TMM43_HUMAN - dbPTM
TMM43_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMM43_HUMAN
UniProt AC Q9BTV4
Protein Name Transmembrane protein 43
Gene Name TMEM43
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Endoplasmic reticulum. Nucleus inner membrane
Multi-pass membrane protein. Retained in the inner nuclear membrane through interaction with EMD and A- and B-lamins. The N- and C-termini are oriented towards the nucleoplasm. The majority of the hydrop
Protein Description May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity)..
Protein Sequence MAANYSSTSTRREHVKVKTSSQPGFLERLSETSGGMFVGLMAFLLSFYLIFTNEGRALKTATSLAEGLSLVVSPDSIHSVAPENEGRLVHIIGALRTSKLLSDPNYGVHLPAVKLRRHVEMYQWVETEESREYTEDGQVKKETRYSYNTEWRSEIINSKNFDREIGHKNPSAMAVESFMATAPFVQIGRFFLSSGLIDKVDNFKSLSLSKLEDPHVDIIRRGDFFYHSENPKYPEVGDLRVSFSYAGLSGDDPDLGPAHVVTVIARQRGDQLVPFSTKSGDTLLLLHHGDFSAEEVFHRELRSNSMKTWGLRAAGWMAMFMGLNLMTRILYTLVDWFPVFRDLVNIGLKAFAFCVATSLTLLTVAAGWLFYRPLWALLIAGLALVPILVARTRVPAKKLE
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
2Acetylation------MAANYSSTS
------CCCCCCCCC		12.3825732826
5Phosphorylation---MAANYSSTSTRR
---CCCCCCCCCCCC		10.1628796482
6Phosphorylation--MAANYSSTSTRRE
--CCCCCCCCCCCCC		27.2623401153
7Phosphorylation-MAANYSSTSTRREH
-CCCCCCCCCCCCCC		18.9323401153
8PhosphorylationMAANYSSTSTRREHV
CCCCCCCCCCCCCCE		28.3323401153
9PhosphorylationAANYSSTSTRREHVK
CCCCCCCCCCCCCEE		23.1228355574
10PhosphorylationANYSSTSTRREHVKV
CCCCCCCCCCCCEEE		33.5623401153
18MalonylationRREHVKVKTSSQPGF
CCCCEEEECCCCCCH		36.6532601280
19PhosphorylationREHVKVKTSSQPGFL
CCCEEEECCCCCCHH		36.2823312004
20PhosphorylationEHVKVKTSSQPGFLE
CCEEEECCCCCCHHH		22.6622496350
21PhosphorylationHVKVKTSSQPGFLER
CEEEECCCCCCHHHH		45.7023312004
60PhosphorylationNEGRALKTATSLAEG
CCCHHHHHHHHHHCC		35.70-
99UbiquitinationIGALRTSKLLSDPNY
HHHHHHHHHCCCCCC		53.4821890473
102PhosphorylationLRTSKLLSDPNYGVH
HHHHHHCCCCCCCCC		62.55-
114UbiquitinationGVHLPAVKLRRHVEM
CCCCCHHHHHHHHHH		38.08-
122PhosphorylationLRRHVEMYQWVETEE
HHHHHHHHEEECCHH		5.9229759185
127PhosphorylationEMYQWVETEESREYT
HHHEEECCHHHHCCC		35.1229759185
131MethylationWVETEESREYTEDGQ
EECCHHHHCCCCCCC		44.19115918637
1592-HydroxyisobutyrylationRSEIINSKNFDREIG
HHHHHHCCCCCCCCC		58.08-
159UbiquitinationRSEIINSKNFDREIG
HHHHHHCCCCCCCCC		58.08-
181PhosphorylationAVESFMATAPFVQIG
HHHHHHHCCCHHHHH		24.0730257219
193PhosphorylationQIGRFFLSSGLIDKV
HHHHHHHHCCCCCCC		19.7328674151
194PhosphorylationIGRFFLSSGLIDKVD
HHHHHHHCCCCCCCC		39.5028674151
199AcetylationLSSGLIDKVDNFKSL
HHCCCCCCCCCCCCC		44.4826051181
1992-HydroxyisobutyrylationLSSGLIDKVDNFKSL
HHCCCCCCCCCCCCC		44.48-
199UbiquitinationLSSGLIDKVDNFKSL
HHCCCCCCCCCCCCC		44.48-
2042-HydroxyisobutyrylationIDKVDNFKSLSLSKL
CCCCCCCCCCCHHHC		57.66-
204UbiquitinationIDKVDNFKSLSLSKL
CCCCCCCCCCCHHHC		57.66-
205PhosphorylationDKVDNFKSLSLSKLE
CCCCCCCCCCHHHCC		21.0326437602
207PhosphorylationVDNFKSLSLSKLEDP
CCCCCCCCHHHCCCC		37.3724719451
209PhosphorylationNFKSLSLSKLEDPHV
CCCCCCHHHCCCCCC		31.6420068231
210UbiquitinationFKSLSLSKLEDPHVD
CCCCCHHHCCCCCCC		62.28-
210AcetylationFKSLSLSKLEDPHVD
CCCCCHHHCCCCCCC		62.2826051181
232AcetylationFYHSENPKYPEVGDL
CCCCCCCCCCCCCCE		82.2526051181
232UbiquitinationFYHSENPKYPEVGDL
CCCCCCCCCCCCCCE		82.2521890473
233PhosphorylationYHSENPKYPEVGDLR
CCCCCCCCCCCCCEE		13.09-
244PhosphorylationGDLRVSFSYAGLSGD
CCEEEEEEECCCCCC		13.43-
249PhosphorylationSFSYAGLSGDDPDLG
EEEECCCCCCCCCCC		38.98-
268MethylationVTVIARQRGDQLVPF
EEEEEECCCCEEEEE		45.14115918641
278UbiquitinationQLVPFSTKSGDTLLL
EEEEEECCCCCEEEE		51.77-
282PhosphorylationFSTKSGDTLLLLHHG
EECCCCCEEEEEECC		23.88-
292PhosphorylationLLHHGDFSAEEVFHR
EEECCCCCHHHHHHH		39.24-
307UbiquitinationELRSNSMKTWGLRAA
HHHHCCCCHHHHHHH		40.73-
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 TMM43_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMM43_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 TMM43_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FDFT_HUMANFDFT1physical
16169070
VATE1_HUMANATP6V1E1physical
22939629
CUL4B_HUMANCUL4Bphysical
26186194
CUL4B_HUMANCUL4Bphysical
28514442
Drug and Disease Associations
Kegg Disease
H00293 Arrhythmogenic right ventricular cardiomyopathy (ARVC)
OMIM Disease
604400Arrhythmogenic right ventricular dysplasia, familial, 5 (ARVD5)
614302Emery-Dreifuss muscular dystrophy 7, autosomal dominant (EDMD7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TMM43_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory