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Reviewed, UniProtKB/Swiss-Prot P13797 (PLST_HUMAN)

Last modified January 19, 2010. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Plastin-3
Alternative name(s):
    T-plastin
Gene names
Name: PLS3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in a variety of organs, including muscle, brain, uterus and esophagus.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9

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 componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandActin-binding
Calcium
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN2Q997001EBI-698052,EBI-697691
HLA-BP304801EBI-698052,EBI-1054175
IKBKEQ141641EBI-698052,EBI-307369

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Plastin-3
PRO_0000073747

Regions

Domain12 – 4736EF-hand 1
Domain52 – 8736EF-hand 2
Domain109 – 382274Actin-binding 1
Domain123 – 239117CH 1
Domain267 – 378112CH 2
Domain383 – 627245Actin-binding 2
Domain397 – 506110CH 3
Domain518 – 627110CH 4
Calcium binding25 – 36121 By similarity
Calcium binding65 – 76122 By similarity

Amino acid modifications

Modified residue1171Phosphothreonine Ref.7
Modified residue3261Phosphoserine Ref.9
Modified residue3911Phosphothreonine Ref.9
Modified residue4771Phosphoserine Ref.8
Modified residue4921Phosphothreonine Ref.8
Cross-link168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Natural variations

Natural variant4881D → A in a breast cancer sample; somatic mutation. Ref.13
VAR_035462

Secondary structure

1 ...................................................... 630
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13797-1 [UniParc].

Last modified April 14, 2009. Version 4.
Checksum: 631E6F803DC56A56

FASTA63070,811
        10         20         30         40         50         60 
MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL 

        70         80         90        100        110        120 
MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS 

       130        140        150        160        170        180 
YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE 

       190        200        210        220        230        240 
RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF 

       250        260        270        280        290        300 
ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK 

       310        320        330        340        350        360 
AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS 

       370        380        390        400        410        420 
GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY 

       430        440        450        460        470        480 
ADLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KHPAKFSLVG 

       490        500        510        520        530        540 
IGGQDLNDGN QTLTLALVWQ LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS 

       550        560        570        580        590        600 
IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV 

       610        620        630 
YALPEDLVEV KPKMVMTVFA CLMGRGMKRV

« Hide

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References

« Hide '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], 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: SEQUENCE REVISION.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Placenta and Skin.
[5]"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 588-630.
[6]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168, MASS SPECTROMETRY.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117, MASS SPECTROMETRY.
[8]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND THR-492, MASS SPECTROMETRY.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-391, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"The structure of an actin-crosslinking domain from human fimbrin."
Goldsmith S.C., Pokala N., Shen W., Fedorov A.A., Matsudaira P., Almo S.C.
Nat. Struct. Biol. 4:708-712(1997) [PubMed: 9302997] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-375.
[12]"Solution structure of the fourth CH domain from human plastin 3 T-isoform."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 520-630.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-488.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22299 mRNA. Translation: AAB02844.1.
M34427 mRNA. Translation: AAA36759.1.
AL589842, AC005000 Genomic DNA. Translation: CAI39884.1. Different initiation.
BC039049 mRNA. Translation: AAH39049.1.
BC056898 mRNA. Translation: AAH56898.1.
L05491 Genomic DNA. Translation: AAA61214.1.
IPIIPI00216694.
PIRA34789.
RefSeqNP_001129497.1.
NP_005023.2.
UniGeneHs.496622

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOAX-ray2.40A101-375[»]
1WJONMR-A520-627[»]
SMRP13797. Positions 14-103, 122-624.
ModBaseSearch...

Protein-protein interaction databases

IntActP13797. 10 interactions.
STRINGP13797.

PTM databases

PhosphoSiteP13797.

Proteomic databases

PRIDEP13797.

Genome annotation databases

EnsemblENST00000355899; ENSP00000348163; ENSG00000102024; Homo sapiens. [Genome view]
ENST00000420625; ENSP00000398945; ENSG00000102024; Homo sapiens. [Genome view]
GeneID5358.
KEGGhsa:5358.

Organism-specific databases

CTD5358.
GeneCardsGC0XP114618.
H-InvDBHIX0028362.
HGNCHGNC:9091. PLS3.
MIM300131. gene.
PharmGKBPA33418.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16165.
HOGENOMHBG316743.
HOVERGENP13797.
InParanoidP13797.
OMAMLQQADR.
OrthoDBEOG96X1TN.
PhylomeDBP13797.

Gene expression databases

ArrayExpressP13797.
BgeeP13797.
CleanExHS_PLS3.
GenevestigatorP13797.
GermOnlineENSG00000102024. Homo sapiens.

Family and domain databases

InterProIPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 4 hits.
G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF00307. CH. 4 hits.
[Graphical view]
SMARTSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00019. ACTININ_1. 2 hits.
PS00020. ACTININ_2. 2 hits.
PS50021. CH. 4 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20770.
SOURCESearch...

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Entry information

Entry namePLST_HUMAN
AccessionPrimary (citable) accession number: P13797
Secondary accession number(s): B1AQ09, Q86YI6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 14, 2009
Last modified: January 19, 2010
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents