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P13797

- PLST_HUMAN

UniProt

P13797 - PLST_HUMAN

Protein

Plastin-3

Gene

PLS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi25 – 36121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi65 – 76122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. bone development Source: UniProtKB

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plastin-3
    Alternative name(s):
    T-plastin
    Gene namesi
    Name:PLS3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9091. PLS3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti253 – 2531A → AN in OSTEOP; associated with disease susceptibility. 1 Publication
    VAR_070278

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi166710. phenotype.
    300910. phenotype.
    Orphaneti391330. X-linked osteoporosis with fractures.
    PharmGKBiPA33418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630Plastin-3PRO_0000073747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki168 – 168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei293 – 2931Phosphoserine1 Publication
    Modified residuei326 – 3261Phosphoserine2 Publications
    Modified residuei391 – 3911Phosphothreonine2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP13797.
    PaxDbiP13797.
    PRIDEiP13797.

    PTM databases

    PhosphoSiteiP13797.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP13797.
    BgeeiP13797.
    CleanExiHS_PLS3.
    GenevestigatoriP13797.

    Organism-specific databases

    HPAiHPA020433.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi111372. 25 interactions.
    IntActiP13797. 10 interactions.
    MINTiMINT-3008106.
    STRINGi9606.ENSP00000348163.

    Structurei

    Secondary structure

    1
    630
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi123 – 13614
    Turni137 – 1393
    Turni144 – 1463
    Turni151 – 1544
    Helixi155 – 1595
    Helixi160 – 1623
    Helixi164 – 17310
    Helixi180 – 1823
    Helixi190 – 20617
    Helixi216 – 2205
    Helixi224 – 24421
    Helixi261 – 2655
    Helixi269 – 28315
    Turni294 – 2985
    Helixi300 – 30910
    Beta strandi315 – 3173
    Turni326 – 3294
    Helixi333 – 34412
    Turni345 – 3484
    Helixi355 – 3595
    Helixi363 – 37412
    Helixi522 – 53514
    Helixi549 – 5513
    Helixi553 – 56210
    Turni569 – 5713
    Helixi579 – 59517
    Helixi604 – 6096
    Turni612 – 6165
    Helixi617 – 6259

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AOAX-ray2.40A101-375[»]
    1WJONMR-A520-630[»]
    ProteinModelPortaliP13797.
    SMRiP13797. Positions 15-83, 121-375, 399-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13797.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 4736EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini52 – 8736EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini109 – 382274Actin-binding 1Add
    BLAST
    Domaini123 – 239117CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 378112CH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini383 – 627245Actin-binding 2Add
    BLAST
    Domaini397 – 506110CH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini518 – 627110CH 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.
    InParanoidiP13797.
    KOiK17336.
    OMAiEPQIDIN.
    PhylomeDBiP13797.
    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.
    PF13499. EF-hand_7. 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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13797-1) [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

    MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG    50
    YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK 100
    EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN 150
    PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA 200
    LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA 250
    LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK 300
    AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR 350
    QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE 400
    RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY 450
    PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ 500
    LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS 550
    SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV 600
    YALPEDLVEV KPKMVMTVFA CLMGRGMKRV 630
    Length:630
    Mass (Da):70,811
    Last modified:April 14, 2009 - v4
    Checksum:i631E6F803DC56A56
    GO
    Isoform 2 (identifier: P13797-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MDEMATTQISKDELDELKEAFAKV → ME
         296-296: I → IKLIDFSNSV

    Note: No experimental confirmation available.

    Show »
    Length:617
    Mass (Da):69,350
    Checksum:i7DD45809B012DE95
    GO
    Isoform 3 (identifier: P13797-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:585
    Mass (Da):65,632
    Checksum:i9291617EAC62FA5F
    GO

    Sequence cautioni

    The sequence CAI39884.1 differs from that shown. Reason: Erroneous initiation.

    Polymorphismi

    Genetic variations in PLS3 define the bone mineral density quantitative trait locus 18 (BMND18) [MIMi:300910]. Variance in bone mineral density influences bone mass, contributes to size determination in the general population, and is a susceptibility factor for osteoporotic fractures.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti253 – 2531A → AN in OSTEOP; associated with disease susceptibility. 1 Publication
    VAR_070278
    Natural varianti488 – 4881D → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035462

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4545Missing in isoform 3. CuratedVSP_056235Add
    BLAST
    Alternative sequencei1 – 2424MDEMA…AFAKV → ME in isoform 2. 1 PublicationVSP_056236Add
    BLAST
    Alternative sequencei296 – 2961I → IKLIDFSNSV in isoform 2. 1 PublicationVSP_056237

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22299 mRNA. Translation: AAB02844.1.
    M34427 mRNA. Translation: AAA36759.1.
    AK291194 mRNA. Translation: BAF83883.1.
    AK294509 mRNA. Translation: BAG57725.1.
    AK300575 mRNA. Translation: BAH13307.1.
    AK312391 mRNA. Translation: BAG35308.1.
    AC003983 Genomic DNA. No translation available.
    AL589842, AC005000 Genomic DNA. Translation: CAI39884.1. Different initiation.
    CH471120 Genomic DNA. Translation: EAX02614.1.
    BC039049 mRNA. Translation: AAH39049.1.
    BC056898 mRNA. Translation: AAH56898.1.
    L05491 Genomic DNA. Translation: AAA61214.1.
    CCDSiCCDS14568.1.
    PIRiA34789.
    RefSeqiNP_001129497.1. NM_001136025.4.
    NP_001165806.1. NM_001172335.2.
    NP_001269266.1. NM_001282337.1.
    NP_001269267.1. NM_001282338.1.
    NP_005023.2. NM_005032.6.
    UniGeneiHs.496622.

    Genome annotation databases

    EnsembliENST00000355899; ENSP00000348163; ENSG00000102024.
    ENST00000420625; ENSP00000398945; ENSG00000102024.
    ENST00000537301; ENSP00000445105; ENSG00000102024.
    ENST00000539310; ENSP00000445339; ENSG00000102024.
    GeneIDi5358.
    KEGGihsa:5358.
    UCSCiuc004eqd.3. human.

    Polymorphism databases

    DMDMi226694201.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22299 mRNA. Translation: AAB02844.1 .
    M34427 mRNA. Translation: AAA36759.1 .
    AK291194 mRNA. Translation: BAF83883.1 .
    AK294509 mRNA. Translation: BAG57725.1 .
    AK300575 mRNA. Translation: BAH13307.1 .
    AK312391 mRNA. Translation: BAG35308.1 .
    AC003983 Genomic DNA. No translation available.
    AL589842 , AC005000 Genomic DNA. Translation: CAI39884.1 . Different initiation.
    CH471120 Genomic DNA. Translation: EAX02614.1 .
    BC039049 mRNA. Translation: AAH39049.1 .
    BC056898 mRNA. Translation: AAH56898.1 .
    L05491 Genomic DNA. Translation: AAA61214.1 .
    CCDSi CCDS14568.1.
    PIRi A34789.
    RefSeqi NP_001129497.1. NM_001136025.4.
    NP_001165806.1. NM_001172335.2.
    NP_001269266.1. NM_001282337.1.
    NP_001269267.1. NM_001282338.1.
    NP_005023.2. NM_005032.6.
    UniGenei Hs.496622.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AOA X-ray 2.40 A 101-375 [» ]
    1WJO NMR - A 520-630 [» ]
    ProteinModelPortali P13797.
    SMRi P13797. Positions 15-83, 121-375, 399-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111372. 25 interactions.
    IntActi P13797. 10 interactions.
    MINTi MINT-3008106.
    STRINGi 9606.ENSP00000348163.

    PTM databases

    PhosphoSitei P13797.

    Polymorphism databases

    DMDMi 226694201.

    Proteomic databases

    MaxQBi P13797.
    PaxDbi P13797.
    PRIDEi P13797.

    Protocols and materials databases

    DNASUi 5358.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355899 ; ENSP00000348163 ; ENSG00000102024 .
    ENST00000420625 ; ENSP00000398945 ; ENSG00000102024 .
    ENST00000537301 ; ENSP00000445105 ; ENSG00000102024 .
    ENST00000539310 ; ENSP00000445339 ; ENSG00000102024 .
    GeneIDi 5358.
    KEGGi hsa:5358.
    UCSCi uc004eqd.3. human.

    Organism-specific databases

    CTDi 5358.
    GeneCardsi GC0XP114795.
    HGNCi HGNC:9091. PLS3.
    HPAi HPA020433.
    MIMi 166710. phenotype.
    300131. gene.
    300910. phenotype.
    neXtProti NX_P13797.
    Orphaneti 391330. X-linked osteoporosis with fractures.
    PharmGKBi PA33418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000213447.
    HOVERGENi HBG003082.
    InParanoidi P13797.
    KOi K17336.
    OMAi EPQIDIN.
    PhylomeDBi P13797.
    TreeFami TF300680.

    Miscellaneous databases

    ChiTaRSi PLS3. human.
    EvolutionaryTracei P13797.
    GeneWikii PLS3.
    GenomeRNAii 5358.
    NextBioi 20770.
    PROi P13797.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13797.
    Bgeei P13797.
    CleanExi HS_PLS3.
    Genevestigatori P13797.

    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.
    PF13499. EF-hand_7. 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. "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] (ISOFORM 1), 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] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "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).
      Tissue: Amygdala.
    4. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Placenta and Skin.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 588-630.
    8. "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] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168.
      Tissue: Mammary cancer.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-326 AND THR-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: POSSIBLE FUNCTION AS REGULATOR OF BONE DEVELOPMENT, POLYMORPHISM, VARIANT OSTEOP ASN-253 INS.
    14. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-375.
    15. "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.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-488.

    Entry informationi

    Entry nameiPLST_HUMAN
    AccessioniPrimary (citable) accession number: P13797
    Secondary accession number(s): A8K579
    , B1AQ09, B4DGB4, B7Z6M1, Q86YI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 163 of the entry and version 4 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 X
      Human chromosome X: 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