DNJB2_HUMAN - dbPTM
DNJB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJB2_HUMAN
UniProt AC P25686
Protein Name DnaJ homolog subfamily B member 2 {ECO:0000305}
Gene Name DNAJB2 {ECO:0000312|HGNC:HGNC:5228}
Organism Homo sapiens (Human).
Sequence Length 324
Subcellular Localization Isoform 2: Cytoplasm . Nucleus .
Isoform 1: Endoplasmic reticulum membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family. [PubMed: 7957263]
Protein Sequence MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTSRSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPAGGREAQHRRQGRPKAQHQDPGLGGTQEGARGEATKRSPSPEEKASRCLIL
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
2Acetylation------MASYYEILD
------CCCCEECCC		13.26-
3Phosphorylation-----MASYYEILDV
-----CCCCEECCCC		27.2717322306
4Phosphorylation----MASYYEILDVP
----CCCCEECCCCC		8.7928851738
5Phosphorylation---MASYYEILDVPR
---CCCCEECCCCCC		8.2628851738
13PhosphorylationEILDVPRSASADDIK
ECCCCCCCCCHHHHH		22.0917322306
15PhosphorylationLDVPRSASADDIKKA
CCCCCCCCHHHHHHH		33.2128851738
20UbiquitinationSASADDIKKAYRRKA
CCCHHHHHHHHHHHH		38.0421906983
20 (in isoform 3)Ubiquitination-38.0421890473
20 (in isoform 2)Ubiquitination-38.0421890473
20UbiquitinationSASADDIKKAYRRKA
CCCHHHHHHHHHHHH		38.0421890473
21UbiquitinationASADDIKKAYRRKAL
CCHHHHHHHHHHHHH		51.4922817900
26UbiquitinationIKKAYRRKALQWHPD
HHHHHHHHHHHCCCC		44.4433845483
34 (in isoform 2)Ubiquitination-74.8821890473
34 (in isoform 3)Ubiquitination-74.8821890473
34UbiquitinationALQWHPDKNPDNKEF
HHHCCCCCCCCCHHH		74.8821890473
34UbiquitinationALQWHPDKNPDNKEF
HHHCCCCCCCCCHHH		74.8827667366
39UbiquitinationPDKNPDNKEFAEKKF
CCCCCCCHHHHHHHH		62.6822817900
39 (in isoform 2)Ubiquitination-62.6821890473
39UbiquitinationPDKNPDNKEFAEKKF
CCCCCCCHHHHHHHH		62.6821890473
39 (in isoform 3)Ubiquitination-62.6821890473
44UbiquitinationDNKEFAEKKFKEVAE
CCHHHHHHHHHHHHH		61.1422817900
45UbiquitinationNKEFAEKKFKEVAEA
CHHHHHHHHHHHHHH		53.8523503661
47UbiquitinationEFAEKKFKEVAEAYE
HHHHHHHHHHHHHHH		61.2229901268
59UbiquitinationAYEVLSDKHKREIYD
HHHHHCHHHHHHHHH		47.8821890473
59 (in isoform 2)Ubiquitination-47.8821890473
59UbiquitinationAYEVLSDKHKREIYD
HHHHHCHHHHHHHHH		47.8823000965
59 (in isoform 3)Ubiquitination-47.8821890473
61UbiquitinationEVLSDKHKREIYDRY
HHHCHHHHHHHHHHH		58.4223000965
61UbiquitinationEVLSDKHKREIYDRY
HHHCHHHHHHHHHHH		58.4221890473
61 (in isoform 3)Ubiquitination-58.4221890473
61 (in isoform 2)Ubiquitination-58.4221890473
65PhosphorylationDKHKREIYDRYGREG
HHHHHHHHHHHCCCC		6.9329496907
74PhosphorylationRYGREGLTGTGTGPS
HHCCCCCCCCCCCCC		43.4822210691
76PhosphorylationGREGLTGTGTGPSRA
CCCCCCCCCCCCCCC		26.7421406692
78PhosphorylationEGLTGTGTGPSRAEA
CCCCCCCCCCCCCCC		45.8421406692
81PhosphorylationTGTGTGPSRAEAGSG
CCCCCCCCCCCCCCC		45.5321406692
87PhosphorylationPSRAEAGSGGPGFTF
CCCCCCCCCCCCCEE		47.8530266825
93PhosphorylationGSGGPGFTFTFRSPE
CCCCCCCEEEECCHH		27.9030266825
95PhosphorylationGGPGFTFTFRSPEEV
CCCCCEEEECCHHHH		18.3230266825
98PhosphorylationGFTFTFRSPEEVFRE
CCEEEECCHHHHHHH		32.2621815630
124PhosphorylationFDDLGPFSELQNRGS
HHCCCCHHHHHHCCC		40.3029523821
131PhosphorylationSELQNRGSRHSGPFF
HHHHHCCCCCCCCCE		24.4729523821
166PhosphorylationPGAGAFRSVSTSTTF
CCCCCCCEECCCCCE		17.6126699800
168PhosphorylationAGAFRSVSTSTTFVQ
CCCCCEECCCCCEEC		20.2125106551
168O-linked_GlycosylationAGAFRSVSTSTTFVQ
CCCCCEECCCCCEEC		20.2130379171
169PhosphorylationGAFRSVSTSTTFVQG
CCCCEECCCCCEECC		28.1226699800
170PhosphorylationAFRSVSTSTTFVQGR
CCCEECCCCCEECCC		20.2426699800
202PhosphorylationEEDGQLKSVTINGVP
