CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023918
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
573GIVLDPLKATHAVKGubiquitination[1]
Reference
 [1] 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
MQHSCIPTPP SPFSAPPAFL PVVTRESRRG LSSGGSAGRN AGVTATAAAA DGWKGRLPSP 60
LVLLPRSARC QARRRRGGRT SSLLLLPPTP ERALFASPSP DPSPRGLGAS SGAAEGAGAG 120
LLLGCRASMS DNQSWNSSGS EEDPETESGP PVERCGVLSK WTNYIHGWQD RWVVLKNNAL 180
SYYKSEDETE YGCRGSICLS KAVITPHDFD ECRFDISVND SVWYLRAQDP DHRQQWIDAI 240
EQHKTESGYG SESSLRRHGS MVSLVSGASG YSATSTSSFK KGHSLREKLA EMETFRDILC 300
RQVDTLQKYF DACADAVSKD ELQRDKVVED DEDDFPTTRS DGDFLHSTNG NKEKLFPHVT 360
PKGINGIDFK GEAITFKATT AGILATLSHC IELMVKREDS WQKRLDKETE KKRRTEEAYK 420
NAMTELKKKS HFGGPDYEEG PNSLINEEEF FDAVEAALDR QDKIEEQSQS EKVRLHWPTS 480
LPSGDAFSSV GTHRFVQKPY SRSSSMSSID LVSASDDVHR FSSQVEEMVQ NHMTYSLQDV 540
GGDANWQLVV EEGEMKVYRR EVEENGIVLD PLKATHAVKG VTGHEVCNYF WNVDVRNDWE 600
TTIENFHVVE TLADNAIIIY QTHKRVWPAS QRDVLYLSVI RKIPALTEND PETWIVCNFS 660
VDHDSAPLNN RCVRAKINVA MICQTLVSPP EGNQEISRDN ILCKITYVAN VNPGGWAPAS 720
VLRAVAKREY PKFLKRFTSY VQEKTAGKPI LF 752 
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