CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016786
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Synaptopodin 
Protein Synonyms/Alias
  
Gene Name
 Synpo 
Gene Synonyms/Alias
 Kiaa1029 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
255SLLRHLEKVASEEEEubiquitination[1]
391SSILLIDKVSAPPSAubiquitination[1]
463EVHLTLAKPASVVNRubiquitination[1]
499GRRQFGEKAWAPPASubiquitination[1]
581LYPSSDPKPSHLKGQubiquitination[1]
586DPKPSHLKGQVAPANubiquitination[1]
594GQVAPANKTGILEESubiquitination[1]
609MARRGSRKSMFTFVEubiquitination[1]
617SMFTFVEKPKVTPNPubiquitination[1]
619FTFVEKPKVTPNPDLubiquitination[1]
636LVQTADEKRRQRDHGubiquitination[1]
710NLSEASGKGAELYARubiquitination[1]
724RRQSRMEKYVIESSGubiquitination[1]
750MSLPSSWKYTTNAPGubiquitination[1]
808LYALSPVKEPAKASSubiquitination[1]
812SPVKEPAKASSRATSubiquitination[1]
836PRAASPAKPSSLDLVubiquitination[1]
923GIEAQVWKPSFCFK*ubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity. 
Sequence Annotation
 MOTIF 549 552 PPxY motif.
 MOTIF 568 571 PPxY motif.
 MOD_RES 258 258 Phosphoserine.
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 512 512 Phosphoserine (By similarity).
 MOD_RES 535 535 Phosphoserine.
 MOD_RES 567 567 Phosphoserine (By similarity).
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 689 689 Phosphoserine (By similarity).
 MOD_RES 740 740 Phosphoserine.
 MOD_RES 833 833 Phosphoserine.
 MOD_RES 882 882 Phosphoserine.
 MOD_RES 884 884 Phosphothreonine.  
Keyword
 Actin-binding; Alternative splicing; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 929 AA 
Protein Sequence
MLGAHFPPPP LGASEGRAAP CTFQIPDGSY RCLALEAEES SSEDGLQGEV RLVDLEEEGT 60
SQSRANHGTP PLSRAPAIIQ PSSCHREARG GFQRSDRPSH DWDVVQARKV MTASGSSSPV 120
PRVAQKPALG RSTSFTENDL KEAKARSQQI AAQLTTPPSS NSRGVQLFNR RRQRVNEFTL 180
ESRGQRSPKL NQEALQTGRP LSPIGHAPGP SVKPTSPSKP GSPKHPSPQS PSRGVAGHIM 240
EGYSEEASLL RHLEKVASEE EEVPLVVYLK ENAALLTANG LHLSQSRETQ QSSPNPPDTE 300
VPSPAADINQ NPSSPNATLT TLASSSHHSQ PTADINQNPP AAITPVPQNS SQAQCSPNGT 360
LDSKPGTLCA DDGQSPVPAE EVRSSILLID KVSAPPSAAS TFSREATPLS SSGPPAADLM 420
SSSLLIDMQP STLVAPAEQE VPGHVAVTTP TKVYSEVHLT LAKPASVVNR TARPFGIQSP 480
GTSQIEQSPM MGRRQFGEKA WAPPASSMAD RSPQPQRHIM SRSPMVERRL LGQRSPVLER 540
RPLGNFTPPP TYAETLSTAP VASRVRSPPS YSTLYPSSDP KPSHLKGQVA PANKTGILEE 600
SMARRGSRKS MFTFVEKPKV TPNPDLLDLV QTADEKRRQR DHGEVGMEEE PFALGAEASN 660
FQQEPIARDR ASPAAAEEAV PEWASCLKSP RIQAKPKPKP NQNLSEASGK GAELYARRQS 720
RMEKYVIESS GHAELARCPS PTMSLPSSWK YTTNAPGGFR VASLSPARTP PASLYHGYLP 780
ENGVLRPEPT KQQPYQMRPS LYALSPVKEP AKASSRATSS RTPSRTVSPR AASPAKPSSL 840
DLVPNLPRAG LPPSPALPRP SRSSPGLYTA PVQDSLQPTA VSPTYSSDIS PVSPSRAWSP 900
RAKQAPRPSF STRNAGIEAQ VWKPSFCFK 929 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:MGI.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0043197; C:dendritic spine; NAS:UniProtKB.
 GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; IDA:MGI.
 GO:0030865; P:cortical cytoskeleton organization; NAS:UniProtKB.
 GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:UniProtKB.
 GO:0051492; P:regulation of stress fiber assembly; IDA:UniProtKB. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS