TMM64_HUMAN - dbPTM
TMM64_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMM64_HUMAN
UniProt AC Q6YI46
Protein Name Transmembrane protein 64
Gene Name TMEM64
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization Membrane
Multi-pass membrane protein . Endoplasmic reticulum .
Protein Description Positively regulates TNFSF11-induced osteoclast differentiation. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with SERCA2 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation. Negatively regulates osteoblast differentiation and positively regulates adipocyte differentiation via modulation of the canonical Wnt signaling pathway. Mediates the switch in lineage commitment to osteogenesis rather than to adipogenesis in mesenchymal stem cells by negatively regulating the expression, activity and nuclear localization of CTNNB1..
Protein Sequence MRSPGGILLQALPRLLQHAALPGLAELPARWALPRGAGGDGPADRLPRGGGASAAAAAAAASGALLGAYLERHGPPEASELPEPGGALAGGPGSGGGGVVVGVAEVRNWRCCCLGSTCWCRSLVLVCVLAALCFASLALVRRYLHHLLLWVESLDSLLGVLLFVVGFIVVSFPCGWGYIVLNVAAGYLYGFVLGMGLMMVGVLIGTFIAHVVCKRLLTAWVAARIQSSEKLSAVIRVVEGGSGLKVVALARLTPIPFGLQNAVFSITDLSLPNYLMASSVGLLPTQLLNSYLGTTLRTMEDVIAEQSVSGYFVFCLQIIISIGLMFYVVHRAQVELNAAIVACEMELKSSLVKGNQPNTSGSSFYNKRTLTFSGGGINVV
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
36 (in isoform 2)Ubiquitination-27.0021906983
51 (in isoform 2)Ubiquitination-21.1221906983
53PhosphorylationLPRGGGASAAAAAAA
CCCCCHHHHHHHHHH
23.01-
69PhosphorylationSGALLGAYLERHGPP
HHHHHHHHHHHHCCC
13.8027642862
159 (in isoform 2)Ubiquitination-17.2021906983
173 (in isoform 2)Ubiquitination-14.2721906983
230 (in isoform 1)Ubiquitination-50.0921906983
230UbiquitinationARIQSSEKLSAVIRV
HHHCCCCCCCEEEEE
50.0933845483
245 (in isoform 1)Ubiquitination-37.8821906983
245UbiquitinationVEGGSGLKVVALARL
EECCCCCEEEEEEEC
37.8821906983
301UbiquitinationTTLRTMEDVIAEQSV
CCCCCHHHHHHHCCC
26.7121963094
315UbiquitinationVSGYFVFCLQIIISI
CCHHHHHHHHHHHHH
1.9927667366
353 (in isoform 1)Ubiquitination-58.3921906983
353UbiquitinationELKSSLVKGNQPNTS
HHHHHHHCCCCCCCC
58.3921906983
367 (in isoform 1)Ubiquitination-35.0721906983
367UbiquitinationSGSSFYNKRTLTFSG
CCCCCCCCCEEEEEC
35.0727667366
369PhosphorylationSSFYNKRTLTFSGGG
CCCCCCCEEEEECCC
31.59-
371PhosphorylationFYNKRTLTFSGGGIN
CCCCCEEEEECCCEE
18.3624719451
373PhosphorylationNKRTLTFSGGGINVV
CCCEEEEECCCEECC
31.1528348404

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 TMM64_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMM64_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 TMM64_HUMAN !!

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

Oops, there are no PPI records of TMM64_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 TMM64_HUMAN

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Related Literatures of Post-Translational Modification

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