DNJC2_HUMAN - dbPTM
DNJC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJC2_HUMAN
UniProt AC Q99543
Protein Name DnaJ homolog subfamily C member 2
Gene Name DNAJC2
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Nucleus . Cytoplasm, cytosol .
Protein Description Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'..
Protein Sequence MLLLPSAADGRGTAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCDRLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQASKNTEKSTGGGGNGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVVPQADNATPSERFEGPYTDFTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMKRYKELVEMVKAKKAAQEQVLNASRAKK
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
1Sulfoxidation-------MLLLPSAA
-------CCCCCCCC		5.5521406390
1Acetylation-------MLLLPSAA
-------CCCCCCCC		5.5522223895
6Phosphorylation--MLLLPSAADGRGT
--CCCCCCCCCCCCH		35.7424043423
16PhosphorylationDGRGTAITHALTSAS
CCCCHHHHHHHHCCH		9.9123828894
26GlutathionylationLTSASTLCQVEPVGR
HHCCHHHCEEECCHH		4.2822555962
34UbiquitinationQVEPVGRWFEAFVKR
EEECCHHHHHHHHHH		6.9024816145
40UbiquitinationRWFEAFVKRRNRNAS
HHHHHHHHHHCCCCC		38.90-
47PhosphorylationKRRNRNASASFQELE
HHHCCCCCHHHHHHH		28.1719664994
49PhosphorylationRNRNASASFQELEDK
HCCCCCHHHHHHHHH		25.6019664994
60PhosphorylationLEDKKELSEESEDEE
HHHHHHHCCCCCCCC		40.1720201521
63PhosphorylationKKELSEESEDEELQL
HHHHCCCCCCCCCCH		46.4220201521
90PhosphorylationDWKNQDHYAVLGLGH
HHCCCCCEEEECCHH		13.4928450419
91UbiquitinationWKNQDHYAVLGLGHV
HCCCCCEEEECCHHH		6.1424816145
100PhosphorylationLGLGHVRYKATQRQI
ECCHHHHHHHHHHHH		12.13-
103O-linked_GlycosylationGHVRYKATQRQIKAA
HHHHHHHHHHHHHHH		21.8230379171
106UbiquitinationRYKATQRQIKAAHKA
HHHHHHHHHHHHHHH		31.5524816145
112AcetylationRQIKAAHKAMVLKHH
HHHHHHHHHHHHHHC		33.1925953088
112UbiquitinationRQIKAAHKAMVLKHH
HHHHHHHHHHHHHHC		33.1929967540
121UbiquitinationMVLKHHPDKRKAAGE
HHHHHCCCHHHCCCC		60.0624816145
131UbiquitinationKAAGEPIKEGDNDYF
HCCCCCCCCCCCCHH		67.3829967540
137PhosphorylationIKEGDNDYFTCITKA
CCCCCCCHHHHHHHH		13.6727642862
142PhosphorylationNDYFTCITKAYEMLS
CCHHHHHHHHHHHHC		16.27-
143UbiquitinationDYFTCITKAYEMLSD
CHHHHHHHHHHHHCC		29.1229967540
145PhosphorylationFTCITKAYEMLSDPV
HHHHHHHHHHHCCHH		11.9227642862
153UbiquitinationEMLSDPVKRRAFNSV
HHHCCHHHHHHHCCC		41.3729967540
163UbiquitinationAFNSVDPTFDNSVPS
HHCCCCCCCCCCCCC		38.8724816145
171UbiquitinationFDNSVPSKSEAKDNF
CCCCCCCHHHHCCCC		46.3629967540
175UbiquitinationVPSKSEAKDNFFEVF
CCCHHHHCCCCHHHH		49.5029967540
178UbiquitinationKSEAKDNFFEVFTPV
HHHHCCCCHHHHHHH		8.7224816145
179UbiquitinationSEAKDNFFEVFTPVF
HHHCCCCHHHHHHHH		11.1124816145
183PhosphorylationDNFFEVFTPVFERNS
CCCHHHHHHHHHHCC		24.5822199227
228PhosphorylationFDSWREFSYLDEEEK
CCCHHHHHCCCHHHH		21.7429449344
229PhosphorylationDSWREFSYLDEEEKE
CCHHHHHCCCHHHHH		24.4029449344
235UbiquitinationSYLDEEEKEKAECRD
HCCCHHHHHHHHHHH		68.7324816145
236UbiquitinationYLDEEEKEKAECRDE
CCCHHHHHHHHHHHH		61.8624816145
237UbiquitinationLDEEEKEKAECRDER
CCHHHHHHHHHHHHH		61.6324816145
249UbiquitinationDERRWIEKQNRATRA
HHHHHHHHHHHHHHH		43.6829967540
250UbiquitinationERRWIEKQNRATRAQ
HHHHHHHHHHHHHHH		31.6724816145
274PhosphorylationRTLVDNAYSCDPRIK
HHHHHHHHCCCHHHH		18.9828152594
275PhosphorylationTLVDNAYSCDPRIKK
HHHHHHHCCCHHHHH		15.0528152594
276GlutathionylationLVDNAYSCDPRIKKF
HHHHHHCCCHHHHHH		5.6322555962
308UbiquitinationAKRKEQEAKEKQRQA
HHHHHHHHHHHHHHH		25.6324816145
309UbiquitinationKRKEQEAKEKQRQAE
HHHHHHHHHHHHHHH		65.7724816145
324UbiquitinationLEAARLAKEKEEEEV
HHHHHHHHHHHHHHH		74.1224816145
367PhosphorylationCKTWNHFSDNEAERV
HHHCCCCCCCHHHHH		31.7928985074
382UbiquitinationKMMEEVEKLCDRLEL
HHHHHHHHHHHHHHH		60.6424816145
387UbiquitinationVEKLCDRLELASLQC
HHHHHHHHHHHHHHH		3.9524816145
401PhosphorylationCLNETLTSCTKEVGK
HHHHHHHHHHHHHHH		23.9330631047
404UbiquitinationETLTSCTKEVGKAAL
HHHHHHHHHHHHHHH		55.5229967540
413UbiquitinationVGKAALEKQIEEINE
HHHHHHHHHHHHHHH		58.3829967540
421UbiquitinationQIEEINEQIRKEKEE
HHHHHHHHHHHHHHH		35.9832015554
444UbiquitinationSKNTEKSTGGGGNGS
HHCCCCCCCCCCCCC		51.4124816145
451UbiquitinationTGGGGNGSKNWSEDD
CCCCCCCCCCCCHHH		27.1529967540
455UbiquitinationGNGSKNWSEDDLQLL
CCCCCCCCHHHHHHH		40.3129967540
473UbiquitinationVNLFPAGTNSRWEVI
HHCCCCCCCCHHHHH		31.9329967540
474UbiquitinationNLFPAGTNSRWEVIA
HCCCCCCCCHHHHHH		28.7629967540
493UbiquitinationIHSSSGVKRTAKDVI
CCCCCCCCHHHHHHH		47.7832015554
504UbiquitinationKDVIGKAKSLQKLDP
HHHHHHHHHHHHCCC		56.0029967540
508UbiquitinationGKAKSLQKLDPHQKD
HHHHHHHHCCCCCCC		61.2129967540
514 (in isoform 2)Ubiquitination-55.1021906983
514UbiquitinationQKLDPHQKDDINKKA
HHCCCCCCCCCCHHH		55.1032015554
516UbiquitinationLDPHQKDDINKKAFD
CCCCCCCCCCHHHHH		54.0924816145
526UbiquitinationKKAFDKFKKEHGVVP
HHHHHHHHHHHCCCC		64.0929967540
527UbiquitinationKAFDKFKKEHGVVPQ
HHHHHHHHHHCCCCC		59.0629967540
537UbiquitinationGVVPQADNATPSERF
CCCCCCCCCCCCCCC		49.0524816145
539PhosphorylationVPQADNATPSERFEG
CCCCCCCCCCCCCCC		33.3325159151
548PhosphorylationSERFEGPYTDFTPWT
CCCCCCCCCCCCCCC		29.7822817900
556PhosphorylationTDFTPWTTEEQKLLE
CCCCCCCHHHHHHHH		33.3925627689
567UbiquitinationKLLEQALKTYPVNTP
HHHHHHHHHCCCCCH		49.3732015554
567 (in isoform 1)Ubiquitination-49.3721906983
573PhosphorylationLKTYPVNTPERWEKI
HHHCCCCCHHHHHHH		27.1021815630
590UbiquitinationAVPGRTKKDCMKRYK
HCCCCCHHHHHHHHH		56.3924816145
597MalonylationKDCMKRYKELVEMVK
HHHHHHHHHHHHHHH		48.9132601280
597AcetylationKDCMKRYKELVEMVK
HHHHHHHHHHHHHHH		48.9126051181
606MethylationLVEMVKAKKAAQEQV
HHHHHHHHHHHHHHH		36.91-
607MethylationVEMVKAKKAAQEQVL
HHHHHHHHHHHHHHH		54.54-
617PhosphorylationQEQVLNASRAKK---
HHHHHHHHHHCC---		31.5323403867
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 DNJC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJC2_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 DNJC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING2_HUMANRNF2physical
21179169
DDX5_HUMANDDX5physical
26344197
DNMT1_HUMANDNMT1physical
26344197
HSP7E_HUMANHSPA14physical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
HYOU1_HUMANHYOU1physical
26344197
MYO6_HUMANMYO6physical
26344197
HSP7E_HUMANHSPA14physical
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 DNJC2_HUMAN

loading...

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-47; SER-49; SER-60 ANDSER-63, AND MASS SPECTROMETRY.
"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-47; SER-49; SER-60 ANDSER-63, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, 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-47; SER-49; SER-60 ANDSER-63, AND MASS SPECTROMETRY.

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