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P13796

- PLSL_HUMAN

UniProt

P13796 - PLSL_HUMAN

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Protein

Plastin-2

Gene

LCP1

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 – 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
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 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: UniProtKB
  8. filopodium Source: UniProt
  9. focal adhesion Source: UniProt
  10. phagocytic cup Source: Ensembl
  11. plasma membrane Source: HPA
  12. ruffle Source: UniProt
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-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

BgeeiP13796.
CleanExiHS_LCP1.
ExpressionAtlasiP13796. baseline and differential.
GenevestigatoriP13796.

Organism-specific databases

HPAiCAB020673.
HPA019493.

Interactioni

Subunit structurei

Monomer. Interacts with AIF1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi110128. 8 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 – 53213Combined sources
Helixi545 – 5484Combined sources
Helixi550 – 55910Combined sources
Turni566 – 5683Combined sources
Helixi576 – 59318Combined sources
Helixi601 – 6044Combined sources
Turni605 – 6073Combined sources
Helixi609 – 6124Combined sources
Helixi615 – 6206Combined sources
Turni621 – 6233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000005691.
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

        10         20         30         40         50
MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV
60 70 80 90 100
REITENLMAT GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI
110 120 130 140 150
CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT
160 170 180 190 200
NDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS
210 220 230 240 250
ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA
260 270 280 290 300
LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY
310 320 330 340 350
HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV
360 370 380 390 400
TATDVVRGNP KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF
410 420 430 440 450
RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL
460 470 480 490 500
GGNMKKLENC NYAVELGKNQ AKFSLVGIGG QDLNEGNRTL TLALIWQLMR
510 520 530 540 550
RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS FKDPKISTSL
560 570 580 590 600
PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL
610 620
PEDLVEVNPK MVMTVFACLM GKGMKRV
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:
EMBLi
GenBanki
DDBJi
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. [P13796-1]
PIRiA35836.
RefSeqiNP_002289.2. NM_002298.4. [P13796-1]
XP_005266431.1. XM_005266374.1. [P13796-1]
UniGeneiHs.381099.
Hs.658408.

Genome annotation databases

EnsembliENST00000323076; ENSP00000315757; ENSG00000136167. [P13796-1]
ENST00000398576; ENSP00000381581; ENSG00000136167. [P13796-1]
GeneIDi3936.
KEGGihsa:3936.
UCSCiuc001vaz.4. human. [P13796-1]

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:
EMBLi
GenBanki
DDBJi
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. [P13796-1 ]
PIRi A35836.
RefSeqi NP_002289.2. NM_002298.4. [P13796-1 ]
XP_005266431.1. XM_005266374.1. [P13796-1 ]
UniGenei Hs.381099.
Hs.658408.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 8 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 . [P13796-1 ]
ENST00000398576 ; ENSP00000381581 ; ENSG00000136167 . [P13796-1 ]
GeneIDi 3936.
KEGGi hsa:3936.
UCSCi uc001vaz.4. human. [P13796-1 ]

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.
GeneTreei ENSGT00390000005691.
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

Bgeei P13796.
CleanExi HS_LCP1.
ExpressionAtlasi P13796. baseline and differential.
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] (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: November 26, 2014
This is version 174 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

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