MBTP1_HUMAN - dbPTM
MBTP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBTP1_HUMAN
UniProt AC Q14703
Protein Name Membrane-bound transcription factor site-1 protease
Gene Name MBTPS1
Organism Homo sapiens (Human).
Sequence Length 1052
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein . Golgi apparatus membrane
Single-pass type I membrane protein . May sort to other organelles, including lysosomal and/or endosomal compartments.
Protein Description Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes..
Protein Sequence MKLVNIWLLLLVVLLCGKKHLGDRLEKKSFEKAPCPGCSHLTLKVEFSSTVVEYEYIVAFNGYFTAKARNSFISSALKSSEVDNWRIIPRNNPSSDYPSDFEVIQIKEKQKAGLLTLEDHPNIKRVTPQRKVFRSLKYAESDPTVPCNETRWSQKWQSSRPLRRASLSLGSGFWHATGRHSSRRLLRAIPRQVAQTLQADVLWQMGYTGANVRVAVFDTGLSEKHPHFKNVKERTNWTNERTLDDGLGHGTFVAGVIASMRECQGFAPDAELHIFRVFTNNQVSYTSWFLDAFNYAILKKIDVLNLSIGGPDFMDHPFVDKVWELTANNVIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFEDNIARFSSRGMTTWELPGGYGRMKPDIVTYGAGVRGSGVKGGCRALSGTSVASPVVAGAVTLLVSTVQKRELVNPASMKQALIASARRLPGVNMFEQGHGKLDLLRAYQILNSYKPQASLSPSYIDLTECPYMWPYCSQPIYYGGMPTVVNVTILNGMGVTGRIVDKPDWQPYLPQNGDNIEVAFSYSSVLWPWSGYLAISISVTKKAASWEGIAQGHVMITVASPAETESKNGAEQTSTVKLPIKVKIIPTPPRSKRVLWDQYHNLRYPPGYFPRDNLRMKNDPLDWNGDHIHTNFRDMYQHLRSMGYFVEVLGAPFTCFDASQYGTLLMVDSEEEYFPEEIAKLRRDVDNGLSLVIFSDWYNTSVMRKVKFYDENTRQWWMPDTGGANIPALNELLSVWNMGFSDGLYEGEFTLANHDMYYASGCSIAKFPEDGVVITQTFKDQGLEVLKQETAVVENVPILGLYQIPAEGGGRIVLYGDSNCLDDSHRQKDCFWLLDALLQYTSYGVTPPSLSHSGNRQRPPSGAGSVTPERMEGNHLHRYSKVLEAHLGDPKPRPLPACPRLSWAKPQPLNETAPSNLWKHQKLLSIDLDKVVLPNFRSNRPQVRPLSPGESGAWDIPGGIMPGRYNQEVGQTIPVFAFLGAMVVLAFFVVQINKAKSRPKRRKPRVKRPQLMQQVHPPKTPSV
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
78UbiquitinationSFISSALKSSEVDNW
HHHHHHHHCCCCCCE		52.2129967540
107UbiquitinationDFEVIQIKEKQKAGL
CCEEEEEEHHHHCCC		42.3529967540
109UbiquitinationEVIQIKEKQKAGLLT
EEEEEEHHHHCCCEE		52.69-
116PhosphorylationKQKAGLLTLEDHPNI
HHHCCCEECCCCCCC		32.8922210691
127PhosphorylationHPNIKRVTPQRKVFR
CCCCCCCCCCHHHHH		20.1028258704
137UbiquitinationRKVFRSLKYAESDPT
HHHHHHCCCCCCCCC		43.6029967540
138PhosphorylationKVFRSLKYAESDPTV
HHHHHCCCCCCCCCC		22.3930206219
141PhosphorylationRSLKYAESDPTVPCN
HHCCCCCCCCCCCCC		40.4930206219
144PhosphorylationKYAESDPTVPCNETR
CCCCCCCCCCCCCHH		41.9130206219
166O-linked_GlycosylationSRPLRRASLSLGSGF
CCCCCHHEEECCCCC		19.3855830813
166PhosphorylationSRPLRRASLSLGSGF
CCCCCHHEEECCCCC		19.3826091039
168O-linked_GlycosylationPLRRASLSLGSGFWH
CCCHHEEECCCCCHH		28.3426091039
168PhosphorylationPLRRASLSLGSGFWH
CCCHHEEECCCCCHH		28.3428348404
171PhosphorylationRASLSLGSGFWHATG
HHEEECCCCCHHCCC		35.7928348404
177O-linked_GlycosylationGSGFWHATGRHSSRR
CCCCHHCCCCHHHHH		23.1246249445
177PhosphorylationGSGFWHATGRHSSRR
CCCCHHCCCCHHHHH		23.12-
196PhosphorylationIPRQVAQTLQADVLW
CHHHHHHHHHHHHHH		15.8824043423
207PhosphorylationDVLWQMGYTGANVRV
HHHHHCCCCCCCEEE		9.1724043423
208PhosphorylationVLWQMGYTGANVRVA
HHHHCCCCCCCEEEE		24.8824043423
213MethylationGYTGANVRVAVFDTG
CCCCCCEEEEEEECC		15.52115390605
213DimethylationGYTGANVRVAVFDTG
CCCCCCEEEEEEECC		15.52-
224UbiquitinationFDTGLSEKHPHFKNV
EECCCCCCCCCCCCH		60.09-
229UbiquitinationSEKHPHFKNVKERTN
CCCCCCCCCHHHHCC		58.7729967540
235PhosphorylationFKNVKERTNWTNERT
CCCHHHHCCCCCCCC		35.88-
236N-linked_GlycosylationKNVKERTNWTNERTL
CCHHHHCCCCCCCCC		50.20UniProtKB CARBOHYD
