DJB12_HUMAN - dbPTM
DJB12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJB12_HUMAN
UniProt AC Q9NXW2
Protein Name DnaJ homolog subfamily B member 12 {ECO:0000312|HGNC:HGNC:14891}
Gene Name DNAJB12 {ECO:0000312|HGNC:HGNC:14891}
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Nucleus membrane
Single-pass membrane protein . Localizes to the endoplasmic reticulum membrane (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). When overexpressed
Protein Description Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. [PubMed: 21150129]
Protein Sequence MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVRALIESLNQKPQTAGDQPPPTDTTHATHRKAGGTDAPSANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRRLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHRRVTDHLGVVYYVGDTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQSEGLLYRARYFGDTDMYHRAQKMGTPSCSRLSEVQASLHG
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
1Acetylation-------MESNKDEA
-------CCCCHHHH		13.2222814378
33 (in isoform 2)Ubiquitination-52.55-
67UbiquitinationQPPPTDTTHATHRKA
CCCCCCCCCCCCHHC		16.60-
73 (in isoform 2)Ubiquitination-43.72-
81PhosphorylationAGGTDAPSANGEAGG
CCCCCCCCCCCCCCC		35.7721815630
87UbiquitinationPSANGEAGGESTKGY
CCCCCCCCCCCCCCC		35.78-
92UbiquitinationEAGGESTKGYTAEQV
CCCCCCCCCCCHHHH		60.2321906983
92 (in isoform 2)Ubiquitination-60.23-
103 (in isoform 2)Ubiquitination-46.90-
103UbiquitinationAEQVAAVKRVKQCKD
HHHHHHHHHHHHCCC		46.90-
1032-HydroxyisobutyrylationAEQVAAVKRVKQCKD
HHHHHHHHHHHHCCC		46.90-
103MalonylationAEQVAAVKRVKQCKD
HHHHHHHHHHHHCCC		46.9026320211
107UbiquitinationAAVKRVKQCKDYYEI
HHHHHHHHCCCHHHH		36.31-
109 (in isoform 2)Ubiquitination-46.39-
109UbiquitinationVKRVKQCKDYYEILG
HHHHHHCCCHHHHHC		46.39-
112PhosphorylationVKQCKDYYEILGVSR
HHHCCCHHHHHCCCC		13.4622817900
115PhosphorylationCKDYYEILGVSRGAS
CCCHHHHHCCCCCCC		3.5627251275
126UbiquitinationRGASDEDLKKAYRRL
CCCCHHHHHHHHHHH		6.04-
136MalonylationAYRRLALKFHPDKNH
HHHHHHHHHCCCCCC		35.7026320211
137UbiquitinationYRRLALKFHPDKNHA
HHHHHHHHCCCCCCC		11.99-
141UbiquitinationALKFHPDKNHAPGAT
HHHHCCCCCCCCCHH		55.9021890473
141 (in isoform 2)Ubiquitination-55.90-
143UbiquitinationKFHPDKNHAPGATEA
HHCCCCCCCCCHHHH		38.76-
146PhosphorylationPDKNHAPGATEAFKA
CCCCCCCCHHHHHHH		46.01-
156PhosphorylationEAFKAIGTAYAVLSN
HHHHHHHHHHHHHCC		15.4720071362
158PhosphorylationFKAIGTAYAVLSNPE
HHHHHHHHHHHCCHH		9.3323312004
162PhosphorylationGTAYAVLSNPEKRKQ
HHHHHHHCCHHHHHH		43.68-
166 (in isoform 2)Ubiquitination-67.18-
166UbiquitinationAVLSNPEKRKQYDQF
HHHCCHHHHHHHHHH		67.18-
168 (in isoform 2)Ubiquitination-65.36-
170UbiquitinationNPEKRKQYDQFGDDK
CHHHHHHHHHHCCCH		18.10-
170PhosphorylationNPEKRKQYDQFGDDK
CHHHHHHHHHHCCCH		18.1023312004
175UbiquitinationKQYDQFGDDKSQAAR
HHHHHHCCCHHHHHH		62.5521890473
175UbiquitinationKQYDQFGDDKSQAAR
HHHHHHCCCHHHHHH		62.55-
177 (in isoform 2)Ubiquitination-49.56-
177UbiquitinationYDQFGDDKSQAARHG
HHHHCCCHHHHHHHC		49.562190698
178PhosphorylationDQFGDDKSQAARHGH
HHHCCCHHHHHHHCC		31.8523312004
200UbiquitinationGFEADISPEDLFNMF
CCCCCCCHHHHHHHH		39.18-
202UbiquitinationEADISPEDLFNMFFG
CCCCCHHHHHHHHHC		61.00-
211UbiquitinationFNMFFGGGFPSSNVH
HHHHHCCCCCCCCEE		31.50-
212PhosphorylationNMFFGGGFPSSNVHV
HHHHCCCCCCCCEEE		6.3227251275
214PhosphorylationFFGGGFPSSNVHVYS
HHCCCCCCCCEEEEE		32.08-
273PhosphorylationMVSSPPYSLSPRPSV
HHCCCCCCCCCCCCC		28.3024719451
275PhosphorylationSSPPYSLSPRPSVGH
CCCCCCCCCCCCCCC		16.9624719451
321PhosphorylationERNVEDDYIANLRNN
HHHCCHHHHHHHHHC		17.79-
341PhosphorylationQQSEGLLYRARYFGD
HHHCCHHHHHHHHCC		13.79-
345PhosphorylationGLLYRARYFGDTDMY
CHHHHHHHHCCHHHH		15.78-
352PhosphorylationYFGDTDMYHRAQKMG
HHCCHHHHHHHHHHC		7.32-
355PhosphorylationDTDMYHRAQKMGTPS
CHHHHHHHHHHCCCC		10.47-
386Phosphorylation------------------
------------------		-
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 DJB12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DJB12_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 DJB12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
22939629
HSP72_HUMANHSPA2physical
26344197
HSP7C_HUMANHSPA8physical
26344197
GRP75_HUMANHSPA9physical
26344197
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 DJB12_HUMAN

loading...

Related Literatures of Post-Translational Modification

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