CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021147
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Palladin 
Protein Synonyms/Alias
  
Gene Name
 Palld 
Gene Synonyms/Alias
 Kiaa0992 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1293PPPQIFWKKENESLTacetylation[1]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 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. 
Sequence Annotation
 DOMAIN 278 367 Ig-like C2-type 1.
 DOMAIN 448 546 Ig-like C2-type 2.
 DOMAIN 1026 1110 Ig-like C2-type 3.
 DOMAIN 1160 1251 Ig-like C2-type 4.
 DOMAIN 1259 1349 Ig-like C2-type 5.
 REGION 569 573 Interaction with VASP.
 REGION 653 683 Interaction with LASP1.
 REGION 683 713 Interaction with ARGBP2, SPIN90 and SRC
 REGION 782 842 Interaction with EPS8.
 REGION 807 842 Interaction with ARGBP2, SPIN90, SRC and
 REGION 830 834 Interaction with VASP.
 REGION 1162 1251 Interaction with EZR (By similarity).
 REGION 1261 1351 Interaction with EZR (By similarity).
 MOD_RES 700 700 Phosphoserine (By similarity).
 MOD_RES 704 704 Phosphoserine (By similarity).
 MOD_RES 901 901 Phosphoserine (By similarity).
 MOD_RES 1004 1004 Phosphoserine (By similarity).
 MOD_RES 1009 1009 Phosphoserine.
 MOD_RES 1126 1126 Phosphoserine (By similarity).
 MOD_RES 1129 1129 Phosphoserine (By similarity).
 MOD_RES 1131 1131 Phosphoserine (By similarity).
 MOD_RES 1141 1141 Phosphoserine.
 MOD_RES 1143 1143 Phosphoserine; by PKB/AKT1.
 MOD_RES 1146 1146 Phosphoserine.
 DISULFID 299 351 By similarity.
 DISULFID 469 528 By similarity.
 DISULFID 1181 1233 By similarity.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Disulfide bond; Immunoglobulin domain; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1408 AA 
Protein Sequence
MSETSSHDSF YDSLSDVQEE GKSADFFPGL SAFLSQEEIN KSLDLARRAI DSSETEDFDS 60
EKEISQIFSK SPISLCETPS HEEPKSGKQT SSERPQDSRR APVQPLTGDQ AERITSPGSK 120
RKPGVSPLLA SPSYIRSLRK AEKRGAKNPN PSSKPKTAQQ SKAGPQSQLC DKAASFIEEL 180
TSIFREAAKP RNRSPNGESS SPDSGYLSPK NQPSALMSAS ASQSPTADQL DQLEMDAEVK 240
QAQGSLCYQA HQASEETLPL AHIPHPQPQK ARHLPTAPRF IQKLRSQEVA EGSRVYLECR 300
VTGNPTPRVR WFCEGKELYN SPDVQIHCES GELHTLVIAE AFEDDTGRYT CLATNPSGSD 360
STSAEVFIEG ASSTDSDSES LSFISKAGAM PQAQKKTTSV SLTIGSSAPK TGVTTAVIQP 420
LSVPVQQAHS ATSYLCRPDG TTMGCLLPVF TKELQNTAAS EGQVVVLECR VRGAPPLQVQ 480
WFRQGSEIQD SPDFRILQKK PRSTAEPEEI CTLVIAESFP EDAGIFTCSA TNDYGSVTST 540
AQLVITSANN ENCSYDSTGE PNSDHFQHFP PPPPILETGS YELASQKPSE IQQVNSPNLG 600
FSMAALQMQF NTAERETNGV HPSHGVNGLI NGKAYGNKSP PTPTALLSPT KEPPPLLAKP 660
KLDPLKLQQL QNQVRLEQEA CAWPPAPPGV PCNSSSSGSS APPSPPFPPP PPAFPELAAC 720
ASPVPSEPMS ALASRATAMQ SSGSFNYARP KQFIAAQNLG PASGLPTPTS SPSSSSLPSP 780
LSPTPRPFGR APGPPFVEPE AMWGPSSPSP PPPPPPVFSP SAAYPVPDVF PLPPPPPPLP 840
SSTSHCASPA RFGPSQTPAA FLSALLPSQP PPVAVNALGL PKGVTPAGFP KKSSRTARIA 900
SDEEIQGTKD AVIQDLERKL RFKEDLLNNG QPRLTYEERM ARRLLGADSA NVFNIQEPEE 960
TAANQDAGAP RASVGGPLDG QKEYKVSSCE QRLISEIEYR LERSPVDESG DEVQDPDVPV 1020
ENATAPFFEM KLKHYKIFEG MPVTFTCRVA GNPKPKIYWF KDGKQISPKS DHYTIQRDLD 1080
GTCSLHTTAS TLDDDGNYTI MAANPQGRVS CTGRLMVQAV NQRGRSPRSP SGHPHARRPR 1140
SRSRDSGDEN EPIQERFFRP HFLQAPGDLT VQEGKLCRMD CKVSGLPTPD LSWQLDGKPI 1200
RPDSAHKMLV RENGVHSLII EPVTSRDAGI YTCIATNRAG QNSFNLELVV AAKEAHKAPV 1260
FMEKLQNTGV ADGYPVRLEC RVSGVPPPQI FWKKENESLT HSTERVSMHQ DNHGYICLLI 1320
QGATKEDAGW YTVSAKNEAG IVSCTARLDV YTQWHQQPQT TKPKKVRPSA SRYAALSDQG 1380
LDIKAAFQPE ASPSHLTLNS GLVESEDL 1408 
Gene Ontology
 GO:0005884; C:actin filament; ISS:HGNC.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; ISS:HGNC.
 GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR013098; Ig_I-set.
 IPR003598; Ig_sub2. 
Pfam
 PF07679; I-set 
SMART
 SM00408; IGc2 
PROSITE
 PS50835; IG_LIKE 
PRINTS