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Q9ET54

- PALLD_MOUSE

UniProt

Q9ET54 - PALLD_MOUSE

Protein

Palladin

Gene

Palld

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific May be required for the initiation of neural tube closure.4 Publications

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Palladin
    Gene namesi
    Name:Palld
    Synonyms:Kiaa0992
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1919583. Palld.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell junctionfocal adhesion 1 Publication. Cell projectionruffle 1 Publication. Cell projectionlamellipodium 1 Publication. CytoplasmmyofibrilsarcomereZ line 1 Publication
    Note: Localizes to stress fibers and Z lines.

    GO - Cellular componenti

    1. actin filament Source: HGNC
    2. focal adhesion Source: UniProtKB-SubCell
    3. lamellipodium Source: UniProtKB-SubCell
    4. nucleus Source: HGNC
    5. ruffle Source: UniProtKB-SubCell
    6. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Disruption phenotypei

    Death around E15.5 due to severe neural tube closure defects and herniation of liver and intestine. Palld-deficient mouse embryonic fibroblasts display disorganized actin cytoskeleton, decreased polymerized filament actin, and decreased cell adhesion and compromised cell spreading on various extracellular matrix. Mice embryos lacking Palld exhibit defects in erythropoiesis.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14081408PalladinPRO_0000302721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi299 ↔ 351PROSITE-ProRule annotation
    Disulfide bondi469 ↔ 528PROSITE-ProRule annotation
    Modified residuei700 – 7001PhosphoserineBy similarity
    Modified residuei704 – 7041PhosphoserineBy similarity
    Modified residuei901 – 9011Phosphoserine2 Publications
    Modified residuei1004 – 10041PhosphoserineBy similarity
    Modified residuei1009 – 10091PhosphoserineBy similarity
    Modified residuei1126 – 11261PhosphoserineBy similarity
    Modified residuei1129 – 11291PhosphoserineBy similarity
    Modified residuei1131 – 11311PhosphoserineBy similarity
    Modified residuei1141 – 11411PhosphoserineBy similarity
    Modified residuei1143 – 11431Phosphoserine; by PKB/AKT12 Publications
    Modified residuei1146 – 11461Phosphoserine2 Publications
    Disulfide bondi1181 ↔ 1233PROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated predominantly on serines and, to a lesser extent, on tyrosines. Phosphorylation at Ser-1143 by PKB/AKT1 modulates cytoskeletal organization and cell motility By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ET54.
    PaxDbiQ9ET54.
    PRIDEiQ9ET54.

    PTM databases

    PhosphoSiteiQ9ET54.

    Expressioni

    Tissue specificityi

    Detected in both muscle and non-muscle tissues and cells (at protein level). Isoform 3 is widely expressed, isoform 4 is particularly abundant in tissues rich in smooth muscle and in the cardiac muscle and isoform 1 is detected in heart.2 Publications

    Developmental stagei

    Ubiquitously detected in embryonic tissues, and down-regulated in certain adult tissues (at protein level). Isoform 3 is widely expressed in embryonic tissues (at protein level). In adults is detected in spleen and gut, and is almost undetectable in heart, skeletal muscle, liver, and kidney (at protein level). Isoform 4 is widely expressed in neonatal tissues (brain, heart, lung, stomach, intestine, kidney, bone and skin) (at protein level). Late in development expression is restricted to cardiac muscle and to organs rich in smooth muscle (at protein level). Isoform 1 is detected in neonatal striated muscle and bone, and remains highly expressed in adult skeletal and cardiac muscle (at protein level). Adult brain express an isoform of 80-85 kDa. At E8.5 is mainly expressed the rostral and caudal part of neural plate. No expression is detected in somite. At E9.5 and E10.5 is ubiquitously detected.2 Publications

    Gene expression databases

    ArrayExpressiQ9ET54.
    BgeeiQ9ET54.
    CleanExiMM_PALLD.
    GenevestigatoriQ9ET54.

    Interactioni

    Subunit structurei

    Interacts with ACTN, ARGBP2, LPP, PFN1, SPIN90, SRC and EZR By similarity. Interacts with EPS8, LASP1 and VASP.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi215316. 1 interaction.
    IntActiQ9ET54. 2 interactions.
    MINTiMINT-4129416.

    Structurei

    Secondary structure

    1
    1408
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1035 – 10384
    Beta strandi1043 – 10486
    Beta strandi1058 – 10614
    Beta strandi1071 – 10777
    Beta strandi1081 – 10899
    Turni1092 – 10943
    Beta strandi1096 – 11016
    Beta strandi1114 – 11185

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LQRNMR-A1022-1126[»]
    ProteinModelPortaliQ9ET54.
    SMRiQ9ET54. Positions 270-545, 1022-1393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini278 – 36790Ig-like C2-type 1Add
    BLAST
    Domaini448 – 54699Ig-like C2-type 2Add
    BLAST
    Domaini1026 – 111085Ig-like C2-type 3Add
    BLAST
    Domaini1160 – 125192Ig-like C2-type 4Add
    BLAST
    Domaini1259 – 134991Ig-like C2-type 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni569 – 5735Interaction with VASP
    Regioni653 – 68331Interaction with LASP1Add
    BLAST
    Regioni683 – 71331Interaction with ARGBP2, SPIN90 and SRCBy similarityAdd
    BLAST
    Regioni782 – 84261Interaction with EPS8Add
    BLAST
    Regioni807 – 84236Interaction with ARGBP2, SPIN90, SRC and PFN1By similarityAdd
    BLAST
    Regioni830 – 8345Interaction with VASP
    Regioni1162 – 125190Interaction with EZRBy similarityAdd
    BLAST
    Regioni1261 – 135191Interaction with EZRBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi570 – 5745Poly-Pro
    Compositional biasi640 – 872233Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the myotilin/palladin family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiNOG136920.
    GeneTreeiENSGT00690000101977.
    HOGENOMiHOG000028074.
    HOVERGENiHBG059166.
    InParanoidiQ9ET54.
    OMAiTPRVRWF.
    OrthoDBiEOG77WWBP.
    PhylomeDBiQ9ET54.
    TreeFamiTF343193.

    Family and domain databases

    Gene3Di2.60.40.10. 6 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    [Graphical view]
    PfamiPF07679. I-set. 5 hits.
    [Graphical view]
    SMARTiSM00408. IGc2. 5 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 5 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ET54-1) [UniParc]FASTAAdd to Basket

