LFA3_HUMAN - dbPTM
LFA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LFA3_HUMAN
UniProt AC P19256
Protein Name Lymphocyte function-associated antigen 3
Gene Name CD58
Organism Homo sapiens (Human).
Sequence Length 250
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Protein Description Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells..
Protein Sequence MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNGSIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTTCIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN
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
40N-linked_GlycosylationIYGVVYGNVTFHVPS
CEEEEECEEEEECCC
16.39UniProtKB CARBOHYD
62UbiquitinationLWKKQKDKVAELENS
HHHHHHHHHHHHHCC
50.8329967540
78UbiquitinationFRAFSSFKNRVYLDT
HHHHHHCCCCEEEEE
45.88-
94N-linked_GlycosylationSGSLTIYNLTSSDED
CCEEEEEECCCCCCC
32.75UniProtKB CARBOHYD
109N-linked_GlycosylationEYEMESPNITDTMKF
CCEECCCCHHHHHHH
60.10UniProtKB CARBOHYD
135N-linked_GlycosylationTLTCALTNGSIEVQC
CEEEEEECCEEEEEE
42.96UniProtKB CARBOHYD
169N-linked_GlycosylationPMEQCKRNSTSIYFK
CHHHHHHCCCEEEEE
34.8217660510
170PhosphorylationMEQCKRNSTSIYFKM
HHHHHHCCCEEEEEE
27.8029978859
171PhosphorylationEQCKRNSTSIYFKME
HHHHHCCCEEEEEEC
23.7729978859
172PhosphorylationQCKRNSTSIYFKMEN
HHHHCCCEEEEEECC
18.3429978859
174PhosphorylationKRNSTSIYFKMENDL
HHCCCEEEEEECCCC
9.2729978859
195N-linked_GlycosylationTLSNPLFNTTSSIIL
EECCCCCCCCCEEEE
50.56UniProtKB CARBOHYD
209PhosphorylationLTTCIPSSGHSRHRY
EEEECCCCCCCCCCE
34.86-
247 (in isoform 3)Phosphorylation-50.8320068231

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 LFA3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LFA3_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 LFA3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNJA1_HUMANDNAJA1physical
16169070
A4_HUMANAPPphysical
21832049

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
D02800 Alefacept (USAN/INN); Amevive (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LFA3_HUMAN

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Related Literatures of Post-Translational Modification

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