CD1E_HUMAN - dbPTM
CD1E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD1E_HUMAN
UniProt AC P15812
Protein Name T-cell surface glycoprotein CD1e, membrane-associated
Gene Name CD1E
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization T-cell surface glycoprotein CD1e, membrane-associated: Golgi apparatus membrane
Single-pass type I membrane protein. Early endosome. Late endosome. Predominantly localized in the trans-Golgi network in immature dendritic cells, and as a cleaved, sol
Protein Description T-cell surface glycoprotein CD1e, soluble binds diacetylated lipids, including phosphatidyl inositides and diacylated sulfoglycolipids, and is required for the presentation of glycolipid antigens on the cell surface. The membrane-associated form is not active..
Protein Sequence MLLLFLLFEGLCCPGENTAAPQALQSYHLAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTVLGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTCPRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQEQRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLILICLTVIVTLVILVVVDSRLKKQSSNKNILSPHTPSPVFLMGANTQDTKNSRHQFCLAQVSWIKNRVLKKWKTRLNQLW
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
47N-linked_GlycosylationLQTSSFANHSWAHSE
HHCCCCCCCCEECCC
27.93UniProtKB CARBOHYD
78UbiquitinationLGTIRFLKPWSHGNF
HHHHHCCCCCCCCCC
41.55-
84N-linked_GlycosylationLKPWSHGNFSKQELK
CCCCCCCCCCHHHHH
32.37UniProtKB CARBOHYD
87 (in isoform 12)Ubiquitination-43.59-
87UbiquitinationWSHGNFSKQELKNLQ
CCCCCCCHHHHHHHH
43.59-
89 (in isoform 12)Phosphorylation-66.5024275569
102 (in isoform 12)Ubiquitination-14.29-
144 (in isoform 9)Phosphorylation-19.2624275569
170UbiquitinationIRAQNICKVLNRYLD
HHHHHHHHHHHHHCC
46.06-
179UbiquitinationLNRYLDIKEILQSLL
HHHHCCHHHHHHHHH
38.07-
188 (in isoform 7)Phosphorylation-25.0224275569
206 (in isoform 2)Ubiquitination-46.23-
206UbiquitinationEAGESELKRKVKPEA
HHCHHHHHHCCCHHH
46.23-
208UbiquitinationGESELKRKVKPEAWL
CHHHHHHCCCHHHHH
53.69-
208 (in isoform 2)Ubiquitination-53.69-
210UbiquitinationSELKRKVKPEAWLSC
HHHHHCCCHHHHHHC
39.93-
210 (in isoform 2)Ubiquitination-39.93-
220PhosphorylationAWLSCGPSPGPGRLQ
HHHHCCCCCCCCCEE
27.9823532336
243 (in isoform 6)Phosphorylation-1.0524275569
278 (in isoform 4)Phosphorylation-18.4824275569
314PhosphorylationFLILICLTVIVTLVI
HHHHHHHHHHHHHHH
12.0819690332
331 (in isoform 2)Ubiquitination-61.06-
333 (in isoform 2)Phosphorylation-44.7724275569
336UbiquitinationLKKQSSNKNILSPHT
HHCCCCCCCCCCCCC
47.52-
342 (in isoform 2)Phosphorylation-47.21-
345 (in isoform 2)Phosphorylation-34.55-
346 (in isoform 2)Ubiquitination-23.29-
354PhosphorylationVFLMGANTQDTKNSR
EEEEECCCCCCCCCC
27.5624275569
357PhosphorylationMGANTQDTKNSRHQF
EECCCCCCCCCCCCH
23.4724275569
358UbiquitinationGANTQDTKNSRHQFC
ECCCCCCCCCCCCHH
62.30-
361 (in isoform 2)Ubiquitination-36.70-
370PhosphorylationQFCLAQVSWIKNRVL
CHHHHHHHHHHHHHH
15.82-
373UbiquitinationLAQVSWIKNRVLKKW
HHHHHHHHHHHHHHH
32.23-

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 CD1E_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD1E_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 CD1E_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCGRN_HUMANFCGRTphysical
28514442
SUSD5_HUMANSUSD5physical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
C1QRF_HUMANC1QL1physical
28514442
TM59L_HUMANTMEM59Lphysical
28514442
CALX_HUMANCANXphysical
28514442
GPT_HUMANDPAGT1physical
28514442
CTGE5_HUMANCTAGE5physical
28514442
B2MG_HUMANB2Mphysical
28514442
KCNJ8_HUMANKCNJ8physical
28514442
ENTP7_HUMANENTPD7physical
28514442
BACE2_HUMANBACE2physical
28514442
FA69A_HUMANFAM69Aphysical
28514442
POMT1_HUMANPOMT1physical
28514442
MKS3_HUMANTMEM67physical
28514442
SEM4F_HUMANSEMA4Fphysical
28514442
MA2A2_HUMANMAN2A2physical
28514442
STIM1_HUMANSTIM1physical
28514442
ABHEA_HUMANABHD14Aphysical
28514442
NCEH1_HUMANNCEH1physical
28514442
MA1A2_HUMANMAN1A2physical
28514442
PLXA2_HUMANPLXNA2physical
28514442
ITA7_HUMANITGA7physical
28514442
LMA2L_HUMANLMAN2Lphysical
28514442
ANR46_HUMANANKRD46physical
28514442
CC50A_HUMANTMEM30Aphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD1E_HUMAN

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Related Literatures of Post-Translational Modification

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