CD14_HUMAN - dbPTM
CD14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD14_HUMAN
UniProt AC P08571
Protein Name Monocyte differentiation antigen CD14 {ECO:0000303|PubMed:3385210}
Gene Name CD14
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor . Secreted . Membrane raft . Golgi apparatus . Secreted forms may arise by cleavage of the GPI anchor.
Protein Description Coreceptor for bacterial lipopolysaccharide. [PubMed: 1698311]
Protein Sequence MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA
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
37N-linked_GlycosylationEDFRCVCNFSEPQPD
CCEEEEECCCCCCCC		24.07UniProtKB CARBOHYD
95PhosphorylationALRVRRLTVGAAQVP
HHHEEECCCCCCHHH		18.32-
145PhosphorylationEATGLALSSLRLRNV
CHHHHEHHHHHHCCC		23.0130301811
146PhosphorylationATGLALSSLRLRNVS
HHHHEHHHHHHCCCC		20.5425954137
151N-linked_GlycosylationLSSLRLRNVSWATGR
HHHHHHCCCCHHCCH		36.4416335952
275PhosphorylationSAPRCMWSSALNSLN
CCCHHHHHHHHHHCC		4.4627251275
276PhosphorylationAPRCMWSSALNSLNL
CCHHHHHHHHHHCCC		22.6627251275
280PhosphorylationMWSSALNSLNLSFAG
HHHHHHHHCCCCCCC		21.3427251275
282N-linked_GlycosylationSSALNSLNLSFAGLE
HHHHHHCCCCCCCHH		33.2016335952
284PhosphorylationALNSLNLSFAGLEQV
HHHHCCCCCCCHHCC		16.3927251275
323N-linked_GlycosylationDELPEVDNLTLDGNP
CCCCCCCCEEECCCC		39.8519159218
336O-linked_GlycosylationNPFLVPGTALPHEGS
CCCCCCCCCCCCCCC		20.9619838169
345GPI-anchorLPHEGSMNSGVVPAC
CCCCCCCCCCCCCCC		36.99-
362O-linked_GlycosylationSTLSVGVSGTLVLLQ
CEEEEECCCCEEEEE		21.82OGP
364O-linked_GlycosylationLSVGVSGTLVLLQGA
EEEECCCCEEEEECC		13.24OGP
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 CD14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD14_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 CD14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LBP_HUMANLBPphysical
12417309
LBP_HUMANLBPphysical
7583357
TLR2_HUMANTLR2physical
10395652
CANB2_HUMANPPP3R2physical
21988832
CXB2_HUMANGJB2physical
21988832
RPB11_HUMANPOLR2Jphysical
21988832
TNR1B_HUMANTNFRSF1Bphysical
21988832
IRAK3_HUMANIRAK3physical
21988832
ANXA7_HUMANANXA7physical
26496610
BUB1B_HUMANBUB1Bphysical
26496610
AP3S1_HUMANAP3S1physical
26496610
MYPT2_HUMANPPP1R12Bphysical
26496610
SVIL_HUMANSVILphysical
26496610
TAF1_HUMANTAF1physical
26496610
TAF9_HUMANTAF9physical
26496610
ICAM5_HUMANICAM5physical
26496610
OASL_HUMANOASLphysical
26496610
EXO1_HUMANEXO1physical
26496610
HPS5_HUMANHPS5physical
26496610
P20L1_HUMANPHF20L1physical
26496610
PF21A_HUMANPHF21Aphysical
26496610
BCAS3_HUMANBCAS3physical
26496610
WDCP_HUMANC2orf44physical
26496610
ARID2_HUMANARID2physical
26496610
Drug and Disease Associations
Kegg Disease
H00003 Acute myeloid leukemia (AML)
H00079 Asthma
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 CD14_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151 AND ASN-282, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-336, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.

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