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Q8WX93

- PALLD_HUMAN

UniProt

Q8WX93 - PALLD_HUMAN

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Protein

Palladin

Gene

PALLD

Organism
Homo sapiens (Human)
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 subcellular foci.3 Publications

GO - Molecular functioni

  1. muscle alpha-actinin binding Source: HGNC

GO - Biological processi

  1. cytoskeleton organization Source: HGNC
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Palladin
Alternative name(s):
SIH002
Sarcoma antigen NY-SAR-77
Gene namesi
Name:PALLD
Synonyms:KIAA0992
ORF Names:CGI-151
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:17068. PALLD.

Subcellular locationi

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

GO - Cellular componenti

  1. actin filament Source: HGNC
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB-KW
  4. focal adhesion Source: UniProtKB
  5. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Pancreatic cancer 1 (PNCA1) [MIM:606856]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Genetic variations in PALLD may be associated with myocardial infarction.

Organism-specific databases

MIMi606856. phenotype.
PharmGKBiPA142671205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13831383PalladinPRO_0000302720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi292 ↔ 344PROSITE-ProRule annotation
Modified residuei401 – 4011Phosphoserine3 Publications
Disulfide bondi462 ↔ 521PROSITE-ProRule annotation
Modified residuei684 – 6841Phosphoserine1 Publication
Modified residuei688 – 6881Phosphoserine1 Publication
Modified residuei893 – 8931Phosphoserine6 Publications
Modified residuei979 – 9791Phosphoserine2 Publications
Modified residuei984 – 9841Phosphoserine2 Publications
Modified residuei1101 – 11011Phosphoserine1 Publication
Modified residuei1104 – 11041Phosphoserine2 Publications
Modified residuei1106 – 11061Phosphoserine1 Publication
Modified residuei1116 – 11161Phosphoserine2 Publications
Modified residuei1118 – 11181Phosphoserine; by PKB/AKT13 Publications
Modified residuei1121 – 11211Phosphoserine3 Publications
Disulfide bondi1156 ↔ 1208PROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated predominantly on serines and, to a lesser extent, on tyrosines (By similarity). Phosphorylation at Ser-1118 by PKB/AKT1 modulates cytoskeletal organization and cell motility.By similarity8 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ8WX93.
PaxDbiQ8WX93.
PRIDEiQ8WX93.

PTM databases

PhosphoSiteiQ8WX93.

Expressioni

Tissue specificityi

Detected in both muscle and non-muscle tissues. High expression in prostate, ovary, colon, and kidney. Not detected in spleen, skeletal muscle, lung and peripheral blood lymphocytes (at protein level). Protein is overexpressed in FA6, HPAF, IMIM-PC2, SUIT-2 and PancTu-II sporadic pancreatic cancer cell lines.1 Publication

Inductioni

Isoform 3 is expressed de novo. Isoform 4 is up-regulated by TGFB1 during myofibroblast differentiation.1 Publication

Gene expression databases

BgeeiQ8WX93.
ExpressionAtlasiQ8WX93. baseline and differential.
GenevestigatoriQ8WX93.

Interactioni

Subunit structurei

Interacts with EPS8, LASP1 and VASP (By similarity). Interacts with ACTN, ARGBP2, LPP, PFN1, SPIN90, SRC and EZR.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SORBS2O948752EBI-2803991,EBI-311323

Protein-protein interaction databases

BioGridi116662. 15 interactions.
IntActiQ8WX93. 5 interactions.

Structurei

Secondary structure

1
1383
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1003 – 10053Combined sources
Beta strandi1010 – 10134Combined sources
Beta strandi1018 – 10247Combined sources
Beta strandi1031 – 10355Combined sources
Beta strandi1046 – 10527Combined sources
Beta strandi1057 – 10648Combined sources
Turni1067 – 10693Combined sources
Beta strandi1074 – 10785Combined sources
Beta strandi1084 – 10863Combined sources
Beta strandi1090 – 10934Combined sources
Beta strandi1136 – 11394Combined sources
Beta strandi1143 – 11508Combined sources
Beta strandi1155 – 11595Combined sources
Beta strandi1165 – 11673Combined sources
Beta strandi1169 – 11746Combined sources
Beta strandi1179 – 11857Combined sources
Beta strandi1191 – 11977Combined sources
Helixi1200 – 12023Combined sources
Beta strandi1204 – 12063Combined sources
Beta strandi1208 – 12114Combined sources
Beta strandi1216 – 12194Combined sources
Beta strandi1222 – 12265Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DM2NMR-A1000-1096[»]
2DM3NMR-A1133-1229[»]
ProteinModelPortaliQ8WX93.
SMRiQ8WX93. Positions 1000-1096, 1133-1230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WX93.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 36090Ig-like C2-type 1Add
BLAST
Domaini440 – 539100Ig-like C2-type 2Add
BLAST
Domaini1001 – 108585Ig-like C2-type 3Add
BLAST
Domaini1135 – 122692Ig-like C2-type 4Add
BLAST
Domaini1233 – 132492Ig-like C2-type 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni562 – 5665Interaction with VASPBy similarity
Regioni646 – 67631Interaction with LASP1By similarityAdd
BLAST
Regioni676 – 69621Interaction with ARGBP2, SPIN90 and SRCAdd
BLAST
Regioni766 – 83166Interaction with EPS8By similarityAdd
BLAST
Regioni796 – 83136Interaction with ARGBP2, SPIN90, SRC and PFN1Add
BLAST
Regioni819 – 8235Interaction with VASPBy similarity
Regioni833 – 89058Interaction with ACTNAdd
BLAST
Regioni1137 – 122690Interaction with EZRAdd
BLAST
Regioni1236 – 132691Interaction with EZRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi563 – 5675Poly-Pro
Compositional biasi634 – 864231Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the myotilin/palladin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiNOG136920.
GeneTreeiENSGT00760000119215.
HOGENOMiHOG000028074.
HOVERGENiHBG059166.
InParanoidiQ8WX93.
OMAiTPRVRWF.
OrthoDBiEOG77WWBP.
PhylomeDBiQ8WX93.
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 (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WX93-1) [UniParc]FASTAAdd to Basket

Also known as: 200-kDa

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
MSGTSSHESF YDSLSDMQEE SKNTDFFPGL SAFLSQEEIN KSLDLARRAI
60 70 80 90 100
ADSETEDFDS EKEISQIFST SPASLCEHPS HKETKLGEHA SRRPQDNRST
110 120 130 140 150
PVQPLAEKQT KSISSPVSKR KPAMSPLLTR PSYIRSLRKA EKRGAKTPST
160 170 180 190 200
NVKPKTPHQR KGGPQSQLCD KAANLIEELT SIFKAAKPRN RSPNGESSSP
210 220 230 240 250
DSGYLSPKNQ PSALLSASAS QSPMEDQGEM EREVKSPGAR HCYQDNQDLA
260 270 280 290 300
VPHNRKSHPQ PHSALHFPAA PRFIQKLRSQ EVAEGSRVYL ECRVTGNPTP
310 320 330 340 350
RVRWFCEGKE LHNTPDIQIH CEGGDLHTLI IAEAFEDDTG RYTCLATNPS
360 370 380 390 400
GSDTTSAEVF IEGASSTDSD SESLAFKSRA GAMPQAQKKT TSVSLTIGSS
410 420 430 440 450
SPKTGVTTAV IQPLSVPVQQ VHSPTSYLCR PDGTTTAYFP PVFTKELQNT
460 470 480 490 500
AVAEGQVVVL ECRVRGAPPL QVQWFRQGSE IQDSPDFRIL QKKPRSTAEP
510 520 530 540 550
EEICTLVIAE TFPEDAGIFT CSARNDYGSA TSTAQLVVTS ANTENCSYES
560 570 580 590 600
MGESNNDHFQ HFPPPPPILE TSSLELASKK PSEIQQVNNP ELGLSRAALQ
610 620 630 640 650
MQFNAAERET NGVHPSRGVN GLINGKANSN KSLPTPAVLL SPTKEPPPLL
660 670 680 690 700
AKPKLDPLKL QQLQNQIRLE QEAGARQPPP APRSAPPSPP FPPPPAFPEL
710 720 730 740 750
AACTPPASPE PMSALASRSA PAMQSSGSFN YARPKQFIAA QNLGPASGHG
760 770 780 790 800
TPASSPSSSS LPSPMSPTPR QFGRAPVPPF AQPFGAEPEA PWGSSSPSPP
810 820 830 840 850
PPPPPVFSPT AAFPVPDVFP LPPPPPPLPS PGQASHCSSP ATRFGHSQTP
860 870 880 890 900
AAFLSALLPS QPPPAAVNAL GLPKGVTPAG FPKKASRTAR IASDEEIQGT
910 920 930 940 950
KDAVIQDLER KLRFKEDLLN NGQPRLTYEE RMARRLLGAD SATVFNIQEP
960 970 980 990 1000
EEETANQEYK VSSCEQRLIS EIEYRLERSP VDESGDEVQY GDVPVENGMA
1010 1020 1030 1040 1050
PFFEMKLKHY KIFEGMPVTF TCRVAGNPKP KIYWFKDGKQ ISPKSDHYTI
1060 1070 1080 1090 1100
QRDLDGTCSL HTTASTLDDD GNYTIMAANP QGRISCTGRL MVQAVNQRGR
1110 1120 1130 1140 1150
SPRSPSGHPH VRRPRSRSRD SGDENEPIQE RFFRPHFLQA PGDLTVQEGK
1160 1170 1180 1190 1200
LCRMDCKVSG LPTPDLSWQL DGKPVRPDSA HKMLVRENGV HSLIIEPVTS
1210 1220 1230 1240 1250
RDAGIYTCIA TNRAGQNSFS LELVVAAKEA HKPPVFIEKL QNTGVADGYP
1260 1270 1280 1290 1300
VRLECRVLGV PPPQIFWKKE NESLTHSTDR VSMHQDNHGY ICLLIQGATK
1310 1320 1330 1340 1350
EDAGWYTVSA KNEAGIVSCT ARLDVYTQWH QQSQSTKPKK VRPSASRYAA
1360 1370 1380
LSDQGLDIKA AFQPEANPSH LTLNTALVES EDL
Length:1,383
Mass (Da):150,564
Last modified:November 30, 2010 - v3
Checksum:i2CABAE1A6FEE855F
GO
Isoform 2 (identifier: Q8WX93-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     656-879: Missing.
     1326-1383: YTQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTALVESEDL → YISRH

Show »
Length:1,106
Mass (Da):122,047
Checksum:i11CC06FA94B4758B
GO
Isoform 3 (identifier: Q8WX93-3) [UniParc]FASTAAdd to Basket

Also known as: 140-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-382: Missing.

Show »
Length:1,001
Mass (Da):108,632
Checksum:iE1A3F96F80B40B4B
GO
Isoform 4 (identifier: Q8WX93-4) [UniParc]FASTAAdd to Basket

Also known as: 90-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-711: Missing.

Show »
Length:672
Mass (Da):73,322
Checksum:i94168879EA796261
GO
Isoform 5 (identifier: Q8WX93-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     656-879: Missing.

Note: No experimental confirmation available.

Show »
Length:1,159
Mass (Da):127,826
Checksum:i0B1482F9B0C36C25
GO
Isoform 6 (identifier: Q8WX93-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     500-1383: PEEICTLVIA...NTALVESEDL → PDVLYVFVRVRCHQMKIQYYNLAHLISSWLSSFL

Note: No experimental confirmation available.

Show »
Length:533
Mass (Da):58,796
Checksum:i608AB2AD12868576
GO
Isoform 7 (identifier: Q8WX93-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-998: Missing.

Show »
Length:385
Mass (Da):42,933
Checksum:i15853FB78B8E41B9
GO
Isoform 8 (identifier: Q8WX93-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-382: Missing.
     656-879: Missing.

