DNJC1_HUMAN - dbPTM
DNJC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJC1_HUMAN
UniProt AC Q96KC8
Protein Name DnaJ homolog subfamily C member 1
Gene Name DNAJC1
Organism Homo sapiens (Human).
Sequence Length 554
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein. Nucleus membrane
Single-pass type I membrane protein. Microsome membrane
Single-pass type I membrane protein.
Protein Description May modulate protein synthesis..
Protein Sequence MTAPCSQPAQLPGRRQLGLVPFPPPPPRTPLLWLLLLLLAAVAPARGWESGDLELFDLVEEVQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYYRRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLSRKKREKKKKTGSKSVDVSKLGASEKNERLLMKPQWHDLLPCKLGIWFCLTLKALPHLIQDAGQFYAKYKETRLKEKEDALTRTELETLQKQKKVKKPKPEFPVYTPLETTYIQSYDHGTSIEEIEEQMDDWLENRNRTQKKQAPEWTEEDLSQLTRSMVKFPGGTPGRWEKIAHELGRSVTDVTTKAKQLKDSVTCSPGMVRLSELKSTVQNSRPIKTATTLPDDMITQREDAEGVAAEEEQEGDSGEQETGATDARPRRRKPARLLEATAKPEPEEKSRAKRQKDFDIAEQNESSDEESLRKERARSAEEPWTQNQQKLLELALQQYPRGSSDRWDKIARCVPSKSKEDCIARYKLLVELVQKKKQAKS
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
6Phosphorylation--MTAPCSQPAQLPG
--CCCCCCCCCCCCC
37.8320068231
89PhosphorylationRKAYRKLSLTLHPDK
HHHHHHHHCEECCCC
23.4927067055
96UbiquitinationSLTLHPDKNKDENAE
HCEECCCCCCCCCHH
71.0529967540
117UbiquitinationVAIYEVLKDDERRQR
HHHHHHHCCCHHHHH
69.20-
184PhosphorylationKQLDELLSRKKREKK
HHHHHHHHHHHHHHH
55.4626074081
197UbiquitinationKKKKTGSKSVDVSKL
HHCCCCCCCCCHHHC
56.7133845483
202PhosphorylationGSKSVDVSKLGASEK
CCCCCCHHHCCCCHH
20.0729214152
203UbiquitinationSKSVDVSKLGASEKN
CCCCCHHHCCCCHHH
51.2733845483
2032-HydroxyisobutyrylationSKSVDVSKLGASEKN
CCCCCHHHCCCCHHH
51.27-
207PhosphorylationDVSKLGASEKNERLL
CHHHCCCCHHHCCCC
47.5123403867
209UbiquitinationSKLGASEKNERLLMK
HHCCCCHHHCCCCCC
62.7133845483
216UbiquitinationKNERLLMKPQWHDLL
HHCCCCCCCCHHHHH
33.7429967540
234PhosphorylationLGIWFCLTLKALPHL
HHHHHHHHHHHHHHH
27.65-
249PhosphorylationIQDAGQFYAKYKETR
HHHHHHHHHHHHHHH
8.36-
258UbiquitinationKYKETRLKEKEDALT
HHHHHHHHHHHHHHH
64.55-
2602-HydroxyisobutyrylationKETRLKEKEDALTRT
HHHHHHHHHHHHHHH
60.34-
260UbiquitinationKETRLKEKEDALTRT
HHHHHHHHHHHHHHH
60.3424816145
274UbiquitinationTELETLQKQKKVKKP
HHHHHHHHHHCCCCC
68.1733845483
295PhosphorylationYTPLETTYIQSYDHG
CCCCCCEEEEECCCC
12.3722817900
299PhosphorylationETTYIQSYDHGTSIE
CCEEEEECCCCCCHH
8.7922817900
322PhosphorylationWLENRNRTQKKQAPE
HHHHCCHHHHHCCCC
48.5729083192
325UbiquitinationNRNRTQKKQAPEWTE
HCCHHHHHCCCCCCH
41.7029967540
331PhosphorylationKKQAPEWTEEDLSQL
HHCCCCCCHHHHHHH
28.0329083192
339PhosphorylationEEDLSQLTRSMVKFP
HHHHHHHHHHHHCCC
17.0429083192
349PhosphorylationMVKFPGGTPGRWEKI
HHCCCCCCCCHHHHH
28.6021815630
363PhosphorylationIAHELGRSVTDVTTK
HHHHHCCCHHHHHHH
27.8028555341
365PhosphorylationHELGRSVTDVTTKAK
HHHCCCHHHHHHHHH
26.4628348404
375MalonylationTTKAKQLKDSVTCSP
HHHHHHHHHCCCCCC
45.5226320211
377PhosphorylationKAKQLKDSVTCSPGM
HHHHHHHCCCCCCCE
20.1022199227
379PhosphorylationKQLKDSVTCSPGMVR
HHHHHCCCCCCCEEE
15.9529255136
381PhosphorylationLKDSVTCSPGMVRLS
HHHCCCCCCCEEEHH
18.3423401153
384SulfoxidationSVTCSPGMVRLSELK
CCCCCCCEEEHHHHH
1.4721406390
388PhosphorylationSPGMVRLSELKSTVQ
CCCEEEHHHHHHHHH
30.2526074081
391UbiquitinationMVRLSELKSTVQNSR
EEEHHHHHHHHHHCC
39.7829967540
392PhosphorylationVRLSELKSTVQNSRP
EEHHHHHHHHHHCCC
46.5726074081
393PhosphorylationRLSELKSTVQNSRPI
EHHHHHHHHHHCCCC
25.2326074081
397PhosphorylationLKSTVQNSRPIKTAT
HHHHHHHCCCCCCCC
23.4926074081
402PhosphorylationQNSRPIKTATTLPDD
HHCCCCCCCCCCCHH
29.9223186163
404PhosphorylationSRPIKTATTLPDDMI
CCCCCCCCCCCHHHC
33.8130624053
405PhosphorylationRPIKTATTLPDDMIT
CCCCCCCCCCHHHCC
33.5523917254
412PhosphorylationTLPDDMITQREDAEG
CCCHHHCCCCHHCCC
18.2223186163
430PhosphorylationEEEQEGDSGEQETGA
CHHCCCCCCCCCCCC
55.9029255136
435PhosphorylationGDSGEQETGATDARP
CCCCCCCCCCCCCCC
31.6322167270
438PhosphorylationGEQETGATDARPRRR
CCCCCCCCCCCCCCC
31.3822167270
456AcetylationRLLEATAKPEPEEKS
HHHHHHCCCCHHHHH
45.6326051181
456UbiquitinationRLLEATAKPEPEEKS
HHHHHHCCCCHHHHH
45.6324816145
456MethylationRLLEATAKPEPEEKS
HHHHHHCCCCHHHHH
45.63-
479PhosphorylationDIAEQNESSDEESLR
CHHHHCCCCCHHHHH
51.1129255136
480PhosphorylationIAEQNESSDEESLRK
HHHHCCCCCHHHHHH
42.7529255136
484PhosphorylationNESSDEESLRKERAR
CCCCCHHHHHHHHHH
31.2729255136
487AcetylationSDEESLRKERARSAE
CCHHHHHHHHHHHCC
57.777683449
492PhosphorylationLRKERARSAEEPWTQ
HHHHHHHHCCCCCHH
38.7625159151
498PhosphorylationRSAEEPWTQNQQKLL
HHCCCCCHHHHHHHH
28.4923898821
539PhosphorylationKEDCIARYKLLVELV
HHHHHHHHHHHHHHH
9.2828152594

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 DNJC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJC1_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 DNJC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AACT_HUMANSERPINA3physical
14668352
GRP78_HUMANHSPA5physical
26085089
RMND1_HUMANRMND1physical
28514442
1C07_HUMANHLA-Cphysical
28514442
COR1A_HUMANCORO1Aphysical
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 DNJC1_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-430, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-484, ANDMASS 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-381 AND SER-430, ANDMASS SPECTROMETRY.

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