LIRB1_HUMAN - dbPTM
LIRB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIRB1_HUMAN
UniProt AC Q8NHL6
Protein Name Leukocyte immunoglobulin-like receptor subfamily B member 1
Gene Name LILRB1
Organism Homo sapiens (Human).
Sequence Length 650
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Isoform 5: Secreted .
Protein Description Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions..
Protein Sequence MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH
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
58NitrationGGQETQEYRLYREKK
CCCCCCEEEEECCCC
8.97-
99NitrationHAGRYRCYYGSDTAG
ECCEEEEEECCCCCC
11.23-
100NitrationAGRYRCYYGSDTAGR
CCEEEEEECCCCCCC
17.49-
122NitrationELVVTGAYIKPTLSA
EEEEECCEECCCCCC
15.72-
252NitrationQCGSDAGYNRFVLYK
EECCCCCCCEEEEEE
12.60-
281N-linked_GlycosylationQAGLSQANFTLGPVS
CCCCCCCCEEECCCC
23.85UniProtKB CARBOHYD
302N-linked_GlycosylationYRCYGAHNLSSEWSA
EEEECCCCCCCCCCC
40.87UniProtKB CARBOHYD
341N-linked_GlycosylationPTVASGENVTLLCQS
CEECCCCCEEEEEEC
35.28UniProtKB CARBOHYD
378PhosphorylationSTYQSQKYQAEFPMG
CHHHHHEEEEECCCC
12.81-
378NitrationSTYQSQKYQAEFPMG
CHHHHHEEEEECCCC
12.81-
406NitrationGSQSSKPYLLTHPSD
CCCCCCCEEEECCCC
20.34-
521PhosphorylationDRGLQWRSSPAADAQ
CCCCCCCCCCCCHHH
37.4028450419
522 (in isoform 3)Phosphorylation-15.2424719451
522PhosphorylationRGLQWRSSPAADAQE
CCCCCCCCCCCHHHH
15.2426657352
523PhosphorylationGLQWRSSPAADAQEE
CCCCCCCCCCHHHHH
32.4827251275
533PhosphorylationDAQEENLYAAVKHTQ
HHHHHCHHHHHHCCC
12.2329978859
534PhosphorylationAQEENLYAAVKHTQP
HHHHCHHHHHHCCCC
14.67-
549 (in isoform 4)Phosphorylation-31.5630108239
550 (in isoform 3)Phosphorylation-43.8830108239
551PhosphorylationGVEMDTRSPHDEDPQ
CCCCCCCCCCCCCCC
28.7830108239
552 (in isoform 4)Phosphorylation-35.3430108239
553 (in isoform 3)Phosphorylation-52.9530108239
561PhosphorylationDEDPQAVTYAEVKHS
CCCCCCCCCEEECCC
21.7423532336
562 (in isoform 4)Phosphorylation-8.3129978859
562PhosphorylationEDPQAVTYAEVKHSR
CCCCCCCCEEECCCC
8.3129978859
563 (in isoform 4)Phosphorylation-13.0229978859
563 (in isoform 3)Phosphorylation-13.0229978859
563 (in isoform 2)Phosphorylation-13.0225587033
564 (in isoform 3)Phosphorylation-41.5029978859
564PhosphorylationPQAVTYAEVKHSRPR
CCCCCCEEECCCCCC
41.50-
576PhosphorylationRPRREMASPPSPLSG
CCCCCCCCCCCCCCC
35.7128450419
579PhosphorylationREMASPPSPLSGEFL
CCCCCCCCCCCCCCC
41.6928355574
581PhosphorylationMASPPSPLSGEFLDT
CCCCCCCCCCCCCCH
13.9120166139
582PhosphorylationASPPSPLSGEFLDTK
CCCCCCCCCCCCCHH
39.3928450419
584PhosphorylationPPSPLSGEFLDTKDR
CCCCCCCCCCCHHHH
39.39-
588PhosphorylationLSGEFLDTKDRQAEE
CCCCCCCHHHHHHHH
36.6730108239
606PhosphorylationMDTEAAASEAPQDVT
HCHHHHHHHCCCCCC
29.5727486199
613PhosphorylationSEAPQDVTYAQLHSL
HHCCCCCCHHHHHHH
22.7928857561
614PhosphorylationEAPQDVTYAQLHSLT
HCCCCCCHHHHHHHE
7.6915474475
619PhosphorylationVTYAQLHSLTLRREA
CCHHHHHHHEEEECC
31.4828857561
621PhosphorylationYAQLHSLTLRREATE
HHHHHHHEEEECCCC
22.6428857561
644PhosphorylationSPAVPSIYATLAIH-
CCCCCCEEEEECCC-
9.629285411

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
-KUbiquitinationE3 ubiquitin ligaseMARCHF9Q86YJ5
PMID:19457934

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIRB1_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 LIRB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1A02_HUMANHLA-Aphysical
12897781
1A03_HUMANHLA-Aphysical
12897781
1A01_HUMANHLA-Aphysical
12897781
1A26_HUMANHLA-Aphysical
12897781
1B07_HUMANHLA-Bphysical
12853576
1B18_HUMANHLA-Bphysical
12853576
1C07_HUMANHLA-Cphysical
12853576
HLAG_HUMANHLA-Gphysical
12853576
HLAF_HUMANHLA-Fphysical
11169396
PTN6_HUMANPTPN6physical
9842885

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 LIRB1_HUMAN

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Related Literatures of Post-Translational Modification

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