Show »
Length:777
Mass (Da):85,894
Checksum:iD0EE5BAF3028E2BB
GO
Isoform 9 (identifier: Q8WX93-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     656-879: Missing.
     957-957: Q → QDIGSPHASVGSPLDGQK
     1327-1383: TQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTALVESEDL → ISRH

Show »
Length:1,123
Mass (Da):123,693
Checksum:i12D8DFEEBE3DF2B2
GO

Sequence cautioni

The sequence AAD34146.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAO65174.1 differs from that shown. Reason: Frameshift at positions 1150 and 1154. Curated
The sequence BAA76836.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC04796.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771L → P in BAC04796. (PubMed:14702039)Curated
Sequence conflicti472 – 4721V → D in BAC04796. (PubMed:14702039)Curated
Sequence conflicti611 – 6111N → S in AAL69964. 1 PublicationCurated
Sequence conflicti847 – 8471S → G in BAA76836. (PubMed:10231032)Curated
Sequence conflicti1126 – 11261E → D in AAO65174. (PubMed:12601173)Curated
Sequence conflicti1146 – 11461V → G in AAO65174. (PubMed:12601173)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241M → I.
Corresponds to variant rs7671781 [ dbSNP | Ensembl ].
VAR_034940
Natural varianti224 – 2241M → T.1 Publication
Corresponds to variant rs7655494 [ dbSNP | Ensembl ].
VAR_059401

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 998998Missing in isoform 7. 2 PublicationsVSP_027925Add
BLAST
Alternative sequencei1 – 711711Missing in isoform 4. 1 PublicationVSP_027926Add
BLAST
Alternative sequencei1 – 382382Missing in isoform 3 and isoform 8. 1 PublicationVSP_027927Add
BLAST
Alternative sequencei500 – 1383884PEEIC…ESEDL → PDVLYVFVRVRCHQMKIQYY NLAHLISSWLSSFL in isoform 6. 1 PublicationVSP_027928Add
BLAST
Alternative sequencei656 – 879224Missing in isoform 2, isoform 5, isoform 8 and isoform 9. 4 PublicationsVSP_027929Add
BLAST
Alternative sequencei957 – 9571Q → QDIGSPHASVGSPLDGQK in isoform 9. 1 PublicationVSP_043794
Alternative sequencei1326 – 138358YTQWH…ESEDL → YISRH in isoform 2. 2 PublicationsVSP_027930Add
BLAST
Alternative sequencei1327 – 138357TQWHQ…ESEDL → ISRH in isoform 9. 1 PublicationVSP_043795Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077041 mRNA. Translation: AAD27774.1.
AF464873 mRNA. Translation: AAL69964.1.
AB023209 mRNA. Translation: BAA76836.1. Different initiation.
AF151909 mRNA. Translation: AAD34146.1. Different initiation.
AK095512 mRNA. Translation: BAG53074.1.
AK096458 mRNA. Translation: BAC04796.1. Different initiation.
AC079858 Genomic DNA. No translation available.
AC079926 Genomic DNA. No translation available.
AC080188 Genomic DNA. No translation available.
AC084353 Genomic DNA. No translation available.
AC115538 Genomic DNA. No translation available.
BC013867 mRNA. Translation: AAH13867.2.
BC144666 mRNA. Translation: AAI44667.1.
AY211921 mRNA. Translation: AAO65174.1. Frameshift.
BX537391 mRNA. Translation: CAD97633.1.
CCDSiCCDS34098.1. [Q8WX93-2]
CCDS54818.1. [Q8WX93-9]
CCDS54819.1. [Q8WX93-8]
CCDS54820.1. [Q8WX93-4]
PIRiT13078.
RefSeqiNP_001159580.1. NM_001166108.1. [Q8WX93-9]
NP_001159581.1. NM_001166109.1. [Q8WX93-8]
NP_001159582.1. NM_001166110.1. [Q8WX93-4]
NP_057165.3. NM_016081.3. [Q8WX93-2]
XP_005262919.1. XM_005262862.2. [Q8WX93-1]
UniGeneiHs.151220.

Genome annotation databases

EnsembliENST00000261509; ENSP00000261509; ENSG00000129116. [Q8WX93-2]
ENST00000505667; ENSP00000425556; ENSG00000129116. [Q8WX93-9]
ENST00000507735; ENSP00000424016; ENSG00000129116. [Q8WX93-4]
ENST00000512127; ENSP00000426947; ENSG00000129116. [Q8WX93-8]
GeneIDi23022.
KEGGihsa:23022.
UCSCiuc003irv.3. human. [Q8WX93-8]
uc003irw.3. human. [Q8WX93-4]
uc003irx.3. human. [Q8WX93-7]
uc011cjx.2. human. [Q8WX93-9]

Polymorphism databases

DMDMi313104206.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077041 mRNA. Translation: AAD27774.1 .
AF464873 mRNA. Translation: AAL69964.1 .
AB023209 mRNA. Translation: BAA76836.1 . Different initiation.
AF151909 mRNA. Translation: AAD34146.1 . Different initiation.
AK095512 mRNA. Translation: BAG53074.1 .
AK096458 mRNA. Translation: BAC04796.1 . Different initiation.
AC079858 Genomic DNA. No translation available.
AC079926 Genomic DNA. No translation available.
AC080188 Genomic DNA. No translation available.
AC084353 Genomic DNA. No translation available.
AC115538 Genomic DNA. No translation available.
BC013867 mRNA. Translation: AAH13867.2 .
BC144666 mRNA. Translation: AAI44667.1 .
AY211921 mRNA. Translation: AAO65174.1 . Frameshift.
BX537391 mRNA. Translation: CAD97633.1 .
CCDSi CCDS34098.1. [Q8WX93-2 ]
CCDS54818.1. [Q8WX93-9 ]
CCDS54819.1. [Q8WX93-8 ]
CCDS54820.1. [Q8WX93-4 ]
PIRi T13078.
RefSeqi NP_001159580.1. NM_001166108.1. [Q8WX93-9 ]
NP_001159581.1. NM_001166109.1. [Q8WX93-8 ]
NP_001159582.1. NM_001166110.1. [Q8WX93-4 ]
NP_057165.3. NM_016081.3. [Q8WX93-2 ]
XP_005262919.1. XM_005262862.2. [Q8WX93-1 ]
UniGenei Hs.151220.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DM2 NMR - A 1000-1096 [» ]
2DM3 NMR - A 1133-1229 [» ]
ProteinModelPortali Q8WX93.
SMRi Q8WX93. Positions 1000-1096, 1133-1230.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116662. 15 interactions.
IntActi Q8WX93. 5 interactions.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q8WX93.

Polymorphism databases

DMDMi 313104206.

Proteomic databases

MaxQBi Q8WX93.
PaxDbi Q8WX93.
PRIDEi Q8WX93.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261509 ; ENSP00000261509 ; ENSG00000129116 . [Q8WX93-2 ]
ENST00000505667 ; ENSP00000425556 ; ENSG00000129116 . [Q8WX93-9 ]
ENST00000507735 ; ENSP00000424016 ; ENSG00000129116 . [Q8WX93-4 ]
ENST00000512127 ; ENSP00000426947 ; ENSG00000129116 . [Q8WX93-8 ]
GeneIDi 23022.
KEGGi hsa:23022.
UCSCi uc003irv.3. human. [Q8WX93-8 ]
uc003irw.3. human. [Q8WX93-4 ]
uc003irx.3. human. [Q8WX93-7 ]
uc011cjx.2. human. [Q8WX93-9 ]

Organism-specific databases

CTDi 23022.
GeneCardsi GC04P169418.
HGNCi HGNC:17068. PALLD.
MIMi 606856. phenotype.
608092. gene.
neXtProti NX_Q8WX93.
PharmGKBi PA142671205.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG136920.
GeneTreei ENSGT00760000119215.
HOGENOMi HOG000028074.
HOVERGENi HBG059166.
InParanoidi Q8WX93.
OMAi TPRVRWF.
OrthoDBi EOG77WWBP.
PhylomeDBi Q8WX93.
TreeFami TF343193.

Miscellaneous databases

ChiTaRSi PALLD. human.
EvolutionaryTracei Q8WX93.
GeneWikii Palladin.
GenomeRNAii 23022.
NextBioi 43970.
PROi Q8WX93.
SOURCEi Search...

Gene expression databases

Bgeei Q8WX93.
ExpressionAtlasi Q8WX93. baseline and differential.
Genevestigatori Q8WX93.

