CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Palladin 
Protein Synonyms/Alias
 SIH002; Sarcoma antigen NY-SAR-77 
Gene Name
 PALLD 
Gene Synonyms/Alias
 KIAA0992; CGI-151 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
659KPKLDPLKLQQLQNQubiquitination[1]
901DEEIQGTKDAVIQDLubiquitination[2]
915LERKLRFKEDLLNNGubiquitination[1]
1044DGKQISPKSDHYTIQubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
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 subcellular foci. 
Sequence Annotation
 DOMAIN 271 360 Ig-like C2-type 1.
 DOMAIN 440 539 Ig-like C2-type 2.
 DOMAIN 1001 1085 Ig-like C2-type 3.
 DOMAIN 1135 1226 Ig-like C2-type 4.
 DOMAIN 1233 1324 Ig-like C2-type 5.
 REGION 562 566 Interaction with VASP (By similarity).
 REGION 646 676 Interaction with LASP1 (By similarity).
 REGION 676 696 Interaction with ARGBP2, SPIN90 and SRC.
 REGION 766 831 Interaction with EPS8 (By similarity).
 REGION 796 831 Interaction with ARGBP2, SPIN90, SRC and
 REGION 819 823 Interaction with VASP (By similarity).
 REGION 833 890 Interaction with ACTN.
 REGION 1137 1226 Interaction with EZR.
 REGION 1236 1326 Interaction with EZR.
 MOD_RES 401 401 Phosphoserine.
 MOD_RES 684 684 Phosphoserine.
 MOD_RES 688 688 Phosphoserine.
 MOD_RES 893 893 Phosphoserine.
 MOD_RES 979 979 Phosphoserine.
 MOD_RES 984 984 Phosphoserine.
 MOD_RES 1101 1101 Phosphoserine.
 MOD_RES 1104 1104 Phosphoserine.
 MOD_RES 1106 1106 Phosphoserine.
 MOD_RES 1116 1116 Phosphoserine.
 MOD_RES 1118 1118 Phosphoserine; by PKB/AKT1.
 MOD_RES 1121 1121 Phosphoserine.
 DISULFID 292 344 By similarity.
 DISULFID 462 521 By similarity.
 DISULFID 1156 1208 By similarity.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Disulfide bond; Immunoglobulin domain; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1383 AA 
Protein Sequence
MSGTSSHESF YDSLSDMQEE SKNTDFFPGL SAFLSQEEIN KSLDLARRAI ADSETEDFDS 60
EKEISQIFST SPASLCEHPS HKETKLGEHA SRRPQDNRST PVQPLAEKQT KSISSPVSKR 120
KPAMSPLLTR PSYIRSLRKA EKRGAKTPST NVKPKTPHQR KGGPQSQLCD KAANLIEELT 180
SIFKAAKPRN RSPNGESSSP DSGYLSPKNQ PSALLSASAS QSPMEDQGEM EREVKSPGAR 240
HCYQDNQDLA VPHNRKSHPQ PHSALHFPAA PRFIQKLRSQ EVAEGSRVYL ECRVTGNPTP 300
RVRWFCEGKE LHNTPDIQIH CEGGDLHTLI IAEAFEDDTG RYTCLATNPS GSDTTSAEVF 360
IEGASSTDSD SESLAFKSRA GAMPQAQKKT TSVSLTIGSS SPKTGVTTAV IQPLSVPVQQ 420
VHSPTSYLCR PDGTTTAYFP PVFTKELQNT AVAEGQVVVL ECRVRGAPPL QVQWFRQGSE 480
IQDSPDFRIL QKKPRSTAEP EEICTLVIAE TFPEDAGIFT CSARNDYGSA TSTAQLVVTS 540
ANTENCSYES MGESNNDHFQ HFPPPPPILE TSSLELASKK PSEIQQVNNP ELGLSRAALQ 600
MQFNAAERET NGVHPSRGVN GLINGKANSN KSLPTPAVLL SPTKEPPPLL AKPKLDPLKL 660
QQLQNQIRLE QEAGARQPPP APRSAPPSPP FPPPPAFPEL AACTPPASPE PMSALASRSA 720
PAMQSSGSFN YARPKQFIAA QNLGPASGHG TPASSPSSSS LPSPMSPTPR QFGRAPVPPF 780
AQPFGAEPEA PWGSSSPSPP PPPPPVFSPT AAFPVPDVFP LPPPPPPLPS PGQASHCSSP 840
ATRFGHSQTP AAFLSALLPS QPPPAAVNAL GLPKGVTPAG FPKKASRTAR IASDEEIQGT 900
KDAVIQDLER KLRFKEDLLN NGQPRLTYEE RMARRLLGAD SATVFNIQEP EEETANQEYK 960
VSSCEQRLIS EIEYRLERSP VDESGDEVQY GDVPVENGMA PFFEMKLKHY KIFEGMPVTF 1020
TCRVAGNPKP KIYWFKDGKQ ISPKSDHYTI QRDLDGTCSL HTTASTLDDD GNYTIMAANP 1080
QGRISCTGRL MVQAVNQRGR SPRSPSGHPH VRRPRSRSRD SGDENEPIQE RFFRPHFLQA 1140
PGDLTVQEGK LCRMDCKVSG LPTPDLSWQL DGKPVRPDSA HKMLVRENGV HSLIIEPVTS 1200
RDAGIYTCIA TNRAGQNSFS LELVVAAKEA HKPPVFIEKL QNTGVADGYP VRLECRVLGV 1260
PPPQIFWKKE NESLTHSTDR VSMHQDNHGY ICLLIQGATK EDAGWYTVSA KNEAGIVSCT 1320
ARLDVYTQWH QQSQSTKPKK VRPSASRYAA LSDQGLDIKA AFQPEANPSH LTLNTALVES 1380
EDL 1383 
Gene Ontology
 GO:0005884; C:actin filament; IDA:HGNC.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HGNC.
 GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0051371; F:muscle alpha-actinin binding; TAS:HGNC.
 GO:0007010; P:cytoskeleton organization; NAS:HGNC. 
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