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Protein

Phosphatidylinositol-binding clathrin assembly protein

Gene

PICALM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei648 – 6492Breakpoint for translocation to form CALM/MLLT10 fusion protein

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. clathrin adaptor activity Source: Alzheimers_University_of_Toronto
  3. clathrin binding Source: UniProtKB
  4. clathrin heavy chain binding Source: BHF-UCL

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. cargo loading into vesicle Source: Alzheimers_University_of_Toronto
  3. cell proliferation Source: Alzheimers_University_of_Toronto
  4. clathrin coat assembly Source: BHF-UCL
  5. clathrin-mediated endocytosis Source: Alzheimers_University_of_Toronto
  6. dendrite morphogenesis Source: Ensembl
  7. endosomal transport Source: BHF-UCL
  8. hemopoiesis Source: Ensembl
  9. iron ion homeostasis Source: Alzheimers_University_of_Toronto
  10. iron ion import into cell Source: Alzheimers_University_of_Toronto
  11. negative regulation of gene expression Source: Alzheimers_University_of_Toronto
  12. negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
  13. negative regulation of receptor-mediated endocytosis Source: BHF-UCL
  14. positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
  15. positive regulation of beta-amyloid formation Source: Alzheimers_University_of_Toronto
  16. positive regulation of neuron death Source: Alzheimers_University_of_Toronto
  17. positive regulation of transcription, DNA-templated Source: BHF-UCL
  18. protein complex assembly Source: ProtInc
  19. receptor internalization Source: BHF-UCL
  20. receptor-mediated endocytosis Source: UniProtKB
  21. regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: Alzheimers_University_of_Toronto
  22. regulation of endocytosis Source: BHF-UCL
  23. regulation of protein localization Source: BHF-UCL
  24. synaptic vesicle maturation Source: Alzheimers_University_of_Toronto
  25. vesicle-mediated transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol-binding clathrin assembly protein
Alternative name(s):
Clathrin assembly lymphoid myeloid leukemia protein
Gene namesi
Name:PICALM
Synonyms:CALM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:15514. PICALM.

Subcellular locationi

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.

GO - Cellular componenti

  1. clathrin coat Source: InterPro
  2. clathrin-coated vesicle Source: UniProtKB-SubCell
  3. coated pit Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB-SubCell
  5. intracellular membrane-bounded organelle Source: HPA
  6. membrane Source: UniProtKB
  7. neurofibrillary tangle Source: Alzheimers_University_of_Toronto
  8. neuronal cell body Source: Alzheimers_University_of_Toronto
  9. nucleus Source: BHF-UCL
  10. perinuclear region of cytoplasm Source: Ensembl
  11. postsynaptic membrane Source: BHF-UCL
  12. presynaptic membrane Source: BHF-UCL
  13. vesicle Source: Alzheimers_University_of_Toronto
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA33287.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 652651Phosphatidylinositol-binding clathrin assembly proteinPRO_0000187062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13492.
PaxDbiQ13492.
PRIDEiQ13492.

PTM databases

PhosphoSiteiQ13492.

Miscellaneous databases

PMAP-CutDBQ13492.

Expressioni

Tissue specificityi

Expressed in all tissues examined.1 Publication

Gene expression databases

BgeeiQ13492.
CleanExiHS_PICALM.
ExpressionAtlasiQ13492. baseline and differential.
GenevestigatoriQ13492.

Organism-specific databases

HPAiHPA019053.
HPA019061.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi113902. 34 interactions.
IntActiQ13492. 11 interactions.
MINTiMINT-1636298.
STRINGi9606.ENSP00000342095.

Structurei

3D structure databases

ProteinModelPortaliQ13492.
SMRiQ13492. Positions 20-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 145132ENTHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 29474Interaction with FAM64AAdd
BLAST

Sequence similaritiesi

Belongs to the PICALM/SNAP91 family.Curated
Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG267212.
GeneTreeiENSGT00390000008805.
HOVERGENiHBG049391.
InParanoidiQ13492.
OMAiWNAATMA.
OrthoDBiEOG76QFM8.
PhylomeDBiQ13492.
TreeFamiTF314861.

Family and domain databases

Gene3Di1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProiIPR011417. ANTH_dom.
IPR014712. Clathrin_AP_2.
IPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR030412. PICALM.
[Graphical view]
PANTHERiPTHR22951:SF16. PTHR22951:SF16. 1 hit.
PfamiPF07651. ANTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13492-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN
60 70 80 90 100
EMNVNIPQLA DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR
110 120 130 140 150
NTLFNLSNFL DKSGLQGYDM STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR
160 170 180 190 200
GADGVMRTMN TEKLLKTVPI IQNQMDALLD FNVNSNELTN GVINAAFMLL
210 220 230 240 250
FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF LTRMTRISEF
260 270 280 290 300
LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT
310 320 330 340 350
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP
360 370 380 390 400
HTSLTTAASP VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT
410 420 430 440 450
FHPSVHPMST ASQVASTWGD PFSATVDAVD DAIPSLNPFL TKSSGDVHLS
460 470 480 490 500
ISSDVSTFTT RTPTHEMFVG FTPSPVAQPH PSAGLNVDFE SVFGNKSTNV
510 520 530 540 550
IVDSGGFDEL GGLLKPTVAS QNQNLPVAKL PPSKLVSDDL DSSLANLVGN
560 570 580 590 600
LGIGNGTTKN DVNWSQPGEK KLTGGSNWQP KVAPTTAWNA ATMAPPVMAY
610 620 630 640 650
PATTPTGMIG YGIPPQMGSV PVMTQPTLIY SQPVMRPPNP FGPVSGAQIQ

FM
Length:652
Mass (Da):70,755
Last modified:October 17, 2006 - v2
Checksum:iAC3227E9D32AFEDA
GO
Isoform 2 (identifier: Q13492-2) [UniParc]FASTAAdd to Basket

Also known as: Type II

The sequence of this isoform differs from the canonical sequence as follows:
     594-613: Missing.

Show »
Length:632
Mass (Da):68,764
Checksum:iD13D4427A30EE4FD
GO
Isoform 3 (identifier: Q13492-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     420-469: Missing.
     593-593: M → MNGMHFPQY

Note: No experimental confirmation available.

Show »
Length:610
Mass (Da):66,393
Checksum:i3B0D0AEB901CF85D
GO
Isoform 4 (identifier: Q13492-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     420-469: Missing.

Note: No experimental confirmation available.

Show »
Length:551
Mass (Da):59,918
Checksum:iA39E7E594F66D57F
GO
Isoform 5 (identifier: Q13492-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     420-426: Missing.

Note: No experimental confirmation available.

Show »
Length:645
Mass (Da):70,037
Checksum:iE4F76B25065B499A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321N → D in BAG62035. (PubMed:14702039)Curated
Sequence conflicti212 – 2121N → H in AAB07762. (PubMed:8643484)Curated
Sequence conflicti331 – 3311E → G in BAG62035. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti158 – 1581T → P.
Corresponds to variant rs12800974 [ dbSNP | Ensembl ].
VAR_028191
Natural varianti383 – 3831S → F.
Corresponds to variant rs12222608 [ dbSNP | Ensembl ].
VAR_028192
Natural varianti578 – 5781W → C.2 Publications
Corresponds to variant rs1043858 [ dbSNP | Ensembl ].
VAR_028193
Natural varianti579 – 5791Q → E.2 Publications
Corresponds to variant rs1043859 [ dbSNP | Ensembl ].
VAR_028194
Natural varianti641 – 6411F → L.
Corresponds to variant rs556337 [ dbSNP | Ensembl ].
VAR_028195

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 4. 1 PublicationVSP_044567Add
BLAST
Alternative sequencei420 – 46950Missing in isoform 3 and isoform 4. 2 PublicationsVSP_009607Add
BLAST
Alternative sequencei420 – 4267Missing in isoform 5. 1 PublicationVSP_044568
Alternative sequencei593 – 5931M → MNGMHFPQY in isoform 3. 1 PublicationVSP_009608
Alternative sequencei594 – 61320Missing in isoform 2. 1 PublicationVSP_004067Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31653.1. [Q13492-3]
CCDS55783.1. [Q13492-4]
CCDS55784.1. [Q13492-5]
CCDS8272.1. [Q13492-1]
RefSeqiNP_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]
UniGeneiHs.163893.

Genome annotation databases

EnsembliENST00000356360; ENSP00000348718; ENSG00000073921. [Q13492-2]
ENST00000393346; ENSP00000377015; ENSG00000073921. [Q13492-1]
ENST00000526033; ENSP00000433846; ENSG00000073921. [Q13492-5]
ENST00000528398; ENSP00000434884; ENSG00000073921. [Q13492-4]
ENST00000532317; ENSP00000436958; ENSG00000073921. [Q13492-3]
GeneIDi8301.
KEGGihsa:8301.
UCSCiuc001pbl.3. human. [Q13492-3]
uc001pbm.3. human. [Q13492-1]

Polymorphism databases

DMDMi116242714.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31653.1. [Q13492-3]
CCDS55783.1. [Q13492-4]
CCDS55784.1. [Q13492-5]
CCDS8272.1. [Q13492-1]
RefSeqiNP_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]
UniGeneiHs.163893.

3D structure databases

ProteinModelPortaliQ13492.
SMRiQ13492. Positions 20-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113902. 34 interactions.
IntActiQ13492. 11 interactions.
MINTiMINT-1636298.
STRINGi9606.ENSP00000342095.

PTM databases

PhosphoSiteiQ13492.

Polymorphism databases

DMDMi116242714.

Proteomic databases

MaxQBiQ13492.
PaxDbiQ13492.
PRIDEiQ13492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356360; ENSP00000348718; ENSG00000073921. [Q13492-2]
ENST00000393346; ENSP00000377015; ENSG00000073921. [Q13492-1]
ENST00000526033; ENSP00000433846; ENSG00000073921. [Q13492-5]
ENST00000528398; ENSP00000434884; ENSG00000073921. [Q13492-4]
ENST00000532317; ENSP00000436958; ENSG00000073921. [Q13492-3]
GeneIDi8301.
KEGGihsa:8301.
UCSCiuc001pbl.3. human. [Q13492-3]
uc001pbm.3. human. [Q13492-1]

Organism-specific databases

CTDi8301.
GeneCardsiGC11M085668.
HGNCiHGNC:15514. PICALM.
HPAiHPA019053.
HPA019061.
MIMi603025. gene.
neXtProtiNX_Q13492.
Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA33287.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG267212.
GeneTreeiENSGT00390000008805.
HOVERGENiHBG049391.
InParanoidiQ13492.
OMAiWNAATMA.
OrthoDBiEOG76QFM8.
PhylomeDBiQ13492.
TreeFamiTF314861.

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiPICALM. human.
GeneWikiiPICALM.
GenomeRNAii8301.
NextBioi31101.
PMAP-CutDBQ13492.
PROiQ13492.
SOURCEiSearch...

Gene expression databases

BgeeiQ13492.
CleanExiHS_PICALM.
ExpressionAtlasiQ13492. baseline and differential.
GenevestigatoriQ13492.

Family and domain databases

Gene3Di1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProiIPR011417. ANTH_dom.
IPR014712. Clathrin_AP_2.
IPR013809. ENTH.
IPR008942. ENTH_VHS.
IPR030412. PICALM.
[Graphical view]
PANTHERiPTHR22951:SF16. PTHR22951:SF16. 1 hit.
PfamiPF07651. ANTH. 1 hit.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPICAL_HUMAN
AccessioniPrimary (citable) accession number: Q13492
Secondary accession number(s): B4DTM3
, E9PN05, F8VPG7, O60700, Q4LE54, Q6GMQ6, Q86XZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.