DJC11_HUMAN - dbPTM
DJC11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DJC11_HUMAN
UniProt AC Q9NVH1
Protein Name DnaJ homolog subfamily C member 11
Gene Name DNAJC11
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Mitochondrion . Isoforms show differential submitochondrial localization. A 57 kDa form (potentially isoform 3) shows either mitochondrial matrix or innermembrane (IM) localization, possibly anchored to the IM facing the matrix. A 35 kDa form behaved
Protein Description Isoform 1: Required for mitochondrial inner membrane organization. Seems to function through its association with the MICOS complex and the mitochondrial outer membrane sorting assembly machinery (SAM) complex..
Protein Sequence MATALSEEELDNEDYYSLLNVRREASSEELKAAYRRLCMLYHPDKHRDPELKSQAERLFNLVHQAYEVLSDPQTRAIYDIYGKRGLEMEGWEVVERRRTPAEIREEFERLQREREERRLQQRTNPKGTISVGVDATDLFDRYDEEYEDVSGSSFPQIEINKMHISQSIEAPLTATDTAILSGSLSTQNGNGGGSINFALRRVTSAKGWGELEFGAGDLQGPLFGLKLFRNLTPRCFVTTNCALQFSSRGIRPGLTTVLARNLDKNTVGYLQWRWGIQSAMNTSIVRDTKTSHFTVALQLGIPHSFALISYQHKFQDDDQTRVKGSLKAGFFGTVVEYGAERKISRHSVLGAAVSVGVPQGVSLKVKLNRASQTYFFPIHLTDQLLPSAMFYATVGPLVVYFAMHRLIIKPYLRAQKEKELEKQRESAATDVLQKKQEAESAVRLMQESVRRIIEAEESRMGLIIVNAWYGKFVNDKSRKSEKVKVIDVTVPLQCLVKDSKLILTEASKAGLPGFYDPCVGEEKNLKVLYQFRGVLHQVMVLDSEALRIPKQSHRIDTDG
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------MATALSEEE
------CCCCCCHHH		11.1122814378
3Phosphorylation-----MATALSEEEL
-----CCCCCCHHHH		27.1730108239
6Phosphorylation--MATALSEEELDNE
--CCCCCCHHHHCCH		40.2628464451
15PhosphorylationEELDNEDYYSLLNVR
HHHCCHHHHHHHHHH		6.7026074081
16PhosphorylationELDNEDYYSLLNVRR
HHCCHHHHHHHHHHH		12.7426074081
17PhosphorylationLDNEDYYSLLNVRRE
HCCHHHHHHHHHHHH		21.8326074081
26PhosphorylationLNVRREASSEELKAA
HHHHHHCCHHHHHHH		33.2623312004
27PhosphorylationNVRREASSEELKAAY
HHHHHCCHHHHHHHH		41.9830622161
31 (in isoform 3)Ubiquitination-33.9621890473
31 (in isoform 2)Ubiquitination-33.9621890473
31 (in isoform 1)Ubiquitination-33.9621890473
31UbiquitinationEASSEELKAAYRRLC
HCCHHHHHHHHHHHH		33.9621906983
34PhosphorylationSEELKAAYRRLCMLY
HHHHHHHHHHHHHHH		10.9223312004
41PhosphorylationYRRLCMLYHPDKHRD
HHHHHHHHCCCCCCC		5.6128509920
52UbiquitinationKHRDPELKSQAERLF
CCCCHHHHHHHHHHH		38.57-
53PhosphorylationHRDPELKSQAERLFN
CCCHHHHHHHHHHHH		47.44-
66PhosphorylationFNLVHQAYEVLSDPQ
HHHHHHHHHHHCCCH		10.4527642862
70PhosphorylationHQAYEVLSDPQTRAI
HHHHHHHCCCHHHHH		53.04-
78PhosphorylationDPQTRAIYDIYGKRG
CCHHHHHHHHHCCCC		8.7029496907
81PhosphorylationTRAIYDIYGKRGLEM
HHHHHHHHCCCCCEE		17.4429496907
83 (in isoform 2)Ubiquitination-26.7321890473
83 (in isoform 3)Ubiquitination-26.7321890473
83UbiquitinationAIYDIYGKRGLEMEG
HHHHHHCCCCCEECC		26.7321890473
832-HydroxyisobutyrylationAIYDIYGKRGLEMEG
HHHHHHCCCCCEECC		26.73-
83 (in isoform 1)Ubiquitination-26.7321890473
99PhosphorylationEVVERRRTPAEIREE
EEHHHCCCHHHHHHH		25.6628555341
126 (in isoform 3)Ubiquitination-71.4121890473
126UbiquitinationLQQRTNPKGTISVGV
HHHHHCCCCCEEEEC		71.4121906983
126 (in isoform 1)Ubiquitination-71.4121890473
126 (in isoform 2)Ubiquitination-71.4121890473
203PhosphorylationNFALRRVTSAKGWGE
EEEEEECCCCCCCEE		22.5824719451
204PhosphorylationFALRRVTSAKGWGEL
EEEEECCCCCCCEEE		25.7328857561
206 (in isoform 2)Ubiquitination-55.77-
226UbiquitinationQGPLFGLKLFRNLTP
CCCCHHHHHHCCCCC		46.06-
232PhosphorylationLKLFRNLTPRCFVTT
HHHHCCCCCCEEEEC		16.5524719451
255PhosphorylationRGIRPGLTTVLARNL
CCCCCCHHHHHCCCC		22.30-
256PhosphorylationGIRPGLTTVLARNLD
CCCCCHHHHHCCCCC		20.68-
264 (in isoform 1)Ubiquitination-58.6521890473
264 (in isoform 2)Ubiquitination-58.6521890473
264 (in isoform 3)Ubiquitination-58.6521890473
264UbiquitinationVLARNLDKNTVGYLQ
HHCCCCCCCCEEEEH		58.6521890473
278PhosphorylationQWRWGIQSAMNTSIV
HHHHHCCHHHCCCEE		27.8020068231
282PhosphorylationGIQSAMNTSIVRDTK
HCCHHHCCCEECCCC		13.5221712546
323UbiquitinationDDDQTRVKGSLKAGF
CCCCCCCCCCCCCCC		39.22-
325O-linked_GlycosylationDQTRVKGSLKAGFFG
CCCCCCCCCCCCCCE		22.4530379171
327MalonylationTRVKGSLKAGFFGTV
CCCCCCCCCCCCEEE		48.4326320211
327AcetylationTRVKGSLKAGFFGTV
CCCCCCCCCCCCEEE		48.4326051181
337PhosphorylationFFGTVVEYGAERKIS
CCEEEEHHCCCCCCC		15.27-
409UbiquitinationAMHRLIIKPYLRAQK
HHHHHHHHHHHHHHH		22.1821890473
409 (in isoform 2)Ubiquitination-22.1821890473
409 (in isoform 1)Ubiquitination-22.1821890473
4342-HydroxyisobutyrylationAATDVLQKKQEAESA
HHHHHHHHHHHHHHH		52.87-
434UbiquitinationAATDVLQKKQEAESA
HHHHHHHHHHHHHHH		52.87-
435UbiquitinationATDVLQKKQEAESAV
HHHHHHHHHHHHHHH		40.17-
448PhosphorylationAVRLMQESVRRIIEA
HHHHHHHHHHHHHHH		12.2021964256
458PhosphorylationRIIEAEESRMGLIIV
HHHHHHHHCCEEEEE		21.0521815630
469PhosphorylationLIIVNAWYGKFVNDK
EEEEECCCHHHCCCC		14.18-
4762-HydroxyisobutyrylationYGKFVNDKSRKSEKV
CHHHCCCCCCCCCCE		47.13-
476UbiquitinationYGKFVNDKSRKSEKV
CHHHCCCCCCCCCCE		47.13-
497AcetylationVPLQCLVKDSKLILT
EEHHHEECCCEEEEE		43.2526051181
497UbiquitinationVPLQCLVKDSKLILT
EEHHHEECCCEEEEE		43.25-
499PhosphorylationLQCLVKDSKLILTEA
HHHEECCCEEEEEEH		24.5230622161
500UbiquitinationQCLVKDSKLILTEAS
HHEECCCEEEEEEHH		50.08-
500AcetylationQCLVKDSKLILTEAS
HHEECCCEEEEEEHH		50.0826051181
507PhosphorylationKLILTEASKAGLPGF
EEEEEEHHHCCCCCC		19.4630622161
508UbiquitinationLILTEASKAGLPGFY
EEEEEHHHCCCCCCC		54.22-
523AcetylationDPCVGEEKNLKVLYQ
CCCCCCCCCHHHHHH		64.3826051181
523UbiquitinationDPCVGEEKNLKVLYQ
CCCCCCCCCHHHHHH		64.38-
526AcetylationVGEEKNLKVLYQFRG
CCCCCCHHHHHHHHC		39.3226051181
526MalonylationVGEEKNLKVLYQFRG
CCCCCCHHHHHHHHC		39.3226320211
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 DJC11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DJC11_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 DJC11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA7_HUMANANXA7physical
26496610
CAPG_HUMANCAPGphysical
26496610
H33_HUMANH3F3Aphysical
26496610
I5P2_HUMANINPP5Bphysical
26496610
PRIC3_HUMANPRICKLE3physical
26496610
RBM4_HUMANRBM4physical
26496610
STXB1_HUMANSTXBP1physical
26496610
TBX3_HUMANTBX3physical
26496610
TRAP1_HUMANTRAP1physical
26496610
HAX1_HUMANHAX1physical
26496610
MIC60_HUMANIMMTphysical
26496610
PIPNB_HUMANPITPNBphysical
26496610
BCOR_HUMANBCORphysical
26496610
MIC19_HUMANCHCHD3physical
26496610
RBM26_HUMANRBM26physical
26496610
C99L2_HUMANCD99L2physical
26496610
RN214_HUMANRNF214physical
26496610
H3C_HUMANH3F3Cphysical
26496610
RN214_HUMANRNF214physical
28514442
PDE6D_HUMANPDE6Dphysical
28514442
WDR73_HUMANWDR73physical
28514442
YTHD1_HUMANYTHDF1physical
28514442
TAXB1_HUMANTAX1BP1physical
28514442
ZNHI2_HUMANZNHIT2physical
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 DJC11_HUMAN

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Related Literatures of Post-Translational Modification

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