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Q13492 (PICAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol-binding clathrin assembly protein
Alternative name(s):
Clathrin assembly lymphoid myeloid leukemia protein
Gene names
Name:PICALM
Synonyms:CALM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8

Subunit structure

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 FAM64A; this interaction may change the subcellular location into the nucleus. Ref.8 Ref.9

Subcellular location

Membraneclathrin-coated pit. Golgi apparatus. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus. Note: Colocalized with clathrin in the Golgi area. Interaction with FAM64A may target PICALM to the nucleus in some cells. Ref.8 Ref.9

Tissue specificity

Expressed in all tissues examined. Ref.1

Involvement in disease

A chromosomal aberration involving PICALM is found in diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14) with MLLT10.

Sequence similarities

Belongs to the PICALM/SNAP91 family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Sequence caution

The sequence BAE06099.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCoated pit
Cytoplasmic vesicle
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

cargo loading into vesicle

Inferred from mutant phenotype PubMed 24577224. Source: Alzheimers_University_of_Toronto

cell proliferation

Inferred from mutant phenotype PubMed 22952941. Source: Alzheimers_University_of_Toronto

clathrin coat assembly

Inferred from mutant phenotype PubMed 16262731. Source: BHF-UCL

clathrin-mediated endocytosis

Inferred from mutant phenotype PubMed 22952941PubMed 24577224. Source: Alzheimers_University_of_Toronto

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

endosomal transport

Inferred from mutant phenotype PubMed 16262731. Source: BHF-UCL

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from mutant phenotype PubMed 22952941. Source: Alzheimers_University_of_Toronto

iron ion import into cell

Inferred from mutant phenotype PubMed 22952941. Source: Alzheimers_University_of_Toronto

negative regulation of gene expression

Inferred from mutant phenotype PubMed 22952941. Source: Alzheimers_University_of_Toronto

negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

negative regulation of receptor-mediated endocytosis

Inferred from direct assay Ref.8. Source: BHF-UCL

positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

positive regulation of beta-amyloid formation

Inferred from mutant phenotype PubMed 24577224. Source: Alzheimers_University_of_Toronto

positive regulation of neuron death

Inferred from mutant phenotype PubMed 23589030. Source: Alzheimers_University_of_Toronto

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11425879. Source: BHF-UCL

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

receptor internalization

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

receptor-mediated endocytosis

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process

Inferred from mutant phenotype PubMed 24577224. Source: Alzheimers_University_of_Toronto

regulation of endocytosis

Inferred from mutant phenotype PubMed 18182011. Source: BHF-UCL

regulation of protein localization

Inferred from direct assay Ref.8. Source: BHF-UCL

synaptic vesicle maturation

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

vesicle-mediated transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin coat

Inferred from electronic annotation. Source: InterPro

clathrin-coated vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

coated pit

Inferred from direct assay Ref.8. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

neurofibrillary tangle

Inferred from mutant phenotype PubMed 23589030. Source: Alzheimers_University_of_Toronto

neuronal cell body

Inferred from direct assay PubMed 23589030. Source: Alzheimers_University_of_Toronto

nucleus

Inferred from direct assay Ref.9. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

presynaptic membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

vesicle

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

   Molecular_function1-phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

clathrin adaptor activity

Inferred from mutant phenotype PubMed 23589030. Source: Alzheimers_University_of_Toronto

clathrin binding

Inferred from direct assay Ref.8. Source: UniProtKB

clathrin heavy chain binding

Inferred from direct assay Ref.8. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13492-1)

Also known as: Type I;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13492-2)

Also known as: Type II;

The sequence of this isoform differs from the canonical sequence as follows:
     594-613: Missing.
Isoform 3 (identifier: Q13492-3)

The sequence of this isoform differs from the canonical sequence as follows:
     420-469: Missing.
     593-593: M → MNGMHFPQY
Note: No experimental confirmation available.
Isoform 4 (identifier: Q13492-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     420-469: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q13492-5)

The sequence of this isoform differs from the canonical sequence as follows:
     420-426: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 652651Phosphatidylinositol-binding clathrin assembly protein
PRO_0000187062

Regions

Domain14 – 145132ENTH
Region221 – 29474Interaction with FAM64A

Sites

Site648 – 6492Breakpoint for translocation to form CALM/MLLT10 fusion protein

Amino acid modifications

Modified residue21N-acetylserine Ref.11 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 5151Missing in isoform 4.
VSP_044567
Alternative sequence420 – 46950Missing in isoform 3 and isoform 4.
VSP_009607
Alternative sequence420 – 4267Missing in isoform 5.
VSP_044568
Alternative sequence5931M → MNGMHFPQY in isoform 3.
VSP_009608
Alternative sequence594 – 61320Missing in isoform 2.
VSP_004067
Natural variant1581T → P.
Corresponds to variant rs12800974 [ dbSNP | Ensembl ].
VAR_028191
Natural variant3831S → F.
Corresponds to variant rs12222608 [ dbSNP | Ensembl ].
VAR_028192
Natural variant5781W → C. Ref.1 Ref.7
Corresponds to variant rs1043858 [ dbSNP | Ensembl ].
VAR_028193
Natural variant5791Q → E. Ref.1 Ref.7
Corresponds to variant rs1043859 [ dbSNP | Ensembl ].
VAR_028194
Natural variant6411F → L.
Corresponds to variant rs556337 [ dbSNP | Ensembl ].
VAR_028195

Experimental info

Sequence conflict1321N → D in BAG62035. Ref.2
Sequence conflict2121N → H in AAB07762. Ref.1
Sequence conflict3311E → G in BAG62035. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Type I) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: AC3227E9D32AFEDA

FASTA65270,755
        10         20         30         40         50         60 
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN EMNVNIPQLA 

        70         80         90        100        110        120 
DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR NTLFNLSNFL DKSGLQGYDM 

       130        140        150        160        170        180 
STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR GADGVMRTMN TEKLLKTVPI IQNQMDALLD 

       190        200        210        220        230        240 
FNVNSNELTN GVINAAFMLL FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF 

       250        260        270        280        290        300 
LTRMTRISEF LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 

       310        320        330        340        350        360 
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP HTSLTTAASP 

       370        380        390        400        410        420 
VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT FHPSVHPMST ASQVASTWGD 

       430        440        450        460        470        480 
PFSATVDAVD DAIPSLNPFL TKSSGDVHLS ISSDVSTFTT RTPTHEMFVG FTPSPVAQPH 

       490        500        510        520        530        540 
PSAGLNVDFE SVFGNKSTNV IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL 

       550        560        570        580        590        600 
DSSLANLVGN LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMAPPVMAY 

       610        620        630        640        650 
PATTPTGMIG YGIPPQMGSV PVMTQPTLIY SQPVMRPPNP FGPVSGAQIQ FM 

« Hide

Isoform 2 (Type II) [UniParc].

Checksum: D13D4427A30EE4FD
Show »

FASTA63268,764
Isoform 3 [UniParc].

Checksum: 3B0D0AEB901CF85D
Show »

FASTA61066,393
Isoform 4 [UniParc].

Checksum: A39E7E594F66D57F
Show »

FASTA55159,918
Isoform 5 [UniParc].

Checksum: E4F76B25065B499A
Show »

FASTA64570,037

References

« Hide 'large scale' references
[1]"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."
Dreyling M.H., Martinez-Climent J.A., Zheng M., Mao J., Rowley J.D., Bohlander S.K.
Proc. Natl. Acad. Sci. U.S.A. 93:4804-4809(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE SPECIFICITY, VARIANTS CYS-578 AND GLU-579.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Placenta.
[3]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
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. expand/collapse author list , 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.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: PNS.
[7]"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."
Silliman C.C., McGavran L., Wei Q., Miller L.A., Li S., Hunger S.P.
Leukemia 12:1404-1410(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 575-652 (ISOFORMS 1 AND 2), VARIANTS CYS-578 AND GLU-579.
Tissue: Bone marrow.
[8]"Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic."
Tebar F., Bohlander S.K., Sorkin A.
Mol. Biol. Cell 10:2687-2702(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
[9]"The novel CALM interactor CATS influences the subcellular localization of the leukemogenic fusion protein CALM/AF10."
Archangelo L.F., Glaesner J., Krause A., Bohlander S.K.
Oncogene 25:4099-4109(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FAM64A.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U45976 mRNA. Translation: AAB07762.1.
AK300275 mRNA. Translation: BAG62035.1.
AB210017 mRNA. Translation: BAE06099.1. Different initiation.
AP000767 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75120.1.
BC048259 mRNA. Translation: AAH48259.2.
BC064357 mRNA. Translation: AAH64357.1.
BC073961 mRNA. Translation: AAH73961.1.
AF060939 mRNA. Translation: AAC16711.1.
AF060940 mRNA. Translation: AAC16712.1.
CCDSCCDS31653.1. [Q13492-3]
CCDS55783.1. [Q13492-4]
CCDS55784.1. [Q13492-5]
CCDS8272.1. [Q13492-1]
RefSeqNP_001008660.1. NM_001008660.2. [Q13492-3]
NP_001193875.1. NM_001206946.1. [Q13492-5]
NP_001193876.1. NM_001206947.1. [Q13492-4]
NP_009097.2. NM_007166.3. [Q13492-1]
XP_005274388.1. XM_005274331.1. [Q13492-2]
UniGeneHs.163893.

3D structure databases

ProteinModelPortalQ13492.
SMRQ13492. Positions 20-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113902. 26 interactions.
IntActQ13492. 11 interactions.
MINTMINT-1636298.
STRING9606.ENSP00000342095.

PTM databases

PhosphoSiteQ13492.

Polymorphism databases

DMDM116242714.

Proteomic databases

MaxQBQ13492.
PaxDbQ13492.
PRIDEQ13492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356360; ENSP00000348718; ENSG00000073921. [Q13492-2]
ENST00000393346; ENSP00000377015; ENSG00000073921. [Q13492-1]
ENST00000526033; ENSP00000433846; ENSG00000073921. [Q13492-5]
ENST00000528398; ENSP00000434884; ENSG00000073921. [Q13492-4]
ENST00000532317; ENSP00000436958; ENSG00000073921. [Q13492-3]
GeneID8301.
KEGGhsa:8301.
UCSCuc001pbl.3. human. [Q13492-3]
uc001pbm.3. human. [Q13492-1]

Organism-specific databases

CTD8301.
GeneCardsGC11M085668.
HGNCHGNC:15514. PICALM.
HPAHPA019053.
HPA019061.
MIM603025. gene.
neXtProtNX_Q13492.
Orphanet99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA33287.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267212.
HOVERGENHBG049391.
OMAWNAATMA.
OrthoDBEOG76QFM8.
PhylomeDBQ13492.
TreeFamTF314861.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ13492.
BgeeQ13492.
CleanExHS_PICALM.
GenevestigatorQ13492.

Family and domain databases

Gene3D1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProIPR011417. ANTH_dom.
IPR014712. Clathrin_Pinositid-bd_GAT-like.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
[Graphical view]
PfamPF07651. ANTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPICALM. human.
GeneWikiPICALM.
GenomeRNAi8301.
NextBio31101.
PMAP-CutDBQ13492.
PROQ13492.
SOURCESearch...

Entry information

Entry namePICAL_HUMAN
AccessionPrimary (citable) accession number: Q13492
Secondary accession number(s): B4DTM3 expand/collapse secondary AC list , E9PN05, F8VPG7, O60700, Q4LE54, Q6GMQ6, Q86XZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM