EPN4_HUMAN
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 03-AUG-2022, entry version 201.
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; P63010: AP2B1; NbExp=2; IntAct=EBI-1171113, EBI-432924;
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 -!- 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};
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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; 162.
DR DIP; DIP-45604N; -.
DR ELM; Q14677; -.
DR IntAct; Q14677; 121.
DR MINT; Q14677; -.
DR STRING; 9606.ENSP00000429824; -.
DR TCDB; 8.A.137.1.1; the clathrin (clathrin) family.
DR GlyGen; Q14677; 6 sites, 1 O-linked glycan (6 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; Q14677; -.
DR PeptideAtlas; Q14677; -.
DR PRIDE; Q14677; -.
DR ProteomicsDB; 60109; -. [Q14677-1]
DR ProteomicsDB; 60110; -. [Q14677-2]
DR ProteomicsDB; 60111; -. [Q14677-3]
DR Antibodypedia; 28472; 276 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 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; AHYTGEK; -.
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; 18 hits in 1080 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 210 other tissues.
DR ExpressionAtlas; Q14677; baseline and differential.
DR Genevisible; Q14677; HS.
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:0006897; P:endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR030544; CLINT1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR12276:SF83; PTHR12276:SF83; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
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 VTI1B R-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
