CLH1_HUMAN
ID CLH1_HUMAN Reviewed; 1675 AA.
AC Q00610; D3DU00; Q6N0A0; Q86TF2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Clathrin heavy chain 1 {ECO:0000303|PubMed:26822784, ECO:0000303|PubMed:29100083};
DE AltName: Full=Clathrin heavy chain on chromosome 17;
DE Short=CLH-17;
GN Name=CLTC {ECO:0000303|PubMed:26822784, ECO:0000303|PubMed:29100083,
GN ECO:0000312|HGNC:HGNC:2092}; Synonyms=CLH17, CLTCL2, KIAA0034;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=PNS, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-864 (ISOFORMS 1/2).
RC TISSUE=Colon;
RX PubMed=1765375; DOI=10.1016/0888-7543(91)90115-u;
RA Dodge G.R., Kovalszky I., McBride O.W., Yi H.F., Chu M.-L., Saitta B.,
RA Stokes D.G., Iozzo R.V.;
RT "Human clathrin heavy chain (CLTC): partial molecular cloning, expression,
RT and mapping of the gene to human chromosome 17q11-qter.";
RL Genomics 11:174-178(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 2-8; 64-78; 87-96; 164-205; 228-245; 270-278; 298-320;
RP 355-382; 469-481; 507-519; 572-610; 626-638; 799-806; 831-852; 855-865;
RP 882-903; 1011-1037; 1074-1101; 1123-1130; 1166-1179; 1183-1204; 1216-1245;
RP 1312-1326; 1398-1406; 1435-1453; 1482-1498; 1502-1508; 1510-1516 AND
RP 1610-1620, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Hepatoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Boldt K.,
RA von Kriegsheim A.F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP INTERACTION WITH HIP1.
RX PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
RA Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R., Goehler H.,
RA Gauss C., Sathasivam K., Bates G.P., Lehrach H., Wanker E.E.;
RT "The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-
RT binding protein involved in receptor-mediated endocytosis.";
RL Hum. Mol. Genet. 10:1807-1817(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP INTERACTION WITH ERBB2.
RX PubMed=16314522; DOI=10.1128/mcb.25.24.11005-11018.2005;
RA Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G.,
RA Wang S.C., Hung M.C.;
RT "Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell
RT surface receptor.";
RL Mol. Cell. Biol. 25:11005-11018(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15858577; DOI=10.1038/nature03502;
RA Royle S.J., Bright N.A., Lagnado L.;
RT "Clathrin is required for the function of the mitotic spindle.";
RL Nature 434:1152-1157(2005).
RN [12]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16968737; DOI=10.1242/jcs.03192;
RA Royle S.J., Lagnado L.;
RT "Trimerisation is important for the function of clathrin at the mitotic
RT spindle.";
RL J. Cell Sci. 119:4071-4078(2006).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [14]
RP INTERACTION WITH FKBP6.
RX PubMed=18529014; DOI=10.1021/bi8001506;
RA Jarczowski F., Fischer G., Edlich F.;
RT "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.";
RL Biochemistry 47:6946-6952(2008).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1494, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-634 AND TYR-1477, AND
RP IDENTIFICATION BY 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-856; LYS-1441 AND LYS-1501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP FUNCTION, AND INTERACTION WITH ATG16L1.
RX PubMed=20639872; DOI=10.1038/ncb2078;
RA Ravikumar B., Moreau K., Jahreiss L., Puri C., Rubinsztein D.C.;
RT "Plasma membrane contributes to the formation of pre-autophagosomal
RT structures.";
RL Nat. Cell Biol. 12:747-757(2010).
RN [21]
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 [22]
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 [23]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=21297582; DOI=10.1038/emboj.2011.15;
RA Booth D.G., Hood F.E., Prior I.A., Royle S.J.;
RT "A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-
RT microtubule bridging.";
RL EMBO J. 30:906-919(2011).
RN [24]
RP INTERACTION WITH RFTN1.
RX PubMed=21266579; DOI=10.1074/jbc.m110.185793;
RA Watanabe A., Tatematsu M., Saeki K., Shibata S., Shime H., Yoshimura A.,
RA Obuse C., Seya T., Matsumoto M.;
RT "Raftlin is involved in the nucleocapture complex to induce poly(I:C)-
RT mediated TLR3 activation.";
RL J. Biol. Chem. 286:10702-10711(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP INTERACTION WITH TACC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-65;
RP SER-67; THR-87; GLN-89; LYS-96; LYS-98 AND 480-LYS--VAL-484.
RX PubMed=23918938; DOI=10.1083/jcb.201211127;
RA Hood F.E., Williams S.J., Burgess S.G., Richards M.W., Roth D., Straube A.,
RA Pfuhl M., Bayliss R., Royle S.J.;
RT "Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly
RT and mitotic spindle binding.";
RL J. Cell Biol. 202:463-478(2013).
RN [28]
RP FUNCTION OF THE TACC3/CH-TOG/CLATHRIN COMPLEX.
RX PubMed=23532825; DOI=10.1242/jcs.124834;
RA Cheeseman L.P., Harry E.F., McAinsh A.D., Prior I.A., Royle S.J.;
RT "Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates
RT kinetochore fiber tension.";
RL J. Cell Sci. 126:2102-2113(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-394; SER-1229 AND
RP SER-1494, AND 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-1494, 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 [31]
RP SUBCELLULAR LOCATION.
RX PubMed=25596274; DOI=10.1242/bio.201410843;
RA Gutierrez-Caballero C., Burgess S.G., Bayliss R., Royle S.J.;
RT "TACC3-ch-TOG track the growing tips of microtubules independently of
RT clathrin and Aurora-A phosphorylation.";
RL Biol. Open 4:170-179(2015).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [33]
RP INTERACTION WITH RFTN1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27022195; DOI=10.4049/jimmunol.1501734;
RA Tatematsu M., Yoshida R., Morioka Y., Ishii N., Funami K., Watanabe A.,
RA Saeki K., Seya T., Matsumoto M.;
RT "Raftlin controls lipopolysaccharide-induced TLR4 internalization and
RT TICAM-1 signaling in a cell type-specific manner.";
RL J. Immunol. 196:3865-3876(2016).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-364 IN COMPLEX WITH INHIBITORS,
RP AND WD40-LIKE REPEATS.
RX PubMed=21816279; DOI=10.1016/j.cell.2011.06.025;
RA von Kleist L., Stahlschmidt W., Bulut H., Gromova K., Puchkov D.,
RA Robertson M.J., MacGregor K.A., Tomilin N., Pechstein A., Chau N.,
RA Chircop M., Sakoff J., von Kries J.P., Saenger W., Krausslich H.G.,
RA Shupliakov O., Robinson P.J., McCluskey A., Haucke V.;
RT "Role of the clathrin terminal domain in regulating coated pit dynamics
RT revealed by small molecule inhibition.";
RL Cell 146:471-484(2011).
RN [35]
RP INTERACTION WITH USP2.
RX PubMed=26756164; DOI=10.1371/journal.pone.0145155;
RA Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
RA Katanaev V.L., Gachon F., Staub O.;
RT "USP2-45 is a circadian clock output effector regulating calcium absorption
RT at the post-translational level.";
RL PLoS ONE 11:E0145155-E0145155(2016).
RN [36]
RP INVOLVEMENT IN MRD56.
RX PubMed=26822784; DOI=10.1002/ajmg.a.37506;
RA DeMari J., Mroske C., Tang S., Nimeh J., Miller R., Lebel R.R.;
RT "CLTC as a clinically novel gene associated with multiple malformations and
RT developmental delay.";
RL Am. J. Med. Genet. A 170A:958-966(2016).
RN [37]
RP INVOLVEMENT IN MRD56, AND VARIANTS MRD56 554-MET--TYR-556 DEL; LEU-890;
RP PRO-1047; ARG-1108; 1199-GLN--MET-1675 DEL; ASP-1207 DEL;
RP 1555-GLN--MET-1675 DEL AND 1556-TRP--MET-1675 DEL.