CCCCCEEEEEECCCC		32.84-
204PhosphorylationDGQLKSVTINGVPDD
CCCEEEEEECCCCCC		18.80-
219PhosphorylationLALGLELSRREQQPS
HHHHHHHHHHHCCCC		21.66-
231PhosphorylationQPSVTSRSGGTQVQQ
CCCCCCCCCCCCCEE		41.1428270605
234PhosphorylationVTSRSGGTQVQQTPA
CCCCCCCCCCEECCC		29.1428270605
239PhosphorylationGGTQVQQTPASCPLD
CCCCCEECCCCCCCC		12.0628270605
242PhosphorylationQVQQTPASCPLDSDL
CCEECCCCCCCCCCC		19.9228270605
247PhosphorylationPASCPLDSDLSEDED
CCCCCCCCCCCCCHH		48.4029802988
250PhosphorylationCPLDSDLSEDEDLQL
CCCCCCCCCCHHHHH		48.2529802988
261PhosphorylationDLQLAMAYSLSEMEA
HHHHHHHHHHHHHHH		9.3228270605
262PhosphorylationLQLAMAYSLSEMEAA
HHHHHHHHHHHHHHC		18.8428270605
264PhosphorylationLAMAYSLSEMEAAGK
HHHHHHHHHHHHCCC		29.0228270605
288UbiquitinationHRRQGRPKAQHQDPG
HHHCCCCCCCCCCCC		60.3623000965
288MethylationHRRQGRPKAQHQDPG
HHHCCCCCCCCCCCC		60.36-
299PhosphorylationQDPGLGGTQEGARGE
CCCCCCCCCCCCCCC		22.9627134283
308PhosphorylationEGARGEATKRSPSPE
CCCCCCCCCCCCCHH		23.7627362937
311PhosphorylationRGEATKRSPSPEEKA
CCCCCCCCCCHHHHH		31.1430266825
313PhosphorylationEATKRSPSPEEKASR
CCCCCCCCHHHHHHH		46.3030266825
319PhosphorylationPSPEEKASRCLIL--
CCHHHHHHHCCCC--		34.3029083192
321S-nitrosylationPEEKASRCLIL----
HHHHHHHCCCC----		2.2824105792
321MethylationPEEKASRCLIL----
HHHHHHHCCCC----		2.2812754272
321GeranylgeranylationPEEKASRCLIL----
HHHHHHHCCCC----		2.2812754272
321GeranylgeranylationPEEKASRCLIL----
HHHHHHHCCCC----		2.2812754272
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
247SPhosphorylationKinaseCSNK2A1P68400
GPS
250SPhosphorylationKinaseCSNK2A1P68400
GPS
264SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJB2_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 DNJB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP74_HUMANHSPA4physical
21625540
ATX3_HUMANATXN3physical
21625540
UBC_HUMANUBCphysical
15936278
PSA6_HUMANPSMA6physical
15936278
HSP7C_HUMANHSPA8physical
15936278
OPSD_HUMANRHOphysical
12754272
SODC_MOUSESod1physical
24023695
HS90B_MOUSEHsp90ab1physical
22396390
HS71B_MOUSEHspa1bphysical
22396390
SQSTM_MOUSESqstm1physical
22396390
SPB5_MOUSESerpinb5physical
22396390
UBB_HUMANUBBphysical
26186194
BGAL_HUMANGLB1physical
26186194
TROP_HUMANTROphysical
26186194
ATP7A_HUMANATP7Aphysical
26186194
ATP7B_HUMANATP7Bphysical
26186194
BIG2_HUMANARFGEF2physical
26186194
PPGB_HUMANCTSAphysical
26186194
PJA1_HUMANPJA1physical
26186194
FA83H_HUMANFAM83Hphysical
26186194
MO4L1_HUMANMORF4L1physical
26186194
ASNA_HUMANASNA1physical
26186194
BIRC2_HUMANBIRC2physical
26186194
RN19B_HUMANRNF19Bphysical
26186194
CYHR1_HUMANCYHR1physical
26186194
RFWD3_HUMANRFWD3physical
26186194
KCTD3_HUMANKCTD3physical
26186194
TRAF2_HUMANTRAF2physical
26186194
LACC1_HUMANLACC1physical
26186194
NEK4_HUMANNEK4physical
26186194
RN115_HUMANRNF115physical
26186194
TADBP_HUMANTARDBPphysical
26936937
CYHR1_HUMANCYHR1physical
28514442
UBB_HUMANUBBphysical
28514442
LACC1_HUMANLACC1physical
28514442
BIRC2_HUMANBIRC2physical
28514442
TROP_HUMANTROphysical
28514442
RFWD3_HUMANRFWD3physical
28514442
BGAL_HUMANGLB1physical
28514442
RN19B_HUMANRNF19Bphysical
28514442
RNF12_HUMANRLIMphysical
28514442
PPGB_HUMANCTSAphysical
28514442
TRAF2_HUMANTRAF2physical
28514442
FA83H_HUMANFAM83Hphysical
28514442
HSP74_HUMANHSPA4physical
22219199
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614881Distal spinal muscular atrophy, autosomal recessive, 5 (DSMA5)
616233Charcot-Marie-Tooth disease 2T (CMT2T)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJB2_HUMAN

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