WDR48_HUMAN - dbPTM
WDR48_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR48_HUMAN
UniProt AC Q8TAF3
Protein Name WD repeat-containing protein 48
Gene Name WDR48
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus . Cytoplasm . Lysosome . Late endosome . Mainly in cytoplasmic compartments (PubMed:12196293, PubMed:18032488). In case of infection by papillomavirus HPV11, translocates to the nucleus via its interaction with papillomavirus HPV11 (PubMed:18
Protein Description Regulator of deubiquitinating complexes. Acts as a strong activator of USP1 and USP46. [PubMed: 18082604]
Protein Sequence MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVNPMDEEENEVNHVNGEQENRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST
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
20 (in isoform 2)Ubiquitination-1.9421890473
24 (in isoform 4)Ubiquitination-42.6021890473
28PhosphorylationIRDEVEKYNRNGVNA
EHHHHHHHCCCCCCH
13.07-
39AcetylationGVNALQLDPALNRLF
CCCHHHCCHHHHHHH
17.2919608861
52PhosphorylationLFTAGRDSIIRIWSV
HHHCCCCCEEEEEEC
20.6724719451
63UbiquitinationIWSVNQHKQDPYIAS
EEECCCCCCCCCEEE
46.78-
63 (in isoform 2)Ubiquitination-46.7821890473
97 (in isoform 3)Ubiquitination-35.1221890473
106 (in isoform 1)Ubiquitination-51.8021890473
106AcetylationVKVWNAHKGFCMSTL
EEEEECCCCCCHHHH
51.8026051181
106UbiquitinationVKVWNAHKGFCMSTL
EEEEECCCCCCHHHH
51.8021890473
112AcetylationHKGFCMSTLRTHKDY
CCCCCHHHHHHCHHH
8.0619608861
121AcetylationRTHKDYVKALAYAKD
HHCHHHHHHHHHHCC
31.3019608861
129UbiquitinationALAYAKDKELVASAG
HHHHHCCHHHHHHCC
52.84-
132AcetylationYAKDKELVASAGLDR
HHCCHHHHHHCCCCC
4.0819608861
172PhosphorylationSGNKDSIYSLAMNQL
CCCHHHHHHHHHHCC
11.1128857561
173PhosphorylationGNKDSIYSLAMNQLG
CCHHHHHHHHHHCCC
14.1628857561
185PhosphorylationQLGTIIVSGSTEKVL
CCCEEEEECCCCCEE
19.3328857561
187PhosphorylationGTIIVSGSTEKVLRV
CEEEEECCCCCEEEE
26.3628857561
188PhosphorylationTIIVSGSTEKVLRVW
EEEEECCCCCEEEEE
43.2728857561
205AcetylationRTCAKLMKLKGHTDN
HHHHHHHHHCCCCCC
58.4419608861
207UbiquitinationCAKLMKLKGHTDNVK
HHHHHHHCCCCCCCE
43.03-
214AcetylationKGHTDNVKALLLNRD
CCCCCCCEEEEECCC
39.3019608861
214UbiquitinationKGHTDNVKALLLNRD
CCCCCCCEEEEECCC
39.30-
223PhosphorylationLLLNRDGTQCLSGSS
EEECCCCCCCCCCCC
22.0130257219
227PhosphorylationRDGTQCLSGSSDGTI
CCCCCCCCCCCCCEE
44.2324732914
229PhosphorylationGTQCLSGSSDGTIRL
CCCCCCCCCCCEEEE
23.1424732914
230PhosphorylationTQCLSGSSDGTIRLW
CCCCCCCCCCEEEEE
43.5124732914
233PhosphorylationLSGSSDGTIRLWSLG
CCCCCCCEEEEEEEC
14.1224732914
245 (in isoform 4)Ubiquitination-3.3221890473
275UbiquitinationYSGGRDRKIYCTDLR
EECCCCCEEEEECCC
42.17-
277PhosphorylationGGRDRKIYCTDLRNP
CCCCCEEEEECCCCC
7.7329496907
294AcetylationRVLICEEKAPVLKME
EEEEECCCCCEEEEE
35.3826051181
294UbiquitinationRVLICEEKAPVLKME
EEEEECCCCCEEEEE
35.38-
299UbiquitinationEEKAPVLKMELDRSA
CCCCCEEEEECCCCC
30.48-
305PhosphorylationLKMELDRSADPPPAI
EEEECCCCCCCCCEE
36.37-
308 (in isoform 5)Ubiquitination-36.1721890473
318 (in isoform 3)Ubiquitination-39.5121890473
318UbiquitinationAIWVATTKSTVNKWT
EEEEEECCHHHCCEE
39.51-
323AcetylationTTKSTVNKWTLKGIH
ECCHHHCCEECCEEE
36.9025953088
325PhosphorylationKSTVNKWTLKGIHNF
CHHHCCEECCEEECC
21.8728961369
327 (in isoform 1)Ubiquitination-48.7421890473
327UbiquitinationTVNKWTLKGIHNFRA
HHCCEECCEEECCCC
48.7421890473
335PhosphorylationGIHNFRASGDYDNDC
EEECCCCCCCCCCCC
28.1323401153
338PhosphorylationNFRASGDYDNDCTNP
CCCCCCCCCCCCCCC
21.8530278072
343PhosphorylationGDYDNDCTNPITPLC
CCCCCCCCCCCCCCC
47.0630278072
347PhosphorylationNDCTNPITPLCTQPD
CCCCCCCCCCCCCCC
16.0923927012
351PhosphorylationNPITPLCTQPDQVIK
CCCCCCCCCCCCEEE
51.3123927012
358UbiquitinationTQPDQVIKGGASIIQ
CCCCCEEECCCCEEE
53.05-
372UbiquitinationQCHILNDKRHILTKD
EEEECCCCCCEEEEC
44.81-
377PhosphorylationNDKRHILTKDTNNNV
CCCCCEEEECCCCCE
26.69-
378UbiquitinationDKRHILTKDTNNNVA
CCCCEEEECCCCCEE
60.14-
386PhosphorylationDTNNNVAYWDVLKAC
CCCCCEEHHHHHHHC
9.6225147952
391UbiquitinationVAYWDVLKACKVEDL
EEHHHHHHHCCCHHH
52.14-
400UbiquitinationCKVEDLGKVDFEDEI
CCCHHHCCCCCHHHH
46.02-
408UbiquitinationVDFEDEIKKRFKMVY
CCCHHHHHHHCEEEE
35.53-
451PhosphorylationSAKDAGFSSPDGSDP
EHHHCCCCCCCCCCC
39.79-
452PhosphorylationAKDAGFSSPDGSDPK
HHHCCCCCCCCCCCC
25.42-
456PhosphorylationGFSSPDGSDPKLNLG
CCCCCCCCCCCCCHH
59.11-
496 (in isoform 4)Ubiquitination-55.4521890473
496AcetylationVNHVNGEQENRVQKG
CCCCCHHHCCCEECC
55.4519608861
564AcetylationKNMPKFNKIPFYLQP
CCCCCCCCCCEEECC
55.6925953088
568PhosphorylationKFNKIPFYLQPHASS
CCCCCCEEECCCCCC
10.0828152594
569 (in isoform 3)Ubiquitination-6.9921890473
569AcetylationFNKIPFYLQPHASSG
CCCCCEEECCCCCCC
6.9919608861
574PhosphorylationFYLQPHASSGAKTLK
EEECCCCCCCCCCCC
26.6925627689
575PhosphorylationYLQPHASSGAKTLKK
EECCCCCCCCCCCCC
43.4825159151
578UbiquitinationPHASSGAKTLKKDRL
CCCCCCCCCCCCCCC
58.8921890473
578 (in isoform 1)Ubiquitination-58.8921890473
578AcetylationPHASSGAKTLKKDRL
CCCCCCCCCCCCCCC
58.8923954790
586PhosphorylationTLKKDRLSASDMLQV
CCCCCCCCHHHHHHH
26.9830108239
588PhosphorylationKKDRLSASDMLQVRK
CCCCCCHHHHHHHHH
21.8520860994
611PhosphorylationIINLDNESQTTSSSN
HHCCCCCCCCCCCCC
38.8025159151
613PhosphorylationNLDNESQTTSSSNNE
CCCCCCCCCCCCCCC
37.6127373336
614PhosphorylationLDNESQTTSSSNNEK
CCCCCCCCCCCCCCC
20.9725850435
615PhosphorylationDNESQTTSSSNNEKP
CCCCCCCCCCCCCCC
34.8525850435
616PhosphorylationNESQTTSSSNNEKPG
CCCCCCCCCCCCCCC
34.6929514088
617PhosphorylationESQTTSSSNNEKPGE
CCCCCCCCCCCCCCC
43.3627050516
621 (in isoform 1)Ubiquitination-61.5221890473
621UbiquitinationTSSSNNEKPGEQEKE
CCCCCCCCCCCHHHH
61.522190698
663AcetylationTVKHFIWKSGGDLTL
HHEEEHHHCCCCEEE
34.1126051181
664PhosphorylationVKHFIWKSGGDLTLH
HEEEHHHCCCCEEEE
32.7724719451
672PhosphorylationGGDLTLHYRQKST--
CCCEEEEEEECCC--
20.1824719451

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 WDR48_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR48_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 WDR48_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCR_HUMANBCRphysical
19615732
BRCA1_HUMANBRCA1physical
19615732
CSK21_HUMANCSNK2A1physical
19615732
CSK22_HUMANCSNK2A2physical
19615732
CSK2B_HUMANCSNK2Bphysical
19615732
CTND1_HUMANCTNND1physical
19615732
DKC1_HUMANDKC1physical
19615732
DMWD_HUMANDMWDphysical
19615732
RPB7_HUMANPOLR2Gphysical
19615732
RPB9_HUMANPOLR2Iphysical
19615732
PPIB_HUMANPPIBphysical
19615732
SET_HUMANSETphysical
19615732
STK11_HUMANSTK11physical
19615732
SPT6H_HUMANSUPT6Hphysical
19615732
TARB1_HUMANTARBP1physical
19615732
TCOF_HUMANTCOF1physical
19615732
P53_HUMANTP53physical
19615732
UBP1_HUMANUSP1physical
19615732
WRN_HUMANWRNphysical
19615732
NELFE_HUMANNELFEphysical
19615732
CUL4B_HUMANCUL4Bphysical
19615732
EIF3A_HUMANEIF3Aphysical
19615732
EIF3F_HUMANEIF3Fphysical
19615732
EIF3H_HUMANEIF3Hphysical
19615732
ARHGA_HUMANARHGEF10physical
19615732
KDM4A_HUMANKDM4Aphysical
19615732
KAISO_HUMANZBTB33physical
19615732
PSME3_HUMANPSME3physical
19615732
CRTAP_HUMANCRTAPphysical
19615732
UN13B_HUMANUNC13Bphysical
19615732
R51A1_HUMANRAD51AP1physical
19615732
SAHH2_HUMANAHCYL1physical
19615732
SMAP_HUMANC11orf58physical
19615732
GPN1_HUMANGPN1physical
19615732
PHLP2_HUMANPHLPP2physical
19615732
MYCB2_HUMANMYCBP2physical
19615732
PHLP1_HUMANPHLPP1physical
19615732
BOP1_HUMANBOP1physical
19615732
SAHH3_HUMANAHCYL2physical
19615732
AP3M1_HUMANAP3M1physical
19615732
GPN3_HUMANGPN3physical
19615732
ZN639_HUMANZNF639physical
19615732
UBR5_HUMANUBR5physical
19615732
WDR70_HUMANWDR70physical
19615732
SHQ1_HUMANSHQ1physical
19615732
NOP10_HUMANNOP10physical
19615732
NEB1_HUMANPPP1R9Aphysical
19615732
NHP2_HUMANNHP2physical
19615732
IWS1_HUMANIWS1physical
19615732
YLPM1_HUMANYLPM1physical
19615732
ZBTB2_HUMANZBTB2physical
19615732
TRM11_HUMANTRMT11physical
19615732
P3H1_HUMANP3H1physical
19615732
NEB2_HUMANPPP1R9Bphysical
19615732
WDR20_HUMANWDR20physical
19615732
NAF1_HUMANNAF1physical
19615732
F122B_HUMANFAM122Bphysical
19615732
UBP12_HUMANUSP12physical
19615732
UBP46_HUMANUSP46physical
19615732
WDR20_HUMANWDR20physical
20147737
UBP1_HUMANUSP1physical
18082604
PCNA_HUMANPCNAphysical
18082604
FANCI_HUMANFANCIphysical
21896657
ATAD5_HUMANATAD5physical
21896657
UBP1_HUMANUSP1physical
22701671
UBP1_HUMANUSP1physical
19075014
UBP12_HUMANUSP12physical
19075014
UBP46_HUMANUSP46physical
19075014
UBP1_HUMANUSP1physical
24850727
UBP12_HUMANUSP12physical
24850727
UBP46_HUMANUSP46physical
24850727
BASP1_HUMANBASP1physical
26344197
SYYC_HUMANYARSphysical
26344197
UBP46_HUMANUSP46physical
26388029
UBC_HUMANUBCphysical
26388029
UBP1_HUMANUSP1physical
27463890
UBP12_HUMANUSP12physical
27463890
UBP46_HUMANUSP46physical
27463890
PHLP1_HUMANPHLPP1physical
27463890
PHLP2_HUMANPHLPP2physical
27463890
WDR20_HUMANWDR20physical
27463890
R51A1_HUMANRAD51AP1physical
27463890
UBP12_HUMANUSP12physical
27373336
USH1C_HUMANUSH1Cphysical
27173435
R51A1_HUMANRAD51AP1physical
27239033
RAD51_HUMANRAD51physical
27239033
UBP1_HUMANUSP1physical
27239033
ATAD5_HUMANATAD5physical
27239033
FANCI_HUMANFANCIphysical
27239033
PHLP1_HUMANPHLPP1physical
24145035
UBP12_HUMANUSP12physical
24145035

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 WDR48_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121; LYS-214 AND LYS-578,AND MASS SPECTROMETRY.

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