MA1B1_HUMAN - dbPTM
MA1B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MA1B1_HUMAN
UniProt AC Q9UKM7
Protein Name Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Gene Name MAN1B1
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2)..
Protein Sequence MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENYDNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQKMRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDGTQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQGTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWILGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGNRLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEAVEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQETQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHGLPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPETVESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFFLGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA
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
9PhosphorylationAACEGRRSGALGSSQ
CCCCCCCCCCCCCCC		27.3628122231
14PhosphorylationRRSGALGSSQSDFLT
CCCCCCCCCCCCCCC		26.5028348404
15PhosphorylationRSGALGSSQSDFLTP
CCCCCCCCCCCCCCC		31.7228348404
17PhosphorylationGALGSSQSDFLTPPV
CCCCCCCCCCCCCCC		32.0728348404
21PhosphorylationSSQSDFLTPPVGGAP
CCCCCCCCCCCCCCC		26.0725159151
53PhosphorylationHRDFISVTLSFGENY
CCCCEEEEEECCCCC		15.1928985074
60PhosphorylationTLSFGENYDNSKSWR
EEECCCCCCCCCHHH		16.52-
63PhosphorylationFGENYDNSKSWRRRS
CCCCCCCCCHHHHHH		25.7628985074
129UbiquitinationRPEIAGLKPANPPVL
CHHHCCCCCCCCCCC		40.9629967540
144O-linked_GlycosylationPAPQKADTDPENLPE
CCCCCCCCCHHCCHH		59.31OGP
144PhosphorylationPAPQKADTDPENLPE
CCCCCCCCCHHCCHH		59.3120068231
153O-linked_GlycosylationPENLPEISSQKTQRH
HHCCHHHCCHHHHHH		25.67OGP
154O-linked_GlycosylationENLPEISSQKTQRHI
HCCHHHCCHHHHHHH		41.16OGP
156UbiquitinationLPEISSQKTQRHIQR
CHHHCCHHHHHHHHC		48.8821906983
174O-linked_GlycosylationHLQIRPPSQDLKDGT
CCCCCCCCCCCCCCC		38.7255832937
204O-linked_GlycosylationPEGDPQRTVISWRGA
CCCCCCCEEEEEECE		19.5555834883
207PhosphorylationDPQRTVISWRGAVIE
CCCCEEEEEECEEEC		13.3424719451
219O-linked_GlycosylationVIEPEQGTELPSRRA
EECCCCCCCCCCCCC		33.7655827851
219PhosphorylationVIEPEQGTELPSRRA
EECCCCCCCCCCCCC		33.7623403867
223O-linked_GlycosylationEQGTELPSRRAEVPT
CCCCCCCCCCCCCCC		47.2055827857
223PhosphorylationEQGTELPSRRAEVPT
CCCCCCCCCCCCCCC		47.2023403867
230O-linked_GlycosylationSRRAEVPTKPPLPPA
CCCCCCCCCCCCCCC		62.4555834847
239O-linked_GlycosylationPPLPPARTQGTPVHL
CCCCCCCCCCCCCCC		33.1955834851
242O-linked_GlycosylationPPARTQGTPVHLNYR
CCCCCCCCCCCCCCC		16.6055834855
275UbiquitinationAWGHDELKPVSRSFS
CCCCCCCCCCCCCHH		41.13-
341PhosphorylationRILGGLLSAYHLSGD
HHHHHHHHHHHHCCC		31.65-
354AcetylationGDSLFLRKAEDFGNR
CCCCCEEEHHHHHHC		59.2730590271
3542-HydroxyisobutyrylationGDSLFLRKAEDFGNR
CCCCCEEEHHHHHHC		59.27-
370O-linked_GlycosylationMPAFRTPSKIPYSDV
CCCCCCCCCCCCCCC		42.47OGP
371UbiquitinationPAFRTPSKIPYSDVN
CCCCCCCCCCCCCCC		49.2421906983
379UbiquitinationIPYSDVNIGTGVAHP
CCCCCCCCCCCCCCC		5.4021987572
381O-linked_GlycosylationYSDVNIGTGVAHPPR
CCCCCCCCCCCCCCC		25.3755835395
390O-linked_GlycosylationVAHPPRWTSDSTVAE
CCCCCCCCCCCHHEE		24.76OGP
399O-linked_GlycosylationDSTVAEVTSIQLEFR
CCHHEEEEEEEEHHH		16.18OGP
425O-linked_GlycosylationQEAVEKVTQHIHGLS
HHHHHHHHHHHHHCC		26.04OGP
4342-HydroxyisobutyrylationHIHGLSGKKDGLVPM
HHHHCCCCCCCCEEE		44.29-
434UbiquitinationHIHGLSGKKDGLVPM
HHHHCCCCCCCCEEE		44.2929967540
478UbiquitinationKQWIQGGKQETQLLE
HHHHHCCHHHHHHHH		52.3521987572
487PhosphorylationETQLLEDYVEAIEGV
HHHHHHHHHHHHHHH		7.27-
508O-linked_GlycosylationHSEPSKLTFVGELAH
CCCCCCEEEEEHHHC		21.7355824379
565PhosphorylationQMNRQMETGLSPEIV
HHHHHHHHCCCCCEE		37.7722461510
577PhosphorylationEIVHFNLYPQPGRRD
CEEEEECCCCCCCCC		10.8322461510
588UbiquitinationGRRDVEVKPADRHNL
CCCCCCCCCCCCCCC		22.4521906983
640O-linked_GlycosylationVPSGGYSSINNVQDP
CCCCCCCCCCCCCCC		22.35OGP
649UbiquitinationNNVQDPQKPEPRDKM
CCCCCCCCCCCCHHH		57.652190698
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 MA1B1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MA1B1_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 MA1B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MA1B1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614202Mental retardation, autosomal recessive 15 (MRT15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MA1B1_HUMAN

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Related Literatures of Post-Translational Modification

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