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P13796 (PLSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plastin-2
Alternative name(s):
L-plastin
LC64P
Lymphocyte cytosolic protein 1
Short name=LCP-1
Gene names
Name:LCP1
Synonyms:PLS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length627 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69. Ref.14 Ref.15

Subunit structure

Monomer. Interacts with AIF1 By similarity. Ref.14

Subcellular location

Cytoplasmcytoskeleton. Cell junction. Cell projection. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Relocalizes to the immunological synapse between peripheral blood T-lymphocytes and antibody-presenting cells in response to costimulation through TCR/CD3 and CD2 or CD28. Associated with the actin cytoskeleton at membrane ruffles By similarity. Relocalizes to actin-rich cell projections upon serine phosphorylation. Ref.14 Ref.15

Tissue specificity

Detected in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia, in spleen and other lymph node-containing organs. Expressed in peripheral blood T-lymphocytes, neutrophils, monocytes, B-lymphocytes, and myeloid cells. Ref.11

Post-translational modification

Phosphorylated on a serine residue in response to costimulation through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes association with the actin cytoskeleton and targeting to peripheral cell projections. Ref.14 Ref.15

Involvement in disease

Chromosomal aberrations involving LCP1 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;13)(q27;q14), with BCL6.

Sequence similarities

Contains 2 actin-binding domains.

Contains 4 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation involved in immune response

Inferred from direct assay Ref.15. Source: UniProtKB

actin filament bundle assembly

Inferred from mutant phenotype Ref.14. Source: UniProt

cell migration

Inferred from mutant phenotype Ref.14. Source: UniProt

organ regeneration

Inferred from electronic annotation. Source: Ensembl

protein kinase A signaling

Inferred from mutant phenotype Ref.14. Source: UniProt

regulation of intracellular protein transport

Inferred from direct assay Ref.15. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

actin filament

Inferred from mutant phenotype Ref.14. Source: UniProt

actin filament bundle

Inferred from mutant phenotype Ref.14. Source: UniProt

cytoplasm

Non-traceable author statement Ref.7. Source: UniProtKB

cytosol

Inferred from direct assay Ref.15Ref.10. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 16502470PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

filopodium

Inferred from mutant phenotype Ref.14. Source: UniProt

focal adhesion

Inferred from mutant phenotype Ref.14. Source: UniProt

phagocytic cup

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from mutant phenotype Ref.14. Source: UniProt

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionactin binding

Non-traceable author statement Ref.1. Source: UniProtKB

actin filament binding

Inferred from mutant phenotype Ref.14. Source: UniProt

calcium ion binding

Non-traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 627626Plastin-2
PRO_0000073743

Regions

Domain9 – 4436EF-hand 1
Domain49 – 8436EF-hand 2
Domain106 – 379274Actin-binding 1
Domain120 – 236117CH 1
Domain264 – 375112CH 2
Domain380 – 624245Actin-binding 2
Domain394 – 503110CH 3
Domain515 – 624110CH 4
Calcium binding22 – 33121 By similarity
Calcium binding62 – 73122 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue51Phosphoserine Ref.14 Ref.15 Ref.20
Modified residue71Phosphoserine Ref.17
Modified residue281Phosphotyrosine Ref.17
Modified residue301Phosphoserine Ref.17
Modified residue761N6-acetyllysine Ref.18
Modified residue881N6-acetyllysine Ref.18
Modified residue1241Phosphotyrosine Ref.13
Modified residue2571Phosphoserine Ref.17
Modified residue2941N6-acetyllysine Ref.18
Modified residue2971N6-acetyllysine Ref.18
Modified residue3231Phosphoserine Ref.17
Modified residue3611N6-acetyllysine Ref.18
Modified residue4721N6-acetyllysine Ref.18
Modified residue5421N6-acetyllysine Ref.18
Modified residue5791N6-acetyllysine Ref.18

Natural variations

Natural variant241D → E.
VAR_001371
Natural variant5331K → E. Ref.1 Ref.2 Ref.5 Ref.6 Ref.10
Corresponds to variant rs4941543 [ dbSNP | Ensembl ].
VAR_024398
Natural variant5441P → A.
Corresponds to variant rs17067725 [ dbSNP | Ensembl ].
VAR_030826

Experimental info

Mutagenesis51S → A: Abolishes phosphorylation and reduces the cell surface expression of CD69 and IL2RA. Reduces association with the actin cytoskeleton. Ref.14 Ref.15
Mutagenesis51S → E: Promotes association with the actin cytoskeleton. Ref.14 Ref.15
Sequence conflict6111M → T AA sequence Ref.11

Secondary structure

................... 627
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13796 [UniParc].

Last modified October 5, 2010. Version 6.
Checksum: 668E4AA6A3FC7B58

FASTA62770,288
        10         20         30         40         50         60 
MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV REITENLMAT 

        70         80         90        100        110        120 
GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE 

       130        140        150        160        170        180 
EEKYAFVNWI NKALENDPDC RHVIPMNPNT NDLFNAVGDG IVLCKMINLS VPDTIDERTI 

       190        200        210        220        230        240 
NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI 

       250        260        270        280        290        300 
ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY 

       310        320        330        340        350        360 
HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP 

       370        380        390        400        410        420 
KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL 

       430        440        450        460        470        480 
SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVELGKNQ AKFSLVGIGG 

       490        500        510        520        530        540 
QDLNEGNRTL TLALIWQLMR RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS 

       550        560        570        580        590        600 
FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL 

       610        620 
PEDLVEVNPK MVMTVFACLM GKGMKRV 

« Hide

References

« Hide 'large scale' references
[1]"65-kilodalton protein phosphorylated by interleukin 2 stimulation bears two putative actin-binding sites and two calcium-binding sites."
Zu Y., Shigesada K., Nishida E., Kubota I., Kohno M., Hanaoka M., Namba Y.
Biochemistry 29:8319-8324(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-533.
[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], VARIANT GLU-533.
Tissue: Amygdala.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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], VARIANT GLU-533.
Tissue: Lymph and Placenta.
[6]"Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts."
Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J.
Mol. Cell. Biol. 8:4659-4668(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-627, PARTIAL PROTEIN SEQUENCE, VARIANT GLU-533.
[7]"Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain."
Lin C.-S., Aebersold R.H., Leavitt J.
Mol. Cell. Biol. 10:1818-1821(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-140, SEQUENCE REVISION.
[8]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 20-31; 184-192 AND 534-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[9]"Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells."
Lin C.-S., Park T., Chen Z.P., Leavitt J.
J. Biol. Chem. 268:2781-2792(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627.
[10]"Characterization of interleukin 2 stimulated 65-kilodalton phosphoprotein in human T cells."
Zu Y., Kohno M., Kubota I., Nishida E., Hanaoka M., Namba Y.
Biochemistry 29:1055-1062(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 264-283; 517-533 AND 593-609, VARIANT GLU-533.
[11]"Purification and characterization of a cytosolic 65-kilodalton phosphoprotein in human leukocytes whose phosphorylation is augmented by stimulation with interleukin 1."
Matsushima K., Shiroo M., Kung H.F., Copeland T.D.
Biochemistry 27:3765-3770(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 590-611, TISSUE SPECIFICITY.
[12]"Nonrandom fusion of L-plastin(LCP1) and LAZ3(BCL6) genes by t(3;13)(q27;q14) chromosome translocation in two cases of B-cell non-Hodgkin lymphoma."
Galiegue-Zouitina S., Quief S., Hildebrand M.P., Denis C., Detourmignies L., Lai J.L., Kerckaert J.P.
Genes Chromosomes Cancer 26:97-105(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, CHROMOSOMAL TRANSLOCATION WITH BCL6.
[13]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells."
Janji B., Giganti A., De Corte V., Catillon M., Bruyneel E., Lentz D., Plastino J., Gettemans J., Friederich E.
J. Cell Sci. 119:1947-1960(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIN-BINDING, INTERACTION WITH ACTIN FIBERS, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-5, PHOSPHORYLATION AT SER-5.
[15]"Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25."
Wabnitz G.H., Koecher T., Lohneis P., Stober C., Konstandin M.H., Funk B., Sester U., Wilm M., Klemke M., Samstag Y.
Eur. J. Immunol. 37:649-662(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-5, PHOSPHORYLATION AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-28; SER-30; SER-257 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-88; LYS-294; LYS-297; LYS-361; LYS-472; LYS-542 AND LYS-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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].
[20]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Solution structure of the fourth CH domain from human L-plastin."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 513-627.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02923 mRNA. Translation: AAA63236.1.
AK312393 mRNA. Translation: BAG35310.1.
AL137141 Genomic DNA. Translation: CAI12168.2.
CH471075 Genomic DNA. Translation: EAX08757.1.
BC007673 mRNA. Translation: AAH07673.1.
BC010271 mRNA. Translation: AAH10271.1.
M22300 mRNA. Translation: AAB02845.1.
AH002870 Genomic DNA. Translation: AAA59529.1.
M34426 mRNA. Translation: AAA36184.1.
CCDSCCDS9403.1.
PIRA35836.
RefSeqNP_002289.2. NM_002298.4.
XP_005266431.1. XM_005266374.1.
UniGeneHs.381099.
Hs.658408.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D85NMR-A517-627[»]
ProteinModelPortalP13796.
SMRP13796. Positions 7-77, 118-627.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110128. 6 interactions.
IntActP13796. 7 interactions.
MINTMINT-3008082.
STRING9606.ENSP00000315757.

PTM databases

PhosphoSiteP13796.

Polymorphism databases

DMDM308153685.

Proteomic databases

MaxQBP13796.
PaxDbP13796.
PRIDEP13796.

Protocols and materials databases

DNASU3936.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323076; ENSP00000315757; ENSG00000136167.
ENST00000398576; ENSP00000381581; ENSG00000136167.
GeneID3936.
KEGGhsa:3936.
UCSCuc001vaz.4. human.

Organism-specific databases

CTD3936.
GeneCardsGC13M046700.
H-InvDBHIX0130592.
HGNCHGNC:6528. LCP1.
HPACAB020673.
HPA019493.
MIM153430. gene.
neXtProtNX_P13796.
PharmGKBPA30312.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000213447.
HOVERGENHBG003082.
InParanoidP13796.
KOK17276.
OMAHLYADID.
OrthoDBEOG7K9K2D.
PhylomeDBP13796.
TreeFamTF300680.

Gene expression databases

ArrayExpressP13796.
BgeeP13796.
CleanExHS_LCP1.
GenevestigatorP13796.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF00307. CH. 4 hits.
PF00036. EF-hand_1. 1 hit.
[Graphical view]
SMARTSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 2 hits.
PS00020. ACTININ_2. 2 hits.
PS50021. CH. 4 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLCP1. human.
EvolutionaryTraceP13796.
GeneWikiLCP1.
GenomeRNAi3936.
NextBio15457.
PROP13796.
SOURCESearch...

Entry information

Entry namePLSL_HUMAN
AccessionPrimary (citable) accession number: P13796
Secondary accession number(s): B2R613, Q5TBN4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 171 of the entry and version 6 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 13

Human chromosome 13: entries, gene names and cross-references to MIM