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Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein)

 PICAL_HUMAN             Reviewed;         652 AA.
Q13492; B4DTM3; E9PN05; F8VPG7; O60700; Q4LE54; Q6GMQ6; Q86XZ9;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 168.
RecName: Full=Phosphatidylinositol-binding clathrin assembly protein;
AltName: Full=Clathrin assembly lymphoid myeloid leukemia protein;
Name=PICALM; Synonyms=CALM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION,
TISSUE SPECIFICITY, AND VARIANTS CYS-578 AND GLU-579.
PubMed=8643484; DOI=10.1073/pnas.93.10.4804;
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, encoding a new member of the AP-3 clathrin
assembly protein family.";
Proc. Natl. Acad. Sci. U.S.A. 93:4804-4809(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 575-652 (ISOFORMS 1 AND 2), AND VARIANTS
CYS-578 AND GLU-579.
TISSUE=Bone marrow;
PubMed=9737689; DOI=10.1038/sj.leu.2401109;
Silliman C.C., McGavran L., Wei Q., Miller L.A., Li S., Hunger S.P.;
"Alternative splicing in wild-type AF10 and CALM cDNAs and in AF10-
CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-
q21) suggests a potential role for truncated AF10 polypeptides.";
Leukemia 12:1404-1410(1998).
[8]
FUNCTION, INTERACTION WITH CLATHRIN, AND SUBCELLULAR LOCATION.
PubMed=10436022; DOI=10.1091/mbc.10.8.2687;
Tebar F., Bohlander S.K., Sorkin A.;
"Clathrin assembly lymphoid myeloid leukemia (CALM) protein:
localization in endocytic-coated pits, interactions with clathrin, and
the impact of overexpression on clathrin-mediated traffic.";
Mol. Biol. Cell 10:2687-2702(1999).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH PIMREG.
PubMed=16491119; DOI=10.1038/sj.onc.1209438;
Archangelo L.F., Glaesner J., Krause A., Bohlander S.K.;
"The novel CALM interactor CATS influences the subcellular
localization of the leukemogenic fusion protein CALM/AF10.";
Oncogene 25:4099-4109(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-20; SER-303 AND
SER-315, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Assembly protein recruiting clathrin and adapter protein
complex 2 (AP2) to cell membranes at sites of coated-pit formation
and clathrin-vesicle assembly. May be required to determine the
amount of membrane to be recycled, possibly by regulating the size
of the clathrin cage. Involved in AP2-dependent clathrin-mediated
endocytosis at the neuromuscular junction.
{ECO:0000269|PubMed:10436022}.
-!- SUBUNIT: Binds clathrin; involves primarily the C-terminal
sequences, but the full-length protein is required for full
binding capacity. Binds phosphatidylinositol 4,5- bisphosphate.
Interacts with PIMREG; this interaction may change the subcellular
location into the nucleus. {ECO:0000269|PubMed:10436022,
ECO:0000269|PubMed:16491119}.
-!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
{ECO:0000269|PubMed:10436022}. Golgi apparatus
{ECO:0000269|PubMed:10436022}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000269|PubMed:10436022}. Nucleus
{ECO:0000269|PubMed:16491119}. Note=Colocalized with clathrin in
the Golgi area (PubMed:10436022). Interaction with PIMREG may
target PICALM to the nucleus in some cells (PubMed:16491119).
{ECO:0000269|PubMed:10436022, ECO:0000269|PubMed:16491119}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Type I;
IsoId=Q13492-1; Sequence=Displayed;
Name=2; Synonyms=Type II;
IsoId=Q13492-2; Sequence=VSP_004067;
Name=3;
IsoId=Q13492-3; Sequence=VSP_009607, VSP_009608;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q13492-4; Sequence=VSP_044567, VSP_009607;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q13492-5; Sequence=VSP_044568;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined.
{ECO:0000269|PubMed:8643484}.
-!- DISEASE: Note=A chromosomal aberration involving PICALM is found
in diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14)
with MLLT10. {ECO:0000269|PubMed:8643484}.
-!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE06099.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CALMID64.html";
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EMBL; U45976; AAB07762.1; -; mRNA.
EMBL; AK300275; BAG62035.1; -; mRNA.
EMBL; AB210017; BAE06099.1; ALT_INIT; mRNA.
EMBL; AP000767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW75120.1; -; Genomic_DNA.
EMBL; BC048259; AAH48259.2; -; mRNA.
EMBL; BC064357; AAH64357.1; -; mRNA.
EMBL; BC073961; AAH73961.1; -; mRNA.
EMBL; AF060939; AAC16711.1; -; mRNA.
EMBL; AF060940; AAC16712.1; -; mRNA.
CCDS; CCDS31653.1; -. [Q13492-3]
CCDS; CCDS55783.1; -. [Q13492-4]
CCDS; CCDS55784.1; -. [Q13492-5]
CCDS; CCDS8272.1; -. [Q13492-1]
RefSeq; NP_001008660.1; NM_001008660.2. [Q13492-3]
RefSeq; NP_001193875.1; NM_001206946.1. [Q13492-5]
RefSeq; NP_001193876.1; NM_001206947.1. [Q13492-4]
RefSeq; NP_009097.2; NM_007166.3. [Q13492-1]
RefSeq; XP_005274388.1; XM_005274331.2. [Q13492-2]
UniGene; Hs.163893; -.
ProteinModelPortal; Q13492; -.
SMR; Q13492; -.
BioGrid; 113902; 102.
ELM; Q13492; -.
IntAct; Q13492; 54.
MINT; MINT-1636298; -.
STRING; 9606.ENSP00000377015; -.
iPTMnet; Q13492; -.
PhosphoSitePlus; Q13492; -.
SwissPalm; Q13492; -.
BioMuta; PICALM; -.
DMDM; 116242714; -.
EPD; Q13492; -.
MaxQB; Q13492; -.
PaxDb; Q13492; -.
PeptideAtlas; Q13492; -.
PRIDE; Q13492; -.
Ensembl; ENST00000356360; ENSP00000348718; ENSG00000073921. [Q13492-2]
Ensembl; ENST00000393346; ENSP00000377015; ENSG00000073921. [Q13492-1]
Ensembl; ENST00000526033; ENSP00000433846; ENSG00000073921. [Q13492-5]
Ensembl; ENST00000528398; ENSP00000434884; ENSG00000073921. [Q13492-4]
Ensembl; ENST00000532317; ENSP00000436958; ENSG00000073921. [Q13492-3]
GeneID; 8301; -.
KEGG; hsa:8301; -.
UCSC; uc001pbl.4; human. [Q13492-1]
CTD; 8301; -.
DisGeNET; 8301; -.
EuPathDB; HostDB:ENSG00000073921.17; -.
GeneCards; PICALM; -.
HGNC; HGNC:15514; PICALM.
HPA; HPA019053; -.
HPA; HPA019061; -.
MalaCards; PICALM; -.
MIM; 603025; gene.
neXtProt; NX_Q13492; -.
OpenTargets; ENSG00000073921; -.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA33287; -.
eggNOG; KOG0251; Eukaryota.
eggNOG; ENOG410XQ90; LUCA.
GeneTree; ENSGT00390000008805; -.
HOGENOM; HOG000015764; -.
HOVERGEN; HBG049391; -.
InParanoid; Q13492; -.
KO; K20044; -.
OMA; PTGMMAY; -.
OrthoDB; EOG091G0810; -.
PhylomeDB; Q13492; -.
TreeFam; TF314861; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SIGNOR; Q13492; -.
ChiTaRS; PICALM; human.
GeneWiki; PICALM; -.
GenomeRNAi; 8301; -.
PMAP-CutDB; Q13492; -.
PRO; PR:Q13492; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000073921; -.
CleanEx; HS_PICALM; -.
ExpressionAtlas; Q13492; baseline and differential.
Genevisible; Q13492; HS.
GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IMP:ARUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
GO; GO:0070381; C:endosome to plasma membrane transport vesicle; IDA:ARUK-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031224; C:intrinsic component of membrane; ISS:ARUK-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0097418; C:neurofibrillary tangle; IMP:Alzheimers_University_of_Toronto.
GO; GO:0043025; C:neuronal cell body; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
GO; GO:0031982; C:vesicle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0035615; F:clathrin adaptor activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
GO; GO:0032050; F:clathrin heavy chain binding; IDA:BHF-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:ARUK-UCL.
GO; GO:0017137; F:Rab GTPase binding; IPI:ARUK-UCL.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0035459; P:cargo loading into vesicle; IMP:Alzheimers_University_of_Toronto.
GO; GO:0008283; P:cell proliferation; IMP:Alzheimers_University_of_Toronto.
GO; GO:0048268; P:clathrin coat assembly; IMP:BHF-UCL.
GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:Alzheimers_University_of_Toronto.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0016197; P:endosomal transport; IMP:BHF-UCL.
GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
GO; GO:0055072; P:iron ion homeostasis; IMP:Alzheimers_University_of_Toronto.
GO; GO:0098711; P:iron ion import across plasma membrane; IMP:Alzheimers_University_of_Toronto.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0097753; P:membrane bending; IMP:ARUK-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0090647; P:modulation of age-related behavioral decline; ISS:ARUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:ARUK-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; NAS:ARUK-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IMP:Alzheimers_University_of_Toronto.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
GO; GO:1902959; P:regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
GO; GO:0030100; P:regulation of endocytosis; IMP:BHF-UCL.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:0097494; P:regulation of vesicle size; IMP:ARUK-UCL.
GO; GO:0016188; P:synaptic vesicle maturation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
GO; GO:0016050; P:vesicle organization; IMP:ARUK-UCL.
GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
Gene3D; 1.20.58.150; -; 1.
Gene3D; 1.25.40.90; -; 1.
InterPro; IPR011417; ANTH_dom.
InterPro; IPR014712; Clathrin_AP_dom2.
InterPro; IPR013809; ENTH.
InterPro; IPR008942; ENTH_VHS.
InterPro; IPR030412; PICALM.
PANTHER; PTHR22951:SF16; PTHR22951:SF16; 1.
Pfam; PF07651; ANTH; 1.
SMART; SM00273; ENTH; 1.
SUPFAM; SSF48464; SSF48464; 1.
PROSITE; PS50942; ENTH; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromosomal rearrangement;
Coated pit; Complete proteome; Cytoplasmic vesicle; Endocytosis;
Golgi apparatus; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
CHAIN 2 652 Phosphatidylinositol-binding clathrin
assembly protein.
/FTId=PRO_0000187062.
DOMAIN 14 145 ENTH. {ECO:0000255|PROSITE-
ProRule:PRU00243}.
REGION 221 294 Interaction with PIMREG.
{ECO:0000269|PubMed:16491119}.
SITE 648 649 Breakpoint for translocation to form
CALM/MLLT10 fusion protein.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 238 238 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 1 51 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044567.
VAR_SEQ 420 469 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009607.
VAR_SEQ 420 426 Missing (in isoform 5).
{ECO:0000303|Ref.3}.
/FTId=VSP_044568.
VAR_SEQ 593 593 M -> MNGMHFPQY (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009608.
VAR_SEQ 594 613 Missing (in isoform 2).
{ECO:0000303|PubMed:9737689}.
/FTId=VSP_004067.
VARIANT 158 158 T -> P (in dbSNP:rs12800974).
/FTId=VAR_028191.
VARIANT 383 383 S -> F (in dbSNP:rs12222608).
/FTId=VAR_028192.
VARIANT 578 578 W -> C (in dbSNP:rs1043858).
{ECO:0000269|PubMed:8643484,
ECO:0000269|PubMed:9737689}.
/FTId=VAR_028193.
VARIANT 579 579 Q -> E (in dbSNP:rs1043859).
{ECO:0000269|PubMed:8643484,
ECO:0000269|PubMed:9737689}.
/FTId=VAR_028194.
VARIANT 641 641 F -> L (in dbSNP:rs556337).
/FTId=VAR_028195.
CONFLICT 132 132 N -> D (in Ref. 2; BAG62035).
{ECO:0000305}.
CONFLICT 212 212 N -> H (in Ref. 1; AAB07762).
{ECO:0000305}.
CONFLICT 331 331 E -> G (in Ref. 2; BAG62035).
{ECO:0000305}.
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


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