RX PubMed=29100083; DOI=10.1016/j.ajhg.2017.09.008;
RG Deciphering Developmental Disorders Study;
RA Hamdan F.F., Myers C.T., Cossette P., Lemay P., Spiegelman D.,
RA Laporte A.D., Nassif C., Diallo O., Monlong J., Cadieux-Dion M.,
RA Dobrzeniecka S., Meloche C., Retterer K., Cho M.T., Rosenfeld J.A., Bi W.,
RA Massicotte C., Miguet M., Brunga L., Regan B.M., Mo K., Tam C.,
RA Schneider A., Hollingsworth G., FitzPatrick D.R., Donaldson A., Canham N.,
RA Blair E., Kerr B., Fry A.E., Thomas R.H., Shelagh J., Hurst J.A.,
RA Brittain H., Blyth M., Lebel R.R., Gerkes E.H., Davis-Keppen L., Stein Q.,
RA Chung W.K., Dorison S.J., Benke P.J., Fassi E., Corsten-Janssen N.,
RA Kamsteeg E.J., Mau-Them F.T., Bruel A.L., Verloes A., Ounap K.,
RA Wojcik M.H., Albert D.V.F., Venkateswaran S., Ware T., Jones D., Liu Y.C.,
RA Mohammad S.S., Bizargity P., Bacino C.A., Leuzzi V., Martinelli S.,
RA Dallapiccola B., Tartaglia M., Blumkin L., Wierenga K.J., Purcarin G.,
RA O'Byrne J.J., Stockler S., Lehman A., Keren B., Nougues M.C., Mignot C.,
RA Auvin S., Nava C., Hiatt S.M., Bebin M., Shao Y., Scaglia F., Lalani S.R.,
RA Frye R.E., Jarjour I.T., Jacques S., Boucher R.M., Riou E., Srour M.,
RA Carmant L., Lortie A., Major P., Diadori P., Dubeau F., D'Anjou G.,
RA Bourque G., Berkovic S.F., Sadleir L.G., Campeau P.M., Kibar Z.,
RA Lafreniere R.G., Girard S.L., Mercimek-Mahmutoglu S., Boelman C.,
RA Rouleau G.A., Scheffer I.E., Mefford H.C., Andrade D.M., Rossignol E.,
RA Minassian B.A., Michaud J.L.;
RT "High rate of recurrent de novo mutations in developmental and epileptic
RT encephalopathies.";
RL Am. J. Hum. Genet. 101:664-685(2017).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Two different adapter protein complexes link
CC the clathrin lattice either to the plasma membrane or to the trans-
CC Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex
CC proposed to contribute to stabilization of kinetochore fibers of the
CC mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577,
CC PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is
CC required for the maintenance of kinetochore fiber tension
CC (PubMed:23532825). Plays a role in early autophagosome formation
CC (PubMed:20639872). {ECO:0000269|PubMed:15858577,
CC ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:20639872,
CC ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat (PubMed:16968737).
CC In the presence of light chains, hub assembly is influenced by both the
CC pH and the concentration of calcium. Interacts with HIP1
CC (PubMed:11532990). Interacts with DENND1A, DENND1B and DENND1C (By
CC similarity). May interact with OCRL (By similarity). Interacts with
CC ERBB2 (PubMed:16314522). Interacts with FKBP6 (PubMed:18529014).
CC Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin
CC complex located at spindle inter-microtubules bridges; the complex
CC implicates clathrin triskelions; TACC3 and CLTC are proposed to form a
CC composite microtubule interaction surface (PubMed:21297582). Interacts
CC with ATG16L1 (via N-terminus) (PubMed:20639872). Interacts with RFTN1;
CC the interaction occurs in response to pathogens (PubMed:27022195,
CC PubMed:21266579). Interacts with USP2 isoform 4 (PubMed:26756164).
CC {ECO:0000250|UniProtKB:P49951, ECO:0000250|UniProtKB:Q68FD5,
CC ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:16314522,
CC ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:18529014,
CC ECO:0000269|PubMed:20639872, ECO:0000269|PubMed:21266579,
CC ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:26756164,
CC ECO:0000269|PubMed:27022195}.
CC -!- INTERACTION:
CC Q00610; P09496: CLTA; NbExp=2; IntAct=EBI-354967, EBI-1171169;
CC Q00610; Q9NYZ3: GTSE1; NbExp=4; IntAct=EBI-354967, EBI-2511327;
CC Q00610; O75030: MITF; NbExp=3; IntAct=EBI-354967, EBI-3910192;
CC Q00610; P10242: MYB; NbExp=4; IntAct=EBI-354967, EBI-298355;
CC Q00610; Q01968: OCRL; NbExp=10; IntAct=EBI-354967, EBI-6148898;
CC Q00610; Q07912: TNK2; NbExp=3; IntAct=EBI-354967, EBI-603457;
CC Q00610; O75674: TOM1L1; NbExp=4; IntAct=EBI-354967, EBI-712991;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17081065}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17081065}; Cytoplasmic side
CC {ECO:0000269|PubMed:17081065}. Membrane, coated pit
CC {ECO:0000269|PubMed:17081065}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17081065}; Cytoplasmic side
CC {ECO:0000269|PubMed:17081065}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737,
CC ECO:0000269|PubMed:23918938}. Note=Cytoplasmic face of coated pits and
CC vesicles. Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV. In complex with TACC3 and CKAP5 (forming the
CC TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges
CC in mitotic spindles. {ECO:0000269|PubMed:25596274}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q00610-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00610-2; Sequence=VSP_011570, VSP_011571;
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 56
CC (MRD56) [MIM:617854]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period.
CC {ECO:0000269|PubMed:26822784, ECO:0000269|PubMed:29100083}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04801.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CLTCID360.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Clathrin entry;
CC URL="https://en.wikipedia.org/wiki/Clathrin";
CC ---------------------------------------------------------------------------
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DR EMBL; D21260; BAA04801.2; ALT_INIT; mRNA.
DR EMBL; BX640615; CAE45761.1; -; mRNA.
DR EMBL; CH471109; EAW94396.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94399.1; -; Genomic_DNA.
DR EMBL; BC051800; AAH51800.1; -; mRNA.
DR EMBL; BC054489; AAH54489.1; -; mRNA.
DR EMBL; X55878; CAA39363.1; -; mRNA.
DR CCDS; CCDS32696.1; -. [Q00610-1]
DR PIR; A40573; A40573.
DR RefSeq; NP_004850.1; NM_004859.3. [Q00610-1]
DR PDB; 2XZG; X-ray; 1.70 A; A=1-364.
DR PDB; 4G55; X-ray; 1.69 A; A=1-364.
DR PDB; 6E4L; X-ray; 1.60 A; A=1-364.
DR PDB; 6QNN; X-ray; 2.03 A; A=1-364.
DR PDB; 6QNP; X-ray; 2.70 A; A/B/C/D=1-364.
DR PDB; 7BN1; X-ray; 1.97 A; A/B=1-364.
DR PDB; 7BN2; X-ray; 1.97 A; AAA/BBB=1-364.
DR PDBsum; 2XZG; -.
DR PDBsum; 4G55; -.
DR PDBsum; 6E4L; -.
DR PDBsum; 6QNN; -.
DR PDBsum; 6QNP; -.
DR PDBsum; 7BN1; -.
DR PDBsum; 7BN2; -.
DR AlphaFoldDB; Q00610; -.
DR SMR; Q00610; -.
DR BioGRID; 107623; 509.
DR CORUM; Q00610; -.
DR ELM; Q00610; -.
DR IntAct; Q00610; 252.
DR MINT; Q00610; -.
DR STRING; 9606.ENSP00000479606; -.
DR BindingDB; Q00610; -.
DR ChEMBL; CHEMBL3108634; -.
DR MoonDB; Q00610; Curated.
DR TCDB; 8.A.137.1.1; the clathrin (clathrin) family.
DR GlyGen; Q00610; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q00610; -.
DR MetOSite; Q00610; -.
DR PhosphoSitePlus; Q00610; -.
DR SwissPalm; Q00610; -.
DR BioMuta; CLTC; -.
DR DMDM; 1705916; -.
DR CPTAC; CPTAC-182; -.
DR CPTAC; CPTAC-183; -.
DR EPD; Q00610; -.
DR jPOST; Q00610; -.
DR MassIVE; Q00610; -.
DR MaxQB; Q00610; -.
DR PaxDb; Q00610; -.
DR PeptideAtlas; Q00610; -.
DR PRIDE; Q00610; -.
DR ProteomicsDB; 57862; -. [Q00610-1]
DR ProteomicsDB; 57863; -. [Q00610-2]
DR ABCD; Q00610; 1 sequenced antibody.
DR Antibodypedia; 4164; 488 antibodies from 40 providers.
DR DNASU; 1213; -.
DR Ensembl; ENST00000269122.8; ENSP00000269122.3; ENSG00000141367.12. [Q00610-1]
DR Ensembl; ENST00000393043.5; ENSP00000376763.1; ENSG00000141367.12. [Q00610-2]
DR GeneID; 1213; -.
DR KEGG; hsa:1213; -.
DR MANE-Select; ENST00000269122.8; ENSP00000269122.3; NM_004859.4; NP_004850.1.
DR UCSC; uc002ixp.4; human. [Q00610-1]
DR CTD; 1213; -.
DR DisGeNET; 1213; -.
DR GeneCards; CLTC; -.
DR HGNC; HGNC:2092; CLTC.
DR HPA; ENSG00000141367; Low tissue specificity.
DR MalaCards; CLTC; -.
DR MIM; 118955; gene.
DR MIM; 617854; phenotype.
DR neXtProt; NX_Q00610; -.
DR OpenTargets; ENSG00000141367; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR Orphanet; 319308; MiT family translocation renal cell carcinoma.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA26618; -.
DR VEuPathDB; HostDB:ENSG00000141367; -.
DR eggNOG; KOG0985; Eukaryota.
DR GeneTree; ENSGT00950000183166; -.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; Q00610; -.
DR OrthoDB; 17940at2759; -.
DR PhylomeDB; Q00610; -.
DR TreeFam; TF300059; -.
DR PathwayCommons; Q00610; -.
DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-190873; Gap junction degradation.
DR Reactome; R-HSA-196025; Formation of annular gap junctions.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation. [Q00610-1]
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. [Q00610-1]
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. [Q00610-1]
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-8964038; LDL clearance.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR SignaLink; Q00610; -.
DR SIGNOR; Q00610; -.
DR BioGRID-ORCS; 1213; 642 hits in 1088 CRISPR screens.
DR ChiTaRS; CLTC; human.
DR EvolutionaryTrace; Q00610; -.
DR GeneWiki; CLTC; -.
DR GenomeRNAi; 1213; -.
DR Pharos; Q00610; Tbio.
DR PRO; PR:Q00610; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q00610; protein.
DR Bgee; ENSG00000141367; Expressed in pons and 208 other tissues.
DR ExpressionAtlas; Q00610; baseline and differential.
DR Genevisible; Q00610; HS.
DR GO; GO:0030118; C:clathrin coat; IMP:CAFA.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0071439; C:clathrin complex; IDA:FlyBase.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0032051; F:clathrin light chain binding; IPI:FlyBase.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IMP:ARUK-UCL.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:CAFA.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:ARUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; IMP:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
DR IDEAL; IID00662; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR016025; Clathrin_H-chain_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 5.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cell cycle;
KW Cell division; Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Intellectual disability;
KW Membrane; Mitosis; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..1675
FT /note="Clathrin heavy chain 1"
FT /id="PRO_0000205778"
FT REPEAT 537..683
FT /note="CHCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 686..828
FT /note="CHCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 833..972
FT /note="CHCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 979..1124
FT /note="CHCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 1128..1269
FT /note="CHCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 1274..1420
FT /note="CHCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REPEAT 1423..1566
FT /note="CHCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006,
FT ECO:0000269|PubMed:21816279"
FT REGION 2..479
FT /note="Globular terminal domain"
FT REGION 24..67
FT /note="WD40-like repeat 1"
FT REGION 68..107
FT /note="WD40-like repeat 2"
FT REGION 108..149
FT /note="WD40-like repeat 3"
FT REGION 150..195
FT /note="WD40-like repeat 4"
FT REGION 196..257
FT /note="WD40-like repeat 5"
FT REGION 258..301
FT /note="WD40-like repeat 6"
FT REGION 302..330
FT /note="WD40-like repeat 7"
FT REGION 449..465
FT /note="Binding site for the uncoating ATPase, involved in
FT lattice disassembly"
FT /evidence="ECO:0000255"
FT REGION 457..507
FT /note="Involved in spindle localization and interaction
FT with TACC3"
FT /evidence="ECO:0000269|PubMed:23918938"
FT REGION 480..523
FT /note="Flexible linker"
FT REGION 524..1675
FT /note="Heavy chain arm"
FT REGION 524..634
FT /note="Distal segment"
FT REGION 639..1675
FT /note="Proximal segment"
FT REGION 1213..1522
FT /note="Involved in binding clathrin light chain"
FT /evidence="ECO:0000250"
FT REGION 1550..1675
FT /note="Trimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 184
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 737
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 856
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 899
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 1206
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1441
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1441
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 1477
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1487
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1501
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1636..1639
FT /note="QPQL -> NLSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011570"
FT VAR_SEQ 1640..1675
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011571"
FT VARIANT 554..556
FT /note="Missing (in MRD56; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080721"
FT VARIANT 890
FT /note="P -> L (in MRD56; dbSNP:rs1555606635)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080722"
FT VARIANT 1047
FT /note="L -> P (in MRD56; unknown pathological significance;
FT dbSNP:rs1555607159)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080723"
FT VARIANT 1108
FT /note="W -> R (in MRD56; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080724"
FT VARIANT 1199..1675
FT /note="Missing (in MRD56)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080725"
FT VARIANT 1207
FT /note="Missing (in MRD56; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080726"
FT VARIANT 1555..1675
FT /note="Missing (in MRD56)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080727"
FT VARIANT 1556..1675
FT /note="Missing (in MRD56)"
FT /evidence="ECO:0000269|PubMed:29100083"
FT /id="VAR_080728"
FT MUTAGEN 65
FT /note="P->N: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 67
FT /note="S->G: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 87
FT /note="T->A: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 89
FT /note="Q->A: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 96
FT /note="K->E: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 98
FT /note="K->E: Disrupts spindle localization."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 444
FT /note="R->E: Disrupts spindle localization; when associated
FT with E-445, E-500 E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 445
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-444, E-500, E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 480..484
FT /note="LRANV->ERGQC: Disrupts spindle localization and
FT interaction with TACC3."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 481
FT /note="R->E: Disrupts spindle localization; when associated
FT with E-487, E-500, E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 487
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-481, E-500, E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 500
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-444, E-445, E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 500
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-481, E-487, E-506 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 506
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-444, E-445, E-500 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 506
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-481, E-487, E-500 and E-507."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 507
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-444, E-445, E-500 and E-506."
FT /evidence="ECO:0000269|PubMed:23918938"
FT MUTAGEN 507
FT /note="K->E: Disrupts spindle localization; when associated
FT with E-481, E-487, E-500 and E-506."
FT /evidence="ECO:0000269|PubMed:23918938"
FT CONFLICT 560
FT /note="Q -> R (in Ref. 5; CAA39363)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="G -> V (in Ref. 5; CAA39363)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="R -> H (in Ref. 2; CAE45761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1563
FT /note="R -> G (in Ref. 2; CAE45761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1652
FT /note="Q -> R (in Ref. 2; CAE45761)"
FT /evidence="ECO:0000305"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 115..135
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6E4L"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6E4L"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:6E4L"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:6E4L"
SQ SEQUENCE 1675 AA; 191615 MW; 6C4F2D54950079E2 CRC64;
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV
EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV
VQAANTSGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN
HPTDAWKEGQ FKDIITKVAN VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM
