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O75781 (PALM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paralemmin-1
Alternative name(s):
Paralemmin
Gene names
Name:PALM
Synonyms:KIAA0270
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. Ref.6

Subunit structure

Interacts with dopamine receptor DRD3. Ref.7

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projectionfilopodium membrane; Lipid-anchor. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Basolateral cell membrane; Lipid-anchor By similarity. Apicolateral cell membrane; Lipid-anchor By similarity. Note: Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity. Ref.6

Tissue specificity

Widely expressed with highest expression in brain and testis and intermediate expression in heart and adrenal gland.

Sequence similarities

Belongs to the paralemmin family.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMLipoprotein
Methylation
Palmitate
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Traceable author statement Ref.2. Source: ProtInc

cellular response to electrical stimulus

Inferred from electronic annotation. Source: Compara

cytoskeleton organization

Inferred from electronic annotation. Source: Compara

negative regulation of adenylate cyclase activity

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of dopamine receptor signaling pathway

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of dendritic spine development

Inferred from electronic annotation. Source: Compara

positive regulation of filopodium assembly

Inferred from direct assay Ref.6. Source: UniProtKB

protein targeting to plasma membrane

Inferred from electronic annotation. Source: Compara

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

synapse maturation

Inferred from electronic annotation. Source: Compara

   Cellular_componentapicolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle

Traceable author statement Ref.2. Source: ProtInc

dendrite membrane

Inferred from electronic annotation. Source: Compara

dendritic spine membrane

Inferred from electronic annotation. Source: Compara

filopodium membrane

Inferred from direct assay Ref.6. Source: UniProtKB

integral to plasma membrane

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75781-1)

Also known as: Paralemmin-L;

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: O75781-2)

Also known as: Paralemmin-S;

The sequence of this isoform differs from the canonical sequence as follows:
     168-211: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Paralemmin-1
PRO_0000058218
Propeptide385 – 3873Removed in mature form Potential
PRO_0000396689

Regions

Coiled coil9 – 10193 Potential

Amino acid modifications

Modified residue1161Phosphoserine Ref.9
Modified residue1241Phosphoserine Ref.9
Modified residue1411Phosphothreonine Ref.8 Ref.9
Modified residue1451Phosphothreonine Ref.8 Ref.9
Modified residue1521Phosphoserine By similarity
Modified residue1621Phosphoserine Ref.8
Modified residue3461Phosphoserine By similarity
Modified residue3671Phosphothreonine By similarity
Modified residue3691Phosphoserine By similarity
Modified residue3841Cysteine methyl ester Potential
Lipidation3811S-palmitoyl cysteine Potential
Lipidation3831S-palmitoyl cysteine Potential
Lipidation3841S-farnesyl cysteine Potential

Natural variations

Alternative sequence168 – 21144Missing in isoform 2.
VSP_003918
Natural variant1071T → A. Ref.1
Corresponds to variant rs1050457 [ dbSNP | Ensembl ].
VAR_053803

Experimental info

Mutagenesis381 – 3833CKC → SKS: Inhibits axonal and dendritic filopodia formation and reduces axonal and dendritic branching. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Paralemmin-L) [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: 46D455D5D12C3135

FASTA38742,076
        10         20         30         40         50         60 
MEVLAAETTS QQERLQAIAE KRKRQAEIEN KRRQLEDERR QLQHLKSKAL RERWLLEGTP 

        70         80         90        100        110        120 
SSASEGDEDL RRQMQDDEQK TRLLEDSVSR LEKEIEVLER GDSAPATAKE NAAAPSPVRA 

       130        140        150        160        170        180 
PAPSPAKEER KTEVVMNSQQ TPVGTPKDKR VSNTPLRTVD GSPMMKAAMY SVEITVEKDK 

       190        200        210        220        230        240 
VTGETRVLSS TTLLPRQPLP LGIKVYEDET KVVHAVDGTA ENGIHPLSSS EVDELIHKAD 

       250        260        270        280        290        300 
EVTLSEAGST AGAAETRGAV EGAARTTPSR REITGVQAQP GEATSGPPGI QPGQEPPVTM 

       310        320        330        340        350        360 
IFMGYQNVED EAETKKVLGL QDTITAELVV IEDAAEPKEP APPNGSAAEP PTEAASREEN 

       370        380 
QAGPEATTSD PQDLDMKKHR CKCCSIM 

« Hide

Isoform 2 (Paralemmin-S) [UniParc].

Checksum: 8DF5F9BAA42B314F
Show »

FASTA34337,157

References

« Hide 'large scale' references
[1]"Structure of the human paralemmin gene (PALM), mapping to human chromosome 19p13.3 and mouse chromosome 10, and exclusion of coding mutations in grizzled, mocha, jittery, and hesitant mice."
Burwinkel B., Miglierini G., Jenne D.E., Gilbert D.J., Copeland N.G., Jenkins N.A., Ring H.Z., Francke U., Kilimann M.W.
Genomics 49:462-466(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-107.
Tissue: Blood.
[2]"Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons and implicated in plasma membrane dynamics and cell process formation."
Kutzleb C., Sanders G., Yamamoto R., Wang X., Lichte B., Petrasch-Parwez E., Kilimann M.W.
J. Cell Biol. 143:795-813(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Brain.
[5]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-387 (ISOFORM 1).
Tissue: Brain.
[6]"Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 381-CYS--CYS-383.
[7]"Paralemmin interacts with D3 dopamine receptors: implications for membrane localization and cAMP signaling."
Basile M., Lin R., Kabbani N., Karpa K., Kilimann M., Simpson I., Kester M.
Arch. Biochem. Biophys. 446:60-68(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DRD3.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145 AND SER-162, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-124; THR-141 AND THR-145, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y16270 expand/collapse EMBL AC list , Y16271, Y16272, Y16273, Y16274, Y16275, Y16276, Y16277 Genomic DNA. Translation: CAA76151.1.
Y16278 mRNA. Translation: CAA76152.1.
Y14770 mRNA. Translation: CAB37400.1.
Y14770 mRNA. Translation: CAB37401.1.
BC032449 mRNA. Translation: AAH32449.1.
AC004030 Genomic DNA. No translation available.
AC005763 Genomic DNA. Translation: AAC62429.1.
D87460 mRNA. Translation: BAA13400.1.
IPIIPI00220002.
IPI00301023.
PIRT00635.
RefSeqNP_001035224.1. NM_001040134.1.
NP_002570.2. NM_002579.2.
UniGeneHs.631841.

3D structure databases

ProteinModelPortalO75781.
ModBaseSearch...

Protein-protein interaction databases

IntActO75781. 1 interaction.
STRING9606.ENSP00000341911.

PTM databases

PhosphoSiteO75781.

Proteomic databases

PaxDbO75781.
PRIDEO75781.

Protocols and materials databases

DNASU5064.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264560; ENSP00000264560; ENSG00000099864.
ENST00000338448; ENSP00000341911; ENSG00000099864.
GeneID5064.
KEGGhsa:5064.
UCSCuc002lpm.1. human.
uc002lpn.1. human.

Organism-specific databases

CTD5064.
GeneCardsGC19P000708.
HGNCHGNC:8594. PALM.
HPAHPA041713.
MIM608134. gene.
neXtProtNX_O75781.
PharmGKBPA32923.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46471.
HOGENOMHOG000043092.
HOVERGENHBG007431.
InParanoidO75781.
KOK16519.
OMARCKCCSI.
PhylomeDBO75781.

Gene expression databases

ArrayExpressO75781.
BgeeO75781.
CleanExHS_PALM.
GenevestigatorO75781.
GermOnlineENSG00000099864. Homo sapiens.

Family and domain databases

InterProIPR004965. Paralemmin.
[Graphical view]
PfamPF03285. Paralemmin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5064.
NextBio19506.
SOURCESearch...

Entry information

Entry namePALM_HUMAN
AccessionPrimary (citable) accession number: O75781
Secondary accession number(s): O43359 expand/collapse secondary AC list , O95673, Q92559, Q9UPJ4, Q9UQS2, Q9UQS3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 104 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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families