MICA_HUMAN - dbPTM
MICA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MICA_HUMAN
UniProt AC Q29983
Protein Name MHC class I polypeptide-related sequence A
Gene Name MICA {ECO:0000312|EMBL:CAI41907.1}
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cytoplasm . Expressed on the cell surface in gastric epithelium, endothelial cells and fibroblasts and in the cytoplasm in keratinocytes and monocytes. Infection with human adenovirus 5 suppresses
Protein Description Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T-cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis..
Protein Sequence MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA
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
31N-linked_GlycosylationEPHSLRYNLTVLSWD
CCCCCEEEEEEEEEC
23.85UniProtKB CARBOHYD
79N-linked_GlycosylationWAEDVLGNKTWDRET
CHHHHHCCCCCCCCC
34.13UniProtKB CARBOHYD
94UbiquitinationRDLTGNGKDLRMTLA
CCCCCCCCCHHHHHH
58.55-
104UbiquitinationRMTLAHIKDQKEGLH
HHHHHHHHCHHCCHH
44.21-
194PhosphorylationCLQELRRYLKSGVVL
HHHHHHHHHHHCCEE
16.4320068231
197PhosphorylationELRRYLKSGVVLRRT
HHHHHHHHCCEEEEC
33.9420068231
204PhosphorylationSGVVLRRTVPPMVNV
HCCEEEECCCCEEEE
30.8122210691
210N-linked_GlycosylationRTVPPMVNVTRSEAS
ECCCCEEEEECCCCC
24.16UniProtKB CARBOHYD
212PhosphorylationVPPMVNVTRSEASEG
CCCEEEEECCCCCCC
24.2322210691
220N-linked_GlycosylationRSEASEGNITVTCRA
CCCCCCCCEEEEEEC
23.78UniProtKB CARBOHYD
238PhosphorylationYPWNITLSWRQDGVS
ECEEEEEEEECCCEE
16.1524719451
261N-linked_GlycosylationGDVLPDGNGTYQTWV
CCCCCCCCCCEEEEE
47.19UniProtKB CARBOHYD
330S-palmitoylationIIIFYVRCCKKKTSA
HHHHHHHHHCCCCCC
2.5921928280
331S-palmitoylationIIFYVRCCKKKTSAA
HHHHHHHHCCCCCCC
5.1921928280
335PhosphorylationVRCCKKKTSAAEGPE
HHHHCCCCCCCCCCC
32.2623312004
336PhosphorylationRCCKKKTSAAEGPEL
HHHCCCCCCCCCCCE
34.0723312004
345PhosphorylationAEGPELVSLQVLDQH
CCCCCEEEEEEECCC
26.2123312004
356PhosphorylationLDQHPVGTSDHRDAT
ECCCCCCCCCCCHHH
31.0823312004
357PhosphorylationDQHPVGTSDHRDATQ
CCCCCCCCCCCHHHH
26.0323312004
372PhosphorylationLGFQPLMSDLGSTGS
HCCCCCHHHCCCCCC
37.0529485707
376PhosphorylationPLMSDLGSTGSTEGA
CCHHHCCCCCCCCCC
36.5729485707

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 MICA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MICA_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 MICA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAC14_HUMANVAC14physical
26186194
FLVC1_HUMANFLVCR1physical
26186194
TNPO2_HUMANTNPO2physical
26186194
SCAM1_HUMANSCAMP1physical
26186194
RYK_HUMANRYKphysical
26186194
ADAP2_HUMANADAP2physical
26186194
TNPO3_HUMANTNPO3physical
26186194
NR3L1_HUMANNCR3LG1physical
26186194
ERLEC_HUMANERLEC1physical
26186194
VAMP3_HUMANVAMP3physical
26186194
PGRC2_HUMANPGRMC2physical
26186194
TR10B_HUMANTNFRSF10Bphysical
26186194
TNFL9_HUMANTNFSF9physical
26186194
ADAP2_HUMANADAP2physical
28514442
SCAM1_HUMANSCAMP1physical
28514442
FLVC1_HUMANFLVCR1physical
28514442
VAMP3_HUMANVAMP3physical
28514442
RYK_HUMANRYKphysical
28514442
TNPO3_HUMANTNPO3physical
28514442
ERLEC_HUMANERLEC1physical
28514442
TNFL9_HUMANTNFSF9physical
28514442
TR10B_HUMANTNFRSF10Bphysical
28514442
TNPO2_HUMANTNPO2physical
28514442

Drug and Disease Associations
Kegg Disease
H00288 Familial Mediterranean fever (FMF); Familial hereditary periodic fever syndromes
OMIM Disease
Note=Anti-MICA antibodies and ligand shedding are involved in the progression of monoclonal gammopathy of undetermined significance (MGUS)to multiple myeloma.
177900
607507Psoriatic arthritis (PSORAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MICA_HUMAN

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Related Literatures of Post-Translational Modification

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