ID EPN4_HUMAN Reviewed; 625 AA. AC Q14677; B7Z6F8; D3DQJ6; Q8NAF1; Q96E05; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Clathrin interactor 1; DE AltName: Full=Clathrin-interacting protein localized in the trans-Golgi region; DE Short=Clint; DE AltName: Full=Enthoprotin; DE AltName: Full=Epsin-4; DE AltName: Full=Epsin-related protein; DE Short=EpsinR; GN Name=CLINT1; Synonyms=ENTH, EPN4, EPNR, KIAA0171; 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 [GENOMIC DNA], PROTEIN SEQUENCE OF 14-27; 30-49; RP 110-129; 134-146; 157-171; 201-218; 248-274 AND 284-297 (ISOFORM 1), RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CLATHRIN; AP1G1 AND RP GGA2, AND SUBCELLULAR LOCATION. RX PubMed=12213833; DOI=10.1083/jcb.200205078; RA Wasiak S., Legendre-Guillemin V., Puertollano R., Blondeau F., Girard M., RA de Heuvel E., Boismenu D., Bell A.W., Bonifacino J.S., McPherson P.S.; RT "Enthoprotin: a novel clathrin-associated protein identified through RT subcellular proteomics."; RL J. Cell Biol. 158:855-862(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Hong W.; RT "KIAA0171 as a new member (epsin 4) of the epsin family."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Placenta, and Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, and 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 [8] RP FUNCTION, MUTAGENESIS OF 423-LEU--LEU-426, INTERACTION WITH CLATHRIN; AP1G1 RP AND AP-2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=12429846; DOI=10.1091/mbc.e02-03-0171; RA Kalthoff C., Groos S., Kohl R., Mahrhold S., Ungewickell E.J.; RT "Clint: a novel clathrin-binding ENTH-domain protein at the Golgi."; RL Mol. Biol. Cell 13:4060-4073(2002). RN [9] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-29; RP ASP-34; ASP-349; ASP-371 AND ASP-422, AND INTERACTION WITH AP1G1; AP-2 AND RP CLATHRIN. RX PubMed=12538641; DOI=10.1083/jcb.200208023; RA Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E., RA Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.; RT "EpsinR: an AP1/clathrin interacting protein involved in vesicle RT trafficking."; RL J. Cell Biol. 160:213-222(2003). RN [10] RP INTERACTION WITH AP1G1; AP1G2 AND GGA2. RX PubMed=14665628; DOI=10.1074/jbc.m311873200; RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.; RT "Definition of the consensus motif recognized by gamma-adaptin ear RT domains."; RL J. Biol. Chem. 279:8018-8028(2004). RN [11] RP POSSIBLE SUSCEPTIBILITY TO SCHIZOPHRENIA. RX PubMed=15793701; DOI=10.1086/430095; RA Pimm J., McQuillin A., Thirumalai S., Lawrence J., Quested D., Bass N., RA Lamb G., Moorey H., Datta S.R., Kalsi G., Badacsonyi A., Kelly K., RA Morgan J., Punukollu B., Curtis D., Gurling H.; RT "The Epsin 4 gene on chromosome 5q, which encodes the clathrin-associated RT protein enthoprotin, is involved in the genetic susceptibility to RT schizophrenia."; RL Am. J. Hum. Genet. 76:902-907(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, AND 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-299, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-173; SER-210; RP SER-245; SER-299; THR-308; SER-312 AND SER-624, AND IDENTIFICATION BY MASS RP 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-299, AND 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-165. RA Lunin V.V., Munger C., Mazzoni I., Wagner J., Cygler M.; RT "The crystal structure of human enthoprotin N-terminal domain."; RL Submitted (SEP-2004) to the PDB data bank. RN [25] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-166 IN COMPLEX WITH VTI1B, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-41; GLU-46; PHE-52; RP 53-MET-TYR-54; GLU-95; ARG-96; ARG-146; LYS-153 AND TYR-159. RX PubMed=18033301; DOI=10.1038/nature06353; RA Miller S.E., Collins B.M., McCoy A.J., Robinson M.S., Owen D.J.; RT "A SNARE-adaptor interaction is a new mode of cargo recognition in RT clathrin-coated vesicles."; RL Nature 450:570-574(2007). CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- CC bisphosphate (PtdIns(4,5)P2). May have a role in transport via CC clathrin-coated vesicles from the trans-Golgi network to endosomes. CC Stimulates clathrin assembly. {ECO:0000269|PubMed:12429846, CC ECO:0000269|PubMed:12538641}. CC -!- SUBUNIT: Binds clathrin heavy chain and AP-2 (PubMed:12213833, CC PubMed:12429846, PubMed:12538641). Interacts with VTI1B CC (PubMed:18033301). Interacts with GGA2 (via GAE domain) CC (PubMed:12213833, PubMed:14665628). Interacts with AP1G1 (via GAE CC domain) (PubMed:12213833, PubMed:12429846, PubMed:12538641, CC PubMed:14665628). Interacts with AP1G2 (via GAE domain) CC (PubMed:14665628). {ECO:0000269|PubMed:12213833, CC ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641, CC ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:18033301}. CC -!- INTERACTION: CC Q14677; Q9NSY1: BMP2K; NbExp=6; IntAct=EBI-1171113, EBI-1383367; CC Q14677; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-1171113, EBI-746969; CC Q14677; Q8WTR4-3: GDPD5; NbExp=3; IntAct=EBI-1171113, EBI-16430931; CC Q14677; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1171113, EBI-10975473; CC Q14677; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-1171113, EBI-373144; CC Q14677; O76024: WFS1; NbExp=3; IntAct=EBI-1171113, EBI-720609; CC Q14677; P22892: Ap1g1; Xeno; NbExp=10; IntAct=EBI-1171113, EBI-1040262; CC Q14677; O88384: Vti1b; Xeno; NbExp=6; IntAct=EBI-1171113, EBI-775853; CC Q14677; PRO_0000037943 [P29991]; Xeno; NbExp=2; IntAct=EBI-1171113, EBI-9118921; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. CC Membrane; Peripheral membrane protein. Cytoplasmic vesicle, clathrin- CC coated vesicle. Note=Found throughout the cell, with the exception of CC the cell surface. Concentrated in the perinuclear region and associated CC with clathrin-coated vesicles close to the trans-Golgi network. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q14677-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14677-2; Sequence=VSP_009160, VSP_009161; CC Name=3; CC IsoId=Q14677-3; Sequence=VSP_043302; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low to intermediate CC levels. {ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12538641}. CC -!- POLYMORPHISM: Genetic variations in CLINT1 may contribute to CC susceptibility to schizophrenia (SCZD1) and psychotic disorders in some CC populations. {ECO:0000269|PubMed:15793701}. CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA11488.2; Type=Erroneous initiation; Evidence={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; BK000414; DAA00062.1; -; Genomic_DNA. DR EMBL; AF434813; AAL30768.1; -; mRNA. DR EMBL; D79993; BAA11488.2; ALT_INIT; mRNA. DR EMBL; AK092765; BAC03971.1; -; mRNA. DR EMBL; AK300257; BAH13244.1; -; mRNA. DR EMBL; AC011394; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026407; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61585.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61588.1; -; Genomic_DNA. DR EMBL; BC004467; AAH04467.1; -; mRNA. DR EMBL; BC013091; AAH13091.1; -; mRNA. DR CCDS; CCDS47330.1; -. [Q14677-1] DR CCDS; CCDS56388.1; -. [Q14677-2] DR CCDS; CCDS56389.1; -. [Q14677-3] DR RefSeq; NP_001182484.1; NM_001195555.1. [Q14677-3] DR RefSeq; NP_001182485.1; NM_001195556.1. [Q14677-2] DR RefSeq; NP_055481.1; NM_014666.3. [Q14677-1] DR PDB; 1XGW; X-ray; 1.90 A; A=1-165. DR PDB; 2QY7; X-ray; 2.00 A; A/B/C=20-166. DR PDB; 2V8S; X-ray; 2.22 A; E=20-166. DR PDBsum; 1XGW; -. DR PDBsum; 2QY7; -. DR PDBsum; 2V8S; -. DR AlphaFoldDB; Q14677; -. DR SMR; Q14677; -. DR BioGRID; 115038; 217. DR DIP; DIP-45604N; -. DR ELM; Q14677; -. DR IntAct; Q14677; 136. DR