CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023917
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Collagen type IV alpha-3-binding protein 
Protein Synonyms/Alias
 Ceramide transfer protein; hCERT; Goodpasture antigen-binding protein; GPBP; START domain-containing protein 11; StARD11; StAR-related lipid transfer protein 11 
Gene Name
 COL4A3BP 
Gene Synonyms/Alias
 CERT; STARD11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
198KDELQRDKVVEDDEDubiquitination[1]
344EEQSQSEKVRLHWPTubiquitination[1]
445GIVLDPLKATHAVKGubiquitination[2]
Reference
 [1] 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]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner. 
Sequence Annotation
 DOMAIN 23 117 PH.
 DOMAIN 389 618 START.
 MOTIF 321 327 FFAT.
 BINDING 472 472 Ceramide.
 BINDING 493 493 Ceramide.
 BINDING 530 530 Ceramide.
 BINDING 579 579 Ceramide.
 MOD_RES 132 132 Phosphoserine; by PKD.
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 377 377 Phosphoserine.
 MOD_RES 380 380 Phosphoserine (By similarity).
 MOD_RES 611 611 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Lipid transport; Lipid-binding; Phosphoprotein; Polymorphism; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 624 AA 
Protein Sequence
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE 60
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG 120
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK 180
YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID 240
FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK 300
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDAFS 360
SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL 420
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV 480
VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL 540
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR 600
EYPKFLKRFT SYVQEKTAGK PILF 624 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0097001; F:ceramide binding; IDA:UniProtKB.
 GO:0035620; F:ceramide transporter activity; IDA:UniProtKB.
 GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
 GO:0004672; F:protein kinase activity; TAS:ProtInc.
 GO:0000902; P:cell morphogenesis; IEA:Compara.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0006672; P:ceramide metabolic process; IEA:Compara.
 GO:0007029; P:endoplasmic reticulum organization; IEA:Compara.
 GO:0035621; P:ER to Golgi ceramide transport; IMP:UniProtKB.
 GO:0003007; P:heart morphogenesis; IEA:Compara.
 GO:0006955; P:immune response; NAS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0055088; P:lipid homeostasis; IEA:Compara.
 GO:0070584; P:mitochondrion morphogenesis; IEA:Compara.
 GO:0006936; P:muscle contraction; IEA:Compara.
 GO:0034976; P:response to endoplasmic reticulum stress; IEA:Compara.
 GO:0007165; P:signal transduction; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome. 
Interpro
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR023393; START-like_dom.
 IPR002913; START_lipid-bd_dom. 
Pfam
 PF00169; PH
 PF01852; START 
SMART
 SM00233; PH
 SM00234; START 
PROSITE
 PS50003; PH_DOMAIN
 PS50848; START 
PRINTS