Plastin-2 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Plastin-2
Alternative name(s):
    L-plastin
    Lymphocyte cytosolic protein 1
      Short name=LCP-1
    LC64P

Gene names

Name:	LCP1
Synonyms:	PLS2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Actin-binding protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Tissue specificity	Restricted to the spleen and other lymph node-containing organs. Expressed in neutrophils, monocytes, B lymphocytes, and myeloid cells. Ref.9
Post-translational modification	Phosphorylated. Ref.10 Ref.11 The N-terminus is blocked.
Sequence similarities	Contains 2 actin-binding domains. Contains 4 CH (calponin-homology) domains. Contains 2 EF-hand domains.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytosol Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Ref.2 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN2	Q99700	1	EBI-698036,EBI-697691

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.6

Chain

2 – 627

626

Plastin-2

PRO_0000073743

Regions

Domain

9 – 44

36

EF-hand 1

Domain

49 – 84

36

EF-hand 2

Domain

106 – 379

274

Actin-binding 1

Domain

120 – 236

117

CH 1

Domain

264 – 375

112

CH 2

Domain

380 – 624

245

Actin-binding 2

Domain

394 – 503

110

CH 3

Domain

515 – 624

110

CH 4

Calcium binding

22 – 33

12

1 By similarity

Calcium binding

62 – 73

12

2 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

5

1

Phosphoserine By similarity

Modified residue

7

1

Phosphoserine By similarity

Modified residue

28

1

Phosphotyrosine Ref.11

Modified residue

124

1

Phosphotyrosine Ref.10

Modified residue

276

1

Phosphotyrosine Ref.11

Natural variations

Natural variant

24

1

D → E

VAR_001371

Natural variant

533

1

E → K: dbSNP rs4941543.

VAR_024398

Natural variant

544

1

P → A: dbSNP rs17067725.

VAR_030826

Experimental info

Sequence conflict

611

1

M → T AA sequence Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

P13796-1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 6E2CC08E09DC75B6
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FASTA

627

70,289

        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 EAEKSSSISS 

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

       610        620 
PEDLVEVNPK MVMTVFACLM GKGMKRV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 3211125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-627, PARTIAL PROTEIN SEQUENCE.
[2]	"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: 2378651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-140, SEQUENCE REVISION.
[3]	"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: 2252891] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Placenta.
[6]	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, MASS SPECTROMETRY. Tissue: T-cell.
[7]	"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: 8428952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627.
[8]	"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: 2111166] [Abstract] Cited for: PROTEIN SEQUENCE OF 264-283; 517-533 AND 593-609.
[9]	"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: 3261603] [Abstract] Cited for: PROTEIN SEQUENCE OF 590-611, TISSUE SPECIFICITY.
[10]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, MASS SPECTROMETRY.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND TYR-276, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

M22300 mRNA. Translation: AAB02845.1.
M34426 mRNA. Translation: AAA36184.1.
J02923 mRNA. Translation: AAA63236.1.
AK312393 mRNA. Translation: BAG35310.1.
BC007673 mRNA. Translation: AAH07673.1.
BC010271 mRNA. Translation: AAH10271.1.
L05492 Genomic DNA. Translation: AAA59529.1.

IPI

IPI00010471.

PIR

A35836.

RefSeq

NP_002289.2.

UniGene

Hs.381099
Hs.710563

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D85	NMR	-	A	517-627	[»]

SMR

P13796. Positions 117-371, 118-372.

ModBase

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Protein-protein interaction databases

IntAct

P13796. 1 interaction.

PTM databases

PhosphoSite

P13796.

Proteomic databases

PRIDE

P13796.

Genome annotation databases

Ensembl

ENSG00000136167. Homo sapiens. [Contig view]

GeneID

3936.

KEGG

hsa:3936.

Organism-specific databases

GeneCards

GC13M045598.

HGNC

HGNC:6528. LCP1.

MIM

153430. gene.

PharmGKB

PA134924593.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P13796.

HOVERGEN

P13796.

Gene expression databases

ArrayExpress

P13796.

Bgee

P13796.

CleanEx

HS_LCP1.

GermOnline

ENSG00000136167. Homo sapiens.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. Calponin_act_bd.
IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 4 hits.
G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00307. CH. 4 hits.
PF00036. efhand. 2 hits.
[Graphical view]

ProDom

PD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

SOURCE

Search...

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Entry information

Entry name

PLSL_HUMAN

Accession

Primary (citable) accession number: P13796
Secondary accession number(s): B2R613

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 26, 2009
This is version 118 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 13

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents