DJC21_HUMAN - dbPTM
DJC21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJC21_HUMAN
UniProt AC Q5F1R6
Protein Name DnaJ homolog subfamily C member 21
Gene Name DNAJC21
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleolus . Within the nucleus, localizes primarily to the nucleolus.
Protein Description May act as a co-chaperone for HSP70. May play a role in ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S subunit. Binds the precursor 45S rRNA..
Protein Sequence MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDDSLDLLRYFTVTCYSGYGDDEKGFYTVYRNVFEMIAKEELESVLEEEVDDFPTFGDSQSDYDTVVHPFYAYWQSFCTQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLYCPACDKSFKTEKAMKNHEKSKKHREMVALLKQQLEEEEENFSRPQIDENPLDDNSEEEMEDAPKQKLSKKQKKKKQKPAQNYDDNFNVNGPGEGVKVDPEDTNLNQDSAKELEDSPQENVSVTEIIKPCDDPKSEAKSVPKPKGKKTKDMKKPVRVPAEPQTMSVLISCTTCHSEFPSRNKLFDHLKATGHARAPSSSSLNSATSSQSKKEKRKNR
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
2Methylation------MKCHYEALG
------CCCHHHHHC		29.7123644510
15PhosphorylationLGVRRDASEEELKKA
HCCCCCCCHHHHHHH		50.2421815630
15 (in isoform 2)Phosphorylation-50.2424719451
25UbiquitinationELKKAYRKLALKWHP
HHHHHHHHHHHHHCC		25.9923000965
29 (in isoform 3)Ubiquitination-37.5421890473
29 (in isoform 2)Ubiquitination-37.5421890473
29 (in isoform 1)Ubiquitination-37.5421890473
29UbiquitinationAYRKLALKWHPDKNL
HHHHHHHHHCCCCCC		37.5423000965
34UbiquitinationALKWHPDKNLDNAAE
HHHHCCCCCCCHHHH		64.9523000965
47UbiquitinationAEAAEQFKLIQAAYD
HHHHHHHHHHHHHHH		44.3629967540
81PhosphorylationKGGFDGEYQDDSLDL
HCCCCCCCCCCCCHH		23.8328796482
81 (in isoform 3)Phosphorylation-23.8327642862
91PhosphorylationDSLDLLRYFTVTCYS
CCCHHHHHEEEEEEC		11.9925072903
93PhosphorylationLDLLRYFTVTCYSGY
CHHHHHEEEEEECCC		13.1325072903
95PhosphorylationLLRYFTVTCYSGYGD
HHHHEEEEEECCCCC		11.5825072903
97PhosphorylationRYFTVTCYSGYGDDE
HHEEEEEECCCCCCC		8.8625072903
98PhosphorylationYFTVTCYSGYGDDEK
HEEEEEECCCCCCCC		27.9025072903
100PhosphorylationTVTCYSGYGDDEKGF
EEEEECCCCCCCCCE		16.0825072903
112UbiquitinationKGFYTVYRNVFEMIA
CCEEEEHHHHHHHHH		28.6223000965
116UbiquitinationTVYRNVFEMIAKEEL
EEHHHHHHHHHHHHH		25.9521890473
121UbiquitinationVFEMIAKEELESVLE
HHHHHHHHHHHHHHH		59.8123000965
167UbiquitinationTQKNFAWKEEYDTRQ
HHCCCCCHHHHCHHH		36.9229967540
190UbiquitinationAMEKENKKIRDKARK
HHHHHHHHHHHHHHH		55.3324816145
231 (in isoform 2)Ubiquitination-51.59-
231UbiquitinationVEEQNAEKARKAEEM
HHHHHHHHHHHHHHH		51.5924816145
248UbiquitinationQQKLKQAKLVEQYRE
HHHHHHHHHHHHHHH		51.0429967540
257PhosphorylationVEQYREQSWMTMANL
HHHHHHHHHHHHHHH		17.6721712546
260PhosphorylationYREQSWMTMANLEKE
HHHHHHHHHHHHHHH		13.5829116813
275PhosphorylationLQEMEARYEKEFGDG
HHHHHHHHHHHHCCC		38.10-
277UbiquitinationEMEARYEKEFGDGSD
HHHHHHHHHHCCCCC		49.7824816145
283 (in isoform 2)Phosphorylation-46.6324719451
283PhosphorylationEKEFGDGSDENEMEE
HHHHCCCCCHHHHHH		46.6328355574
302 (in isoform 2)Phosphorylation-40.6227251275
302PhosphorylationDEEDGKDSDEAEDAE
CCCCCCCCCHHHHHH		40.6227362937
311PhosphorylationEAEDAELYDDLYCPA
HHHHHHHHHHCCCCC		10.0230576142
315PhosphorylationAELYDDLYCPACDKS
HHHHHHCCCCCCCCC		11.9030576142
315 (in isoform 2)Phosphorylation-11.90-
318UbiquitinationYDDLYCPACDKSFKT
HHHCCCCCCCCCHHH		15.5824816145
357PhosphorylationEEEEENFSRPQIDEN
HHHHHHCCCCCCCCC		55.4128176443
370 (in isoform 2)Phosphorylation-54.0727251275
370PhosphorylationENPLDDNSEEEMEDA
CCCCCCCCHHHHCHH		54.0725159151
392UbiquitinationKQKKKKQKPAQNYDD
HHHHHCCCCCCCCCC		51.7229967540
397PhosphorylationKQKPAQNYDDNFNVN
CCCCCCCCCCCCCCC		16.7625159151
410 (in isoform 3)Phosphorylation-4.8027642862
417PhosphorylationVKVDPEDTNLNQDSA
CCCCCCCCCCCHHHH		39.6922167270
423PhosphorylationDTNLNQDSAKELEDS
CCCCCHHHHHHHCCC		31.3222167270
430PhosphorylationSAKELEDSPQENVSV
HHHHHCCCCCCCCCC		21.0722167270
436PhosphorylationDSPQENVSVTEIIKP
CCCCCCCCCEEEEEC		34.6029632367
438PhosphorylationPQENVSVTEIIKPCD
CCCCCCCEEEEECCC		17.6029632367
442AcetylationVSVTEIIKPCDDPKS
CCCEEEEECCCCCHH		45.3026051181
448AcetylationIKPCDDPKSEAKSVP
EECCCCCHHHCCCCC		68.8426051181
449PhosphorylationKPCDDPKSEAKSVPK
ECCCCCHHHCCCCCC		48.4521712546
460AcetylationSVPKPKGKKTKDMKK
CCCCCCCCCCCCCCC		64.4922369005
468 (in isoform 2)Phosphorylation-17.3921406692
475 (in isoform 2)Phosphorylation-36.7327251275
481 (in isoform 2)Phosphorylation-1.5527251275
511PhosphorylationTGHARAPSSSSLNSA
HCCCCCCCCCCCCCC		41.7025159151
512PhosphorylationGHARAPSSSSLNSAT
CCCCCCCCCCCCCCC		23.9226657352
513PhosphorylationHARAPSSSSLNSATS
CCCCCCCCCCCCCCC		43.0928450419
514PhosphorylationARAPSSSSLNSATSS
CCCCCCCCCCCCCCC		33.2528985074
517PhosphorylationPSSSSLNSATSSQSK
CCCCCCCCCCCCHHH		37.9125159151
519PhosphorylationSSSLNSATSSQSKKE
CCCCCCCCCCHHHHH		28.8229396449
520PhosphorylationSSLNSATSSQSKKEK
CCCCCCCCCHHHHHH		26.5425159151
521PhosphorylationSLNSATSSQSKKEKR
CCCCCCCCHHHHHHH		33.8329507054
523PhosphorylationNSATSSQSKKEKRKN
CCCCCCHHHHHHHHC		47.8725159151
524PhosphorylationSATSSQSKKEKRKNR
CCCCCHHHHHHHHCC		58.2633259812
525UbiquitinationATSSQSKKEKRKNR-
CCCCHHHHHHHHCC-		73.9624816145
556Phosphorylation--------------------------------
--------------------------------		33259812
556 (in isoform 2)Phosphorylation-27251275
558 (in isoform 2)Phosphorylation-24719451
559 (in isoform 2)Phosphorylation-27251275
566 (in isoform 2)Phosphorylation-27251275
570Ubiquitination----------------------------------------------
----------------------------------------------		24816145
625Ubiquitination-----------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------		24816145
670Ubiquitination--------------------------------------------------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------------------------------------------------		24816145
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 DJC21_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DJC21_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 DJC21_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRPE1_HUMANGRPEL1physical
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 DJC21_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASSSPECTROMETRY.
"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-370, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302 ANDSER-370, AND MASS SPECTROMETRY.

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