C2C2L_HUMAN - dbPTM
C2C2L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C2C2L_HUMAN
UniProt AC O14523
Protein Name Phospholipid transfer protein C2CD2L {ECO:0000305}
Gene Name C2CD2L {ECO:0000312|HGNC:HGNC:29000}
Organism Homo sapiens (Human).
Sequence Length 706
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Cell membrane
Peripheral membrane protein . Localizes to sites of contact between the endoplasmic reticulum and the cell membrane (PubMed:28209843). Embedded into the endoplamic reticu
Protein Description Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. [PubMed: 28209843 It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling]
Protein Sequence MDPGWGQRDVGWAALLILFAASLLTVFAWLLQYARGLWLARARGDRGPGPALAGEPAGSLRELGVWRSLLRLRATRAGAAEEPGVRGLLASLFAFKSFRENWQRAWVRALNEQACRNGSSIQIAFEEVPQLPPRASISHVTCVDQSEHTMVLRCQLSAEEVRFPVSVTQQSPAAVSMETYHVTLTLPPTQLEVNLEEIPGEGLLISWAFTDRPDLSLTVLPKLQARERGEEQVELSTIEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPMMPQAQPAIPRPNRLFLRQLRASHLGNELEGTEELCCVAELDNPMQQKWTKPARAGSEVEWTEDLALDLGPQSRELTLKVLRSSSCGDTELLGQATLPVGSPSRPLSRRQLCPLTPGPGKALGPAATMAVELHYEEGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTIVTTVTTVQSRPRIDGKLDSPSRSPSKVEVTEKTTTVLSESSGPSNTSHSSSRDSHLSNGLDPVAETAIRQLTEPSGRVAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASVQDDAGTSGGPSSPPSDPPAMSPGPLDALSSPTSVQEADETTRSDISERPSVDDIESETGSTGALETRSLKDHKVSFLRSGTKLIFRRRPRQKEAGLSQSHDDLSNATATPSVRKKAGSFSRRLIKRFSFKSKPKANGNPSPQL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
59PhosphorylationLAGEPAGSLRELGVW
CCCCCCCHHHHHHHH		26.7629255136
68PhosphorylationRELGVWRSLLRLRAT
HHHHHHHHHHHHHHH		18.9524719451
75PhosphorylationSLLRLRATRAGAAEE
HHHHHHHHCCCCCCC		18.0230576142
216PhosphorylationFTDRPDLSLTVLPKL
ECCCCCCEEEEHHHH		29.4024719451
218PhosphorylationDRPDLSLTVLPKLQA
CCCCCEEEEHHHHHH		19.3423312004
248PhosphorylationLIKDAIVSTQPAMMV
HHHHHHHHCCCEEEE		18.4023401153
261PhosphorylationMVNLRACSAPGGLVP
EEEEEECCCCCCCCC		36.19-
271 (in isoform 2)Ubiquitination-59.77-
271UbiquitinationGGLVPSEKPPMMPQA
CCCCCCCCCCCCCCC		59.7729967540
330PhosphorylationTKPARAGSEVEWTED
CCCCCCCCCCEECHH		37.1728348404
352UbiquitinationQSRELTLKVLRSSSC
CCHHEEHHHHHHCCC		33.7129967540
352 (in isoform 2)Ubiquitination-33.71-
356PhosphorylationLTLKVLRSSSCGDTE
EEHHHHHHCCCCCCE		23.5726074081
357PhosphorylationTLKVLRSSSCGDTEL
EHHHHHHCCCCCCEE		24.1826074081
358PhosphorylationLKVLRSSSCGDTELL
HHHHHHCCCCCCEEE		24.3026074081
362PhosphorylationRSSSCGDTELLGQAT
HHCCCCCCEEECEEE		17.5126074081
369PhosphorylationTELLGQATLPVGSPS
CEEECEEECCCCCCC		24.5730108239
374PhosphorylationQATLPVGSPSRPLSR
EEECCCCCCCCCCCH		21.6730278072
376PhosphorylationTLPVGSPSRPLSRRQ
ECCCCCCCCCCCHHC		48.5030278072
380PhosphorylationGSPSRPLSRRQLCPL
CCCCCCCCHHCCCCC		28.2730108239
388PhosphorylationRRQLCPLTPGPGKAL
HHCCCCCCCCCCCCC		16.0221815630
400PhosphorylationKALGPAATMAVELHY
CCCCHHHEEEEEEEE		14.0430108239
407PhosphorylationTMAVELHYEEGSPRN
EEEEEEEECCCCCCC		28.4430108239
411PhosphorylationELHYEEGSPRNLGTP
EEEECCCCCCCCCCC		24.7825159151
417PhosphorylationGSPRNLGTPTSSTPR
CCCCCCCCCCCCCCC		26.9330266825
419PhosphorylationPRNLGTPTSSTPRPS
CCCCCCCCCCCCCCC		34.8430266825
420PhosphorylationRNLGTPTSSTPRPSI
CCCCCCCCCCCCCCC		33.1630266825
421PhosphorylationNLGTPTSSTPRPSIT
CCCCCCCCCCCCCCC		44.9330266825
422PhosphorylationLGTPTSSTPRPSITP
CCCCCCCCCCCCCCC		24.0830266825
426PhosphorylationTSSTPRPSITPTKKI
CCCCCCCCCCCCCCE		40.1330266825
428PhosphorylationSTPRPSITPTKKIEL
CCCCCCCCCCCCEEE		29.2830266825
430PhosphorylationPRPSITPTKKIELDR
CCCCCCCCCCEEECC		36.0030266825
447O-linked_GlycosylationMPDGTIVTTVTTVQS
CCCCCEEEEEEEECC		16.2328657654
448O-linked_GlycosylationPDGTIVTTVTTVQSR
CCCCEEEEEEEECCC		12.6428657654
450O-linked_GlycosylationGTIVTTVTTVQSRPR
CCEEEEEEEECCCCC		21.1128657654
451O-linked_GlycosylationTIVTTVTTVQSRPRI
CEEEEEEEECCCCCC		16.5328657654
464PhosphorylationRIDGKLDSPSRSPSK
CCCCCCCCCCCCCCE		34.9030266825
466PhosphorylationDGKLDSPSRSPSKVE
CCCCCCCCCCCCEEE		49.7130266825
468PhosphorylationKLDSPSRSPSKVEVT
CCCCCCCCCCEEEEE		37.5530266825
470PhosphorylationDSPSRSPSKVEVTEK
CCCCCCCCEEEEEEC		51.0530266825
475PhosphorylationSPSKVEVTEKTTTVL
CCCEEEEEECCEEEE		20.4729255136
478PhosphorylationKVEVTEKTTTVLSES
EEEEEECCEEEEECC		22.8228258704
479PhosphorylationVEVTEKTTTVLSESS
EEEEECCEEEEECCC		26.4428258704
480PhosphorylationEVTEKTTTVLSESSG
EEEECCEEEEECCCC		25.3623312004
483PhosphorylationEKTTTVLSESSGPSN
ECCEEEEECCCCCCC		30.9728258704
485PhosphorylationTTTVLSESSGPSNTS
CEEEEECCCCCCCCC		36.9023312004
486PhosphorylationTTVLSESSGPSNTSH
EEEEECCCCCCCCCC		51.1523312004
489PhosphorylationLSESSGPSNTSHSSS
EECCCCCCCCCCCCH		57.1525159151
491PhosphorylationESSGPSNTSHSSSRD
CCCCCCCCCCCCHHH		31.9625159151
492PhosphorylationSSGPSNTSHSSSRDS
CCCCCCCCCCCHHHH		26.1425159151
494PhosphorylationGPSNTSHSSSRDSHL
CCCCCCCCCHHHHHH		29.7623312004
495PhosphorylationPSNTSHSSSRDSHLS
CCCCCCCCHHHHHHH		24.7823312004
496PhosphorylationSNTSHSSSRDSHLSN
CCCCCCCHHHHHHHC		43.0223312004
499PhosphorylationSHSSSRDSHLSNGLD
CCCCHHHHHHHCCCC		25.8029523821
502PhosphorylationSSRDSHLSNGLDPVA
CHHHHHHHCCCCHHH		24.3525849741
511PhosphorylationGLDPVAETAIRQLTE
CCCHHHHHHHHHHHC		20.04-
532PhosphorylationKKTPTKRSTLIISGV
CCCCCCCCEEEEECC		29.1728857561
533PhosphorylationKTPTKRSTLIISGVS
CCCCCCCEEEEECCC		26.4728555341
606PhosphorylationEADETTRSDISERPS
HCCCCCCCCCCCCCC		36.8823663014
609PhosphorylationETTRSDISERPSVDD
CCCCCCCCCCCCHHH		32.3229255136
613PhosphorylationSDISERPSVDDIESE
CCCCCCCCHHHHCCC		44.3829255136
619PhosphorylationPSVDDIESETGSTGA
CCHHHHCCCCCCCCC		40.5729255136
621PhosphorylationVDDIESETGSTGALE
HHHHCCCCCCCCCEE		45.7929255136
623PhosphorylationDIESETGSTGALETR
HHCCCCCCCCCEEEE		30.9629255136
624PhosphorylationIESETGSTGALETRS
HCCCCCCCCCEEEEC		28.0229255136
625PhosphorylationESETGSTGALETRSL
CCCCCCCCCEEEECC		29.8432645325
629PhosphorylationGSTGALETRSLKDHK
CCCCCEEEECCCCCC		26.8023663014
631PhosphorylationTGALETRSLKDHKVS
CCCEEEECCCCCCEE		47.3820873877
638PhosphorylationSLKDHKVSFLRSGTK
CCCCCCEEEECCCCE		24.3020873877
644PhosphorylationVSFLRSGTKLIFRRR
EEEECCCCEEEEECC		24.7528857561
660PhosphorylationRQKEAGLSQSHDDLS
HHHHCCCCCCHHHHH		28.8129255136
662PhosphorylationKEAGLSQSHDDLSNA
HHCCCCCCHHHHHHC		26.0529255136
663PhosphorylationEAGLSQSHDDLSNAT
HCCCCCCHHHHHHCC		25.6032645325
667PhosphorylationSQSHDDLSNATATPS
CCCHHHHHHCCCCHH		31.2630266825
670PhosphorylationHDDLSNATATPSVRK
HHHHHHCCCCHHHHH		35.0029255136
672PhosphorylationDLSNATATPSVRKKA
HHHHCCCCHHHHHHC		16.2529255136
674PhosphorylationSNATATPSVRKKAGS
HHCCCCHHHHHHCCH		30.1429255136
681PhosphorylationSVRKKAGSFSRRLIK
HHHHHCCHHHHHHHH		25.5530576142
683PhosphorylationRKKAGSFSRRLIKRF
HHHCCHHHHHHHHHH		20.4229514088
691PhosphorylationRRLIKRFSFKSKPKA
HHHHHHHCCCCCCCC		35.4823927012
694PhosphorylationIKRFSFKSKPKANGN
HHHHCCCCCCCCCCC		52.7823312004
703PhosphorylationPKANGNPSPQL----
CCCCCCCCCCC----		29.3123403867
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of C2C2L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C2C2L_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of C2C2L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of C2C2L_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C2C2L_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417; SER-420; THR-430;SER-464 AND SER-468, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory