Q8WX93 (PALLD_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Palladin Alternative name(s): SIH002 Sarcoma antigen NY-SAR-77 | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1383 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.10 Ref.11 Ref.18 |
| Subunit structure | Interacts with EPS8, LASP1 and VASP By similarity. Interacts with ACTN, ARGBP2, LPP, PFN1, SPIN90, SRC and EZR. Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 |
| Subcellular location | Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cell projection › ruffle. Cell projection › lamellipodium. Cytoplasm › myofibril › sarcomere › Z line. Note: Localizes to stress fibers and Z lines. Ref.10 Ref.12 Ref.17 Ref.18 |
| Tissue specificity | 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. Ref.10 |
| Induction | Isoform 3 is expressed de novo. Isoform 4 is up-regulated by TGFB1 during myofibroblast differentiation. Ref.15 |
| Post-translational modification | 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. Ref.18 Ref.25 |
| Involvement in disease | 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. Genetic variations in PALLD may be associated with myocardial infarction. |
| Sequence similarities | Belongs to the myotilin/palladin family. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. |
| Caution | Was wrongly assigned as myoneurin (Ref.2). |
| Sequence caution | The sequence AAD34146.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAO65174.1 differs from that shown. Reason: Frameshift at positions 1150 and 1154. The sequence BAA76836.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAC04796.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Cell projection Cytoplasm Cytoskeleton |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Immunoglobulin domain Repeat |
| Ligand | Actin-binding |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cytoskeleton organization Non-traceable author statement Ref.10. Source: HGNC |
| Cellular_component | Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell actin filamentInferred from direct assay Ref.10. Source: HGNC focal adhesionInferred from electronic annotation. Source: UniProtKB-SubCell lamellipodiumInferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from direct assay Ref.10. Source: HGNC ruffleInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | muscle alpha-actinin binding Traceable author statement Ref.12. Source: HGNC |
| Complete GO annotation... | |
Alternative products
| This entry describes 9 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8WX93-1) 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. | ||||||
| Isoform 2 (identifier: Q8WX93-2) The sequence of this isoform differs from the canonical sequence as follows: 656-879: Missing. 1326-1383: YTQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTALVESEDL → YISRH | ||||||
| Isoform 3 (identifier: Q8WX93-3) Also known as: 140-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-382: Missing. | ||||||
| Isoform 4 (identifier: Q8WX93-4) Also known as: 90-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-711: Missing. | ||||||
| Isoform 5 (identifier: Q8WX93-5) The sequence of this isoform differs from the canonical sequence as follows: 656-879: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 6 (identifier: Q8WX93-6) The sequence of this isoform differs from the canonical sequence as follows: 500-1383: PEEICTLVIA...NTALVESEDL → PDVLYVFVRVRCHQMKIQYYNLAHLISSWLSSFL | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 7 (identifier: Q8WX93-7) The sequence of this isoform differs from the canonical sequence as follows: 1-998: Missing. | ||||||
| Isoform 8 (identifier: Q8WX93-8) The sequence of this isoform differs from the canonical sequence as follows: 1-382: Missing. 656-879: Missing. | ||||||
| Isoform 9 (identifier: Q8WX93-9) The sequence of this isoform differs from the canonical sequence as follows: 656-879: Missing. 957-957: Q → QDIGSPHASVGSPLDGQK 1327-1383: TQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTALVESEDL → ISRH |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1383 | 1383 | Palladin | PRO_0000302720 | |||||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 271 – 360 | 90 | Ig-like C2-type 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 440 – 539 | 100 | Ig-like C2-type 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1001 – 1085 | 85 | Ig-like C2-type 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1135 – 1226 | 92 | Ig-like C2-type 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1233 – 1324 | 92 | Ig-like C2-type 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 562 – 566 | 5 | Interaction with VASP By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 646 – 676 | 31 | Interaction with LASP1 By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 676 – 696 | 21 | Interaction with ARGBP2, SPIN90 and SRC | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 