Full text data of PICALM
PICALM
(CALM)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein)
Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein)
hRBCD
IPI00472438
IPI00472438 PICALM protein PICALM protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a membrane bound n/a found at its expected molecular weight found at molecular weight
IPI00472438 PICALM protein PICALM protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 n/a n/a membrane bound n/a found at its expected molecular weight found at molecular weight
UniProt
Q13492
ID PICAL_HUMAN Reviewed; 652 AA.
AC Q13492; B4DTM3; E9PN05; F8VPG7; O60700; Q4LE54; Q6GMQ6; Q86XZ9;
read moreDT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 127.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION,
RP TISSUE 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
RT the AF10 gene and CALM, encoding a new member of the AP-3 clathrin
RT assembly 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long
RT cDNAs 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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-
RT CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-
RT q21) suggests a 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:
RT localization in endocytic-coated pits, interactions with clathrin, and
RT the impact of overexpression on clathrin-mediated traffic.";
RL Mol. Biol. Cell 10:2687-2702(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FAM64A.
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
RT localization of the leukemogenic fusion protein CALM/AF10.";
RL Oncogene 25:4099-4109(2006).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Assembly protein recruiting clathrin and adapter protein
CC complex 2 (AP2) to cell membranes at sites of coated-pit formation
CC and clathrin-vesicle assembly. May be required to determine the
CC amount of membrane to be recycled, possibly by regulating the size
CC of the clathrin cage. Involved in AP2-dependent clathrin-mediated
CC endocytosis at the neuromuscular junction.
CC -!- SUBUNIT: Binds clathrin; involves primarily the C-terminal
CC sequences, but the full-length protein is required for full
CC binding capacity. Binds phosphatidylinositol 4,5- bisphosphate.
CC Interacts with FAM64A; this interaction may change the subcellular
CC location into the nucleus.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Golgi
CC apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus.
CC Note=Colocalized with clathrin in the Golgi area. Interaction with
CC FAM64A may target PICALM to the nucleus in some cells.
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q13492-4; Sequence=VSP_044567, VSP_009607;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q13492-5; Sequence=VSP_044568;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DISEASE: Note=A chromosomal aberration involving PICALM is found
CC in diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14)
CC with MLLT10.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family.
CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06099.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CALM.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 RefSeq; NP_001008660.1; NM_001008660.2.
DR RefSeq; NP_001193875.1; NM_001206946.1.
DR RefSeq; NP_001193876.1; NM_001206947.1.
DR RefSeq; NP_009097.2; NM_007166.3.
DR RefSeq; XP_005274388.1; XM_005274331.1.
DR UniGene; Hs.163893; -.
DR ProteinModelPortal; Q13492; -.
DR SMR; Q13492; 20-288.
DR IntAct; Q13492; 10.
DR MINT; MINT-1636298; -.
DR STRING; 9606.ENSP00000342095; -.
DR PhosphoSite; Q13492; -.
DR DMDM; 116242714; -.
DR PaxDb; Q13492; -.
DR PRIDE; Q13492; -.
DR Ensembl; ENST00000356360; ENSP00000348718; ENSG00000073921.
DR Ensembl; ENST00000393346; ENSP00000377015; ENSG00000073921.
DR Ensembl; ENST00000526033; ENSP00000433846; ENSG00000073921.
DR Ensembl; ENST00000528398; ENSP00000434884; ENSG00000073921.
DR Ensembl; ENST00000532317; ENSP00000436958; ENSG00000073921.
DR GeneID; 8301; -.
DR KEGG; hsa:8301; -.
DR UCSC; uc001pbn.3; human.
DR CTD; 8301; -.
DR GeneCards; GC11M085668; -.
DR HGNC; HGNC:15514; PICALM.
DR HPA; HPA019053; -.
DR HPA; HPA019061; -.
DR MIM; 603025; gene.
DR neXtProt; NX_Q13492; -.
DR PharmGKB; PA33287; -.
DR eggNOG; NOG267212; -.
DR HOVERGEN; HBG049391; -.
DR OMA; WNAATMA; -.
DR OrthoDB; EOG76QFM8; -.
DR PhylomeDB; Q13492; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; PICALM; human.
DR GeneWiki; PICALM; -.
DR GenomeRNAi; 8301; -.
DR NextBio; 31101; -.
DR PMAP-CutDB; Q13492; -.
DR PRO; PR:Q13492; -.
DR ArrayExpress; Q13492; -.
DR Bgee; Q13492; -.
DR CleanEx; HS_PICALM; -.
DR Genevestigator; Q13492; -.
DR GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:BHF-UCL.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; IMP:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013809; Epsin-like_N.
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; Chromosomal rearrangement;
KW Coated pit; Complete proteome; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Membrane; Nucleus; Polymorphism; Proto-oncogene;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 652 Phosphatidylinositol-binding clathrin
FT assembly protein.
FT /FTId=PRO_0000187062.
FT DOMAIN 14 145 ENTH.
FT REGION 221 294 Interaction with FAM64A.
FT SITE 648 649 Breakpoint for translocation to form
FT CALM/MLLT10 fusion protein.
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 1 51 Missing (in isoform 4).
FT /FTId=VSP_044567.
FT VAR_SEQ 420 469 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_009607.
FT VAR_SEQ 420 426 Missing (in isoform 5).
FT /FTId=VSP_044568.
FT VAR_SEQ 593 593 M -> MNGMHFPQY (in isoform 3).
FT /FTId=VSP_009608.
FT VAR_SEQ 594 613 Missing (in isoform 2).
FT /FTId=VSP_004067.
FT VARIANT 158 158 T -> P (in dbSNP:rs12800974).
FT /FTId=VAR_028191.
FT VARIANT 383 383 S -> F (in dbSNP:rs12222608).
FT /FTId=VAR_028192.
FT VARIANT 578 578 W -> C (in dbSNP:rs1043858).
FT /FTId=VAR_028193.
FT VARIANT 579 579 Q -> E (in dbSNP:rs1043859).
FT /FTId=VAR_028194.
FT VARIANT 641 641 F -> L (in dbSNP:rs556337).
FT /FTId=VAR_028195.
FT CONFLICT 132 132 N -> D (in Ref. 2; BAG62035).
FT CONFLICT 212 212 N -> H (in Ref. 1; AAB07762).
FT CONFLICT 331 331 E -> G (in Ref. 2; BAG62035).
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
//
ID PICAL_HUMAN Reviewed; 652 AA.
AC Q13492; B4DTM3; E9PN05; F8VPG7; O60700; Q4LE54; Q6GMQ6; Q86XZ9;
read moreDT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 127.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION,
RP TISSUE 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
RT the AF10 gene and CALM, encoding a new member of the AP-3 clathrin
RT assembly 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long
RT cDNAs 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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-
RT CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-
RT q21) suggests a 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:
RT localization in endocytic-coated pits, interactions with clathrin, and
RT the impact of overexpression on clathrin-mediated traffic.";
RL Mol. Biol. Cell 10:2687-2702(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FAM64A.
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
RT localization of the leukemogenic fusion protein CALM/AF10.";
RL Oncogene 25:4099-4109(2006).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Assembly protein recruiting clathrin and adapter protein
CC complex 2 (AP2) to cell membranes at sites of coated-pit formation
CC and clathrin-vesicle assembly. May be required to determine the
CC amount of membrane to be recycled, possibly by regulating the size
CC of the clathrin cage. Involved in AP2-dependent clathrin-mediated
CC endocytosis at the neuromuscular junction.
CC -!- SUBUNIT: Binds clathrin; involves primarily the C-terminal
CC sequences, but the full-length protein is required for full
CC binding capacity. Binds phosphatidylinositol 4,5- bisphosphate.
CC Interacts with FAM64A; this interaction may change the subcellular
CC location into the nucleus.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit. Golgi
CC apparatus. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus.
CC Note=Colocalized with clathrin in the Golgi area. Interaction with
CC FAM64A may target PICALM to the nucleus in some cells.
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q13492-4; Sequence=VSP_044567, VSP_009607;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q13492-5; Sequence=VSP_044568;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DISEASE: Note=A chromosomal aberration involving PICALM is found
CC in diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14)
CC with MLLT10.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family.
CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06099.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CALM.html";
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001008660.1; NM_001008660.2.
DR RefSeq; NP_001193875.1; NM_001206946.1.
DR RefSeq; NP_001193876.1; NM_001206947.1.
DR RefSeq; NP_009097.2; NM_007166.3.
DR RefSeq; XP_005274388.1; XM_005274331.1.
DR UniGene; Hs.163893; -.
DR ProteinModelPortal; Q13492; -.
DR SMR; Q13492; 20-288.
DR IntAct; Q13492; 10.
DR MINT; MINT-1636298; -.
DR STRING; 9606.ENSP00000342095; -.
DR PhosphoSite; Q13492; -.
DR DMDM; 116242714; -.
DR PaxDb; Q13492; -.
DR PRIDE; Q13492; -.
DR Ensembl; ENST00000356360; ENSP00000348718; ENSG00000073921.
DR Ensembl; ENST00000393346; ENSP00000377015; ENSG00000073921.
DR Ensembl; ENST00000526033; ENSP00000433846; ENSG00000073921.
DR Ensembl; ENST00000528398; ENSP00000434884; ENSG00000073921.
DR Ensembl; ENST00000532317; ENSP00000436958; ENSG00000073921.
DR GeneID; 8301; -.
DR KEGG; hsa:8301; -.
DR UCSC; uc001pbn.3; human.
DR CTD; 8301; -.
DR GeneCards; GC11M085668; -.
DR HGNC; HGNC:15514; PICALM.
DR HPA; HPA019053; -.
DR HPA; HPA019061; -.
DR MIM; 603025; gene.
DR neXtProt; NX_Q13492; -.
DR PharmGKB; PA33287; -.
DR eggNOG; NOG267212; -.
DR HOVERGEN; HBG049391; -.
DR OMA; WNAATMA; -.
DR OrthoDB; EOG76QFM8; -.
DR PhylomeDB; Q13492; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; PICALM; human.
DR GeneWiki; PICALM; -.
DR GenomeRNAi; 8301; -.
DR NextBio; 31101; -.
DR PMAP-CutDB; Q13492; -.
DR PRO; PR:Q13492; -.
DR ArrayExpress; Q13492; -.
DR Bgee; Q13492; -.
DR CleanEx; HS_PICALM; -.
DR Genevestigator; Q13492; -.
DR GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:BHF-UCL.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; IMP:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013809; Epsin-like_N.
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; Chromosomal rearrangement;
KW Coated pit; Complete proteome; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Membrane; Nucleus; Polymorphism; Proto-oncogene;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 652 Phosphatidylinositol-binding clathrin
FT assembly protein.
FT /FTId=PRO_0000187062.
FT DOMAIN 14 145 ENTH.
FT REGION 221 294 Interaction with FAM64A.
FT SITE 648 649 Breakpoint for translocation to form
FT CALM/MLLT10 fusion protein.
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 1 51 Missing (in isoform 4).
FT /FTId=VSP_044567.
FT VAR_SEQ 420 469 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_009607.
FT VAR_SEQ 420 426 Missing (in isoform 5).
FT /FTId=VSP_044568.
FT VAR_SEQ 593 593 M -> MNGMHFPQY (in isoform 3).
FT /FTId=VSP_009608.
FT VAR_SEQ 594 613 Missing (in isoform 2).
FT /FTId=VSP_004067.
FT VARIANT 158 158 T -> P (in dbSNP:rs12800974).
FT /FTId=VAR_028191.
FT VARIANT 383 383 S -> F (in dbSNP:rs12222608).
FT /FTId=VAR_028192.
FT VARIANT 578 578 W -> C (in dbSNP:rs1043858).
FT /FTId=VAR_028193.
FT VARIANT 579 579 Q -> E (in dbSNP:rs1043859).
FT /FTId=VAR_028194.
FT VARIANT 641 641 F -> L (in dbSNP:rs556337).
FT /FTId=VAR_028195.
FT CONFLICT 132 132 N -> D (in Ref. 2; BAG62035).
FT CONFLICT 212 212 N -> H (in Ref. 1; AAB07762).
FT CONFLICT 331 331 E -> G (in Ref. 2; BAG62035).
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
//
MIM
603025
*RECORD*
*FIELD* NO
603025
*FIELD* TI
*603025 PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN; PICALM
;;CLATHRIN ASSEMBLY LYMPHOID-MYELOID LEUKEMIA GENE; CALM;;
read moreCLTH;;
LAP, DROSOPHILA, HOMOLOG OF; LAP
PICALM/AF10 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
In the course of the molecular characterization of the translocation
t(10;11)(p13;q14) in the monocytic cell line U937, Dreyling et al.
(1996) identified a breakpoint on chromosome 11 involving the previously
unknown gene, CALM. CALM has a very high homology to the murine clathrin
assembly protein ap3 (Morris et al., 1993).
BIOCHEMICAL FEATURES
Ford et al. (2001) presented the structure of the N-terminal domain of
CALM bound to phosphatidylinositol-4,5-bisphosphate via a lysine-rich
motif. This motif is found in other proteins predicted to have domains
of similar structure (e.g., Huntingtin-interacting protein-1; 601767).
The structure is in part similar to the epsin (607262) N-terminal (ENTH)
domain, but epsin lacks the
phosphatidylinositol-4,5-bisphosphate-binding site.
Mao et al. (2001) determined the crystal structure of the N-terminal
domain (the NAP domain) of the Drosophila Lap protein, which is
homologous to human PICALM. The structure revealed a novel fold
consisting of a large double layer of sheets of 10 alpha helices and a
unique site for binding phosphoinositides.
CYTOGENETICS
- PICALM/AF10 Fusion Gene
Dreyling et al. (1996) identified a breakpoint on chromosome 11
involving the CALM gene in the translocation t(10;11)(p13;q14) in the
monocytic cell line U937. The fusion partner of the CALM gene on
chromosome 11 was the putative transcription factor AF10 (602409)
located on 10p13. Dreyling et al. (1998) found that both MLL (159555)
and CALM are fused to AF10 in morphologically distinct subsets of acute
leukemia with t(10;11). Both rearrangements were associated with a poor
prognosis.
Bohlander et al. (2000) and Carlson et al. (2000) performed molecular
analyses of the CALM/AF10 fusion in cases of leukemia. Bohlander et al.
(2000) studied a series of 3 patients with AML, 1 patient with T-ALL,
and 2 patients with precursor T lymphoblastic lymphoma. The
rearrangements were essentially identical in all. In all 6 patients the
breakpoint in CALM was at the 3-prime end of the coding region. Three
breakpoints could be identified in AF10. The findings indicated that
CALM/AF10 fusions differ only slightly with respect to the portion of
AF10 present and that there is no obvious difference between the fusions
found in AML patients compared to those found in patients with lymphoid
malignancies. Carlson et al. (2000) studied 6 patients with myeloid
leukemia and 3 with T-cell lymphoblastic leukemia. They identified 4
different CALM/AF10 fusion products in 5 patients and AF10/CALM
reciprocal message in 1. Carlson et al. (2000) concluded that the fusion
of CALM and AF10 is a recurring abnormality in both lymphoid and myeloid
leukemias of various types including AML-M5; that the breakpoints in the
2 types of leukemia do not differ; and that the CALM/AF10 fusion product
on the derivative chromosome 10 is critical to leukemogenesis.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
PICALM gene and late-onset Alzheimer disease, see 104300.
ANIMAL MODEL
Treusch et al. (2011) modeled amyloid-beta (see 104760) toxicity in
yeast by directing the peptide to the secretory pathway. A genomewide
screen for toxicity modifiers identified the yeast homolog of PICALM and
other endocytic factors connected to Alzheimer disease (104300) whose
relationship to amyloid-beta had been unknown. The factors identified in
yeast modified amyloid-beta toxicity in glutamatergic neurons of C.
elegans and in primary rat cortical neurons. In yeast, amyloid-beta
impaired the endocytic trafficking of a plasma membrane receptor, which
was ameliorated by endocytic pathway factors identified in the yeast
screen. Treusch et al. (2011) concluded that links between amyloid-beta,
endocytosis, and human Alzheimer disease risk factors can be ascertained
with yeast as a model system.
NOMENCLATURE
Mao et al. (2001) referred to PICALM as 'the human AP180.' However, the
true homolog of AP180 is SNAP91 (607923), a paralog of PICALM.
*FIELD* RF
1. Bohlander, S. K.; Muschinsky, V.; Schrader, K.; Siebert, R.; Schlegelberger,
B.; Harder, L.; Schemmel, V.; Fonatsch, C.; Ludwig, W.-D.; Hiddemann,
W.; Dreyling, M. H.: Molecular analysis of the CALM/AF10 fusion:
identical rearrangements in acute myeloid leukemia, acute lymphoblastic
leukemia and malignant lymphoma patients. Leukemia 14: 93-99, 2000.
2. Carlson, K. M.; Vignon, C.; Bohlander, S.; Martinez-Climent, J.
A.; Le Beau, M. M.; Rowley, J. D.: Identification and molecular characterization
of CALM/AF10 fusion products in T cell acute lymphoblastic leukemia
and acute myeloid leukemia. Leukemia 14: 100-104, 2000.
3. Dreyling, M. H.; Martinez-Climent, J. A.; Zheng, M.; Mao, J.; Rowley,
J. D.; Bohlander, S. K.: The t(10;11)(p13;q14) in the U937 cell line
results in the fusion of the AF10 gene and CALM, a new member of the
AP-3 clathrin assembly protein family. Proc. Nat. Acad. Sci. 93:
4804-4809, 1996.
4. Dreyling, M. H.; Schrader, K.; Fonatsch, C.; Schlegelberger, B.;
Haase, D.; Schoch, C.; Ludwig, W.-D.; Loffler, H.; Buchner, T.; Wormann,
B.; Hiddemann, W.; Bohlander, S. K.: MLL and CALM are fused to AF10
in morphologically distinct subsets of acute leukemia with translocation
t(10;11): both rearrangements are associated with a poor prognosis. Blood 91:
4662-4667, 1998.
5. Ford, M. G. J.; Pearse, B. M. F.; Higgins, M. K.; Vallis, Y.; Owen,
D. J.; Gibson, A.; Hopkins, C. R.; Evans, P. R.; McMahon, H. T.:
Simultaneous binding of PtdIns(4,5)P(2) and clathrin by AP180 in the
nucleation of clathrin lattices on membranes. Science 291: 1051-1055,
2001.
6. Mao, Y.; Chen, J.; Maynard, J. A.; Zhang, B.; Quiocho, F. A.:
A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide
binding and clathrin assembly in synaptic vesicle endocytosis. Cell 104:
433-440, 2001.
7. Morris, S. A.; Schroder, S.; Plessmann, U.; Weber, K.; Ungewickell,
E.: Clathrin assembly protein AP180: primary structure, domain organization
and identification of a clathrin binding site. EMBO J. 12: 667-675,
1993.
8. Treusch, S.; Hamamichi, S.; Goodman, J. L.; Matlack, K. E. S.;
Chung, C. Y.; Baru, V.; Shulman, J. M.; Parrado, A.; Bevis, B. J.;
Valastyan, J. S.; Han, H.; Lindhagen-Persson, M.; and 9 others:
Functional links between amyloid-beta toxicity, endocytic trafficking,
and Alzheimer's disease risk factors in yeast. Science 334: 1241-1245,
2011.
*FIELD* CN
Ada Hamosh - updated: 1/4/2012
Stylianos E. Antonarakis - updated: 3/8/2001
Ada Hamosh - updated: 2/22/2001
Victor A. McKusick - updated: 4/11/2000
*FIELD* CD
Victor A. McKusick: 9/9/1998
*FIELD* ED
alopez: 01/11/2012
terry: 1/4/2012
wwang: 3/30/2011
ckniffin: 3/15/2011
alopez: 5/14/2009
mgross: 6/26/2003
mgross: 9/27/2002
mgross: 4/6/2001
mgross: 3/8/2001
alopez: 2/26/2001
terry: 2/22/2001
mcapotos: 5/2/2000
mcapotos: 4/27/2000
terry: 4/11/2000
dkim: 9/15/1998
dkim: 9/10/1998
alopez: 9/9/1998
*RECORD*
*FIELD* NO
603025
*FIELD* TI
*603025 PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN; PICALM
;;CLATHRIN ASSEMBLY LYMPHOID-MYELOID LEUKEMIA GENE; CALM;;
read moreCLTH;;
LAP, DROSOPHILA, HOMOLOG OF; LAP
PICALM/AF10 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
In the course of the molecular characterization of the translocation
t(10;11)(p13;q14) in the monocytic cell line U937, Dreyling et al.
(1996) identified a breakpoint on chromosome 11 involving the previously
unknown gene, CALM. CALM has a very high homology to the murine clathrin
assembly protein ap3 (Morris et al., 1993).
BIOCHEMICAL FEATURES
Ford et al. (2001) presented the structure of the N-terminal domain of
CALM bound to phosphatidylinositol-4,5-bisphosphate via a lysine-rich
motif. This motif is found in other proteins predicted to have domains
of similar structure (e.g., Huntingtin-interacting protein-1; 601767).
The structure is in part similar to the epsin (607262) N-terminal (ENTH)
domain, but epsin lacks the
phosphatidylinositol-4,5-bisphosphate-binding site.
Mao et al. (2001) determined the crystal structure of the N-terminal
domain (the NAP domain) of the Drosophila Lap protein, which is
homologous to human PICALM. The structure revealed a novel fold
consisting of a large double layer of sheets of 10 alpha helices and a
unique site for binding phosphoinositides.
CYTOGENETICS
- PICALM/AF10 Fusion Gene
Dreyling et al. (1996) identified a breakpoint on chromosome 11
involving the CALM gene in the translocation t(10;11)(p13;q14) in the
monocytic cell line U937. The fusion partner of the CALM gene on
chromosome 11 was the putative transcription factor AF10 (602409)
located on 10p13. Dreyling et al. (1998) found that both MLL (159555)
and CALM are fused to AF10 in morphologically distinct subsets of acute
leukemia with t(10;11). Both rearrangements were associated with a poor
prognosis.
Bohlander et al. (2000) and Carlson et al. (2000) performed molecular
analyses of the CALM/AF10 fusion in cases of leukemia. Bohlander et al.
(2000) studied a series of 3 patients with AML, 1 patient with T-ALL,
and 2 patients with precursor T lymphoblastic lymphoma. The
rearrangements were essentially identical in all. In all 6 patients the
breakpoint in CALM was at the 3-prime end of the coding region. Three
breakpoints could be identified in AF10. The findings indicated that
CALM/AF10 fusions differ only slightly with respect to the portion of
AF10 present and that there is no obvious difference between the fusions
found in AML patients compared to those found in patients with lymphoid
malignancies. Carlson et al. (2000) studied 6 patients with myeloid
leukemia and 3 with T-cell lymphoblastic leukemia. They identified 4
different CALM/AF10 fusion products in 5 patients and AF10/CALM
reciprocal message in 1. Carlson et al. (2000) concluded that the fusion
of CALM and AF10 is a recurring abnormality in both lymphoid and myeloid
leukemias of various types including AML-M5; that the breakpoints in the
2 types of leukemia do not differ; and that the CALM/AF10 fusion product
on the derivative chromosome 10 is critical to leukemogenesis.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
PICALM gene and late-onset Alzheimer disease, see 104300.
ANIMAL MODEL
Treusch et al. (2011) modeled amyloid-beta (see 104760) toxicity in
yeast by directing the peptide to the secretory pathway. A genomewide
screen for toxicity modifiers identified the yeast homolog of PICALM and
other endocytic factors connected to Alzheimer disease (104300) whose
relationship to amyloid-beta had been unknown. The factors identified in
yeast modified amyloid-beta toxicity in glutamatergic neurons of C.
elegans and in primary rat cortical neurons. In yeast, amyloid-beta
impaired the endocytic trafficking of a plasma membrane receptor, which
was ameliorated by endocytic pathway factors identified in the yeast
screen. Treusch et al. (2011) concluded that links between amyloid-beta,
endocytosis, and human Alzheimer disease risk factors can be ascertained
with yeast as a model system.
NOMENCLATURE
Mao et al. (2001) referred to PICALM as 'the human AP180.' However, the
true homolog of AP180 is SNAP91 (607923), a paralog of PICALM.
*FIELD* RF
1. Bohlander, S. K.; Muschinsky, V.; Schrader, K.; Siebert, R.; Schlegelberger,
B.; Harder, L.; Schemmel, V.; Fonatsch, C.; Ludwig, W.-D.; Hiddemann,
W.; Dreyling, M. H.: Molecular analysis of the CALM/AF10 fusion:
identical rearrangements in acute myeloid leukemia, acute lymphoblastic
leukemia and malignant lymphoma patients. Leukemia 14: 93-99, 2000.
2. Carlson, K. M.; Vignon, C.; Bohlander, S.; Martinez-Climent, J.
A.; Le Beau, M. M.; Rowley, J. D.: Identification and molecular characterization
of CALM/AF10 fusion products in T cell acute lymphoblastic leukemia
and acute myeloid leukemia. Leukemia 14: 100-104, 2000.
3. Dreyling, M. H.; Martinez-Climent, J. A.; Zheng, M.; Mao, J.; Rowley,
J. D.; Bohlander, S. K.: The t(10;11)(p13;q14) in the U937 cell line
results in the fusion of the AF10 gene and CALM, a new member of the
AP-3 clathrin assembly protein family. Proc. Nat. Acad. Sci. 93:
4804-4809, 1996.
4. Dreyling, M. H.; Schrader, K.; Fonatsch, C.; Schlegelberger, B.;
Haase, D.; Schoch, C.; Ludwig, W.-D.; Loffler, H.; Buchner, T.; Wormann,
B.; Hiddemann, W.; Bohlander, S. K.: MLL and CALM are fused to AF10
in morphologically distinct subsets of acute leukemia with translocation
t(10;11): both rearrangements are associated with a poor prognosis. Blood 91:
4662-4667, 1998.
5. Ford, M. G. J.; Pearse, B. M. F.; Higgins, M. K.; Vallis, Y.; Owen,
D. J.; Gibson, A.; Hopkins, C. R.; Evans, P. R.; McMahon, H. T.:
Simultaneous binding of PtdIns(4,5)P(2) and clathrin by AP180 in the
nucleation of clathrin lattices on membranes. Science 291: 1051-1055,
2001.
6. Mao, Y.; Chen, J.; Maynard, J. A.; Zhang, B.; Quiocho, F. A.:
A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide
binding and clathrin assembly in synaptic vesicle endocytosis. Cell 104:
433-440, 2001.
7. Morris, S. A.; Schroder, S.; Plessmann, U.; Weber, K.; Ungewickell,
E.: Clathrin assembly protein AP180: primary structure, domain organization
and identification of a clathrin binding site. EMBO J. 12: 667-675,
1993.
8. Treusch, S.; Hamamichi, S.; Goodman, J. L.; Matlack, K. E. S.;
Chung, C. Y.; Baru, V.; Shulman, J. M.; Parrado, A.; Bevis, B. J.;
Valastyan, J. S.; Han, H.; Lindhagen-Persson, M.; and 9 others:
Functional links between amyloid-beta toxicity, endocytic trafficking,
and Alzheimer's disease risk factors in yeast. Science 334: 1241-1245,
2011.
*FIELD* CN
Ada Hamosh - updated: 1/4/2012
Stylianos E. Antonarakis - updated: 3/8/2001
Ada Hamosh - updated: 2/22/2001
Victor A. McKusick - updated: 4/11/2000
*FIELD* CD
Victor A. McKusick: 9/9/1998
*FIELD* ED
alopez: 01/11/2012
terry: 1/4/2012
wwang: 3/30/2011
ckniffin: 3/15/2011
alopez: 5/14/2009
mgross: 6/26/2003
mgross: 9/27/2002
mgross: 4/6/2001
mgross: 3/8/2001
alopez: 2/26/2001
terry: 2/22/2001
mcapotos: 5/2/2000
mcapotos: 4/27/2000
terry: 4/11/2000
dkim: 9/15/1998
dkim: 9/10/1998
alopez: 9/9/1998