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Q9ET54 (PALLD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Palladin
Gene names
Name:Palld
Synonyms:Kiaa0992
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1408 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 May be required for the initiation of neural tube closure. Ref.4 Ref.9 Ref.10 Ref.13

Subunit structure

Interacts with ACTN, ARGBP2, LPP, PFN1, SPIN90, SRC and EZR By similarity. Interacts with EPS8, LASP1 and VASP. Ref.7 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Cell projectionruffle. Cell projectionlamellipodium. CytoplasmmyofibrilsarcomereZ line. Note: Localizes to stress fibers and Z lines. Ref.4

Tissue specificity

Detected in both muscle and non-muscle tissues and cells (at protein level). Isoform 3 is widely expressed, isoform 4 is particularly abundant in tissues rich in smooth muscle and in the cardiac muscle and isoform 1 is detected in heart. Ref.4 Ref.6

Developmental stage

Ubiquitously detected in embryonic tissues, and down-regulated in certain adult tissues (at protein level). Isoform 3 is widely expressed in embryonic tissues (at protein level). In adults is detected in spleen and gut, and is almost undetectable in heart, skeletal muscle, liver, and kidney (at protein level). Isoform 4 is widely expressed in neonatal tissues (brain, heart, lung, stomach, intestine, kidney, bone and skin) (at protein level). Late in development expression is restricted to cardiac muscle and to organs rich in smooth muscle (at protein level). Isoform 1 is detected in neonatal striated muscle and bone, and remains highly expressed in adult skeletal and cardiac muscle (at protein level). Adult brain express an isoform of80-85 kDa. At E8.5 is mainly expressed the rostral and caudal part of neural plate. No expression is detected in somite. At E9.5 and E10.5 is ubiquitously detected. Ref.4 Ref.9

Post-translational modification

Phosphorylated predominantly on serines and, to a lesser extent, on tyrosines. Phosphorylation at Ser-1143 by PKB/AKT1 modulates cytoskeletal organization and cell motility By similarity. Ref.4

Disruption phenotype

Death around E15.5 due to severe neural tube closure defects and herniation of liver and intestine. Palld-deficient mouse embryonic fibroblasts display disorganized actin cytoskeleton, decreased polymerized filament actin, and decreased cell adhesion and compromised cell spreading on various extracellular matrix. Mice embryos lacking Palld exhibit defects in erythropoiesis. Ref.9 Ref.12 Ref.13

Sequence similarities

Belongs to the myotilin/palladin family.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Sequence caution

The sequence AK031696 differs from that shown. Reason: Frameshift at position 821.

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

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ET54-1)

Also known as: 200 kDa isoform;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ET54-2)

The sequence of this isoform differs from the canonical sequence as follows:
     663-887: Missing.
     966-982: Missing.
     1352-1408: TQWHQQPQTTKPKKVRPSASRYAALSDQGLDIKAAFQPEASPSHLTLNSGLVESEDL → ISRH
Isoform 3 (identifier: Q9ET54-3)

Also known as: 90 kDa isoform; 3Ig isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     1-728: Missing.
     966-982: Missing.
Isoform 4 (identifier: Q9ET54-4)

Also known as: 140 kDa isoform; 4Ig isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     1-389: Missing.
     966-982: Missing.
Isoform 5 (identifier: Q9ET54-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-738: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q9ET54-6)

The sequence of this isoform differs from the canonical sequence as follows:
     966-982: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14081408Palladin
PRO_0000302721

Regions

Domain278 – 36790Ig-like C2-type 1
Domain448 – 54699Ig-like C2-type 2
Domain1026 – 111085Ig-like C2-type 3
Domain1160 – 125192Ig-like C2-type 4
Domain1259 – 134991Ig-like C2-type 5
Region569 – 5735Interaction with VASP
Region653 – 68331Interaction with LASP1
Region683 – 71331Interaction with ARGBP2, SPIN90 and SRC By similarity
Region782 – 84261Interaction with EPS8
Region807 – 84236Interaction with ARGBP2, SPIN90, SRC and PFN1 By similarity
Region830 – 8345Interaction with VASP
Region1162 – 125190Interaction with EZR By similarity
Region1261 – 135191Interaction with EZR By similarity
Compositional bias570 – 5745Poly-Pro
Compositional bias640 – 872233Pro-rich

Amino acid modifications

Modified residue7001Phosphoserine By similarity
Modified residue7041Phosphoserine By similarity
Modified residue9011Phosphoserine Ref.14
Modified residue10041Phosphoserine By similarity
Modified residue10091Phosphoserine By similarity
Modified residue11261Phosphoserine By similarity
Modified residue11291Phosphoserine By similarity
Modified residue11311Phosphoserine By similarity
Modified residue11411Phosphoserine By similarity
Modified residue11431Phosphoserine; by PKB/AKT1 Ref.14
Modified residue11461Phosphoserine Ref.14
Disulfide bond299 ↔ 351 By similarity
Disulfide bond469 ↔ 528 By similarity
Disulfide bond1181 ↔ 1233 By similarity

Natural variations

Alternative sequence1 – 738738Missing in isoform 5.
VSP_027931
Alternative sequence1 – 728728Missing in isoform 3.
VSP_027932
Alternative sequence1 – 389389Missing in isoform 4.
VSP_027933
Alternative sequence663 – 887225Missing in isoform 2.
VSP_027934
Alternative sequence966 – 98217Missing in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_027935
Alternative sequence1352 – 140857TQWHQ…ESEDL → ISRH in isoform 2.
VSP_027936

Experimental info

Sequence conflict10221N → K in AK031696. Ref.5
Sequence conflict10531P → T in AK031696. Ref.5

Secondary structure

................. 1408
Helix Strand Turn

Details...

Sequences

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

Last modified September 11, 2007. Version 2.
Checksum: 5BCF647C110619C9

FASTA1,408152,131
        10         20         30         40         50         60 
MSETSSHDSF YDSLSDVQEE GKSADFFPGL SAFLSQEEIN KSLDLARRAI DSSETEDFDS 

        70         80         90        100        110        120 
EKEISQIFSK SPISLCETPS HEEPKSGKQT SSERPQDSRR APVQPLTGDQ AERITSPGSK 

       130        140        150        160        170        180 
RKPGVSPLLA SPSYIRSLRK AEKRGAKNPN PSSKPKTAQQ SKAGPQSQLC DKAASFIEEL 

       190        200        210        220        230        240 
TSIFREAAKP RNRSPNGESS SPDSGYLSPK NQPSALMSAS ASQSPTADQL DQLEMDAEVK 

       250        260        270        280        290        300 
QAQGSLCYQA HQASEETLPL AHIPHPQPQK ARHLPTAPRF IQKLRSQEVA EGSRVYLECR 

       310        320        330        340        350        360 
VTGNPTPRVR WFCEGKELYN SPDVQIHCES GELHTLVIAE AFEDDTGRYT CLATNPSGSD 

       370        380        390        400        410        420 
STSAEVFIEG ASSTDSDSES LSFISKAGAM PQAQKKTTSV SLTIGSSAPK TGVTTAVIQP 

       430        440        450        460        470        480 
LSVPVQQAHS ATSYLCRPDG TTMGCLLPVF TKELQNTAAS EGQVVVLECR VRGAPPLQVQ 

       490        500        510        520        530        540 
WFRQGSEIQD SPDFRILQKK PRSTAEPEEI CTLVIAESFP EDAGIFTCSA TNDYGSVTST 

       550        560        570        580        590        600 
AQLVITSANN ENCSYDSTGE PNSDHFQHFP PPPPILETGS YELASQKPSE IQQVNSPNLG 

       610        620        630        640        650        660 
FSMAALQMQF NTAERETNGV HPSHGVNGLI NGKAYGNKSP PTPTALLSPT KEPPPLLAKP 

       670        680        690        700        710        720 
KLDPLKLQQL QNQVRLEQEA CAWPPAPPGV PCNSSSSGSS APPSPPFPPP PPAFPELAAC 

       730        740        750        760        770        780 
ASPVPSEPMS ALASRATAMQ SSGSFNYARP KQFIAAQNLG PASGLPTPTS SPSSSSLPSP 

       790        800        810        820        830        840 
LSPTPRPFGR APGPPFVEPE AMWGPSSPSP PPPPPPVFSP SAAYPVPDVF PLPPPPPPLP 

       850        860        870        880        890        900 
SSTSHCASPA RFGPSQTPAA FLSALLPSQP PPVAVNALGL PKGVTPAGFP KKSSRTARIA 

       910        920        930        940        950        960 
SDEEIQGTKD AVIQDLERKL RFKEDLLNNG QPRLTYEERM ARRLLGADSA NVFNIQEPEE 

       970        980        990       1000       1010       1020 
TAANQDAGAP RASVGGPLDG QKEYKVSSCE QRLISEIEYR LERSPVDESG DEVQDPDVPV 

      1030       1040       1050       1060       1070       1080 
ENATAPFFEM KLKHYKIFEG MPVTFTCRVA GNPKPKIYWF KDGKQISPKS DHYTIQRDLD 

      1090       1100       1110       1120       1130       1140 
GTCSLHTTAS TLDDDGNYTI MAANPQGRVS CTGRLMVQAV NQRGRSPRSP SGHPHARRPR 

      1150       1160       1170       1180       1190       1200 
SRSRDSGDEN EPIQERFFRP HFLQAPGDLT VQEGKLCRMD CKVSGLPTPD LSWQLDGKPI 

      1210       1220       1230       1240       1250       1260 
RPDSAHKMLV RENGVHSLII EPVTSRDAGI YTCIATNRAG QNSFNLELVV AAKEAHKAPV 

      1270       1280       1290       1300       1310       1320 
FMEKLQNTGV ADGYPVRLEC RVSGVPPPQI FWKKENESLT HSTERVSMHQ DNHGYICLLI 

      1330       1340       1350       1360       1370       1380 
QGATKEDAGW YTVSAKNEAG IVSCTARLDV YTQWHQQPQT TKPKKVRPSA SRYAALSDQG 

      1390       1400 
LDIKAAFQPE ASPSHLTLNS GLVESEDL 

« Hide

Isoform 2 [UniParc].

Checksum: 2E4249532BDEACEB
Show »

FASTA1,113122,090
Isoform 3 (90 kDa isoform) (3Ig isoform) [UniParc].

Checksum: 87C70C4EDC263B5E
Show »

FASTA66372,368
Isoform 4 (140 kDa isoform) (4Ig isoform) [UniParc].

Checksum: 5E630ABBBF42CB74
Show »

FASTA1,002108,287
Isoform 5 [UniParc].

Checksum: CCF8E48D7ADEDDD6
Show »

FASTA67072,985
Isoform 6 [UniParc].

Checksum: FF63541E07E7E676
Show »

FASTA1,391150,553

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1408 (ISOFORM 6).
Strain: C57BL/6.
Tissue: Eye.
[3]"Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1408 (ISOFORM 6).
Tissue: Embryonic tail.
[4]"Characterization of palladin, a novel protein localized to stress fibers and cell adhesions."
Parast M.M., Otey C.A.
J. Cell Biol. 150:643-656(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 900-1408 (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
Strain: Swiss Webster / NIH.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1015-1408 (ISOFORM 1).
Strain: C57BL/6J.
[6]"Palladin is expressed preferentially in excitatory terminals in the rat central nervous system."
Hwang S.J., Pagliardini S., Boukhelifa M., Parast M.M., Otey C.A., Rustioni A., Valtschanoff J.G.
J. Comp. Neurol. 436:211-224(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Palladin is a novel binding partner for Ena/VASP family members."
Boukhelifa M., Parast M.M., Bear J.E., Gertler F.B., Otey C.A.
Cell Motil. Cytoskeleton 58:17-29(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VASP.
[8]"The palladin/myotilin/myopalladin family of actin-associated scaffolds."
Otey C.A., Rachlin A., Moza M., Arneman D., Carpen O.
Int. Rev. Cytol. 246:31-58(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4).
[9]"Disruption of palladin results in neural tube closure defects in mice."
Luo H., Liu X., Wang F., Huang Q., Shen S., Wang L., Xu G., Sun X., Kong H., Gu M., Chen S., Chen Z., Wang Z.
Mol. Cell. Neurosci. 29:507-515(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[10]"Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin."
Rachlin A.S., Otey C.A.
J. Cell Sci. 119:995-1004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4), INTERACTION OF ISOFORM 3 WITH LASP1.
[11]"Palladin binds to Eps8 and enhances the formation of dorsal ruffles and podosomes in vascular smooth muscle cells."
Goicoechea S., Arneman D., Disanza A., Garcia-Mata R., Scita G., Otey C.A.
J. Cell Sci. 119:3316-3324(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPS8.
[12]"Disruption of palladin leads to defects in definitive erythropoiesis by interfering erythroblastic island formation in mouse fetal liver."
Liu X.-S., Li X.-H., Wang Y., Shu R.-Z., Wang L., Lu S.-Y., Kong H., Jin Y.-E., Zhang L.-J., Fei J., Chen S.-J., Chen Z., Gu M.-M., Lu Z.-Y., Wang Z.-G.
Blood 110:870-876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[13]"Palladin regulates cell and extracellular matrix interaction through maintaining normal actin cytoskeleton architecture and stabilizing beta1-integrin."
Liu X.-S., Luo H.-J., Yang H., Wang L., Kong H., Jin Y.-E., Wang F., Gu M.-M., Chen Z., Lu Z.-Y., Wang Z.-G.
J. Cell. Biochem. 100:1288-1300(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901; SER-1143 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[16]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC121881 Genomic DNA. No translation available.
AC139846 Genomic DNA. No translation available.
AC147616 Genomic DNA. No translation available.
BC076588 mRNA. Translation: AAH76588.1.
BC127081 mRNA. Translation: AAI27082.1.
AK173081 mRNA. Translation: BAD32359.1.
AF205078 mRNA. Translation: AAG00078.1.
AK010350 mRNA. Translation: BAB26871.1. Different initiation.
AK031696 mRNA. No translation available.
CCDSCCDS40350.1. [Q9ET54-2]
RefSeqNP_001074859.1. NM_001081390.1. [Q9ET54-2]
XP_006509564.1. XM_006509501.1. [Q9ET54-1]
XP_006509565.1. XM_006509502.1. [Q9ET54-1]
XP_006509566.1. XM_006509503.1. [Q9ET54-6]
XP_006509569.1. XM_006509506.1. [Q9ET54-4]
XP_006509572.1. XM_006509509.1. [Q9ET54-3]
UniGeneMm.29933.
Mm.458226.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LQRNMR-A1022-1126[»]
ProteinModelPortalQ9ET54.
SMRQ9ET54. Positions 270-545, 1022-1393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215316. 1 interaction.
IntActQ9ET54. 2 interactions.
MINTMINT-4129416.

PTM databases

PhosphoSiteQ9ET54.

Proteomic databases

MaxQBQ9ET54.
PaxDbQ9ET54.
PRIDEQ9ET54.

Protocols and materials databases

DNASU72333.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034057; ENSMUSP00000034057; ENSMUSG00000058056. [Q9ET54-2]
ENSMUST00000121200; ENSMUSP00000112374; ENSMUSG00000058056. [Q9ET54-3]
ENSMUST00000121493; ENSMUSP00000113874; ENSMUSG00000058056. [Q9ET54-4]
ENSMUST00000121785; ENSMUSP00000112442; ENSMUSG00000058056. [Q9ET54-1]
GeneID72333.
KEGGmmu:72333.
UCSCuc009lud.1. mouse. [Q9ET54-3]
uc009lue.1. mouse. [Q9ET54-4]
uc009luf.1. mouse. [Q9ET54-1]
uc009lug.2. mouse. [Q9ET54-2]

Organism-specific databases

CTD23022.
MGIMGI:1919583. Palld.
RougeSearch...

Phylogenomic databases

eggNOGNOG136920.
GeneTreeENSGT00690000101977.
HOGENOMHOG000028074.
HOVERGENHBG059166.
InParanoidQ9ET54.
OMATPRVRWF.
OrthoDBEOG77WWBP.
PhylomeDBQ9ET54.
TreeFamTF343193.

Gene expression databases

ArrayExpressQ9ET54.
BgeeQ9ET54.
CleanExMM_PALLD.
GenevestigatorQ9ET54.

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. mouse.
NextBio336044.
PROQ9ET54.
SOURCESearch...

Entry information

Entry namePALLD_MOUSE
AccessionPrimary (citable) accession number: Q9ET54
Secondary accession number(s): A0JNZ3 expand/collapse secondary AC list , Q69ZT7, Q6DFX7, Q9CWW1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot