WDR61_HUMAN - dbPTM
WDR61_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR61_HUMAN
UniProt AC Q9GZS3
Protein Name WD repeat-containing protein 61
Gene Name WDR61
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C..
Protein Sequence MTNQYGILFKQEQAHDDAIWSVAWGTNKKENSETVVTGSLDDLVKVWKWRDERLDLQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQIKSIDAGPVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYDCPI
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
1Acetylation-------MTNQYGIL
-------CCCCCEEE
7.7722223895
2Acetylation------MTNQYGILF
------CCCCCEEEE
30.9122223895
2Phosphorylation------MTNQYGILF
------CCCCCEEEE
30.9120068231
5Phosphorylation---MTNQYGILFKQE
---CCCCCEEEEECC
14.2720068231
10SumoylationNQYGILFKQEQAHDD
CCCEEEEECCCCCCC
49.86-
28UbiquitinationSVAWGTNKKENSETV
EEEECCCCCCCCEEE
62.39-
29UbiquitinationVAWGTNKKENSETVV
EEECCCCCCCCEEEE
65.2821906983
32PhosphorylationGTNKKENSETVVTGS
CCCCCCCCEEEEEEC
35.4221406692
34PhosphorylationNKKENSETVVTGSLD
CCCCCCEEEEEECHH
21.7921406692
37PhosphorylationENSETVVTGSLDDLV
CCCEEEEEECHHHHH
19.4021406692
39PhosphorylationSETVVTGSLDDLVKV
CEEEEEECHHHHHHH
21.1821406692
45UbiquitinationGSLDDLVKVWKWRDE
ECHHHHHHHEEECCC
50.07-
97UbiquitinationLWDLENGKQIKSIDA
EEECCCCCEEEEECC
61.5021906983
100UbiquitinationLENGKQIKSIDAGPV
CCCCCEEEEECCCCC
38.57-
139AcetylationIFGVESGKKEYSLDT
EEEECCCCEEEEECC
52.2725953088
139UbiquitinationIFGVESGKKEYSLDT
EEEECCCCEEEEECC
52.2721906983
140UbiquitinationFGVESGKKEYSLDTR
EEECCCCEEEEECCC
66.46-
1402-HydroxyisobutyrylationFGVESGKKEYSLDTR
EEECCCCEEEEECCC
66.46-
146PhosphorylationKKEYSLDTRGKFILS
CEEEEECCCCCEEEE
46.7620068231
157PhosphorylationFILSIAYSPDGKYLA
EEEEEEECCCCCEEC
13.9026091039
257UbiquitinationSSSDKSVKVWDVGTR
CCCCCCEEEEECCCC
44.70-
257AcetylationSSSDKSVKVWDVGTR
CCCCCCEEEEECCCC
44.7025953088
301PhosphorylationDDQEIHIYDCPI---
CCCEEEEEECCC---
9.4218083107

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 WDR61_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR61_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 WDR61_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR5_HUMANWDR5physical
17041588
CTR9_HUMANCTR9physical
22451921
LEO1_HUMANLEO1physical
22451921
PAF1_HUMANPAF1physical
22451921
CDC73_HUMANCDC73physical
22451921
HXK1_HUMANHK1physical
22863883
HXK2_HUMANHK2physical
22863883
PLCG1_HUMANPLCG1physical
22863883
PYGB_HUMANPYGBphysical
22863883
SYRC_HUMANRARSphysical
22863883
RIC8A_HUMANRIC8Aphysical
22863883
CDC73_HUMANCDC73physical
26344197
CTR9_HUMANCTR9physical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
DNJC2_HUMANDNAJC2physical
26344197
ERCC2_HUMANERCC2physical
26344197
BRE1B_HUMANRNF40physical
26344197

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 WDR61_HUMAN

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Related Literatures of Post-Translational Modification

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