CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016043
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SEC14 domain and spectrin repeat-containing protein 1 
Protein Synonyms/Alias
 Huntingtin-interacting protein-like protein 
Gene Name
 Sestd1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
543VLLEKHRKFVDVAQSubiquitination[1]
677EHIRDRMKLVSLKRQacetylation[2, 3]
682RMKLVSLKRQQLRHPacetylation[2]
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]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] 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
 May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1 (By similarity). 
Sequence Annotation
 DOMAIN 1 153 CRAL-TRIO.
 REPEAT 275 378 Spectrin 1.
 REPEAT 381 494 Spectrin 2.
 REPEAT 500 602 Spectrin 3.  
Keyword
 Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 696 AA 
Protein Sequence
MEASVILPIL KKKLAFLSGG KDRRSGLILT IPLCLEQTSM DELSVTLDYL LSIPSEKCKA 60
RGFTVIVDGR KSQWNVVKTV VLMLQNVVPA EVSLVCVVKP DEFWDKKVTH FCFWKEKDRL 120
GFEVILVSAN KLTRYIEPCQ LTEDFGGSLT YDHMDWLNKR LVFEKFTKES TSLLDELALI 180
NNGSDKGNEQ EKERSVDLNF LPSVDPETVL QTGHELLSEL QQRRFNGSDG GVSWSPMDDE 240
LLAQPQVMKL LDSLREQYTR YQEVCRQRSK RTQLEEIQQK VMQVVNWLEG PGSEQLRAQW 300
GIGDSIRASQ ALQQKHEEIE SQHSEWFAVY VELNQQIAAL LNAGDEEDLV ELKSLQQQLS 360
DVCYRQASQL EFRQNLLQAA LEFHGVAQDL SQQLDGLLGM LCVDVAPADG ASIQQTLKLL 420
EEKLKSVDVG LQGLREKGQG LLDQISNQAS WAYGKDVTIE NKENVDHIQG VMEDMQLRKQ 480
RCEDMVDVRR LKMLQMVQLF KCEEDASQAV EWLSELLDAL LKTHIRLGDD AQETKVLLEK 540
HRKFVDVAQS TYDYGRQLLQ ATVVLCQSLR CTSRSSGDTL PRLNRVWKQF TVASEERVHR 600
LEMAIAFHSN AEKILQDCPE EPEAMNDEEQ FEEIEAIGKS LLDRLTIPVV YPDGTEQYFG 660
SPSDMASTAE HIRDRMKLVS LKRQQLRHPE LVTTES 696 
Gene Ontology
 GO:0034704; C:calcium channel complex; IEA:Compara.
 GO:0070300; F:phosphatidic acid binding; IEA:Compara.
 GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Compara.
 GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:Compara.
 GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Compara.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Compara.
 GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Compara.
 GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Compara. 
Interpro
 IPR001251; CRAL-TRIO_dom.
 IPR018159; Spectrin/alpha-actinin. 
Pfam
  
SMART
 SM00150; SPEC 
PROSITE
 PS50191; CRAL_TRIO 
PRINTS