LIRB5_HUMAN - dbPTM
LIRB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIRB5_HUMAN
UniProt AC O75023
Protein Name Leukocyte immunoglobulin-like receptor subfamily B member 5
Gene Name LILRB5
Organism Homo sapiens (Human).
Sequence Length 590
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description May act as receptor for class I MHC antigens..
Protein Sequence MTLTLSVLICLGLSVGPRTCVQAGTLPKPTLWAEPASVIARGKPVTLWCQGPLETEEYRLDKEGLPWARKRQNPLEPGAKAKFHIPSTVYDSAGRYRCYYETPAGWSEPSDPLELVATGFYAEPTLLALPSPVVASGGNVTLQCDTLDGLLTFVLVEEEQKLPRTLYSQKLPKGPSQALFPVGPVTPSCRWRFRCYYYYRKNPQVWSNPSDLLEILVPGVSRKPSLLIPQGSVVARGGSLTLQCRSDVGYDIFVLYKEGEHDLVQGSGQQPQAGLSQANFTLGPVSRSHGGQYRCYGAHNLSPRWSAPSDPLDILIAGLIPDIPALSVQPGPKVASGENVTLLCQSWHQIDTFFLTKEGAAHPPLCLKSKYQSYRHQAEFSMSPVTSAQGGTYRCYSAIRSYPYLLSSPSYPQELVVSGPSGDPSLSPTGSTPTPGPEDQPLTPTGLDPQSGLGRHLGVVTGVSVAFVLLLFLLLFLLLRHRHQSKHRTSAHFYRPAGAAGPEPKDQGLQKRASPVADIQEEILNAAVKDTQPKDGVEMDARAAASEAPQDVTYAQLHSLTLRREATEPPPSQEREPPAEPSIYAPLAIH
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
2Phosphorylation------MTLTLSVLI
------CCEEEEHHH
28.5724043423
4Phosphorylation----MTLTLSVLICL
----CCEEEEHHHHH
14.0724043423
6Phosphorylation--MTLTLSVLICLGL
--CCEEEEHHHHHCC
15.0524043423
14PhosphorylationVLICLGLSVGPRTCV
HHHHHCCCCCCCHHH
24.1924043423
88PhosphorylationAKFHIPSTVYDSAGR
CEEECCCEEECCCCC
20.1024719451
90PhosphorylationFHIPSTVYDSAGRYR
EECCCEEECCCCCEE
12.3124719451
139N-linked_GlycosylationPVVASGGNVTLQCDT
CEEECCCCEEEEECC
27.42UniProtKB CARBOHYD
225PhosphorylationPGVSRKPSLLIPQGS
CCCCCCCCEEECCCC
38.5523312004
279N-linked_GlycosylationQAGLSQANFTLGPVS
CCCCCCCCEEECCCC
23.8516335952
339N-linked_GlycosylationPKVASGENVTLLCQS
CCCCCCCCCEEEEEC
35.28UniProtKB CARBOHYD
434O-linked_GlycosylationSPTGSTPTPGPEDQP
CCCCCCCCCCCCCCC
40.75OGP
443O-linked_GlycosylationGPEDQPLTPTGLDPQ
CCCCCCCCCCCCCCC
26.03OGP
445O-linked_GlycosylationEDQPLTPTGLDPQSG
CCCCCCCCCCCCCCC
45.18OGP
489PhosphorylationRHQSKHRTSAHFYRP
HHHHCCCCCCCEECC
29.9523312004
490PhosphorylationHQSKHRTSAHFYRPA
HHHCCCCCCCEECCC
21.5026657352
491PhosphorylationQSKHRTSAHFYRPAG
HHCCCCCCCEECCCC
9.0124719451
494PhosphorylationHRTSAHFYRPAGAAG
CCCCCCEECCCCCCC
13.0623312004
514PhosphorylationQGLQKRASPVADIQE
CCCHHCCCCCHHHHH
24.7624972180
515PhosphorylationGLQKRASPVADIQEE
CCHHCCCCCHHHHHH
25.0824719451
546PhosphorylationMDARAAASEAPQDVT
CCHHHHHHCCCCCCC
29.5727486199
553PhosphorylationSEAPQDVTYAQLHSL
HCCCCCCCHHHHHHH
22.7928857561
554PhosphorylationEAPQDVTYAQLHSLT
CCCCCCCHHHHHHHE
7.6915474475
559PhosphorylationVTYAQLHSLTLRREA
CCHHHHHHHEEECCC
31.4828857561
560PhosphorylationTYAQLHSLTLRREAT
CHHHHHHHEEECCCC
3.49-
561PhosphorylationYAQLHSLTLRREATE
HHHHHHHEEECCCCC
22.6428857561
562PhosphorylationAQLHSLTLRREATEP
HHHHHHEEECCCCCC
6.1924719451
584PhosphorylationPPAEPSIYAPLAIH-
CCCCCCCCCCCCCC-
13.40-

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 LIRB5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIRB5_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 LIRB5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LIRB5_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 LIRB5_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-279, AND MASSSPECTROMETRY.

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