LMAN2_HUMAN - dbPTM
LMAN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMAN2_HUMAN
UniProt AC Q12907
Protein Name Vesicular integral-membrane protein VIP36
Gene Name LMAN2
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Endoplasmic reticulum-Golgi intermediate compartment membrane
Single-pass type I membrane protein . Golgi apparatus membrane
Single-pass membrane protein . Endoplasmic reticulum membrane
Single-pass type I membrane protein .
Protein Description Plays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type glycans (By similarity)..
Protein Sequence MAAEGWIWRWGWGRRCLGRPGLLGPGPGPTTPLFLLLLLGSVTADITDGNSEHLKREHSLIKPYQGVGSSSMPLWDFQGSTMLTSQYVRLTPDERSKEGSIWNHQPCFLKDWEMHVHFKVHGTGKKNLHGDGIALWYTRDRLVPGPVFGSKDNFHGLAIFLDTYPNDETTERVFPYISVMVNNGSLSYDHSKDGRWTELAGCTADFRNRDHDTFLAVRYSRGRLTVMTDLEDKNEWKNCIDITGVRLPTGYYFGASAGTGDLSDNHDIISMKLFQLMVEHTPDEESIDWTKIEPSVNFLKSPKDNVDDPTGNFRSGPLTGWRVFLLLLCALLGIVVCAVVGAVVFQKRQERNKRFY
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
59PhosphorylationEHLKREHSLIKPYQG
HHHHHHHCCCCCCCC		27.3424719451
70O-linked_GlycosylationPYQGVGSSSMPLWDF
CCCCCCCCCCCCCCC		25.40OGP
1252-HydroxyisobutyrylationFKVHGTGKKNLHGDG
EEEECCCCCCCCCCC		38.02-
126UbiquitinationKVHGTGKKNLHGDGI
EEECCCCCCCCCCCE		67.1121890473
178PhosphorylationERVFPYISVMVNNGS
CCCCCEEEEEEECCC		9.79-
183N-linked_GlycosylationYISVMVNNGSLSYDH
EEEEEEECCCCCEEC		29.9812754519
188PhosphorylationVNNGSLSYDHSKDGR
EECCCCCEECCCCCC		23.9822817900
191PhosphorylationGSLSYDHSKDGRWTE
CCCCEECCCCCCEEE		29.5523828894
202GlutathionylationRWTELAGCTADFRNR
CEEEEEEEEEECCCC		2.0622555962
213PhosphorylationFRNRDHDTFLAVRYS
CCCCCCCCEEEEEEE		19.6820068231
225PhosphorylationRYSRGRLTVMTDLED
EEECCCEEEEECCCC		13.5820860994
228PhosphorylationRGRLTVMTDLEDKNE
CCCEEEEECCCCCCC		32.8520860994
243PhosphorylationWKNCIDITGVRLPTG
HHCCEECCCCCCCCE		26.3521406692
249PhosphorylationITGVRLPTGYYFGAS
CCCCCCCCEEEECCC		42.2721406692
251PhosphorylationGVRLPTGYYFGASAG
CCCCCCEEEECCCCC		9.7121406692
252PhosphorylationVRLPTGYYFGASAGT
CCCCCEEEECCCCCC		9.2521406692
256O-linked_GlycosylationTGYYFGASAGTGDLS
CEEEECCCCCCCCCC		27.84OGP
256PhosphorylationTGYYFGASAGTGDLS
CEEEECCCCCCCCCC		27.8421406692
259PhosphorylationYFGASAGTGDLSDNH
EECCCCCCCCCCCCC		27.5221406692
263PhosphorylationSAGTGDLSDNHDIIS
CCCCCCCCCCCCCEE		40.9021406692
270PhosphorylationSDNHDIISMKLFQLM
CCCCCCEEHHHHHHH		15.3621406692
290O-linked_GlycosylationDEESIDWTKIEPSVN
CHHHCCCCEECCCCC		20.56OGP
291UbiquitinationEESIDWTKIEPSVNF
HHHCCCCEECCCCCC		40.60-
295PhosphorylationDWTKIEPSVNFLKSP
CCCEECCCCCCCCCC		19.53-
300UbiquitinationEPSVNFLKSPKDNVD
CCCCCCCCCCCCCCC		61.6521890473
301PhosphorylationPSVNFLKSPKDNVDD
CCCCCCCCCCCCCCC		39.0524719451
303SuccinylationVNFLKSPKDNVDDPT
CCCCCCCCCCCCCCC		69.8623954790
3032-HydroxyisobutyrylationVNFLKSPKDNVDDPT
CCCCCCCCCCCCCCC		69.86-
303UbiquitinationVNFLKSPKDNVDDPT
CCCCCCCCCCCCCCC		69.8621890473
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 LMAN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMAN2_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 LMAN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK09_HUMANMAPK9physical
21988832
SPT5H_HUMANSUPT5Hphysical
21988832
HEAT3_HUMANHEATR3physical
26186194
PLXB2_HUMANPLXNB2physical
26186194
CENPH_HUMANCENPHphysical
26186194
GPC3_HUMANGPC3physical
26186194
TTYH3_HUMANTTYH3physical
26186194
CA2D1_HUMANCACNA2D1physical
26186194
NDUS3_HUMANNDUFS3physical
26344197
TMEDA_HUMANTMED10physical
26344197
TMED2_HUMANTMED2physical
26344197
CENPH_HUMANCENPHphysical
28514442
GPC3_HUMANGPC3physical
28514442
PLXB2_HUMANPLXNB2physical
28514442
HEAT3_HUMANHEATR3physical
28514442
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 LMAN2_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-183.

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