LMBD1_HUMAN - dbPTM
LMBD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMBD1_HUMAN
UniProt AC Q9NUN5
Protein Name Probable lysosomal cobalamin transporter
Gene Name LMBRD1
Organism Homo sapiens (Human).
Sequence Length 540
Subcellular Localization Lysosome membrane
Multi-pass membrane protein .
Protein Description Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors. Isoform 3 may play a role in the assembly of hepatitis delta virus (HDV)..
Protein Sequence MATSGAASAELVIGWCIFGLLLLAILAFCWIYVRKYQSRRESEVVSTITAIFSLAIALITSALLPVDIFLVSYMKNQNGTFKDWANANVSRQIEDTVLYGYYTLYSVILFCVFFWIPFVYFYYEEKDDDDTSKCTQIKTALKYTLGFVVICALLLLVGAFVPLNVPNNKNSTEWEKVKSLFEELGSSHGLAALSFSISSLTLIGMLAAITYTAYGMSALPLNLIKGTRSAAYERLENTEDIEEVEQHIQTIKSKSKDGRPLPARDKRALKQFEERLRTLKKRERHLEFIENSWWTKFCGALRPLKIVWGIFFILVALLFVISLFLSNLDKALHSAGIDSGFIIFGANLSNPLNMLLPLLQTVFPLDYILITIIIMYFIFTSMAGIRNIGIWFFWIRLYKIRRGRTRPQALLFLCMILLLIVLHTSYMIYSLAPQYVMYGSQNYLIETNITSDNHKGNSTLSVPKRCDADAPEDQCTVTRTYLFLHKFWFFSAAYYFGNWAFLGVFLIGLIVSCCKGKKSVIEGVDEDSDISDDEPSVYSA
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
60UbiquitinationSLAIALITSALLPVD
HHHHHHHHHHHCCHH		14.5933845483
78N-linked_GlycosylationVSYMKNQNGTFKDWA
HHHHCCCCCCHHHHH		61.95UniProtKB CARBOHYD
88N-linked_GlycosylationFKDWANANVSRQIED
HHHHHHCCCCHHHHH		31.91UniProtKB CARBOHYD
133UbiquitinationKDDDDTSKCTQIKTA
CCCCCCCHHHHHHHH		43.3133845483
170N-linked_GlycosylationLNVPNNKNSTEWEKV
CCCCCCCCCCHHHHH		57.18UniProtKB CARBOHYD
179UbiquitinationTEWEKVKSLFEELGS
CHHHHHHHHHHHHHC		41.0821963094
183UbiquitinationKVKSLFEELGSSHGL
HHHHHHHHHHCCCHH		51.6132142685
197UbiquitinationLAALSFSISSLTLIG
HHHHHHCHHHHHHHH		2.8233845483
210PhosphorylationIGMLAAITYTAYGMS
HHHHHHHHHHHHCCC		15.3024043423
211PhosphorylationGMLAAITYTAYGMSA
HHHHHHHHHHHCCCC		5.3524043423
212PhosphorylationMLAAITYTAYGMSAL
HHHHHHHHHHCCCCC		12.5424043423
214PhosphorylationAAITYTAYGMSALPL
HHHHHHHHCCCCCCH		12.9324043423
217PhosphorylationTYTAYGMSALPLNLI
HHHHHCCCCCCHHHC		23.4524043423
227PhosphorylationPLNLIKGTRSAAYER
CHHHCCCCHHHHHHH		19.2224043423
229PhosphorylationNLIKGTRSAAYERLE
HHCCCCHHHHHHHHH		19.6524043423
232PhosphorylationKGTRSAAYERLENTE
CCCHHHHHHHHHCCC		10.9924043423
238PhosphorylationAYERLENTEDIEEVE
HHHHHHCCCCHHHHH		26.1719060867
250PhosphorylationEVEQHIQTIKSKSKD
HHHHHHHHHHHCCCC		29.7527762562
252UbiquitinationEQHIQTIKSKSKDGR
HHHHHHHHHCCCCCC		56.0421963094
254UbiquitinationHIQTIKSKSKDGRPL
HHHHHHHCCCCCCCC		57.43-
256UbiquitinationQTIKSKSKDGRPLPA
HHHHHCCCCCCCCCH		68.8632142685
270UbiquitinationARDKRALKQFEERLR
HHHHHHHHHHHHHHH		52.5433845483
347N-linked_GlycosylationGFIIFGANLSNPLNM
CEEEECCCCCCHHHH		44.36UniProtKB CARBOHYD
448N-linked_GlycosylationQNYLIETNITSDNHK
CEEEEEEECCCCCCC		23.81UniProtKB CARBOHYD
457N-linked_GlycosylationTSDNHKGNSTLSVPK
CCCCCCCCCEECCCC		36.3019136951
461PhosphorylationHKGNSTLSVPKRCDA
CCCCCEECCCCCCCC		36.1424719451
519PhosphorylationSCCKGKKSVIEGVDE
HHHCCCCHHHCCCCC		31.6425262027
528PhosphorylationIEGVDEDSDISDDEP
HCCCCCCCCCCCCCC		34.4920201521
531PhosphorylationVDEDSDISDDEPSVY
CCCCCCCCCCCCCCC		43.9620201521
536PhosphorylationDISDDEPSVYSA---
CCCCCCCCCCCC---		31.4720873877
538PhosphorylationSDDEPSVYSA-----
CCCCCCCCCC-----		11.8320873877
539PhosphorylationDDEPSVYSA------
CCCCCCCCC------		25.9127251275
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 LMBD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMBD1_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 LMBD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBOA7_HUMANMBOAT7physical
28514442
Drug and Disease Associations
Kegg Disease
H00174 Methylmalonic aciduria (MMA)
OMIM Disease
277380Methylmalonic aciduria and homocystinuria type cblF (MMAHCF)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LMBD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, ANDMASS SPECTROMETRY.

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