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Q9ET54

- PALLD_MOUSE

UniProt

Q9ET54 - PALLD_MOUSE

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Protein

Palladin

Gene

Palld

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. cell junction Source: UniProtKB-KW
  3. cell projection Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB-KW
  5. nucleus Source: HGNC
Complete GO annotation...

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 – 9011Phosphoserine1 Publication
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/AKT11 Publication
Modified residuei1146 – 11461Phosphoserine1 Publication
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

BgeeiQ9ET54.
CleanExiMM_PALLD.
ExpressionAtlasiQ9ET54. baseline and differential.
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 – 10384Combined sources
Beta strandi1043 – 10486Combined sources
Beta strandi1058 – 10614Combined sources
Beta strandi1071 – 10777Combined sources
Beta strandi1081 – 10899Combined sources
Turni1092 – 10943Combined sources
Beta strandi1096 – 11016Combined sources
Beta strandi1114 – 11185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119215.
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

        10         20         30         40         50
MSETSSHDSF YDSLSDVQEE GKSADFFPGL SAFLSQEEIN KSLDLARRAI
60 70 80 90 100
DSSETEDFDS EKEISQIFSK SPISLCETPS HEEPKSGKQT SSERPQDSRR
110 120 130 140 150
APVQPLTGDQ AERITSPGSK RKPGVSPLLA SPSYIRSLRK AEKRGAKNPN
160 170 180 190 200
PSSKPKTAQQ SKAGPQSQLC DKAASFIEEL TSIFREAAKP RNRSPNGESS
210 220 230 240 250
SPDSGYLSPK NQPSALMSAS ASQSPTADQL DQLEMDAEVK QAQGSLCYQA
260 270 280 290 300
HQASEETLPL AHIPHPQPQK ARHLPTAPRF IQKLRSQEVA EGSRVYLECR
310 320 330 340 350
VTGNPTPRVR WFCEGKELYN SPDVQIHCES GELHTLVIAE AFEDDTGRYT
360 370 380 390 400
CLATNPSGSD STSAEVFIEG ASSTDSDSES LSFISKAGAM PQAQKKTTSV
410 420 430 440 450
SLTIGSSAPK TGVTTAVIQP LSVPVQQAHS ATSYLCRPDG TTMGCLLPVF
460 470 480 490 500
TKELQNTAAS EGQVVVLECR VRGAPPLQVQ WFRQGSEIQD SPDFRILQKK
510 520 530 540 550
PRSTAEPEEI CTLVIAESFP EDAGIFTCSA TNDYGSVTST AQLVITSANN
560 570 580 590 600
ENCSYDSTGE PNSDHFQHFP PPPPILETGS YELASQKPSE IQQVNSPNLG
610 620 630 640 650
FSMAALQMQF NTAERETNGV HPSHGVNGLI NGKAYGNKSP PTPTALLSPT
660 670 680 690 700
KEPPPLLAKP KLDPLKLQQL QNQVRLEQEA CAWPPAPPGV PCNSSSSGSS
710 720 730 740 750
APPSPPFPPP PPAFPELAAC ASPVPSEPMS ALASRATAMQ SSGSFNYARP
760 770 780 790 800
KQFIAAQNLG PASGLPTPTS SPSSSSLPSP LSPTPRPFGR APGPPFVEPE
810 820 830 840 850
AMWGPSSPSP PPPPPPVFSP SAAYPVPDVF PLPPPPPPLP SSTSHCASPA
860 870 880 890 900
RFGPSQTPAA FLSALLPSQP PPVAVNALGL PKGVTPAGFP KKSSRTARIA
910 920 930 940 950
SDEEIQGTKD AVIQDLERKL RFKEDLLNNG QPRLTYEERM ARRLLGADSA
960 970 980 990 1000
NVFNIQEPEE TAANQDAGAP RASVGGPLDG QKEYKVSSCE QRLISEIEYR
1010 1020 1030 1040 1050
LERSPVDESG DEVQDPDVPV ENATAPFFEM KLKHYKIFEG MPVTFTCRVA
1060 1070 1080 1090 1100
GNPKPKIYWF KDGKQISPKS DHYTIQRDLD GTCSLHTTAS TLDDDGNYTI
1110 1120 1130 1140 1150
MAANPQGRVS CTGRLMVQAV NQRGRSPRSP SGHPHARRPR SRSRDSGDEN
1160 1170 1180 1190 1200
EPIQERFFRP HFLQAPGDLT VQEGKLCRMD CKVSGLPTPD LSWQLDGKPI
1210 1220 1230 1240 1250
RPDSAHKMLV RENGVHSLII EPVTSRDAGI YTCIATNRAG QNSFNLELVV
1260 1270 1280 1290 1300
AAKEAHKAPV FMEKLQNTGV ADGYPVRLEC RVSGVPPPQI FWKKENESLT
1310 1320 1330 1340 1350
HSTERVSMHQ DNHGYICLLI QGATKEDAGW YTVSAKNEAG IVSCTARLDV
1360 1370 1380 1390 1400
YTQWHQQPQT TKPKKVRPSA SRYAALSDQG LDIKAAFQPE ASPSHLTLNS

GLVESEDL
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. Curated
The sequence BAB26871.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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]
NP_001280701.1. NM_001293772.1. [Q9ET54-1]
NP_001280703.1. NM_001293774.1. [Q9ET54-3]
XP_006509566.1. XM_006509503.1. [Q9ET54-6]
UniGeneiMm.29933.
Mm.458226.
Mm.487581.

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:
EMBLi
GenBanki
DDBJi
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 ]
NP_001280701.1. NM_001293772.1. [Q9ET54-1 ]
NP_001280703.1. NM_001293774.1. [Q9ET54-3 ]
XP_006509566.1. XM_006509503.1. [Q9ET54-6 ]
UniGenei Mm.29933.
Mm.458226.
Mm.487581.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000119215.
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

Bgeei Q9ET54.
CleanExi MM_PALLD.
ExpressionAtlasi Q9ET54. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 111 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