JMJD6_HUMAN - dbPTM
JMJD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JMJD6_HUMAN
UniProt AC Q6NYC1
Protein Name Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
Gene Name JMJD6
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Nucleus, nucleoplasm. Nucleus, nucleolus. Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the
Protein Description Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses..
Protein Sequence MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
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
15PhosphorylationRIREAKRSARPELKD
HHHHHHHHHCHHHHH
28.1122210691
23 (in isoform 3)Phosphorylation-27.0027251275
23PhosphorylationARPELKDSLDWTRHN
HCHHHHHHCCCHHCC
27.0024275569
31PhosphorylationLDWTRHNYYESFSLS
CCCHHCCCHHHHCCC
11.5027080861
32PhosphorylationDWTRHNYYESFSLSP
CCHHCCCHHHHCCCH
15.4827080861
34PhosphorylationTRHNYYESFSLSPAA
HHCCCHHHHCCCHHH
12.1927080861
36PhosphorylationHNYYESFSLSPAAVA
CCCHHHHCCCHHHHC
36.9028450419
38PhosphorylationYYESFSLSPAAVADN
CHHHHCCCHHHHCCC
15.9925159151
68 (in isoform 3)Ubiquitination-33.74-
68UbiquitinationERYERPYKPVVLLNA
HHCCCCCCCEEEEEC
33.74-
100 (in isoform 3)Ubiquitination-48.65-
100UbiquitinationKYRNQKFKCGEDNDG
HHHCCCCCCCCCCCC
48.65-
100MethylationKYRNQKFKCGEDNDG
HHHCCCCCCCCCCCC
48.65115971591
108PhosphorylationCGEDNDGYSVKMKMK
CCCCCCCCEEEEEEE
17.10-
120PhosphorylationKMKYYIEYMESTRDD
EEEEHHHHHHHCCCC
9.1629759185
128PhosphorylationMESTRDDSPLYIFDS
HHHCCCCCCEEEECC
22.5423312004
131PhosphorylationTRDDSPLYIFDSSYG
CCCCCCEEEECCCCC
11.7020873877
135PhosphorylationSPLYIFDSSYGEHPK
CCEEEECCCCCCCHH
18.0820873877
136PhosphorylationPLYIFDSSYGEHPKR
CEEEECCCCCCCHHH
38.7120873877
137PhosphorylationLYIFDSSYGEHPKRR
EEEECCCCCCCHHHH
30.4122817900
142UbiquitinationSSYGEHPKRRKLLED
CCCCCCHHHHHHHHH
67.7429967540
145 (in isoform 3)Ubiquitination-62.55-
145UbiquitinationGEHPKRRKLLEDYKV
CCCHHHHHHHHHCCC
62.5529967540
151 (in isoform 2)Ubiquitination-65.4721890473
151 (in isoform 3)Ubiquitination-65.4721890473
151 (in isoform 1)Ubiquitination-65.4721890473
151UbiquitinationRKLLEDYKVPKFFTD
HHHHHHCCCCCHHCC
65.4722817900
151SumoylationRKLLEDYKVPKFFTD
HHHHHHCCCCCHHCC
65.47-
154UbiquitinationLEDYKVPKFFTDDLF
HHHCCCCCHHCCHHH
56.9822817900
154SumoylationLEDYKVPKFFTDDLF
HHHCCCCCHHCCHHH
56.98-
154SumoylationLEDYKVPKFFTDDLF
HHHCCCCCHHCCHHH
56.98-
167 (in isoform 2)Ubiquitination-53.4421890473
167UbiquitinationLFQYAGEKRRPPYRW
HHHHCCCCCCCCCEE
53.4421963094
167 (in isoform 3)Ubiquitination-53.4421890473
167 (in isoform 1)Ubiquitination-53.4421890473
204AcetylationNALVQGHKRWCLFPT
HHHHHCCCCEEECCC
55.1926051181
204UbiquitinationNALVQGHKRWCLFPT
HHHHHCCCCEEECCC
55.19-
219UbiquitinationSTPRELIKVTRDEGG
CCHHHHEEEEECCCC
50.6124816145
219 (in isoform 3)Ubiquitination-50.61-
329PhosphorylationELAVLADSVDLQEST
HHHEEECCCCCHHHC
16.3630576142
348PhosphorylationDSSSDSSSSSSSSSS
CCCCCCCCCCCCCCC
37.89-
349PhosphorylationSSSDSSSSSSSSSSD
CCCCCCCCCCCCCCC
35.87-
350PhosphorylationSSDSSSSSSSSSSDS
CCCCCCCCCCCCCCC
35.87-
351PhosphorylationSDSSSSSSSSSSDSD
CCCCCCCCCCCCCCC
35.87-
370PhosphorylationSGSEGDGTVHRRKKR
CCCCCCCCCCCCCCC
20.2030576142
379PhosphorylationHRRKKRRTCSMVGNG
CCCCCCCCEECCCCC
16.9925159151
381PhosphorylationRKKRRTCSMVGNGDT
CCCCCCEECCCCCCC
18.8525159151
381 (in isoform 3)Phosphorylation-18.8524719451
388PhosphorylationSMVGNGDTTSQDDCV
ECCCCCCCCCHHHHH
29.7328450419
388 (in isoform 3)Phosphorylation-29.7324719451
389PhosphorylationMVGNGDTTSQDDCVS
CCCCCCCCCHHHHHC
29.1828450419
390PhosphorylationVGNGDTTSQDDCVSK
CCCCCCCCHHHHHCH
33.4321815630
390 (in isoform 3)Phosphorylation-33.4324719451
396PhosphorylationTSQDDCVSKERSSSR
CCHHHHHCHHHHCCC
34.8228450419
397AcetylationSQDDCVSKERSSSR-
CHHHHHCHHHHCCC-
36.4326051181
400PhosphorylationDCVSKERSSSR----
HHHCHHHHCCC----
33.4828450419
401 (in isoform 3)Phosphorylation-36.0330631047
401PhosphorylationCVSKERSSSR-----
HHCHHHHCCC-----
36.0328450419
402 (in isoform 3)Phosphorylation-43.1630631047
402PhosphorylationVSKERSSSR------
HCHHHHCCC------
43.1628450419

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 JMJD6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JMJD6_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 JMJD6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRD4_HUMANBRD4physical
21555454
LUC7L_HUMANLUC7Lphysical
21555454
RSRC1_HUMANRSRC1physical
21555454
CCNL2_HUMANCCNL2physical
21555454
CLK4_HUMANCLK4physical
21555454
CDCA2_HUMANCDCA2physical
21555454
NSRP1_HUMANNSRP1physical
21555454
PHRF1_HUMANPHRF1physical
21555454
PR38A_HUMANPRPF38Aphysical
21555454
LC7L2_HUMANLUC7L2physical
21555454
MFAP1_HUMANMFAP1physical
21555454
PR40A_HUMANPRPF40Aphysical
21555454
RBM23_HUMANRBM23physical
21555454
RBM25_HUMANRBM25physical
21555454
SFSWA_HUMANSFSWAPphysical
21555454
RSRC2_HUMANRSRC2physical
21555454
ACPH_HUMANAPEHphysical
22863883
INT13_HUMANASUNphysical
22863883
CAND1_HUMANCAND1physical
22863883
SYCC_HUMANCARSphysical
22863883
HSP74_HUMANHSPA4physical
22863883
SYK_HUMANKARSphysical
22863883
PPM1G_HUMANPPM1Gphysical
22863883
2A5G_HUMANPPP2R5Cphysical
22863883
RNBP6_HUMANRANBP6physical
22863883
GLYM_HUMANSHMT2physical
22863883
SWP70_HUMANSWAP70physical
22863883
RO60_HUMANTROVE2physical
22863883
UBC9_HUMANUBE2Iphysical
22863883
NAA50_HUMANNAA50physical
25416956
FRMD6_HUMANFRMD6physical
25416956
SSRP1_HUMANSSRP1physical
26344197
PHRF1_HUMANPHRF1physical
28514442
DDX46_HUMANDDX46physical
28514442
SFSWA_HUMANSFSWAPphysical
28514442
SREK1_HUMANSREK1physical
28514442
PR38B_HUMANPRPF38Bphysical
28514442
RSRC2_HUMANRSRC2physical
28514442
PAXB1_HUMANPAXBP1physical
28514442
CCNL2_HUMANCCNL2physical
28514442
PR38A_HUMANPRPF38Aphysical
28514442
PPIL4_HUMANPPIL4physical
28514442
NSRP1_HUMANNSRP1physical
28514442
RBM23_HUMANRBM23physical
28514442
TFP11_HUMANTFIP11physical
28514442
CLK4_HUMANCLK4physical
28514442
RBM25_HUMANRBM25physical
28514442
CDCA2_HUMANCDCA2physical
28514442
CD11B_HUMANCDK11Bphysical
28514442
ARGL1_HUMANARGLU1physical
28514442
CPSF6_HUMANCPSF6physical
28514442
IKBL1_HUMANNFKBIL1physical
28514442
CPSF7_HUMANCPSF7physical
28514442
CATIN_HUMANCACTINphysical
28514442
SCAFB_HUMANSCAF11physical
28514442
SRS11_HUMANSRSF11physical
28514442
CPSF4_HUMANCPSF4physical
28514442
UBP42_HUMANUSP42physical
28514442
ZMYM1_HUMANZMYM1physical
28514442
U2AF2_HUMANU2AF2physical
28514442
DHX40_HUMANDHX40physical
28514442
SFR15_HUMANSCAF4physical
28514442
RBM26_HUMANRBM26physical
28514442
ZC3H4_HUMANZC3H4physical
28514442
PRP16_HUMANDHX38physical
28514442
SFR19_HUMANSCAF1physical
28514442
RBM40_HUMANRNPC3physical
28514442
CCNL1_HUMANCCNL1physical
28514442
WDR33_HUMANWDR33physical
28514442
BRD4_HUMANBRD4physical
28514442
PPIG_HUMANPPIGphysical
28514442
SCAF8_HUMANSCAF8physical
28514442
WDR48_HUMANWDR48physical
28514442
LC7L3_HUMANLUC7L3physical
28514442
UAP1_HUMANUAP1physical
28514442
T2FA_HUMANGTF2F1physical
28514442
CHERP_HUMANCHERPphysical
28514442
RBM27_HUMANRBM27physical
28514442
TAF7_HUMANTAF7physical
28514442
DIDO1_HUMANDIDO1physical
28514442
RBM39_HUMANRBM39physical
28514442
ZNF24_HUMANZNF24physical
28514442
CPSF5_HUMANNUDT21physical
28514442
HBS1L_HUMANHBS1Lphysical
28514442
RABL6_HUMANRABL6physical
28514442
RN138_HUMANRNF138physical
28514442
PUF60_HUMANPUF60physical
28514442
RBMX2_HUMANRBMX2physical
28514442
SR140_HUMANU2SURPphysical
28514442
DKC1_HUMANDKC1physical
28514442
RS7_HUMANRPS7physical
28514442
CAAP1_HUMANCAAP1physical
28514442
SETD2_HUMANSETD2physical
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 JMJD6_HUMAN

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Related Literatures of Post-Translational Modification

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