPathDB; HostDB:ENSMUSG00000001036; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000157239; -.
DR HOGENOM; CLU_012678_4_2_1; -.
DR InParanoid; Q8CHU3; -.
DR OrthoDB; 1263849at2759; -.
DR PhylomeDB; Q8CHU3; -.
DR TreeFam; TF313361; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13855; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Epn2; mouse.
DR PRO; PR:Q8CHU3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CHU3; protein.
DR Bgee; ENSMUSG00000001036; Expressed in animal zygote and 254 other tissues.
DR ExpressionAtlas; Q8CHU3; baseline and differential.
DR Genevisible; Q8CHU3; MM.
DR GO; GO:0030128; C:clathrin coat of endocytic vesicle; ISO:MGI.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; IGI:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IGI:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027319; Epsin-2_metazoa.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276:SF50; PTHR12276:SF50; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Endocytosis;
KW Lipid-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..595
FT /note="Epsin-2"
FT /id="PRO_0000074517"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 218..237
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 255..274
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 313..315
FT /note="1"
FT REPEAT 325..327
FT /note="2"
FT REPEAT 338..340
FT /note="3"
FT REPEAT 352..354
FT /note="4"
FT REPEAT 370..372
FT /note="5"
FT REPEAT 387..389
FT /note="6"
FT REPEAT 494..496
FT /note="1"
FT REPEAT 508..510
FT /note="2"
FT REPEAT 591..593
FT /note="3"
FT REGION 164..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..389
FT /note="6 X 3 AA repeats of [DE]-P-W"
FT REGION 423..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..593
FT /note="3 X 3 AA repeats of N-P-F"
FT COMPBIAS 164..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z3"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95208"
FT VAR_SEQ 237..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9813051"
FT /id="VSP_009157"
FT CONFLICT 75
FT /note="Y -> S (in Ref. 4; AAC97476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 63472 MW; 255DC7BC7E1B2D13 CRC64;
MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VAFSEIMSMV
WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG
INVREKSKQL VALLKDEERL KVERVQALKT KERMAQVATG VGSNQITFGR GSSQPNLSTS
YSEQEYGKAG GSPASYHGST SPRVSSELEQ ARPQTSGEEE LQLQLALAMS REVAEQSSES
VQTARGSKEE RLRRGDDLRL QMALEESRRD TVKVPKKKEA KACCKPGSHS QQTTLLDLMD
ALPSSGPVTQ KTEPWSAGAS ANQTNPWGGT VAPSNITDPW PSFGTKPAAS VDPWGVPTTA
STQSVPKNSD PWAASQQPAS NAGKTTDAWG AAKPSSASGS FELFSNFNGT VKDDFSEFDN
LRTSKKPAES GASVPPQDSR TTSPDLFESQ SLTSASSKPS SARKTPESFL GPNAALVNLD
SLVTKPAPPA QSLNPFLAPG AAAPAPVNPF QVNQPQPLTL NQLRGSPVLG SSASFGSGPG
VETVAPMTSV APHSSVGASG SSLTPLGPTA MNMVGSVGIP PSAAQSTGTT NPFLL
