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P13796

- PLSL_HUMAN

UniProt

P13796 - PLSL_HUMAN

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Protein
Plastin-2
Gene
LCP1, PLS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 CD69.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi22 – 33121 By similarity
Add
BLAST
Calcium bindingi62 – 73122 By similarity
Add
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. actin filament binding Source: UniProt
  3. calcium ion binding Source: UniProtKB

GO - Biological processi

  1. T cell activation involved in immune response Source: UniProtKB
  2. actin filament bundle assembly Source: UniProt
  3. cell migration Source: UniProt
  4. organ regeneration Source: Ensembl
  5. protein kinase A signaling Source: UniProt
  6. regulation of intracellular protein transport Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Plastin-2
Alternative name(s):
L-plastin
LC64P
Lymphocyte cytosolic protein 1
Short name:
LCP-1
Gene namesi
Name:LCP1
Synonyms:PLS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:6528. LCP1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. actin filament Source: UniProt
  3. actin filament bundle Source: UniProt
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. extracellular space Source: UniProt
  7. extracellular vesicular exosome Source: UniProt
  8. filopodium Source: UniProt
  9. focal adhesion Source: UniProt
  10. phagocytic cup Source: Ensembl
  11. plasma membrane Source: HPA
  12. ruffle Source: UniProt
  13. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51S → A: Abolishes phosphorylation and reduces the cell surface expression of CD69 and IL2RA. Reduces association with the actin cytoskeleton. 2 Publications
Mutagenesisi5 – 51S → E: Promotes association with the actin cytoskeleton. 2 Publications

Organism-specific databases

PharmGKBiPA30312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 627626Plastin-2
PRO_0000073743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51Phosphoserine3 Publications
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei28 – 281Phosphotyrosine1 Publication
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei76 – 761N6-acetyllysine1 Publication
Modified residuei88 – 881N6-acetyllysine1 Publication
Modified residuei124 – 1241Phosphotyrosine1 Publication
Modified residuei257 – 2571Phosphoserine1 Publication
Modified residuei294 – 2941N6-acetyllysine1 Publication
Modified residuei297 – 2971N6-acetyllysine1 Publication
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei361 – 3611N6-acetyllysine1 Publication
Modified residuei472 – 4721N6-acetyllysine1 Publication
Modified residuei542 – 5421N6-acetyllysine1 Publication
Modified residuei579 – 5791N6-acetyllysine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13796.
PaxDbiP13796.
PRIDEiP13796.

PTM databases

PhosphoSiteiP13796.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiP13796.
BgeeiP13796.
CleanExiHS_LCP1.
GenevestigatoriP13796.

Organism-specific databases

HPAiCAB020673.
HPA019493.

Interactioni

Subunit structurei

Monomer. Interacts with AIF1 By similarity.1 Publication

Protein-protein interaction databases

BioGridi110128. 6 interactions.
IntActiP13796. 7 interactions.
MINTiMINT-3008082.
STRINGi9606.ENSP00000315757.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi520 – 53213
Helixi545 – 5484
Helixi550 – 55910
Turni566 – 5683
Helixi576 – 59318
Helixi601 – 6044
Turni605 – 6073
Helixi609 – 6124
Helixi615 – 6206
Turni621 – 6233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D85NMR-A517-627[»]
ProteinModelPortaliP13796.
SMRiP13796. Positions 7-77, 118-627.

Miscellaneous databases

EvolutionaryTraceiP13796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 4436EF-hand 1
Add
BLAST
Domaini49 – 8436EF-hand 2
Add
BLAST
Domaini106 – 379274Actin-binding 1
Add
BLAST
Domaini120 – 236117CH 1
Add
BLAST
Domaini264 – 375112CH 2
Add
BLAST
Domaini380 – 624245Actin-binding 2
Add
BLAST
Domaini394 – 503110CH 3
Add
BLAST
Domaini515 – 624110CH 4
Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiP13796.
KOiK17276.
OMAiHLYADID.
OrthoDBiEOG7K9K2D.
PhylomeDBiP13796.
TreeFamiTF300680.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
PF00036. EF-hand_1. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequencei

Sequence statusi: Complete.