MINT; Q14677; -. DR STRING; 9606.ENSP00000429824; -. DR TCDB; 8.A.137.1.1; the clathrin (clathrin) family. DR GlyCosmos; Q14677; 6 sites, 1 glycan. DR GlyGen; Q14677; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q14677; -. DR MetOSite; Q14677; -. DR PhosphoSitePlus; Q14677; -. DR BioMuta; CLINT1; -. DR DMDM; 41016993; -. DR EPD; Q14677; -. DR jPOST; Q14677; -. DR MassIVE; Q14677; -. DR MaxQB; Q14677; -. DR PaxDb; 9606-ENSP00000429824; -. DR PeptideAtlas; Q14677; -. DR ProteomicsDB; 60109; -. [Q14677-1] DR ProteomicsDB; 60110; -. [Q14677-2] DR ProteomicsDB; 60111; -. [Q14677-3] DR Pumba; Q14677; -. DR Antibodypedia; 28472; 315 antibodies from 29 providers. DR DNASU; 9685; -. DR Ensembl; ENST00000411809.7; ENSP00000388340.2; ENSG00000113282.14. [Q14677-1] DR Ensembl; ENST00000523094.5; ENSP00000429345.1; ENSG00000113282.14. [Q14677-2] DR Ensembl; ENST00000523908.5; ENSP00000429824.1; ENSG00000113282.14. [Q14677-3] DR Ensembl; ENST00000530742.5; ENSP00000433419.1; ENSG00000113282.14. [Q14677-2] DR GeneID; 9685; -. DR KEGG; hsa:9685; -. DR MANE-Select; ENST00000411809.7; ENSP00000388340.2; NM_014666.4; NP_055481.1. DR UCSC; uc003lxi.3; human. [Q14677-1] DR AGR; HGNC:23186; -. DR CTD; 9685; -. DR DisGeNET; 9685; -. DR GeneCards; CLINT1; -. DR HGNC; HGNC:23186; CLINT1. DR HPA; ENSG00000113282; Low tissue specificity. DR MIM; 607265; gene. DR neXtProt; NX_Q14677; -. DR OpenTargets; ENSG00000113282; -. DR PharmGKB; PA145149115; -. DR VEuPathDB; HostDB:ENSG00000113282; -. DR eggNOG; KOG2057; Eukaryota. DR GeneTree; ENSGT00940000155650; -. DR HOGENOM; CLU_032178_1_0_1; -. DR InParanoid; Q14677; -. DR OMA; QTSMAQP; -. DR OrthoDB; 1532at2759; -. DR PhylomeDB; Q14677; -. DR TreeFam; TF313361; -. DR PathwayCommons; Q14677; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR SignaLink; Q14677; -. DR BioGRID-ORCS; 9685; 21 hits in 1159 CRISPR screens. DR ChiTaRS; CLINT1; human. DR EvolutionaryTrace; Q14677; -. DR GeneWiki; CLINT1; -. DR GenomeRNAi; 9685; -. DR Pharos; Q14677; Tbio. DR PRO; PR:Q14677; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q14677; Protein. DR Bgee; ENSG00000113282; Expressed in palpebral conjunctiva and 212 other cell types or tissues. DR ExpressionAtlas; Q14677; baseline and differential. DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0030276; F:clathrin binding; IPI:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl. DR GO; GO:0006897; P:endocytosis; IBA:GO_Central. DR CDD; cd16989; ENTH_EpsinR; 1. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR PANTHER; PTHR12276:SF126; CLATHRIN INTERACTOR 1; 1. DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1. DR Pfam; PF01417; ENTH; 1. DR SMART; SM00273; ENTH; 1. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR PROSITE; PS50942; ENTH; 1. DR Genevisible; Q14677; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle; KW Direct protein sequencing; Endocytosis; Lipid-binding; Membrane; KW Phosphoprotein; Reference proteome. FT CHAIN 1..625 FT /note="Clathrin interactor 1" FT /id="PRO_0000074521" FT DOMAIN 16..149 FT /note="ENTH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243" FT REGION 52..54 FT /note="Interaction with VTI1B" FT /evidence="ECO:0000269|PubMed:18033301, FT ECO:0007744|PDB:2V8S" FT REGION 94..96 FT /note="Interaction with VTI1B" FT /evidence="ECO:0000269|PubMed:18033301, FT ECO:0007744|PDB:2V8S" FT REGION 142..153 FT /note="Interaction with VTI1B" FT /evidence="ECO:0000269|PubMed:18033301, FT ECO:0007744|PDB:2V8S" FT REGION 219..331 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 340..352 FT /note="Interaction with AP1G1, AP1G2 and GGA2" FT /evidence="ECO:0000269|PubMed:14665628" FT REGION 368..380 FT /note="Interaction with AP1G1 and AP1G2" FT /evidence="ECO:0000269|PubMed:14665628" FT COMPBIAS 219..260 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 261..278 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 298..331 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 29 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 67 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 163 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99KN9" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99KN9" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 308 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 624 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..18 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009160" FT VAR_SEQ 459 FT /note="S -> SQPLQNVSTVLQKPNPLYN (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043302" FT VAR_SEQ 460 FT /note="Q -> QPLQNVSTVLQKPNPLYNQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009161" FT MUTAGEN 29 FT /note="R->L: Reduces lipid binding. Abolishes lipid FT binding; when associated with G-34." FT /evidence="ECO:0000269|PubMed:12538641" FT MUTAGEN 34 FT /note="D->G: Abolishes lipid binding; when associated with FT L-29." FT /evidence="ECO:0000269|PubMed:12538641" FT MUTAGEN 41 FT /note="G->S: Normal binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 46 FT /note="E->W: Normal binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 52 FT /note="F->D: Abolished binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 53..54 FT /note="MY->DD: Abolished binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 95 FT /note="E->W: Normal binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 96 FT /note="R->S: Abolished binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 146 FT /note="R->E: Abolished binding to VTI1B. Rescued binding to FT VTI1BR-23 mutant." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 153 FT /note="K->D: Normal binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 159 FT /note="Y->S: Normal binding to VTI1B." FT /evidence="ECO:0000269|PubMed:18033301" FT MUTAGEN 349 FT /note="D->R: Decreases AP-1 and AP-2 binding." FT /evidence="ECO:0000269|PubMed:12538641" FT MUTAGEN 371 FT /note="D->R: Slightly decreases AP-1 binding." FT /evidence="ECO:0000269|PubMed:12538641" FT MUTAGEN 422 FT /note="D->R: Strongly decreases clathrin binding." FT /evidence="ECO:0000269|PubMed:12538641" FT MUTAGEN 423..426 FT /note="LFDL->AFAA: Strongly reduces clathrin binding." FT /evidence="ECO:0000269|PubMed:12429846" FT CONFLICT 476 FT /note="T -> A (in Ref. 4; BAC03971)" FT /evidence="ECO:0000305" FT HELIX 23..31 FT /evidence="ECO:0007829|PDB:1XGW" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:2QY7" FT HELIX 41..50 FT /evidence="ECO:0007829|PDB:1XGW" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 57..69 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 76..92 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 95..103 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 105..109 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 125..139 FT /evidence="ECO:0007829|PDB:1XGW" FT HELIX 142..151 FT /evidence="ECO:0007829|PDB:1XGW" SQ SEQUENCE 625 AA; 68259 MW; 6C8C6689861E9F0D CRC64; MLNMWKVREL VDKATNVVMN YSEIESKVRE ATNDDPWGPS GQLMGEIAKA TFMYEQFPEL MNMLWSRMLK DNKKNWRRVY KSLLLLAYLI RNGSERVVTS AREHIYDLRS LENYHFVDEH GKDQGINIRQ KVKELVEFAQ DDDRLREERK KAKKNKDKYV GVSSDSVGGF RYSERYDPEP KSKWDEEWDK NKSAFPFSDK LGELSDKIGS TIDDTISKFR RKDREDSPER CSDSDEEKKA RRGRSPKGEF KDEEETVTTK HIHITQATET TTTRHKRTAN PSKTIDLGAA AHYTGDKASP DQNASTHTPQ SSVKTSVPSS KSSGDLVDLF DGTSQSTGGS ADLFGGFADF GSAAASGSFP SQVTATSGNG DFGDWSAFNQ APSGPVASSG EFFGSASQPA VELVSGSQSA LGPPPAASNS SDLFDLMGSS QATMTSSQSM NFSMMSTNTV GLGLPMSRSQ NTDMVQKSVS KTLPSTWSDP SVNISLDNLL PGMQPSKPQQ PSLNTMIQQQ NMQQPMNVMT QSFGAVNLSS PSNMLPVRPQ TNALIGGPMP MSMPNVMTGT MGMAPLGNTP MMNQSMMGMN MNIGMSAAGM GLTGTMGMGM PNIAMTSGTV QPKQDAFANF ANFSK //