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Q8WX93 (PALLD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Palladin
Alternative name(s):
SIH002
Sarcoma antigen NY-SAR-77
Gene names
Name:PALLD
Synonyms:KIAA0992
ORF Names:CGI-151
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1383 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Cell projectionruffle. Cell projectionlamellipodium. CytoplasmmyofibrilsarcomereZ 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.19 Ref.21 Ref.22

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SORBS2O948752EBI-2803991,EBI-311323

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13831383Palladin
PRO_0000302720

Regions

Domain271 – 36090Ig-like C2-type 1
Domain440 – 539100Ig-like C2-type 2
Domain1001 – 108585Ig-like C2-type 3
Domain1135 – 122692Ig-like C2-type 4
Domain1233 – 132492Ig-like C2-type 5
Region562 – 5665Interaction with VASP By similarity
Region646 – 67631Interaction with LASP1 By similarity
Region676 – 69621Interaction with ARGBP2, SPIN90 and SRC
Region766 – 83166Interaction with EPS8 By similarity
Region796 – 83136Interaction with ARGBP2, SPIN90, SRC and PFN1
Region819 – 8235Interaction with VASP By similarity
Region833 – 89058Interaction with ACTN
Region1137 – 122690Interaction with EZR
Region1236 – 132691Interaction with EZR
Compositional bias563 – 5675Poly-Pro
Compositional bias634 – 864231Pro-rich

Amino acid modifications

Modified residue4011Phosphoserine Ref.16 Ref.23 Ref.26
Modified residue6841Phosphoserine Ref.26
Modified residue6881Phosphoserine Ref.26
Modified residue8931Phosphoserine Ref.13 Ref.16 Ref.23 Ref.24 Ref.26 Ref.28
Modified residue9791Phosphoserine Ref.23 Ref.26
Modified residue9841Phosphoserine Ref.23 Ref.26
Modified residue11011Phosphoserine Ref.26
Modified residue11041Phosphoserine Ref.26 Ref.28
Modified residue11061Phosphoserine Ref.26
Modified residue11161Phosphoserine Ref.26 Ref.28
Modified residue11181Phosphoserine; by PKB/AKT1 Ref.25 Ref.26 Ref.28
Modified residue11211Phosphoserine Ref.13 Ref.26 Ref.28
Disulfide bond292 ↔ 344 By similarity
Disulfide bond462 ↔ 521 By similarity
Disulfide bond1156 ↔ 1208 By similarity

Natural variations

Alternative sequence1 – 998998Missing in isoform 7.
VSP_027925
Alternative sequence1 – 711711Missing in isoform 4.
VSP_027926
Alternative sequence1 – 382382Missing in isoform 3 and isoform 8.
VSP_027927
Alternative sequence500 – 1383884PEEIC…ESEDL → PDVLYVFVRVRCHQMKIQYY NLAHLISSWLSSFL in isoform 6.
VSP_027928
Alternative sequence656 – 879224Missing in isoform 2, isoform 5, isoform 8 and isoform 9.
VSP_027929
Alternative sequence9571Q → QDIGSPHASVGSPLDGQK in isoform 9.
VSP_043794
Alternative sequence1326 – 138358YTQWH…ESEDL → YISRH in isoform 2.
VSP_027930
Alternative sequence1327 – 138357TQWHQ…ESEDL → ISRH in isoform 9.
VSP_043795
Natural variant2241M → I.
Corresponds to variant rs7671781 [ dbSNP | Ensembl ].
VAR_034940
Natural variant2241M → T. Ref.5
Corresponds to variant rs7655494 [ dbSNP | Ensembl ].
VAR_059401

Experimental info

Sequence conflict2771L → P in BAC04796. Ref.5
Sequence conflict4721V → D in BAC04796. Ref.5
Sequence conflict6111N → S in AAL69964. Ref.2
Sequence conflict8471S → G in BAA76836. Ref.3
Sequence conflict11261E → D in AAO65174. Ref.8
Sequence conflict11461V → G in AAO65174. Ref.8

Secondary structure

............................................. 1383
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (200-kDa) [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 2CABAE1A6FEE855F

FASTA1,383150,564
        10         20         30         40         50         60 
MSGTSSHESF YDSLSDMQEE SKNTDFFPGL SAFLSQEEIN KSLDLARRAI ADSETEDFDS 

        70         80         90        100        110        120 
EKEISQIFST SPASLCEHPS HKETKLGEHA SRRPQDNRST PVQPLAEKQT KSISSPVSKR 

       130        140        150        160        170        180 
KPAMSPLLTR PSYIRSLRKA EKRGAKTPST NVKPKTPHQR KGGPQSQLCD KAANLIEELT 

       190        200        210        220        230        240 
SIFKAAKPRN RSPNGESSSP DSGYLSPKNQ PSALLSASAS QSPMEDQGEM EREVKSPGAR 

       250        260        270        280        290        300 
HCYQDNQDLA VPHNRKSHPQ PHSALHFPAA PRFIQKLRSQ EVAEGSRVYL ECRVTGNPTP 

       310        320        330        340        350        360 
RVRWFCEGKE LHNTPDIQIH CEGGDLHTLI IAEAFEDDTG RYTCLATNPS GSDTTSAEVF 

       370        380        390        400        410        420 
IEGASSTDSD SESLAFKSRA GAMPQAQKKT TSVSLTIGSS SPKTGVTTAV IQPLSVPVQQ 

       430        440        450        460        470        480 
VHSPTSYLCR PDGTTTAYFP PVFTKELQNT AVAEGQVVVL ECRVRGAPPL QVQWFRQGSE 

       490        500        510        520        530        540 
IQDSPDFRIL QKKPRSTAEP EEICTLVIAE TFPEDAGIFT CSARNDYGSA TSTAQLVVTS 

       550        560        570        580        590        600 
ANTENCSYES MGESNNDHFQ HFPPPPPILE TSSLELASKK PSEIQQVNNP ELGLSRAALQ 

       610        620        630        640        650        660 
MQFNAAERET NGVHPSRGVN GLINGKANSN KSLPTPAVLL SPTKEPPPLL AKPKLDPLKL 

       670        680        690        700        710        720 
QQLQNQIRLE QEAGARQPPP APRSAPPSPP FPPPPAFPEL AACTPPASPE PMSALASRSA 

       730        740        750        760        770        780 
PAMQSSGSFN YARPKQFIAA QNLGPASGHG TPASSPSSSS LPSPMSPTPR QFGRAPVPPF 

       790        800        810        820        830        840 
AQPFGAEPEA PWGSSSPSPP PPPPPVFSPT AAFPVPDVFP LPPPPPPLPS PGQASHCSSP 

       850        860        870        880        890        900 
ATRFGHSQTP AAFLSALLPS QPPPAAVNAL GLPKGVTPAG FPKKASRTAR IASDEEIQGT 

       910        920        930        940        950        960 
KDAVIQDLER KLRFKEDLLN NGQPRLTYEE RMARRLLGAD SATVFNIQEP EEETANQEYK 

       970        980        990       1000       1010       1020 
VSSCEQRLIS EIEYRLERSP VDESGDEVQY GDVPVENGMA PFFEMKLKHY KIFEGMPVTF 

      1030       1040       1050       1060       1070       1080 
TCRVAGNPKP KIYWFKDGKQ ISPKSDHYTI QRDLDGTCSL HTTASTLDDD GNYTIMAANP 

      1090       1100       1110       1120       1130       1140 
QGRISCTGRL MVQAVNQRGR SPRSPSGHPH VRRPRSRSRD SGDENEPIQE RFFRPHFLQA 

      1150       1160       1170       1180       1190       1200 
PGDLTVQEGK LCRMDCKVSG LPTPDLSWQL DGKPVRPDSA HKMLVRENGV HSLIIEPVTS 

      1210       1220       1230       1240       1250       1260 
RDAGIYTCIA TNRAGQNSFS LELVVAAKEA HKPPVFIEKL QNTGVADGYP VRLECRVLGV 

      1270       1280       1290       1300       1310       1320 
PPPQIFWKKE NESLTHSTDR VSMHQDNHGY ICLLIQGATK EDAGWYTVSA KNEAGIVSCT 

      1330       1340       1350       1360       1370       1380 
ARLDVYTQWH QQSQSTKPKK VRPSASRYAA LSDQGLDIKA AFQPEANPSH LTLNTALVES 


EDL 

« Hide

Isoform 2 [UniParc].

Checksum: 11CC06FA94B4758B
Show »

FASTA1,106122,047
Isoform 3 (140-kDa) [UniParc].

Checksum: E1A3F96F80B40B4B
Show »

FASTA1,001108,632
Isoform 4 (90-kDa) [UniParc].

Checksum: 94168879EA796261
Show »

FASTA67273,322
Isoform 5 [UniParc].

Checksum: 0B1482F9B0C36C25
Show »

FASTA1,159127,826
Isoform 6 [UniParc].

Checksum: 608AB2AD12868576
Show »

FASTA53358,796
Isoform 7 [UniParc].

Checksum: 15853FB78B8E41B9
Show »

FASTA38542,933
Isoform 8 [UniParc].

Checksum: D0EE5BAF3028E2BB
Show »

FASTA77785,894
Isoform 9 [UniParc].

Checksum: 12D8DFEEBE3DF2B2
Show »

FASTA1,123123,693

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. expand/collapse author list , 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. expand/collapse author list , 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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]"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, 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+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.
CCDSCCDS34098.1. [Q8WX93-2]
CCDS54818.1. [Q8WX93-9]
CCDS54819.1. [Q8WX93-8]
CCDS54820.1. [Q8WX93-4]
PIRT13078.
RefSeqNP_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]
UniGeneHs.151220.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DM2NMR-A1000-1096[»]
2DM3NMR-A1133-1229[»]
ProteinModelPortalQ8WX93.
SMRQ8WX93. Positions 1000-1096, 1133-1230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116662. 13 interactions.
IntActQ8WX93. 5 interactions.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ8WX93.

Polymorphism databases

DMDM313104206.

Proteomic databases

MaxQBQ8WX93.
PaxDbQ8WX93.
PRIDEQ8WX93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261509; ENSP00000261509; ENSG00000129116. [Q8WX93-2]
ENST00000335742; ENSP00000336735; ENSG00000129116. [Q8WX93-3]
ENST00000505667; ENSP00000425556; ENSG00000129116. [Q8WX93-9]
ENST00000507735; ENSP00000424016; ENSG00000129116. [Q8WX93-4]
ENST00000512127; ENSP00000426947; ENSG00000129116. [Q8WX93-8]
GeneID23022.
KEGGhsa:23022.
UCSCuc003irv.3. human. [Q8WX93-8]
uc003irw.3. human. [Q8WX93-4]
uc003irx.3. human. [Q8WX93-7]
uc011cjx.2. human. [Q8WX93-9]

Organism-specific databases

CTD23022.
GeneCardsGC04P169418.
HGNCHGNC:17068. PALLD.
MIM606856. phenotype.
608092. gene.
neXtProtNX_Q8WX93.
PharmGKBPA142671205.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136920.
HOGENOMHOG000028074.
HOVERGENHBG059166.
OMATPRVRWF.
OrthoDBEOG77WWBP.
PhylomeDBQ8WX93.
TreeFamTF343193.

Gene expression databases

ArrayExpressQ8WX93.
BgeeQ8WX93.
GenevestigatorQ8WX93.

Family and domain databases

Gene3D2.60.40.10. 6 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF07679. I-set. 5 hits.
[Graphical view]
SMARTSM00408. IGc2. 5 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPALLD. human.
EvolutionaryTraceQ8WX93.
GeneWikiPalladin.
GenomeRNAi23022.
NextBio43970.
PROQ8WX93.
SOURCESearch...

Entry information

Entry namePALLD_HUMAN
AccessionPrimary (citable) accession number: Q8WX93
Secondary accession number(s): B3KTG2 expand/collapse secondary AC list , B5MD56, B7ZMM5, Q7L3E0, Q7Z3W0, Q86WE8, Q8N1M2, Q9UGA0, Q9UQF5, Q9Y2J6, Q9Y3E9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM