DJB11_HUMAN - dbPTM
DJB11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJB11_HUMAN
UniProt AC Q9UBS4
Protein Name DnaJ homolog subfamily B member 11
Gene Name DNAJB11
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Endoplasmic reticulum lumen . Associated with the ER membrane in a C-terminally epitope-tagged construct.
Protein Description Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity..
Protein Sequence MAPQNLSTFCLLLLYLIGAVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHPIFERRGDDLYTNVTISLVESLVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAREGIKQLLKQGSVQKVYNGLQGY
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
282-HydroxyisobutyrylationIAGRDFYKILGVPRS
HHCCCHHHHHCCCCC		31.29-
28UbiquitinationIAGRDFYKILGVPRS
HHCCCHHHHHCCCCC		31.2921906983
35PhosphorylationKILGVPRSASIKDIK
HHHCCCCCCCHHHHH		21.9423312004
37PhosphorylationLGVPRSASIKDIKKA
HCCCCCCCHHHHHHH		31.2723312004
39UbiquitinationVPRSASIKDIKKAYR
CCCCCCHHHHHHHHH		51.4027667366
43AcetylationASIKDIKKAYRKLAL
CCHHHHHHHHHHHHH		51.4988259
47UbiquitinationDIKKAYRKLALQLHP
HHHHHHHHHHHHHCC		25.9929967540
47AcetylationDIKKAYRKLALQLHP
HHHHHHHHHHHHHCC		25.9988255
56MethylationALQLHPDRNPDDPQA
HHHHCCCCCCCCHHH		62.12-
66AcetylationDDPQAQEKFQDLGAA
CCHHHHHHHHHHHHH		35.92155529
66UbiquitinationDDPQAQEKFQDLGAA
CCHHHHHHHHHHHHH		35.9229967540
78PhosphorylationGAAYEVLSDSEKRKQ
HHHHHHCCCHHHHHH		44.2427251275
80PhosphorylationAYEVLSDSEKRKQYD
HHHHCCCHHHHHHHC		41.4627251275
82UbiquitinationEVLSDSEKRKQYDTY
HHCCCHHHHHHHCCC		69.7022817900
822-HydroxyisobutyrylationEVLSDSEKRKQYDTY
HHCCCHHHHHHHCCC		69.70-
84UbiquitinationLSDSEKRKQYDTYGE
CCCHHHHHHHCCCCH		65.3622817900
88PhosphorylationEKRKQYDTYGEEGLK
HHHHHHCCCCHHHCC		28.61-
188PhosphorylationGPGRFQMTQEVVCDE
CCCCEEECEEEECCC		15.7017525332
200AcetylationCDECPNVKLVNEERT
CCCCCCCEEECCCEE		54.0526051181
200UbiquitinationCDECPNVKLVNEERT
CCCCCCCEEECCCEE		54.0521963094
207PhosphorylationKLVNEERTLEVEIEP
EEECCCEEEEEEEEC		30.4721406692
247UbiquitinationRFRIKVVKHPIFERR
EEEEEEEECCCCEEC		46.8027667366
2472-HydroxyisobutyrylationRFRIKVVKHPIFERR
EEEEEEEECCCCEEC		46.80-
261N-linked_GlycosylationRGDDLYTNVTISLVE
CCCCCCCCHHHHHHH		18.5119159218
291UbiquitinationKVHISRDKITRPGAK
EEEECCCCCCCCCCC		44.8827667366
302UbiquitinationPGAKLWKKGEGLPNF
CCCCHHCCCCCCCCC		51.0833845483
332PhosphorylationDFPKEQLTEEAREGI
CCCHHHHCHHHHHHH		31.3220068231
344UbiquitinationEGIKQLLKQGSVQKV
HHHHHHHHHCCHHHH		62.2929967540
344AcetylationEGIKQLLKQGSVQKV
HHHHHHHHHCCHHHH		62.2971043
3442-HydroxyisobutyrylationEGIKQLLKQGSVQKV
HHHHHHHHHCCHHHH		62.29-
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 DJB11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
188TPhosphorylation

17525332
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 DJB11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
16169070
PTN_HUMANPTNphysical
16169070
UBR1_HUMANUBR1physical
16169070
ABEC1_HUMANAPOBEC1physical
11584023
UBQL4_HUMANUBQLN4physical
21900206
SPRE1_HUMANSPRED1physical
21900206
ZZZ3_HUMANZZZ3physical
21900206
CEP70_HUMANCEP70physical
21900206
NC2A_HUMANDRAP1physical
21900206
EIF3D_HUMANEIF3Dphysical
21900206
EZH2_HUMANEZH2physical
21900206
ANKZ1_HUMANANKZF1physical
21900206
DJC13_HUMANDNAJC13physical
21900206
DDAH2_HUMANDDAH2physical
21900206
UBR1_HUMANUBR1physical
21900206
CO6A1_HUMANCOL6A1physical
21900206
SIMC1_HUMANSIMC1physical
21900206
BAG6_HUMANBAG6physical
21900206
DPYL1_HUMANCRMP1physical
21900206
PTN_HUMANPTNphysical
21900206
SNX5_HUMANSNX5physical
21900206
FAF1_HUMANFAF1physical
21900206
MA2B1_HUMANMAN2B1physical
22939629
ECH1_HUMANECH1physical
22939629
HYEP_HUMANEPHX1physical
22939629
PNPH_HUMANPNPphysical
22939629
RIR1_HUMANRRM1physical
22939629
NDUV1_HUMANNDUFV1physical
22939629
UBXN1_HUMANUBXN1physical
22939629
PPAL_HUMANACP2physical
22939629
DNS2A_HUMANDNASE2physical
22939629
COR1C_HUMANCORO1Cphysical
22863883
SMOC1_HUMANSMOC1physical
22863883
GRP78_HUMANHSPA5physical
21217698
GRP78_HUMANHSPA5physical
26186194
ROCK2_HUMANROCK2physical
26186194
NUBPL_HUMANNUBPLphysical
26186194
KMCP1_HUMANSLC25A30physical
26186194
SDF2_HUMANSDF2physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
TBB8_HUMANTUBB8physical
26186194
SIMC1_HUMANSIMC1physical
26186194
SCPDL_HUMANSCCPDHphysical
26186194
KCD21_HUMANKCTD21physical
26186194
BORA_HUMANBORAphysical
26186194
HSP7C_HUMANHSPA8physical
26344197
HSP7C_HUMANHSPA8physical
11584023
GRP78_HUMANHSPA5physical
26085089
KCD21_HUMANKCTD21physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442
SIMC1_HUMANSIMC1physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
NUBPL_HUMANNUBPLphysical
28514442
GRP78_HUMANHSPA5physical
28514442
BORA_HUMANBORAphysical
28514442
TBB8_HUMANTUBB8physical
28514442
KMCP1_HUMANSLC25A30physical
28514442
TBA1A_HUMANTUBA1Aphysical
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 DJB11_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND MASSSPECTROMETRY.

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