766 – 831 | 66 | Interaction with EPS8 By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 796 – 831 | 36 | Interaction with ARGBP2, SPIN90, SRC and PFN1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 819 – 823 | 5 | Interaction with VASP By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 833 – 890 | 58 | Interaction with ACTN | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1137 – 1226 | 90 | Interaction with EZR | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 1236 – 1326 | 91 | Interaction with EZR | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 563 – 567 | 5 | Poly-Pro | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 634 – 864 | 231 | Pro-rich | ||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 401 | 1 | Phosphoserine Ref.16 Ref.23 Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 684 | 1 | Phosphoserine Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 688 | 1 | Phosphoserine Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 893 | 1 | Phosphoserine Ref.13 Ref.16 Ref.23 Ref.24 Ref.26 Ref.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 979 | 1 | Phosphoserine Ref.23 Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 984 | 1 | Phosphoserine Ref.23 Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1101 | 1 | Phosphoserine Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1104 | 1 | Phosphoserine Ref.26 Ref.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1106 | 1 | Phosphoserine Ref.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1116 | 1 | Phosphoserine Ref.26 Ref.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1118 | 1 | Phosphoserine; by PKB/AKT1 Ref.25 Ref.26 Ref.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1121 | 1 | Phosphoserine Ref.13 Ref.26 Ref.28 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 292 ↔ 344 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 462 ↔ 521 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 1156 ↔ 1208 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 998 | 998 | Missing in isoform 7. | VSP_027925 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 711 | 711 | Missing in isoform 4. | VSP_027926 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 382 | 382 | Missing in isoform 3 and isoform 8. | VSP_027927 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 500 – 1383 | 884 | PEEIC…ESEDL → PDVLYVFVRVRCHQMKIQYY NLAHLISSWLSSFL in isoform 6. | VSP_027928 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 656 – 879 | 224 | Missing in isoform 2, isoform 5, isoform 8 and isoform 9. | VSP_027929 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 957 | 1 | Q → QDIGSPHASVGSPLDGQK in isoform 9. | VSP_043794 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1326 – 1383 | 58 | YTQWH…ESEDL → YISRH in isoform 2. | VSP_027930 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1327 – 1383 | 57 | TQWHQ…ESEDL → ISRH in isoform 9. | VSP_043795 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 224 | 1 | M → I. Corresponds to variant rs7671781 [ dbSNP | Ensembl ]. | VAR_034940 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 224 | 1 | M → T. Ref.5 Corresponds to variant rs7655494 [ dbSNP | Ensembl ]. | VAR_059401 | |||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 277 | 1 | L → P in BAC04796. Ref.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 472 | 1 | V → D in BAC04796. Ref.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 611 | 1 | N → S in AAL69964. Ref.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 847 | 1 | S → G in BAA76836. Ref.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 1126 | 1 | E → D in AAO65174. Ref.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 1146 | 1 | V → G in AAO65174. Ref.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1003 – 1005 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1010 – 1013 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1018 – 1024 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1031 – 1035 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1046 – 1052 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1057 – 1064 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 1067 – 1069 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1074 – 1078 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1084 – 1086 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1090 – 1093 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1136 – 1139 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1143 – 1150 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1155 – 1159 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1165 – 1167 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1169 – 1174 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1179 – 1185 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1191 – 1197 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1200 – 1202 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1204 – 1206 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1208 – 1211 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1216 – 1219 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1222 – 1226 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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. 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] | "Immunomic analysis of human sarcoma." Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J. Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-1160 (ISOFORM 1). |
| [9] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "The proline-rich protein palladin is a binding partner for profilin." Boukhelifa M., Moza M., Johansson T., Rachlin A., Parast M., Huttelmaier S., Roy P., Jockusch B.M., Carpen O., Karlsson R., Otey C.A. FEBS J. 273:26-33(2006) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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] | "Palladin mutation causes familial pancreatic cancer and suggests a new cancer mechanism." Pogue-Geile K.L., Chen R., Bronner M.P., Crnogorac-Jurcevic T., Moyes K.W., Dowen S., Otey C.A., Crispin D.A., George R.D., Whitcomb D.C., Brentnall T.A. PLoS Med. 3:2216-2228(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PNCA1. |
| [20] | "Identification of four gene variants associated with myocardial infarction." Shiffman D., Ellis S.G., Rowland C.M., Malloy M.J., Luke M.M., Iakoubova O.A., Pullinger C.R., Cassano J., Aouizerat B.E., Fenwick R.G., Reitz R.E., Catanese J.J., Leong D.U., Zellner C., Sninsky J.J., Topol E.J., Devlin J.J., Kane J.P. Am. J. Hum. Genet. 77:596-605(2005) [PubMed] [Europe PMC] [Abstract] 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] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-893; SER-979 AND SER-984, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [27] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. |
| [29] | "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. |
| [30] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||
| IPI | IPI00166197. IPI00292009. IPI00383645. IPI00855763. IPI00856001. IPI00856046. IPI00856116. | ||||||||||||||||||
| PIR | T13078. | ||||||||||||||||||
| RefSeq | NP_001159580.1. NM_001166108.1. NP_001159581.1. NM_001166109.1. NP_001159582.1. NM_001166110.1. NP_057165.3. NM_016081.3. | ||||||||||||||||||
| UniGene | Hs.151220. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | Q8WX93. | ||||||||||||||||||
| SMR | Q8WX93. Positions 269-538, 971-1369. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | Q8WX93. 2 interactions. | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| MEROPS | I43.001. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q8WX93. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 158564081. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | Q8WX93. | ||||||||||||||||||
| PRIDE | Q8WX93. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000261509; ENSP00000261509; ENSG00000129116. ENST00000335742; ENSP00000336735; ENSG00000129116. ENST00000505667; ENSP00000425556; ENSG00000129116. ENST00000507735; ENSP00000424016; ENSG00000129116. ENST00000512127; ENSP00000426947; ENSG00000129116. | ||||||||||||||||||
| GeneID | 23022. | ||||||||||||||||||
| KEGG | hsa:23022. | ||||||||||||||||||
| UCSC | uc003irw.3. human. uc003irx.3. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 23022. | ||||||||||||||||||
| GeneCards | GC04P169418. | ||||||||||||||||||
| HGNC | HGNC:17068. PALLD. | ||||||||||||||||||
| MIM | 606856. phenotype. 608092. gene. | ||||||||||||||||||
| neXtProt | NX_Q8WX93. | ||||||||||||||||||
| PharmGKB | PA142671205. | ||||||||||||||||||
| HUGE | Search... | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG136920. | ||||||||||||||||||
| HOGENOM | HOG000028074. | ||||||||||||||||||
| HOVERGEN | HBG059166. | ||||||||||||||||||
| OMA | TRPSYIR. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q8WX93. | ||||||||||||||||||
| Bgee | Q8WX93. | ||||||||||||||||||
| Genevestigator | Q8WX93. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 2.60.40.10. 6 hits. | ||||||||||||||||||
| InterPro | IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003598. Ig_sub2. [Graphical view] | ||||||||||||||||||
| Pfam | PF07679. I-set. 5 hits. [Graphical view] | ||||||||||||||||||
| SMART | SM00408. IGc2. 5 hits. [Graphical view] | ||||||||||||||||||
| PROSITE | PS50835. IG_LIKE. 5 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| ChiTaRS | PALLD. human. | ||||||||||||||||||
| EvolutionaryTrace | Q8WX93. | ||||||||||||||||||
| GenomeRNAi | 23022. | ||||||||||||||||||
| NextBio | 43970. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | PALLD_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WX93 Secondary accession number(s): B3KTG2 Q9Y3E9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 4 Human chromosome 4: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