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

P13796-1 [UniParc]FASTAAdd to Basket

« Hide

MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV    50
REITENLMAT GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI 100
CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT 150
NDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS 200
ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA 250
LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY 300
HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV 350
TATDVVRGNP KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF 400
RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL 450
GGNMKKLENC NYAVELGKNQ AKFSLVGIGG QDLNEGNRTL TLALIWQLMR 500
RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS FKDPKISTSL 550
PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL 600
PEDLVEVNPK MVMTVFACLM GKGMKRV 627
Length:627
Mass (Da):70,288
Last modified:October 5, 2010 - v6
Checksum:i668E4AA6A3FC7B58
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241D → E.
VAR_001371
Natural varianti533 – 5331K → E.5 Publications
Corresponds to variant rs4941543 [ dbSNP | Ensembl ].
VAR_024398
Natural varianti544 – 5441P → A.
Corresponds to variant rs17067725 [ dbSNP | Ensembl ].
VAR_030826

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti611 – 6111M → T AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9403.1.
PIRiA35836.
RefSeqiNP_002289.2. NM_002298.4.
XP_005266431.1. XM_005266374.1.
UniGeneiHs.381099.
Hs.658408.

Genome annotation databases

EnsembliENST00000323076; ENSP00000315757; ENSG00000136167.
ENST00000398576; ENSP00000381581; ENSG00000136167.
GeneIDi3936.
KEGGihsa:3936.
UCSCiuc001vaz.4. human.

Polymorphism databases

DMDMi308153685.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9403.1.
PIRi A35836.
RefSeqi NP_002289.2. NM_002298.4.
XP_005266431.1. XM_005266374.1.
UniGenei Hs.381099.
Hs.658408.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D85 NMR - A 517-627 [» ]
ProteinModelPortali P13796.
SMRi P13796. Positions 7-77, 118-627.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110128. 6 interactions.
IntActi P13796. 7 interactions.
MINTi MINT-3008082.
STRINGi 9606.ENSP00000315757.

PTM databases

PhosphoSitei P13796.

Polymorphism databases

DMDMi 308153685.

Proteomic databases

MaxQBi P13796.
PaxDbi P13796.
PRIDEi P13796.

Protocols and materials databases

DNASUi 3936.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323076 ; ENSP00000315757 ; ENSG00000136167 .
ENST00000398576 ; ENSP00000381581 ; ENSG00000136167 .
GeneIDi 3936.
KEGGi hsa:3936.
UCSCi uc001vaz.4. human.

Organism-specific databases

CTDi 3936.
GeneCardsi GC13M046700.
H-InvDB HIX0130592.
HGNCi HGNC:6528. LCP1.
HPAi CAB020673.
HPA019493.
MIMi 153430. gene.
neXtProti NX_P13796.
PharmGKBi PA30312.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOGENOMi HOG000213447.
HOVERGENi HBG003082.
InParanoidi P13796.
KOi K17276.
OMAi HLYADID.
OrthoDBi EOG7K9K2D.
PhylomeDBi P13796.
TreeFami TF300680.

Miscellaneous databases

ChiTaRSi LCP1. human.
EvolutionaryTracei P13796.
GeneWikii LCP1.
GenomeRNAii 3936.
NextBioi 15457.
PROi P13796.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13796.
Bgeei P13796.
CleanExi HS_LCP1.
Genevestigatori P13796.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF00307. CH. 4 hits.
PF00036. EF-hand_1. 1 hit.
[Graphical view ]
SMARTi SM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiPLSL_HUMAN
AccessioniPrimary (citable) accession number: P13796
Secondary accession number(s): B2R613, Q5TBN4
Entry historyi
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 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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