    Also known as: 200 kDa isoform

    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

    MSETSSHDSF YDSLSDVQEE GKSADFFPGL SAFLSQEEIN KSLDLARRAI     50
    DSSETEDFDS EKEISQIFSK SPISLCETPS HEEPKSGKQT SSERPQDSRR 100
    APVQPLTGDQ AERITSPGSK RKPGVSPLLA SPSYIRSLRK AEKRGAKNPN 150
    PSSKPKTAQQ SKAGPQSQLC DKAASFIEEL TSIFREAAKP RNRSPNGESS 200
    SPDSGYLSPK NQPSALMSAS ASQSPTADQL DQLEMDAEVK QAQGSLCYQA 250
    HQASEETLPL AHIPHPQPQK ARHLPTAPRF IQKLRSQEVA EGSRVYLECR 300
    VTGNPTPRVR WFCEGKELYN SPDVQIHCES GELHTLVIAE AFEDDTGRYT 350
    CLATNPSGSD STSAEVFIEG ASSTDSDSES LSFISKAGAM PQAQKKTTSV 400
    SLTIGSSAPK TGVTTAVIQP LSVPVQQAHS ATSYLCRPDG TTMGCLLPVF 450
    TKELQNTAAS EGQVVVLECR VRGAPPLQVQ WFRQGSEIQD SPDFRILQKK 500
    PRSTAEPEEI CTLVIAESFP EDAGIFTCSA TNDYGSVTST AQLVITSANN 550
    ENCSYDSTGE PNSDHFQHFP PPPPILETGS YELASQKPSE IQQVNSPNLG 600
    FSMAALQMQF NTAERETNGV HPSHGVNGLI NGKAYGNKSP PTPTALLSPT 650
    KEPPPLLAKP KLDPLKLQQL QNQVRLEQEA CAWPPAPPGV PCNSSSSGSS 700
    APPSPPFPPP PPAFPELAAC ASPVPSEPMS ALASRATAMQ SSGSFNYARP 750
    KQFIAAQNLG PASGLPTPTS SPSSSSLPSP LSPTPRPFGR APGPPFVEPE 800
    AMWGPSSPSP PPPPPPVFSP SAAYPVPDVF PLPPPPPPLP SSTSHCASPA 850
    RFGPSQTPAA FLSALLPSQP PPVAVNALGL PKGVTPAGFP KKSSRTARIA 900
    SDEEIQGTKD AVIQDLERKL RFKEDLLNNG QPRLTYEERM ARRLLGADSA 950
    NVFNIQEPEE TAANQDAGAP RASVGGPLDG QKEYKVSSCE QRLISEIEYR 1000
    LERSPVDESG DEVQDPDVPV ENATAPFFEM KLKHYKIFEG MPVTFTCRVA 1050
    GNPKPKIYWF KDGKQISPKS DHYTIQRDLD GTCSLHTTAS TLDDDGNYTI 1100
    MAANPQGRVS CTGRLMVQAV NQRGRSPRSP SGHPHARRPR SRSRDSGDEN 1150
    EPIQERFFRP HFLQAPGDLT VQEGKLCRMD CKVSGLPTPD LSWQLDGKPI 1200
    RPDSAHKMLV RENGVHSLII EPVTSRDAGI YTCIATNRAG QNSFNLELVV 1250
    AAKEAHKAPV FMEKLQNTGV ADGYPVRLEC RVSGVPPPQI FWKKENESLT 1300
    HSTERVSMHQ DNHGYICLLI QGATKEDAGW YTVSAKNEAG IVSCTARLDV 1350
    YTQWHQQPQT TKPKKVRPSA SRYAALSDQG LDIKAAFQPE ASPSHLTLNS 1400
    GLVESEDL 1408
    Length:1,408
    Mass (Da):152,131
    Last modified:September 11, 2007 - v2
    Checksum:i5BCF647C110619C9
    GO
    Isoform 2 (identifier: Q9ET54-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         663-887: Missing.
         966-982: Missing.
         1352-1408: TQWHQQPQTTKPKKVRPSASRYAALSDQGLDIKAAFQPEASPSHLTLNSGLVESEDL → ISRH

    Show »
    Length:1,113
    Mass (Da):122,090
    Checksum:i2E4249532BDEACEB
    GO
    Isoform 3 (identifier: Q9ET54-3) [UniParc]FASTAAdd to Basket

    Also known as: 90 kDa isoform, 3Ig isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         1-728: Missing.
         966-982: Missing.

    Show »
    Length:663
    Mass (Da):72,368
    Checksum:i87C70C4EDC263B5E
    GO
    Isoform 4 (identifier: Q9ET54-4) [UniParc]FASTAAdd to Basket

    Also known as: 140 kDa isoform, 4Ig isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         1-389: Missing.
         966-982: Missing.

    Show »
    Length:1,002
    Mass (Da):108,287
    Checksum:i5E630ABBBF42CB74
    GO
    Isoform 5 (identifier: Q9ET54-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-738: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:670
    Mass (Da):72,985
    Checksum:iCCF8E48D7ADEDDD6
    GO
    Isoform 6 (identifier: Q9ET54-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         966-982: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,391
    Mass (Da):150,553
    Checksum:iFF63541E07E7E676
    GO

    Sequence cautioni

    The sequence AK031696 differs from that shown. Reason: Frameshift at position 821.
    The sequence BAB26871.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1022 – 10221N → K in AK031696. (PubMed:16141072)Curated
    Sequence conflicti1053 – 10531P → T in AK031696. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 738738Missing in isoform 5. 1 PublicationVSP_027931Add
    BLAST
    Alternative sequencei1 – 728728Missing in isoform 3. CuratedVSP_027932Add
    BLAST
    Alternative sequencei1 – 389389Missing in isoform 4. CuratedVSP_027933Add
    BLAST
    Alternative sequencei663 – 887225Missing in isoform 2. CuratedVSP_027934Add
    BLAST
    Alternative sequencei966 – 98217Missing in isoform 2, isoform 3, isoform 4 and isoform 6. 3 PublicationsVSP_027935Add
    BLAST
    Alternative sequencei1352 – 140857TQWHQ…ESEDL → ISRH in isoform 2. CuratedVSP_027936Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC121881 Genomic DNA. No translation available.
    AC139846 Genomic DNA. No translation available.
    AC147616 Genomic DNA. No translation available.
    BC076588 mRNA. Translation: AAH76588.1.
    BC127081 mRNA. Translation: AAI27082.1.
    AK173081 mRNA. Translation: BAD32359.1.
    AF205078 mRNA. Translation: AAG00078.1.
    AK010350 mRNA. Translation: BAB26871.1. Different initiation.
    AK031696 mRNA. No translation available.
    CCDSiCCDS40350.1. [Q9ET54-2]
    RefSeqiNP_001074859.1. NM_001081390.1. [Q9ET54-2]
    XP_006509564.1. XM_006509501.1. [Q9ET54-1]
    XP_006509565.1. XM_006509502.1. [Q9ET54-1]
    XP_006509566.1. XM_006509503.1. [Q9ET54-6]
    XP_006509569.1. XM_006509506.1. [Q9ET54-4]
    XP_006509572.1. XM_006509509.1. [Q9ET54-3]
    UniGeneiMm.29933.
    Mm.458226.

    Genome annotation databases

    EnsembliENSMUST00000034057; ENSMUSP00000034057; ENSMUSG00000058056. [Q9ET54-2]
    ENSMUST00000121200; ENSMUSP00000112374; ENSMUSG00000058056. [Q9ET54-3]
    ENSMUST00000121493; ENSMUSP00000113874; ENSMUSG00000058056. [Q9ET54-4]
    ENSMUST00000121785; ENSMUSP00000112442; ENSMUSG00000058056. [Q9ET54-1]
    GeneIDi72333.
    KEGGimmu:72333.
    UCSCiuc009lud.1. mouse. [Q9ET54-3]
    uc009lue.1. mouse. [Q9ET54-4]
    uc009luf.1. mouse. [Q9ET54-1]
    uc009lug.2. mouse. [Q9ET54-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC121881 Genomic DNA. No translation available.
    AC139846 Genomic DNA. No translation available.
    AC147616 Genomic DNA. No translation available.
    BC076588 mRNA. Translation: AAH76588.1 .
    BC127081 mRNA. Translation: AAI27082.1 .
    AK173081 mRNA. Translation: BAD32359.1 .
    AF205078 mRNA. Translation: AAG00078.1 .
    AK010350 mRNA. Translation: BAB26871.1 . Different initiation.
    AK031696 mRNA. No translation available.
    CCDSi CCDS40350.1. [Q9ET54-2 ]
    RefSeqi NP_001074859.1. NM_001081390.1. [Q9ET54-2 ]
    XP_006509564.1. XM_006509501.1. [Q9ET54-1 ]
    XP_006509565.1. XM_006509502.1. [Q9ET54-1 ]
    XP_006509566.1. XM_006509503.1. [Q9ET54-6 ]
    XP_006509569.1. XM_006509506.1. [Q9ET54-4 ]
    XP_006509572.1. XM_006509509.1. [Q9ET54-3 ]
    UniGenei Mm.29933.
    Mm.458226.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LQR NMR - A 1022-1126 [» ]
    ProteinModelPortali Q9ET54.
    SMRi Q9ET54. Positions 270-545, 1022-1393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215316. 1 interaction.
    IntActi Q9ET54. 2 interactions.
    MINTi MINT-4129416.

    PTM databases

    PhosphoSitei Q9ET54.

    Proteomic databases

    MaxQBi Q9ET54.
    PaxDbi Q9ET54.
    PRIDEi Q9ET54.

    Protocols and materials databases

    DNASUi 72333.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034057 ; ENSMUSP00000034057 ; ENSMUSG00000058056 . [Q9ET54-2 ]
    ENSMUST00000121200 ; ENSMUSP00000112374 ; ENSMUSG00000058056 . [Q9ET54-3 ]
    ENSMUST00000121493 ; ENSMUSP00000113874 ; ENSMUSG00000058056 . [Q9ET54-4 ]
    ENSMUST00000121785 ; ENSMUSP00000112442 ; ENSMUSG00000058056 . [Q9ET54-1 ]
    GeneIDi 72333.
    KEGGi mmu:72333.
    UCSCi uc009lud.1. mouse. [Q9ET54-3 ]
    uc009lue.1. mouse. [Q9ET54-4 ]
    uc009luf.1. mouse. [Q9ET54-1 ]
    uc009lug.2. mouse. [Q9ET54-2 ]

