WDR12_HUMAN - dbPTM
WDR12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR12_HUMAN
UniProt AC Q9GZL7
Protein Name Ribosome biogenesis protein WDR12 {ECO:0000255|HAMAP-Rule:MF_03029}
Gene Name WDR12 {ECO:0000255|HAMAP-Rule:MF_03029}
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm .
Protein Description Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome..
Protein Sequence MAQLQTRFYTDNKKYAVDDVPFSIPAASEIADLSNIINKLLKDKNEFHKHVEFDFLIKGQFLRMPLDKHMEMENISSEEVVEIEYVEKYTAPQPEQCMFHDDWISSIKGAEEWILTGSYDKTSRIWSLEGKSIMTIVGHTDVVKDVAWVKKDSLSCLLLSASMDQTILLWEWNVERNKVKALHCCRGHAGSVDSIAVDGSGTKFCSGSWDKMLKIWSTVPTDEEDEMEESTNRPRKKQKTEQLGLTRTPIVTLSGHMEAVSSVLWSDAEEICSASWDHTIRVWDVESGSLKSTLTGNKVFNCISYSPLCKRLASGSTDRHIRLWDPRTKDGSLVSLSLTSHTGWVTSVKWSPTHEQQLISGSLDNIVKLWDTRSCKAPLYDLAAHEDKVLSVDWTDTGLLLSGGADNKLYSYRYSPTTSHVGA
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------MAQLQTRFY
------CCCCCCEEE		20.8419413330
132-HydroxyisobutyrylationTRFYTDNKKYAVDDV
CEEECCCCCEECCCC		50.39-
14UbiquitinationRFYTDNKKYAVDDVP
EEECCCCCEECCCCC		44.70-
15PhosphorylationFYTDNKKYAVDDVPF
EECCCCCEECCCCCC		17.2924275569
23PhosphorylationAVDDVPFSIPAASEI
ECCCCCCCCCCHHHH		22.9224275569
63MethylationLIKGQFLRMPLDKHM
EECCEEECCCCHHHC		26.43115919921
121UbiquitinationILTGSYDKTSRIWSL
EEEEECCCCCCEEEE		39.92-
121AcetylationILTGSYDKTSRIWSL
EEEEECCCCCCEEEE		39.9226051181
131UbiquitinationRIWSLEGKSIMTIVG
CEEEECCCEEEEEEC		27.68-
150AcetylationVKDVAWVKKDSLSCL
HCCHHHHCCCCHHHH		39.9126051181
180UbiquitinationNVERNKVKALHCCRG
ECCCCCCEEEEECCC		47.00-
191PhosphorylationCCRGHAGSVDSIAVD
ECCCCCCCCCEEEEC		24.4330624053
203UbiquitinationAVDGSGTKFCSGSWD
EECCCCCCCCCCCHH		48.1521890473
203AcetylationAVDGSGTKFCSGSWD
EECCCCCCCCCCCHH		48.1526051181
211AcetylationFCSGSWDKMLKIWST
CCCCCHHHHHHHEEE		39.6126051181
2112-HydroxyisobutyrylationFCSGSWDKMLKIWST
CCCCCHHHHHHHEEE		39.61-
211UbiquitinationFCSGSWDKMLKIWST
CCCCCHHHHHHHEEE		39.61-
211MethylationFCSGSWDKMLKIWST
CCCCCHHHHHHHEEE		39.61115978705
217PhosphorylationDKMLKIWSTVPTDEE
HHHHHHEEECCCCCH		24.0130266825
218PhosphorylationKMLKIWSTVPTDEED
HHHHHEEECCCCCHH		18.6030266825
221PhosphorylationKIWSTVPTDEEDEME
HHEEECCCCCHHHHH		52.2730266825
230PhosphorylationEEDEMEESTNRPRKK
CHHHHHHHCCCCCHH		20.0628450419
231PhosphorylationEDEMEESTNRPRKKQ
HHHHHHHCCCCCHHH		38.2330108239
239AcetylationNRPRKKQKTEQLGLT
CCCCHHHHHHHCCCC		64.0126051181
239UbiquitinationNRPRKKQKTEQLGLT
CCCCHHHHHHHCCCC		64.01-
239SumoylationNRPRKKQKTEQLGLT
CCCCHHHHHHHCCCC		64.0125114211
246PhosphorylationKTEQLGLTRTPIVTL
HHHHCCCCCCCEEEE		30.6025262027
254PhosphorylationRTPIVTLSGHMEAVS
CCCEEEECCCHHHHH		19.79-
291UbiquitinationDVESGSLKSTLTGNK
EECCCCEEEEECCCC		42.99-
298AcetylationKSTLTGNKVFNCISY
EEEECCCCEEEEEEC		49.9326051181
304PhosphorylationNKVFNCISYSPLCKR
CCEEEEEECCHHHHH		23.0428152594
305PhosphorylationKVFNCISYSPLCKRL
CEEEEEECCHHHHHH		8.3928152594
306PhosphorylationVFNCISYSPLCKRLA
EEEEEECCHHHHHHH		12.4728152594
310UbiquitinationISYSPLCKRLASGST
EECCHHHHHHHCCCC		59.12-
3102-HydroxyisobutyrylationISYSPLCKRLASGST
EECCHHHHHHHCCCC		59.12-
319MethylationLASGSTDRHIRLWDP
HHCCCCCCCEEEECC		27.50115919917
328PhosphorylationIRLWDPRTKDGSLVS
EEEECCCCCCCCEEE		38.5824719451
337PhosphorylationDGSLVSLSLTSHTGW
CCCEEEEEEECCCCC		23.3024719451
340PhosphorylationLVSLSLTSHTGWVTS
EEEEEEECCCCCEEE		25.0924719451
3762-HydroxyisobutyrylationLWDTRSCKAPLYDLA
HHCCCCCCCCHHHHH		55.04-
376AcetylationLWDTRSCKAPLYDLA
HHCCCCCCCCHHHHH		55.0425953088
376UbiquitinationLWDTRSCKAPLYDLA
HHCCCCCCCCHHHHH		55.04-
380PhosphorylationRSCKAPLYDLAAHED
CCCCCCHHHHHCCCC		14.0925954137
388UbiquitinationDLAAHEDKVLSVDWT
HHHCCCCCEEEEECC		41.93-
391PhosphorylationAHEDKVLSVDWTDTG
CCCCCEEEEECCCCC		22.4825954137
397PhosphorylationLSVDWTDTGLLLSGG
EEEECCCCCEEEECC		23.5025954137
411PhosphorylationGADNKLYSYRYSPTT
CCCCCEEEEEECCCC		17.3624719451
412PhosphorylationADNKLYSYRYSPTTS
CCCCEEEEEECCCCC		10.4623090842
414PhosphorylationNKLYSYRYSPTTSHV
CCEEEEEECCCCCCC		15.6928152594
415PhosphorylationKLYSYRYSPTTSHVG
CEEEEEECCCCCCCC		13.5328152594
417PhosphorylationYSYRYSPTTSHVGA-
EEEEECCCCCCCCC-		34.6830108239
418PhosphorylationSYRYSPTTSHVGA--
EEEECCCCCCCCC--		21.8830108239
419PhosphorylationYRYSPTTSHVGA---
EEECCCCCCCCC---		20.7530108239
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 WDR12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR12_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 WDR12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR5_HUMANWDR5physical
17041588
BOP1_HUMANBOP1physical
16738141
PESC_HUMANPES1physical
16738141
PESC_HUMANPES1physical
17353269
XPO1_HUMANXPO1physical
22939629
PESC_HUMANPES1physical
16043514
BOP1_HUMANBOP1physical
16043514
WDR12_HUMANWDR12physical
16043514
PP2AB_HUMANPPP2CBphysical
22863883
PP2BB_HUMANPPP3CBphysical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SNF8_HUMANSNF8physical
22863883
SRSF5_HUMANSRSF5physical
22863883
TOM1_HUMANTOM1physical
22863883
TSN_HUMANTSNphysical
22863883
BRX1_HUMANBRIX1physical
26344197
CHMP7_HUMANCHMP7physical
26344197
DD19A_HUMANDDX19Aphysical
26344197
DDX54_HUMANDDX54physical
26344197
EBP2_HUMANEBNA1BP2physical
26344197
SPB1_HUMANFTSJ3physical
26344197
NOG1_HUMANGTPBP4physical
26344197
HNRDL_HUMANHNRNPDLphysical
26344197
NOC3L_HUMANNOC3Lphysical
26344197
TRUA_HUMANPUS1physical
26344197
RL4_HUMANRPL4physical
26344197
EFTU_HUMANTUFMphysical
26344197
DDX27_HUMANDDX27physical
25825154
BOP1_HUMANBOP1physical
25825154
PESC_HUMANPES1physical
25825154
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 WDR12_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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