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.
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PROSITEi PS50835. IG_LIKE. 5 hits.
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Publicationsi

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  1. "Human SIH002 gene."
    Liu T., Zhang J., Ye M., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
  2. Lockwood S.K.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
  5. "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] (ISOFORM 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-1383 (ISOFORM 6), VARIANT THR-224.
    Tissue: Tongue.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 9), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 874-1383 (ISOFORM 1).
    Tissue: Placenta.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-1160 (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1188-1383 (ISOFORM 2).
    Tissue: Heart.
  10. "Characterization of human palladin, a microfilament-associated protein."
    Mykkaenen O.-M., Groenholm M., Roenty M., Lalowski M., Salmikangas P., Suila H., Carpen O.
    Mol. Biol. Cell 12:3060-3073(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Molecular analysis of the interaction between palladin and alpha-actinin."
    Roenty M., Taivainen A., Moza M., Otey C.A., Carpen O.
    FEBS Lett. 566:30-34(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACTN.
  12. "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg kinase adaptor ArgBP2 to the actin cytoskeleton."
    Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.
    Exp. Cell Res. 310:88-98(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARGBP2, SUBCELLULAR LOCATION.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: INTERACTION WITH PFN1.
  15. "Isoform-specific regulation of the actin-organizing protein Palladin during TGF-beta1-induced myofibroblast differentiation."
    Roenty M.J., Leivonen S.-K., Hinz B., Rachlin A., Otey C.A., Kaehaeri V.-M., Carpen O.M.
    J. Invest. Dermatol. 126:2387-2396(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION (ISOFORMS 3 AND 4), INDUCTION.
  16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Angiotensin II, focal adhesion kinase, and PRX1 enhance smooth muscle expression of lipoma preferred partner and its newly identified binding partner palladin to promote cell migration."
    Jin L., Kern M.J., Otey C.A., Wamhoff B.R., Somlyo A.V.
    Circ. Res. 100:817-825(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPP, SUBCELLULAR LOCATION.
  18. "Palladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodeling."
    Ronty M., Taivainen A., Heiska L., Otey C., Ehler E., Song W.K., Carpen O.
    Exp. Cell Res. 313:2575-2585(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AND SRC, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  19. Cited for: INVOLVEMENT IN PNCA1.
  20. Cited for: ASSOCIATION WITH MYOCARDIAL INFARCTION.
  21. "The P239S palladin variant does not account for a significant fraction of hereditary or early onset pancreas cancer."
    Zogopoulous G., Rothenmund H., Eppel A., Ash C., Akbari M.R., Hedley D., Narod S.A., Gallinger S.
    Hum. Genet. 121:635-637(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PNCA1.
  22. "Palladin mutation causes familial pancreatic cancer: absence in European families."
    Slater E., Amrillaeva V., Fendrich V., Bartsch D., Earl J., Vitone L.J., Neoptolemos J.P., Greenhalf W.
    PLoS Med. 4:774-775(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: QUESTIONING OF INVOLVEMENT IN PNCA1.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-893; SER-979 AND SER-984, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "The actin-bundling protein palladin is an Akt1-specific substrate that regulates breast cancer cell migration."
    Chin Y.R., Toker A.
    Mol. Cell 38:333-344(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1118.
  26. "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-401; SER-684; SER-688; SER-893; SER-979; SER-984; SER-1101; SER-1104; SER-1106; SER-1116; SER-1118 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893; SER-1104; SER-1116; SER-1118 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Expression, crystallization and preliminary X-ray studies of the immunoglobulin-like domain 3 of human palladin."
    Liang W., Yang H., Xue X., Huang Q., Bartlam M., Chen S.
    Acta Crystallogr. F 62:556-558(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1233-1324.
  31. "Solution structure of the first and second Ig domains of human palladin."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1000-1230.

Entry informationi

Entry nameiPALLD_HUMAN
AccessioniPrimary (citable) accession number: Q8WX93
Secondary accession number(s): B3KTG2
, B5MD56, B7ZMM5, Q7L3E0, Q7Z3W0, Q86WE8, Q8N1M2, Q9UGA0, Q9UQF5, Q9Y2J6, Q9Y3E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 122 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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