DNJB4_HUMAN - dbPTM
DNJB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJB4_HUMAN
UniProt AC Q9UDY4
Protein Name DnaJ homolog subfamily B member 4
Gene Name DNAJB4
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Cytoplasm . Cell membrane . Cytoplasmic according to PubMed:18837411 and membrane-associated according to PubMed:16542645.
Protein Description Probable chaperone. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). [PubMed: 24318877]
Protein Sequence MGKDYYCILGIEKGASDEDIKKAYRKQALKFHPDKNKSPQAEEKFKEVAEAYEVLSDPKKREIYDQFGEEGLKGGAGGTDGQGGTFRYTFHGDPHATFAAFFGGSNPFEIFFGRRMGGGRDSEEMEIDGDPFSAFGFSMNGYPRDRNSVGPSRLKQDPPVIHELRVSLEEIYSGCTKRMKISRKRLNADGRSYRSEDKILTIEIKKGWKEGTKITFPREGDETPNSIPADIVFIIKDKDHPKFKRDGSNIIYTAKISLREALCGCSINVPTLDGRNIPMSVNDIVKPGMRRRIIGYGLPFPKNPDQRGDLLIEFEVSFPDTISSSSKEVLRKHLPAS
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
3Malonylation-----MGKDYYCILG
-----CCCCEEEEEE		41.0626320211
13UbiquitinationYCILGIEKGASDEDI
EEEEECCCCCCHHHH		58.83-
24PhosphorylationDEDIKKAYRKQALKF
HHHHHHHHHHHHHHH		27.50-
30UbiquitinationAYRKQALKFHPDKNK
HHHHHHHHHCCCCCC		44.64-
37UbiquitinationKFHPDKNKSPQAEEK
HHCCCCCCCHHHHHH		70.07-
38PhosphorylationFHPDKNKSPQAEEKF
HCCCCCCCHHHHHHH		31.4720068231
46UbiquitinationPQAEEKFKEVAEAYE
HHHHHHHHHHHHHHH		63.45-
59UbiquitinationYEVLSDPKKREIYDQ
HHHHCCHHHHHHHHH		70.25-
60UbiquitinationEVLSDPKKREIYDQF
HHHCCHHHHHHHHHH		61.73-
73UbiquitinationQFGEEGLKGGAGGTD
HHCCCCCCCCCCCCC		67.182190698
79PhosphorylationLKGGAGGTDGQGGTF
CCCCCCCCCCCCCEE		35.72-
85PhosphorylationGTDGQGGTFRYTFHG
CCCCCCCEEEEEECC		16.27-
122PhosphorylationRMGGGRDSEEMEIDG
CCCCCCCCCCEEECC		33.8118669648
133PhosphorylationEIDGDPFSAFGFSMN
EECCCCCCCCCEECC		28.2423403867
138PhosphorylationPFSAFGFSMNGYPRD
CCCCCCEECCCCCCC		16.2420068231
142PhosphorylationFGFSMNGYPRDRNSV
CCEECCCCCCCCCCC		7.0620068231
148PhosphorylationGYPRDRNSVGPSRLK
CCCCCCCCCCHHHHC		29.3730576142
152PhosphorylationDRNSVGPSRLKQDPP
CCCCCCHHHHCCCCC		44.2922210691
167PhosphorylationVIHELRVSLEEIYSG
CCEEEECCHHHHHCC		24.5121945579
172PhosphorylationRVSLEEIYSGCTKRM
ECCHHHHHCCCCHHH		11.4221945579
173PhosphorylationVSLEEIYSGCTKRMK
CCHHHHHCCCCHHHH		32.8121945579
175S-nitrosylationLEEIYSGCTKRMKIS
HHHHHCCCCHHHHHC		3.1319483679
175S-nitrosocysteineLEEIYSGCTKRMKIS
HHHHHCCCCHHHHHC		3.13-
176PhosphorylationEEIYSGCTKRMKISR
HHHHCCCCHHHHHCH		25.8021945579
177AcetylationEIYSGCTKRMKISRK
HHHCCCCHHHHHCHH		55.3525953088
201PhosphorylationRSEDKILTIEIKKGW
CCCCCEEEEEEECCC		21.7523403867
213MalonylationKGWKEGTKITFPREG
CCCCCCCEEECCCCC		51.0826320211
213UbiquitinationKGWKEGTKITFPREG
CCCCCCCEEECCCCC		51.08-
223PhosphorylationFPREGDETPNSIPAD
CCCCCCCCCCCCCCC		32.2918669648
236UbiquitinationADIVFIIKDKDHPKF
CCEEEEECCCCCCCC		54.64-
248PhosphorylationPKFKRDGSNIIYTAK
CCCCCCCCCEEEEEE		29.1926657352
252PhosphorylationRDGSNIIYTAKISLR
CCCCCEEEEEEEEHH		9.2426657352
253PhosphorylationDGSNIIYTAKISLRE
CCCCEEEEEEEEHHH		15.8626657352
280PhosphorylationDGRNIPMSVNDIVKP
CCCCCCCCHHHHCCC		16.6520068231
286UbiquitinationMSVNDIVKPGMRRRI
CCHHHHCCCCCCCCE		35.87-
296PhosphorylationMRRRIIGYGLPFPKN
CCCCEEEECCCCCCC		12.70-
302UbiquitinationGYGLPFPKNPDQRGD
EECCCCCCCHHCCCC		79.90-
332UbiquitinationSSKEVLRKHLPAS--
CCHHHHHHHCCCC--		45.38-
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 DNJB4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJB4_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 DNJB4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP76_HUMANHSPA6physical
21988832
SMAD3_HUMANSMAD3physical
21988832
MDM2_HUMANMDM2physical
21988832
TBL1X_HUMANTBL1Xphysical
21988832
DPYL1_HUMANCRMP1physical
22863883
RANB3_HUMANRANBP3physical
22863883
DNJB5_HUMANDNAJB5physical
26186194
DNJB1_HUMANDNAJB1physical
26186194
BGAL_HUMANGLB1physical
26186194
SYNEM_HUMANSYNMphysical
26186194
CC038_HUMANC3orf38physical
26186194
TTL12_HUMANTTLL12physical
26186194
ERF1_HUMANETF1physical
26344197
HYOU1_HUMANHYOU1physical
26344197
STIP1_HUMANSTIP1physical
26344197
NPM_HUMANNPM1physical
20145123
DNJB1_HUMANDNAJB1physical
28514442
SYNEM_HUMANSYNMphysical
28514442
DNJB5_HUMANDNAJB5physical
28514442
CC038_HUMANC3orf38physical
28514442
TTL12_HUMANTTLL12physical
28514442
BGAL_HUMANGLB1physical
28514442
NUDC_HUMANNUDCphysical
27173435
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 DNJB4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-172, AND MASSSPECTROMETRY.

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