305N-linked_GlycosylationLKKIDVLNLSIGGPD
HHHCCEECCCCCCCC		31.43UniProtKB CARBOHYD
388UbiquitinationPGGYGRMKPDIVTYG
CCCCCCCCCCEEEEC		37.87-
411PhosphorylationKGGCRALSGTSVASP
CCCCEECCCCCCCCH		38.7522210691
417PhosphorylationLSGTSVASPVVAGAV
CCCCCCCCHHHHHHH		18.97-
429PhosphorylationGAVTLLVSTVQKREL
HHHHHHHHHHHHHCC		23.88-
441PhosphorylationRELVNPASMKQALIA
HCCCCHHHHHHHHHH		27.9822210691
443UbiquitinationLVNPASMKQALIASA
CCCHHHHHHHHHHHH		29.8922817900
449PhosphorylationMKQALIASARRLPGV
HHHHHHHHHHCCCCC		18.4722210691
452UbiquitinationALIASARRLPGVNMF
HHHHHHHCCCCCCCC		44.9722817900
455UbiquitinationASARRLPGVNMFEQG
HHHHCCCCCCCCCCC		28.2021890473
472PhosphorylationKLDLLRAYQILNSYK
HHHHHHHHHHHHCCC		6.9427174698
477PhosphorylationRAYQILNSYKPQASL
HHHHHHHCCCCCCCC		30.9627174698
478PhosphorylationAYQILNSYKPQASLS
HHHHHHCCCCCCCCC		26.1427174698
507UbiquitinationYCSQPIYYGGMPTVV
CCCCCEEECCCCEEE		14.1322817900
510UbiquitinationQPIYYGGMPTVVNVT
CCEEECCCCEEEEEE		1.8721890473
515N-linked_GlycosylationGGMPTVVNVTILNGM
CCCCEEEEEEEECCC		22.37UniProtKB CARBOHYD
616PhosphorylationIKVKIIPTPPRSKRV
EEEEECCCCCCCCCE		35.2022817900
620PhosphorylationIIPTPPRSKRVLWDQ
ECCCCCCCCCEEHHH		30.5025002506
646UbiquitinationPRDNLRMKNDPLDWN
CCCCCCCCCCCCCCC		52.33-
698PhosphorylationGTLLMVDSEEEYFPE
CEEEEECCCHHHCHH		35.1826074081
702PhosphorylationMVDSEEEYFPEEIAK
EECCCHHHCHHHHHH		27.9326074081
728N-linked_GlycosylationVIFSDWYNTSVMRKV
EEEECCCCCCHHEEE		22.94UniProtKB CARBOHYD
729PhosphorylationIFSDWYNTSVMRKVK
EEECCCCCCHHEEEE		13.6527251275
730PhosphorylationFSDWYNTSVMRKVKF
EECCCCCCHHEEEEE		15.4127251275
819O-linked_GlycosylationLEVLKQETAVVENVP
CHHHEECEEEEECCC		23.43OGP
847PhosphorylationRIVLYGDSNCLDDSH
EEEEECCCCCCCCHH		25.6924114839
875O-linked_GlycosylationQYTSYGVTPPSLSHS
HHHHCCCCCCCCCCC		25.72OGP
894O-linked_GlycosylationRPPSGAGSVTPERME
CCCCCCCCCCHHHHC		23.45OGP
894PhosphorylationRPPSGAGSVTPERME
CCCCCCCCCCHHHHC		23.4526437602
896PhosphorylationPSGAGSVTPERMEGN
CCCCCCCCHHHHCCC		22.5626437602
896O-linked_GlycosylationPSGAGSVTPERMEGN
CCCCCCCCHHHHCCC		22.5655833933
934UbiquitinationCPRLSWAKPQPLNET
CCCCCCCCCCCCCCC		37.62-
939N-linked_GlycosylationWAKPQPLNETAPSNL
CCCCCCCCCCCCCCH		51.78UniProtKB CARBOHYD
948UbiquitinationTAPSNLWKHQKLLSI
CCCCCHHHHCEEEEC		39.0522817900
951UbiquitinationSNLWKHQKLLSIDLD
CCHHHHCEEEECCCC		51.6322817900
951UbiquitinationSNLWKHQKLLSIDLD
CCHHHHCEEEECCCC		51.6321890473
967O-linked_GlycosylationVVLPNFRSNRPQVRP
HCCCCCCCCCCCCCC		32.81OGP
976O-linked_GlycosylationRPQVRPLSPGESGAW
CCCCCCCCCCCCCCC		33.28OGP
1036AcetylationKRRKPRVKRPQLMQQ
CCCCCCCCCHHHHHH		60.6930590301
1048AcetylationMQQVHPPKTPSV---
HHHCCCCCCCCC---		77.0030590307
1049PhosphorylationQQVHPPKTPSV----
HHCCCCCCCCC----		26.9428555341
1051PhosphorylationVHPPKTPSV------
CCCCCCCCC------		45.7718491316
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
168SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBTP1_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 MBTP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
19729656
HDAC2_HUMANHDAC2physical
19729656
BIRC3_HUMANBIRC3physical
24464131
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 MBTP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-616, AND MASSSPECTROMETRY.

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