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P13796

- PLSL_HUMAN

UniProt

P13796 - PLSL_HUMAN

Protein

Plastin-2

Gene

LCP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 6 (05 Oct 2010)
      Previous versions | rss
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    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 – 33121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi62 – 73122PROSITE-ProRule annotationAdd
    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. actin filament bundle assembly Source: UniProt
    2. cell migration Source: UniProt
    3. organ regeneration Source: Ensembl
    4. protein kinase A signaling Source: UniProt
    5. regulation of intracellular protein transport Source: UniProtKB
    6. T cell activation involved in immune response Source: UniProtKB

    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 By similarity; Peripheral membrane protein By similarity; 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.By similarity

    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

    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-2PRO_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.5 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.By similarity

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    627
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13796.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 2 actin-binding domains.Curated
    Contains 4 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 2 EF-hand domains.PROSITE-ProRule annotation

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13796-1) [UniParc]FASTAAdd to Basket

    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

    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
    Isoform 2 (identifier: P13796-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MARGSVSDEEMMELREAFAKVDTDG → MCAEDGDSKFSMSISMNSPFLEILH
         26-456: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:196
    Mass (Da):21,792
    Checksum:i06D5580FBCC9F5E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti611 – 6111M → T AA sequence (PubMed:3261603)Curated

    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MARGS…VDTDG → MCAEDGDSKFSMSISMNSPF LEILH in isoform 2. 1 PublicationVSP_056450Add
    BLAST
    Alternative sequencei26 – 456431Missing in isoform 2. 1 PublicationVSP_056451Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02923 mRNA. Translation: AAA63236.1.
    AK300556 mRNA. Translation: BAG62262.1.
    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.
    ENST00000435666; ENSP00000405134; ENSG00000136167.
    GeneIDi3936.
    KEGGihsa:3936.
    UCSCiuc001vaz.4. human.

    Polymorphism databases

    DMDMi308153685.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02923 mRNA. Translation: AAA63236.1 .
    AK300556 mRNA. Translation: BAG62262.1 .
    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 .
    ENST00000435666 ; ENSP00000405134 ; 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

    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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2), VARIANT GLU-533.
      Tissue: Amygdala and Prostate.
    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] (ISOFORM 1), 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 (ISOFORM 1), 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 (ISOFORM 1), 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, B4DUA0, Q5TBN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 172 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