PICAL_HUMAN
ID PICAL_HUMAN Reviewed; 652 AA.
AC Q13492; B4DTM3; E9PN05; F8VPG7; O60700; Q4LE54; Q6GMQ6; Q86XZ9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Phosphatidylinositol-binding clathrin assembly protein;
DE AltName: Full=Clathrin assembly lymphoid myeloid leukemia protein;
GN Name=PICALM; Synonyms=CALM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS CYS-578 AND GLU-579.
RX PubMed=8643484; DOI=10.1073/pnas.93.10.4804;
RA Dreyling M.H., Martinez-Climent J.A., Zheng M., Mao J., Rowley J.D.,
RA Bohlander S.K.;
RT "The t(10;11)(p13;q14) in the U937 cell line results in the fusion of the
RT AF10 gene and CALM, encoding a new member of the AP-3 clathrin assembly
RT protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4804-4809(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=PNS;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 575-652 (ISOFORMS 1 AND 2), AND VARIANTS
RP CYS-578 AND GLU-579.
RC TISSUE=Bone marrow;
RX PubMed=9737689; DOI=10.1038/sj.leu.2401109;
RA Silliman C.C., McGavran L., Wei Q., Miller L.A., Li S., Hunger S.P.;
RT "Alternative splicing in wild-type AF10 and CALM cDNAs and in AF10-CALM and
RT CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-q21) suggests a
RT potential role for truncated AF10 polypeptides.";
RL Leukemia 12:1404-1410(1998).
RN [8]
RP FUNCTION, INTERACTION WITH CLATHRIN, AND SUBCELLULAR LOCATION.
RX PubMed=10436022; DOI=10.1091/mbc.10.8.2687;
RA Tebar F., Bohlander S.K., Sorkin A.;
RT "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization
RT in endocytic-coated pits, interactions with clathrin, and the impact of
RT overexpression on clathrin-mediated traffic.";
RL Mol. Biol. Cell 10:2687-2702(1999).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AP2A1 AND CLATHRIN.
RX PubMed=16262731; DOI=10.1111/j.1600-0854.2005.00355.x;
RA Meyerholz A., Hinrichsen L., Groos S., Esk P.C., Brandes G.,
RA Ungewickell E.J.;
RT "Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on
RT clathrin coat formation.";
RL Traffic 6:1225-1234(2005).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PIMREG.
RX PubMed=16491119; DOI=10.1038/sj.onc.1209438;
RA Archangelo L.F., Glaesner J., Krause A., Bohlander S.K.;
RT "The novel CALM interactor CATS influences the subcellular localization of
RT the leukemogenic fusion protein CALM/AF10.";
RL Oncogene 25:4099-4109(2006).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
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 [14]
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 [15]
RP FUNCTION, AND INTERACTION WITH VAMP2; VAMP3 AND VAMP8.
RX PubMed=22118466; DOI=10.1016/j.cell.2011.10.038;
RA Miller S.E., Sahlender D.A., Graham S.C., Honing S., Robinson M.S.,
RA Peden A.A., Owen D.J.;
RT "The molecular basis for the endocytosis of small R-SNAREs by the clathrin
RT adaptor CALM.";
RL Cell 147:1118-1131(2011).
RN [16]
RP FUNCTION, AND INTERACTION WITH VAMP2.
RX PubMed=21808019; DOI=10.1073/pnas.1107067108;
RA Koo S.J., Markovic S., Puchkov D., Mahrenholz C.C., Beceren-Braun F.,
RA Maritzen T., Dernedde J., Volkmer R., Oschkinat H., Haucke V.;
RT "SNARE motif-mediated sorting of synaptobrevin by the endocytic adaptors
RT clathrin assembly lymphoid myeloid leukemia (CALM) and AP180 at synapses.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13540-13545(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [19]
RP FUNCTION, AND INTERACTION WITH VAMP7.
RX PubMed=23741335; DOI=10.1371/journal.pone.0064514;
RA Sahlender D.A., Kozik P., Miller S.E., Peden A.A., Robinson M.S.;
RT "Uncoupling the functions of CALM in VAMP sorting and clathrin-coated pit
RT formation.";
RL PLoS ONE 8:E64514-E64514(2013).
RN [20]
RP FUNCTION, AND INTERACTION WITH LC3/MAP1LC3A.
RX PubMed=24067654; DOI=10.1073/pnas.1315110110;
RA Tian Y., Chang J.C., Fan E.Y., Flajolet M., Greengard P.;
RT "Adaptor complex AP2/PICALM, through interaction with LC3, targets
RT Alzheimer's APP-CTF for terminal degradation via autophagy.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17071-17076(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-20; SER-303 AND
RP SER-315, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [24]
RP FUNCTION.
RX PubMed=25241929; DOI=10.1038/ncomms5998;
RA Moreau K., Fleming A., Imarisio S., Lopez Ramirez A., Mercer J.L.,
RA Jimenez-Sanchez M., Bento C.F., Puri C., Zavodszky E., Siddiqi F.,
RA Lavau C.P., Betton M., O'Kane C.J., Wechsler D.S., Rubinsztein D.C.;
RT "PICALM modulates autophagy activity and tau accumulation.";
RL Nat. Commun. 5:4998-4998(2014).
RN [25]
RP FUNCTION.
RX PubMed=25898166; DOI=10.1016/j.devcel.2015.03.002;
RA Miller S.E., Mathiasen S., Bright N.A., Pierre F., Kelly B.T., Kladt N.,
RA Schauss A., Merrifield C.J., Stamou D., Hoening S., Owen D.J.;
RT "CALM regulates clathrin-coated vesicle size and maturation by directly
RT sensing and driving membrane curvature.";
RL Dev. Cell 33:163-175(2015).
RN [26]
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 [27]
RP FUNCTION.
RX PubMed=27574975; DOI=10.1371/journal.pone.0162050;
RA Moshkanbaryans L., Xue J., Wark J.R., Robinson P.J., Graham M.E.;
RT "A Novel Sequence in AP180 and CALM Promotes Efficient Clathrin Binding and
RT Assembly.";
RL PLoS ONE 11:E0162050-E0162050(2016).
CC -!- FUNCTION: Cytoplasmic adapter protein that plays a critical role in
CC clathrin-mediated endocytosis which is important in processes such as
CC internalization of cell receptors, synaptic transmission or removal of
CC apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the
CC cytoplasmic side of plasma membrane leading to clathrin-coated vesicles
CC (CCVs) assembly (PubMed:10436022, PubMed:16262731, PubMed:27574975).
CC Furthermore, regulates clathrin-coated vesicle size and maturation by
CC directly sensing and driving membrane curvature (PubMed:25898166). In
CC addition to binding to clathrin, mediates the endocytosis of small R-
CC SNARES (Soluble NSF Attachment Protein REceptors) between plasma
CC membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8
CC (PubMed:22118466, PubMed:21808019, PubMed:23741335). In turn, PICALM-
CC dependent SNARE endocytosis is required for the formation and
CC maturation of autophagic precursors (PubMed:25241929). Modulates
CC thereby autophagy and the turnover of autophagy substrates such as
CC MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-
CC CTF) (PubMed:25241929, PubMed:24067654). {ECO:0000269|PubMed:10436022,
CC ECO:0000269|PubMed:16262731, ECO:0000269|PubMed:21808019,
CC ECO:0000269|PubMed:22118466, ECO:0000269|PubMed:23741335,
CC ECO:0000269|PubMed:24067654, ECO:0000269|PubMed:25241929,
CC ECO:0000269|PubMed:25898166, ECO:0000269|PubMed:27574975}.
CC -!- SUBUNIT: Binds to clathrin; involves primarily the C-terminal
CC sequences, but the full-length protein is required for full binding
CC capacity. Binds phosphatidylinositol 4,5- bisphosphate. Interacts with
CC PIMREG; this interaction may change the subcellular location into the
CC nucleus (PubMed:16491119). Interacts with AP2A1 (via its alpha-
CC appendage domain) (PubMed:16262731). Interacts (via N-terminus) with
CC VAMP2; VAMP3; VAMP7 and VAMP8 (Via N-terminus) (PubMed:22118466,
CC PubMed:21808019, PubMed:23741335). Interacts with LC3/MAP1LC3A
CC (PubMed:24067654). {ECO:0000269|PubMed:16262731,
CC ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:21808019,
CC ECO:0000269|PubMed:22118466, ECO:0000269|PubMed:23741335,
CC ECO:0000269|PubMed:24067654}.
CC -!- INTERACTION:
CC Q13492; P42566: EPS15; NbExp=2; IntAct=EBI-2803688, EBI-396684;
CC Q13492; Q14192: FHL2; NbExp=8; IntAct=EBI-2803688, EBI-701903;
CC Q13492-3; P54253: ATXN1; NbExp=3; IntAct=EBI-11031437, EBI-930964;
CC Q13492-3; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-11031437, EBI-8624731;
CC Q13492-3; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-11031437, EBI-742550;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16262731}.
CC Membrane, clathrin-coated pit {ECO:0000269|PubMed:10436022}. Golgi
CC apparatus {ECO:0000269|PubMed:10436022}. Cytoplasmic vesicle, clathrin-
CC coated vesicle {ECO:0000269|PubMed:10436022}. Nucleus
CC {ECO:0000269|PubMed:16491119}. Note=Colocalized with clathrin in the
CC Golgi area (PubMed:10436022). Interaction with PIMREG may target PICALM
CC to the nucleus in some cells (PubMed:16491119).
CC {ECO:0000269|PubMed:10436022, ECO:0000269|PubMed:16491119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Type I;
CC IsoId=Q13492-1; Sequence=Displayed;
CC Name=2; Synonyms=Type II;
CC IsoId=Q13492-2; Sequence=VSP_004067;
CC Name=3;
CC IsoId=Q13492-3; Sequence=VSP_009607, VSP_009608;
CC Name=4;
CC IsoId=Q13492-4; Sequence=VSP_044567, VSP_009607;
CC Name=5;
CC IsoId=Q13492-5; Sequence=VSP_044568;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC {ECO:0000269|PubMed:8643484}.
CC -!- DISEASE: Note=A chromosomal aberration involving PICALM is found in
CC diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14) with
CC MLLT10. {ECO:0000269|PubMed:8643484}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06099.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CALMID64.html";
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DR EMBL; U45976; AAB07762.1; -; mRNA.
DR EMBL; AK300275; BAG62035.1; -; mRNA.
DR EMBL; AB210017; BAE06099.1; ALT_INIT; mRNA.
DR EMBL; AP000767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW75120.1; -; Genomic_DNA.
DR EMBL; BC048259; AAH48259.2; -; mRNA.
DR EMBL; BC064357; AAH64357.1; -; mRNA.
DR EMBL; BC073961; AAH73961.1; -; mRNA.
DR EMBL; AF060939; AAC16711.1; -; mRNA.
DR EMBL; AF060940; AAC16712.1; -; mRNA.
DR CCDS; CCDS31653.1; -. [Q13492-3]
DR CCDS; CCDS55783.1; -. [Q13492-4]
DR CCDS; CCDS55784.1; -. [Q13492-5]
DR CCDS; CCDS8272.1; -. [Q13492-1]
DR RefSeq; NP_001008660.1; NM_001008660.2. [Q13492-3]
DR RefSeq; NP_001193875.1; NM_001206946.1. [Q13492-5]
DR RefSeq; NP_001193876.1; NM_001206947.1. [Q13492-4]
DR RefSeq; NP_009097.2; NM_007166.3. [Q13492-1]
DR RefSeq; XP_005274388.1; XM_005274331.2. [Q13492-2]
DR AlphaFoldDB; Q13492; -.
DR SMR; Q13492; -.
DR BioGRID; 113902; 209.
DR ELM; Q13492; -.
DR IntAct; Q13492; 85.
DR MINT; Q13492; -.
DR STRING; 9606.ENSP00000377015; -.
DR MoonDB; Q13492; Curated.
DR MoonProt; Q13492; -.
DR GlyGen; Q13492; 16 sites, 2 O-linked glycans (16 sites).
DR iPTMnet; Q13492; -.
DR MetOSite; Q13492; -.
DR PhosphoSitePlus; Q13492; -.
DR SwissPalm; Q13492; -.
DR BioMuta; PICALM; -.
DR DMDM; 116242714; -.
DR EPD; Q13492; -.
DR jPOST; Q13492; -.
DR MassIVE; Q13492; -.
DR MaxQB; Q13492; -.
DR PaxDb; Q13492; -.
DR PeptideAtlas; Q13492; -.
DR PRIDE; Q13492; -.
DR ProteomicsDB; 22268; -.
DR ProteomicsDB; 28286; -.
DR ProteomicsDB; 59489; -. [Q13492-1]
DR ProteomicsDB; 59490; -. [Q13492-2]
DR ProteomicsDB; 59491; -. [Q13492-3]
DR Antibodypedia; 17636; 214 antibodies from 34 providers.
DR DNASU; 8301; -.
DR Ensembl; ENST00000356360.9; ENSP00000348718.5; ENSG00000073921.18. [Q13492-2]
DR Ensembl; ENST00000393346.8; ENSP00000377015.3; ENSG00000073921.18. [Q13492-1]
DR Ensembl; ENST00000526033.5; ENSP00000433846.1; ENSG00000073921.18. [Q13492-5]
DR Ensembl; ENST00000528398.5; ENSP00000434884.1; ENSG00000073921.18. [Q13492-4]
DR Ensembl; ENST00000532317.5; ENSP00000436958.1; ENSG00000073921.18. [Q13492-3]
DR GeneID; 8301; -.
DR KEGG; hsa:8301; -.
DR MANE-Select; ENST00000393346.8; ENSP00000377015.3; NM_007166.4; NP_009097.2.
DR UCSC; uc001pbl.4; human. [Q13492-1]
DR CTD; 8301; -.
DR DisGeNET; 8301; -.
DR GeneCards; PICALM; -.
DR HGNC; HGNC:15514; PICALM.
DR HPA; ENSG00000073921; Low tissue specificity.
DR MalaCards; PICALM; -.
DR MIM; 603025; gene.
DR neXtProt; NX_Q13492; -.
DR NIAGADS; ENSG00000073921; -.
DR OpenTargets; ENSG00000073921; -.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA33287; -.
DR VEuPathDB; HostDB:ENSG00000073921; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_014080_0_0_1; -.
DR InParanoid; Q13492; -.
DR OMA; XPFSATV; -.
DR OrthoDB; 1592722at2759; -.
DR PhylomeDB; Q13492; -.
DR TreeFam; TF314861; -.
DR PathwayCommons; Q13492; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; Q13492; -.
DR SIGNOR; Q13492; -.
DR BioGRID-ORCS; 8301; 44 hits in 1087 CRISPR screens.
DR ChiTaRS; PICALM; human.
DR GeneWiki; PICALM; -.
DR GenomeRNAi; 8301; -.
DR Pharos; Q13492; Tbio.
DR PRO; PR:Q13492; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13492; protein.
DR Bgee; ENSG00000073921; Expressed in calcaneal tendon and 201 other tissues.
DR ExpressionAtlas; Q13492; baseline and differential.
DR Genevisible; Q13492; HS.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0030132; C:clathrin coat of coated pit; IDA:BHF-UCL.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IMP:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
DR GO; GO:0070381; C:endosome to plasma membrane transport vesicle; IDA:ARUK-UCL.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:ARUK-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0097418; C:neurofibrillary tangle; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0043025; C:neuronal cell body; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:BHF-UCL.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:ARUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:ARUK-UCL.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; IPI:Alzheimers_University_of_Toronto.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IGI:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:BHF-UCL.
DR GO; GO:1905224; P:clathrin-coated pit assembly; IDA:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR GO; GO:0097753; P:membrane bending; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:ARUK-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:ARUK-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:1902959; P:regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR GO; GO:0097494; P:regulation of vesicle size; IMP:ARUK-UCL.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0006900; P:vesicle budding from membrane; IMP:ARUK-UCL.
DR GO; GO:0035459; P:vesicle cargo loading; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR030412; PICALM.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR PANTHER; PTHR22951:SF16; PTHR22951:SF16; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane;
KW Chromosomal rearrangement; Coated pit; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT CHAIN 2..652
FT /note="Phosphatidylinositol-binding clathrin assembly
FT protein"
FT /id="PRO_0000187062"
FT DOMAIN 14..145
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 221..294
FT /note="Interaction with PIMREG"
FT /evidence="ECO:0000269|PubMed:16491119"
FT REGION 559..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 648..649
FT /note="Breakpoint for translocation to form CALM/MLLT10
FT fusion protein"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044567"
FT VAR_SEQ 420..469
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009607"
FT VAR_SEQ 420..426
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044568"
FT VAR_SEQ 593
FT /note="M -> MNGMHFPQY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009608"
FT VAR_SEQ 594..613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9737689"
FT /id="VSP_004067"
FT VARIANT 158
FT /note="T -> P (in dbSNP:rs12800974)"
FT /id="VAR_028191"
FT VARIANT 383
FT /note="S -> F (in dbSNP:rs12222608)"
FT /id="VAR_028192"
FT VARIANT 578
FT /note="W -> C (in dbSNP:rs1043858)"
FT /evidence="ECO:0000269|PubMed:8643484,
FT ECO:0000269|PubMed:9737689"
FT /id="VAR_028193"
FT VARIANT 579
FT /note="Q -> E (in dbSNP:rs1043859)"
FT /evidence="ECO:0000269|PubMed:8643484,
FT ECO:0000269|PubMed:9737689"
FT /id="VAR_028194"
FT VARIANT 641
FT /note="F -> L (in dbSNP:rs556337)"
FT /id="VAR_028195"
FT CONFLICT 132
FT /note="N -> D (in Ref. 2; BAG62035)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="N -> H (in Ref. 1; AAB07762)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> G (in Ref. 2; BAG62035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 70755 MW; AC3227E9D32AFEDA CRC64;
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN EMNVNIPQLA
DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR NTLFNLSNFL DKSGLQGYDM
STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR GADGVMRTMN TEKLLKTVPI IQNQMDALLD
FNVNSNELTN GVINAAFMLL FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF
LTRMTRISEF LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP HTSLTTAASP
VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT FHPSVHPMST ASQVASTWGD
PFSATVDAVD DAIPSLNPFL TKSSGDVHLS ISSDVSTFTT RTPTHEMFVG FTPSPVAQPH
PSAGLNVDFE SVFGNKSTNV IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL
DSSLANLVGN LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMAPPVMAY
PATTPTGMIG YGIPPQMGSV PVMTQPTLIY SQPVMRPPNP FGPVSGAQIQ FM
