WDR83_HUMAN - dbPTM
WDR83_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR83_HUMAN
UniProt AC Q9BRX9
Protein Name WD repeat domain-containing protein 83
Gene Name WDR83
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic. Partially nuclear..
Protein Description Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. Also involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). May also be involved in pre-mRNA splicing..
Protein Sequence MAFPEPKPRPPELPQKRLKTLDCGQGAVRAVRFNVDGNYCLTCGSDKTLKLWNPLRGTLLRTYSGHGYEVLDAAGSFDNSSLCSGGGDKAVVLWDVASGQVVRKFRGHAGKVNTVQFNEEATVILSGSIDSSIRCWDCRSRRPEPVQTLDEARDGVSSVKVSDHEILAGSVDGRVRRYDLRMGQLFSDYVGSPITCTCFSRDGQCTLVSSLDSTLRLLDKDTGELLGEYKGHKNQEYKLDCCLSERDTHVVSCSEDGKVFFWDLVEGALALALPVGSGVVQSLAYHPTEPCLLTAMGGSVQCWREEAYEAEDGAG
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
16UbiquitinationRPPELPQKRLKTLDC
CCCCCCHHHCCEECC
58.7329967540
19UbiquitinationELPQKRLKTLDCGQG
CCCHHHCCEECCCCC
51.5822505724
39PhosphorylationRFNVDGNYCLTCGSD
EEEECCCEEEEECCC
8.3827642862
47UbiquitinationCLTCGSDKTLKLWNP
EEEECCCCEEECCCC
58.4129967540
50UbiquitinationCGSDKTLKLWNPLRG
ECCCCEEECCCCCCC
57.6029967540
160UbiquitinationRDGVSSVKVSDHEIL
CCCCCEEEECCCEEE
37.66-
206PhosphorylationFSRDGQCTLVSSLDS
ECCCCEEEEEECHHH
23.4726074081
209PhosphorylationDGQCTLVSSLDSTLR
CCEEEEEECHHHHEE
28.4426074081
210PhosphorylationGQCTLVSSLDSTLRL
CEEEEEECHHHHEEE
28.8126074081
213PhosphorylationTLVSSLDSTLRLLDK
EEEECHHHHEEEECC
34.3326074081
214PhosphorylationLVSSLDSTLRLLDKD
EEECHHHHEEEECCC
18.6326074081
220UbiquitinationSTLRLLDKDTGELLG
HHEEEECCCHHHHCC
58.1029967540
222PhosphorylationLRLLDKDTGELLGEY
EEEECCCHHHHCCCC
37.9926074081
230UbiquitinationGELLGEYKGHKNQEY
HHHCCCCCCCCCCEE
50.6829967540
233UbiquitinationLGEYKGHKNQEYKLD
CCCCCCCCCCEEEEE
69.83-
238UbiquitinationGHKNQEYKLDCCLSE
CCCCCEEEEEEECCC
36.7829967540
244PhosphorylationYKLDCCLSERDTHVV
EEEEEECCCCCCEEE
19.3730631047

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 WDR83_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR83_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 WDR83_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LTOR3_HUMANLAMTOR3physical
15118098
RU1C_HUMANSNRPCphysical
22365833
SF3B4_HUMANSF3B4physical
22365833
SF01_HUMANSF1physical
22365833
PRP8_HUMANPRPF8physical
22365833
LSM3_HUMANLSM3physical
22365833
PPIL1_HUMANPPIL1physical
22365833
AQR_HUMANAQRphysical
22365833
HSPB1_HUMANHSPB1physical
22365833
UBL5_HUMANUBL5physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
PCBP2_HUMANPCBP2physical
22365833
BAG2_HUMANBAG2physical
22365833
TOE1_HUMANTOE1physical
22365833
GPKOW_HUMANGPKOWphysical
22365833
RACK1_HUMANGNB2L1physical
22365833
KDM1A_HUMANKDM1Aphysical
23455924
PAR6B_HUMANPARD6Bphysical
23439680
CRUM3_HUMANCRB3physical
23439680
TCPH_HUMANCCT7physical
26186194
UBB_HUMANUBBphysical
26186194
K1671_HUMANKIAA1671physical
26186194
NUMA1_HUMANNUMA1physical
26186194
TCPG_HUMANCCT3physical
26186194
RB15B_HUMANRBM15Bphysical
26186194
C19L2_HUMANCWF19L2physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPB_HUMANCCT2physical
26186194
TCPQ_HUMANCCT8physical
26186194
SYF1_HUMANXAB2physical
26186194
GPTC1_HUMANGPATCH1physical
26186194
TCPD_HUMANCCT4physical
26186194
DHX35_HUMANDHX35physical
26186194
CRNL1_HUMANCRNKL1physical
26186194
CUX1_HUMANCUX1physical
26186194
CASP_HUMANCUX1physical
26186194
NEK1_HUMANNEK1physical
26186194
CDC5L_HUMANCDC5Lphysical
26186194
TCPA_HUMANTCP1physical
26186194
FYV1_HUMANPIKFYVEphysical
26186194
DPYL2_HUMANDPYSL2physical
26186194
IF4E2_HUMANEIF4E2physical
26186194
IASPP_HUMANPPP1R13Lphysical
26186194
SGO2_HUMANSGOL2physical
26186194
SNW1_HUMANSNW1physical
26186194
GGYF2_HUMANGIGYF2physical
26186194
ZHX1_HUMANZHX1physical
26186194
DCA13_HUMANDCAF13physical
26186194
SLIRP_HUMANSLIRPphysical
26186194
PSMG2_HUMANPSMG2physical
26186194
ARHG2_HUMANARHGEF2physical
26186194
AAKG2_HUMANPRKAG2physical
26186194
EXO1_HUMANEXO1physical
26186194
ISY1_HUMANISY1physical
26186194
PRP17_HUMANCDC40physical
26186194
AQR_HUMANAQRphysical
26186194
KCTD3_HUMANKCTD3physical
26186194
SHKB1_HUMANSHKBP1physical
26186194
RN187_HUMANRNF187physical
26186194
SYF2_HUMANSYF2physical
26186194
SI1L1_HUMANSIPA1L1physical
26186194
RIMS4_HUMANRIMS4physical
26186194
SI1L3_HUMANSIPA1L3physical
26186194
FRM4A_HUMANFRMD4Aphysical
26186194
F122B_HUMANFAM122Bphysical
26186194
ZN140_HUMANZNF140physical
26186194
MPRIP_HUMANMPRIPphysical
26186194
SH2B2_HUMANSH2B2physical
26186194
CCD12_HUMANCCDC12physical
26186194
GPSM1_HUMANGPSM1physical
26186194
ARHGH_HUMANARHGEF17physical
26186194
CYH3_HUMANCYTH3physical
26186194
BUD31_HUMANBUD31physical
26186194
ARHG8_HUMANNET1physical
26186194
ZHX1_HUMANZHX1physical
28514442
SI1L3_HUMANSIPA1L3physical
28514442
DCA13_HUMANDCAF13physical
28514442
K1671_HUMANKIAA1671physical
28514442
GPTC1_HUMANGPATCH1physical
28514442
SH2B2_HUMANSH2B2physical
28514442
GPSM1_HUMANGPSM1physical
28514442
SGO2_HUMANSGOL2physical
28514442
RB15B_HUMANRBM15Bphysical
28514442
DHX35_HUMANDHX35physical
28514442
KCTD3_HUMANKCTD3physical
28514442
RN187_HUMANRNF187physical
28514442
IASPP_HUMANPPP1R13Lphysical
28514442
PRP19_HUMANPRPF19physical
28514442
F122B_HUMANFAM122Bphysical
28514442
RIMS4_HUMANRIMS4physical
28514442
SHKB1_HUMANSHKBP1physical
28514442
ZN140_HUMANZNF140physical
28514442
ARHG2_HUMANARHGEF2physical
28514442
FYV1_HUMANPIKFYVEphysical
28514442
C19L2_HUMANCWF19L2physical
28514442
NEK1_HUMANNEK1physical
28514442
AAKG2_HUMANPRKAG2physical
28514442
SI1L1_HUMANSIPA1L1physical
28514442
GGYF1_HUMANGIGYF1physical
28514442
NUMA1_HUMANNUMA1physical
28514442
SYF1_HUMANXAB2physical
28514442
FRM4A_HUMANFRMD4Aphysical
28514442
EXO1_HUMANEXO1physical
28514442
PRP17_HUMANCDC40physical
28514442
ISY1_HUMANISY1physical
28514442
AQR_HUMANAQRphysical
28514442
DPYL2_HUMANDPYSL2physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
ARHG8_HUMANNET1physical
28514442
MPRIP_HUMANMPRIPphysical
28514442
CRNL1_HUMANCRNKL1physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPH_HUMANCCT7physical
28514442
BUD31_HUMANBUD31physical
28514442
PSMG2_HUMANPSMG2physical
28514442
CCD12_HUMANCCDC12physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPW_HUMANCCT6Bphysical
28514442
DACH1_HUMANDACH1physical
28514442
CUX1_HUMANCUX1physical
28514442
CASP_HUMANCUX1physical
28514442
TCPA_HUMANTCP1physical
28514442
SNW1_HUMANSNW1physical
28514442
TCPG_HUMANCCT3physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
UBB_HUMANUBBphysical
28514442
ARHGH_HUMANARHGEF17physical
28514442
GGYF2_HUMANGIGYF2physical
28514442
TCPE_HUMANCCT5physical
28514442
XRP2_HUMANRP2physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR83_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP