MICB_HUMAN - dbPTM
MICB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MICB_HUMAN
UniProt AC Q29980
Protein Name MHC class I polypeptide-related sequence B
Gene Name MICB {ECO:0000312|EMBL:CAA62823.1}
Organism Homo sapiens (Human).
Sequence Length 383
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Binding to human cytomegalovirus glycoprotein UL16 causes sequestration in the endoplasmic reticulum.
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 MGLGRVLLFLAVAFPFAPPAAAAEPHSLRYNLMVLSQDESVQSGFLAEGHLDGQPFLRYDRQKRRAKPQGQWAEDVLGAKTWDTETEDLTENGQDLRRTLTHIKDQKGGLHSLQEIRVCEIHEDSSTRGSRHFYYDGELFLSQNLETQESTVPQSSRAQTLAMNVTNFWKEDAMKTKTHYRAMQADCLQKLQRYLKSGVAIRRTVPPMVNVTCSEVSEGNITVTCRASSFYPRNITLTWRQDGVSLSHNTQQWGDVLPDGNGTYQTWVATRIRQGEEQRFTCYMEHSGNHGTHPVPSGKVLVLQSQRTDFPYVSAAMPCFVIIIILCVPCCKKKTSAAEGPELVSLQVLDQHPVGTGDHRDAAQLGFQPLMSATGSTGSTEGA
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
67UbiquitinationDRQKRRAKPQGQWAE
HHHHHCCCCCCCCHH
35.74-
67UbiquitinationDRQKRRAKPQGQWAE
HHHHHCCCCCCCCHH
35.7421906983
67UbiquitinationDRQKRRAKPQGQWAE
HHHHHCCCCCCCCHH
35.7421906983
67UbiquitinationDRQKRRAKPQGQWAE
HHHHHCCCCCCCCHH
35.74-
81PhosphorylationEDVLGAKTWDTETED
HHHHCCCCCCCCCHH
28.21-
84PhosphorylationLGAKTWDTETEDLTE
HCCCCCCCCCHHHHH
36.05-
86PhosphorylationAKTWDTETEDLTENG
CCCCCCCCHHHHHCC
36.57-
99PhosphorylationNGQDLRRTLTHIKDQ
CCHHHHHHHHHHHCC
29.58-
101PhosphorylationQDLRRTLTHIKDQKG
HHHHHHHHHHHCCCC
22.42-
104UbiquitinationRRTLTHIKDQKGGLH
HHHHHHHHCCCCCCC
46.64-
104UbiquitinationRRTLTHIKDQKGGLH
HHHHHHHHCCCCCCC
46.64-
107UbiquitinationLTHIKDQKGGLHSLQ
HHHHHCCCCCCCCCC
66.15-
112PhosphorylationDQKGGLHSLQEIRVC
CCCCCCCCCCEEEEE
36.47-
127UbiquitinationEIHEDSSTRGSRHFY
EEECCCCCCCCEEEE
42.89-
147UbiquitinationFLSQNLETQESTVPQ
EEECCCCCCCCCCCC
40.58-
153UbiquitinationETQESTVPQSSRAQT
CCCCCCCCCCHHHHH
28.5521906983
153UbiquitinationETQESTVPQSSRAQT
CCCCCCCCCCHHHHH
28.5521906983
164N-linked_GlycosylationRAQTLAMNVTNFWKE
HHHHHHHHHHHHHHH
31.67UniProtKB CARBOHYD
170UbiquitinationMNVTNFWKEDAMKTK
HHHHHHHHHHHHHHH
41.39-
190UbiquitinationMQADCLQKLQRYLKS
HHHHHHHHHHHHHHH
33.37-
196UbiquitinationQKLQRYLKSGVAIRR
HHHHHHHHHCCCCCC
35.912190698
196 (in isoform 1)Ubiquitination-35.9121906983
196UbiquitinationQKLQRYLKSGVAIRR
HHHHHHHHHCCCCCC
35.9121906983
210N-linked_GlycosylationRTVPPMVNVTCSEVS
CCCCCEEEEEECEEC
19.68UniProtKB CARBOHYD
220N-linked_GlycosylationCSEVSEGNITVTCRA
ECEECCCEEEEEEEC
23.78UniProtKB CARBOHYD
256UbiquitinationNTQQWGDVLPDGNGT
CCEECCCCCCCCCCE
8.03-
261N-linked_GlycosylationGDVLPDGNGTYQTWV
CCCCCCCCCEEEEEE
47.19UniProtKB CARBOHYD
297O-linked_GlycosylationHGTHPVPSGKVLVLQ
CCCCCCCCCCEEEEE
52.02OGP
297PhosphorylationHGTHPVPSGKVLVLQ
CCCCCCCCCCEEEEE
52.0222210691
305PhosphorylationGKVLVLQSQRTDFPY
CCEEEEECCCCCCCH
19.9122210691
334UbiquitinationCVPCCKKKTSAAEGP
HHHHHCCCCCCCCCC
32.96-
345PhosphorylationAEGPELVSLQVLDQH
CCCCCEEEEEEECCC
26.2123312004
372PhosphorylationLGFQPLMSATGSTGS
HCCCCCCCCCCCCCC
30.2929485707
374PhosphorylationFQPLMSATGSTGSTE
CCCCCCCCCCCCCCC
25.1029485707
376PhosphorylationPLMSATGSTGSTEGA
CCCCCCCCCCCCCCC
25.8223186163
377PhosphorylationLMSATGSTGSTEGA-
CCCCCCCCCCCCCC-
36.1720363803
377PhosphorylationLMSATGSTGSTEGA-
CCCCCCCCCCCCCC-
36.1720363803
379PhosphorylationSATGSTGSTEGA---
CCCCCCCCCCCC---
24.3126503892
379PhosphorylationSATGSTGSTEGA---
CCCCCCCCCCCC---
24.3120363803
380PhosphorylationATGSTGSTEGA----
CCCCCCCCCCC----
39.5226503892

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 MICB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MICB_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 MICB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZCHC8_HUMANZCCHC8physical
22939629

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
180300Rheumatoid arthritis (RA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MICB_HUMAN

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Related Literatures of Post-Translational Modification

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