    Organism-specific databases

    CTDi 23022.
    MGIi MGI:1919583. Palld.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG136920.
    GeneTreei ENSGT00690000101977.
    HOGENOMi HOG000028074.
    HOVERGENi HBG059166.
    InParanoidi Q9ET54.
    OMAi TPRVRWF.
    OrthoDBi EOG77WWBP.
    PhylomeDBi Q9ET54.
    TreeFami TF343193.

    Miscellaneous databases

    ChiTaRSi PALLD. mouse.
    NextBioi 336044.
    PROi Q9ET54.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ET54.
    Bgeei Q9ET54.
    CleanExi MM_PALLD.
    Genevestigatori Q9ET54.

    Family and domain databases

    Gene3Di 2.60.40.10. 6 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    [Graphical view ]
    Pfami PF07679. I-set. 5 hits.
    [Graphical view ]
    SMARTi SM00408. IGc2. 5 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1408 (ISOFORM 6).
      Strain: C57BL/6.
      Tissue: Eye.
    3. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
      DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1408 (ISOFORM 6).
      Tissue: Embryonic tail.
    4. "Characterization of palladin, a novel protein localized to stress fibers and cell adhesions."
      Parast M.M., Otey C.A.
      J. Cell Biol. 150:643-656(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 900-1408 (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
      Strain: Swiss Webster / NIH.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1015-1408 (ISOFORM 1).
      Strain: C57BL/6J.
    6. "Palladin is expressed preferentially in excitatory terminals in the rat central nervous system."
      Hwang S.J., Pagliardini S., Boukhelifa M., Parast M.M., Otey C.A., Rustioni A., Valtschanoff J.G.
      J. Comp. Neurol. 436:211-224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Palladin is a novel binding partner for Ena/VASP family members."
      Boukhelifa M., Parast M.M., Bear J.E., Gertler F.B., Otey C.A.
      Cell Motil. Cytoskeleton 58:17-29(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VASP.
    8. "The palladin/myotilin/myopalladin family of actin-associated scaffolds."
      Otey C.A., Rachlin A., Moza M., Arneman D., Carpen O.
      Int. Rev. Cytol. 246:31-58(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4).
    9. "Disruption of palladin results in neural tube closure defects in mice."
      Luo H., Liu X., Wang F., Huang Q., Shen S., Wang L., Xu G., Sun X., Kong H., Gu M., Chen S., Chen Z., Wang Z.
      Mol. Cell. Neurosci. 29:507-515(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    10. "Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin."
      Rachlin A.S., Otey C.A.
      J. Cell Sci. 119:995-1004(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4), INTERACTION OF ISOFORM 3 WITH LASP1.
    11. "Palladin binds to Eps8 and enhances the formation of dorsal ruffles and podosomes in vascular smooth muscle cells."
      Goicoechea S., Arneman D., Disanza A., Garcia-Mata R., Scita G., Otey C.A.
      J. Cell Sci. 119:3316-3324(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPS8.
    12. "Disruption of palladin leads to defects in definitive erythropoiesis by interfering erythroblastic island formation in mouse fetal liver."
      Liu X.-S., Li X.-H., Wang Y., Shu R.-Z., Wang L., Lu S.-Y., Kong H., Jin Y.-E., Zhang L.-J., Fei J., Chen S.-J., Chen Z., Gu M.-M., Lu Z.-Y., Wang Z.-G.
      Blood 110:870-876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Palladin regulates cell and extracellular matrix interaction through maintaining normal actin cytoskeleton architecture and stabilizing beta1-integrin."
      Liu X.-S., Luo H.-J., Yang H., Wang L., Kong H., Jin Y.-E., Wang F., Gu M.-M., Chen Z., Lu Z.-Y., Wang Z.-G.
      J. Cell. Biochem. 100:1288-1300(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901; SER-1143 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPALLD_MOUSE
    AccessioniPrimary (citable) accession number: Q9ET54
    Secondary accession number(s): A0JNZ3
    , Q69ZT7, Q6DFX7, Q9CWW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3