CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024330
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 FERM and PDZ domain-containing protein 4 
Protein Synonyms/Alias
 PDZ domain-containing protein 10; PSD-95-interacting regulator of spine morphogenesis; Preso 
Gene Name
 Frmpd4 
Gene Synonyms/Alias
 Gm196; Kiaa0316; Pdzd10; Pdzk10 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1195LCDYHLAKRMSSLQSacetylation[1]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
 Positive regulator of dendritic spine morphogenesis and density (By similarity). Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5- bisphosphate (By similarity). 
Sequence Annotation
 DOMAIN 33 66 WW.
 DOMAIN 78 155 PDZ.
 DOMAIN 204 519 FERM.
 MOD_RES 1250 1250 Phosphoserine.  
Keyword
 Alternative splicing; Cell projection; Complete proteome; Lipid-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1320 AA 
Protein Sequence
MDVFSFVKIP KLSSHRTKSS GWPPPSGTWG LNQVPPYGWE MMTNRDGRDY FINHMTQAIP 60
FDDPRFDSCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI 120
VMINDEAVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF 180
SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK 240
GIEHFSLMLE QRIEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR 300
DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW 360
GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG 420
GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFTEEESLV 480
RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN AGTQDTGSEN 540
KGKHNLLGPD WNCMPQMTTF IGEGEQEAQI TYIDSKQKTV EMTDSTLCPK EHRHLYIDNS 600
YSSDELNQPL TQPGDAPCEA DYRSLAQRSL LTLSGPDTLK KAQESPRGAK VSFIFGDLAL 660
DDGMSPPTIG YERMLEENPE MLEKQRNLYI SSANDMKNLD LTPDTDSIQF VANSVYANIG 720
DVKNFEAPEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LDLSGSSDDI 780
IDLTTLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDTQSQATSF HEDKEQGSSL 840
QNEEIPVSLI DAVPTSAEGK CEKGLDPAVV STLEALEALS EEQQKSENSG VAILRAYSPE 900
SSSDSGNETN SSEMTEGSEL AAAQKQSESL SRMFLATHEG YHPLAEEQTE FPTSKAPSVG 960
LPPKSSHGLA ARPATDLPPK VVPSKQILHS DHMEMEPETM ETKSVTDYFS KLHMGSVAYS 1020
CTSKRKSKLP EGEGKSPLSG NIPGKKQQGT KIAEIEEDTK GKAGTVSSRD NPHLSTFNLE 1080
RTAFRKDSQR WYVASDGGVV EKSGMEAPAM KVFPRGPGLG NREAEGKEDG TVEGGADDAS 1140
VLGQGDRFLT DMACVASAKD LDNPEDTDSP SCDHATKLSE AEDNVARLCD YHLAKRMSSL 1200
QSEGHFSLQS SQGSSVDTGC GPGSSSSACA TPVESPLCPS MGKHMIPDAS GKGGRYISPE 1260
ERAPGHPNHG ATFEELHPQT EGMCPRMTVP ALHTAINADP LFGTLRDGCH RLPKIKETTV 1320 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0043197; C:dendritic spine; ISS:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Compara.
 GO:0051835; P:positive regulation of synapse structural plasticity; ISS:UniProtKB. 
Interpro
 IPR019749; Band_41_domain.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR000299; FERM_domain.
 IPR001478; PDZ.
 IPR001202; WW_dom. 
Pfam
 PF00373; FERM_M
 PF00595; PDZ 
SMART
 SM00295; B41
 SM00228; PDZ 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3
 PS50106; PDZ
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS