WDR82_HUMAN - dbPTM
WDR82_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR82_HUMAN
UniProt AC Q6UXN9
Protein Name WD repeat-containing protein 82
Gene Name WDR82
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Nucleus . Associates with chromatin.
Protein Description Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase..
Protein Sequence MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD
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
2Ubiquitination------MKLTDSVLR
------CCCCHHHHH		61.16-
2Acetylation------MKLTDSVLR
------CCCCHHHHH		61.1625953088
2Methylation------MKLTDSVLR
------CCCCHHHHH		61.16116252993
4Phosphorylation----MKLTDSVLRSF
----CCCCHHHHHHH		22.2528450419
6Phosphorylation--MKLTDSVLRSFRV
--CCCCHHHHHHHHH		20.1623911959
10PhosphorylationLTDSVLRSFRVAKVF
CCHHHHHHHHHHHHH		17.1629514088
62UbiquitinationPKRTLYSKKYGVDLI
CCCEEECCCCCCCEE		36.14-
63AcetylationKRTLYSKKYGVDLIR
CCEEECCCCCCCEEE		41.1025953088
63UbiquitinationKRTLYSKKYGVDLIR
CCEEECCCCCCCEEE		41.1021890473
63MalonylationKRTLYSKKYGVDLIR
CCEEECCCCCCCEEE		41.1026320211
63UbiquitinationKRTLYSKKYGVDLIR
CCEEECCCCCCCEEE		41.1021890473
64PhosphorylationRTLYSKKYGVDLIRY
CEEECCCCCCCEEEE		26.5620068231
71PhosphorylationYGVDLIRYTHAANTV
CCCCEEEEECCCCEE		8.9021406692
72PhosphorylationGVDLIRYTHAANTVV
CCCEEEEECCCCEEE		8.6621406692
77PhosphorylationRYTHAANTVVYSSNK
EEECCCCEEEEECCC		13.4621406692
80PhosphorylationHAANTVVYSSNKIDD
CCCCEEEEECCCHHC		11.3121406692
81PhosphorylationAANTVVYSSNKIDDT
CCCEEEEECCCHHCE		18.8021406692
82PhosphorylationANTVVYSSNKIDDTI
CCEEEEECCCHHCEE		25.1821406692
84AcetylationTVVYSSNKIDDTIRY
EEEEECCCHHCEEEE		49.8426051181
84UbiquitinationTVVYSSNKIDDTIRY
EEEEECCCHHCEEEE		49.8421890473
88PhosphorylationSSNKIDDTIRYLSLH
ECCCHHCEEEEEECC		12.01-
93PhosphorylationDDTIRYLSLHDNKYI
HCEEEEEECCCCCEE		18.0920873877
98UbiquitinationYLSLHDNKYIRYFPG
EEECCCCCEEEECCC		48.3821890473
98AcetylationYLSLHDNKYIRYFPG
EEECCCCCEEEECCC		48.3823236377
98UbiquitinationYLSLHDNKYIRYFPG
EEECCCCCEEEECCC		48.3821906983
108UbiquitinationRYFPGHSKRVVALSM
EECCCCCCEEEEEEE		43.46-
114PhosphorylationSKRVVALSMSPVDDT
CCEEEEEEECCCCCC		13.89-
116PhosphorylationRVVALSMSPVDDTFI
EEEEEEECCCCCCEE		20.56-
126PhosphorylationDDTFISGSLDKTIRL
CCCEEECCCCCEEEE		26.9721712546
129AcetylationFISGSLDKTIRLWDL
EEECCCCCEEEEEEC		51.6625953088
129UbiquitinationFISGSLDKTIRLWDL
EEECCCCCEEEEEEC		51.6621890473
132MethylationGSLDKTIRLWDLRSP
CCCCCEEEEEECCCC		34.65115920033
177MethylationMVKLYDLRSFDKGPF
HEEEECCCCCCCCCC		32.17115920037
181UbiquitinationYDLRSFDKGPFATFK
ECCCCCCCCCCCEEE		67.4819608861
181AcetylationYDLRSFDKGPFATFK
ECCCCCCCCCCCEEE		67.4819608861
188UbiquitinationKGPFATFKMQYDRTC
CCCCCEEEEEECCCC		22.2721890473
188UbiquitinationKGPFATFKMQYDRTC
CCCCCEEEEEECCCC		22.2721890473
193MethylationTFKMQYDRTCEWTGL
EEEEEECCCCEECEE		36.02115920041
201UbiquitinationTCEWTGLKFSNDGKL
CCEECEEEECCCCCE		48.36-
201AcetylationTCEWTGLKFSNDGKL
CCEECEEEECCCCCE		48.3626051181
225UbiquitinationIRLIDAFKGVVMHTF
HHHHHHCCCEEEEEC		53.14-
229SulfoxidationDAFKGVVMHTFGGYA
HHCCCEEEEECCCCC		1.9830846556
273UbiquitinationWNGESGIKVAVLDGK
EECCCCEEEEEECCC		27.89-
280UbiquitinationKVAVLDGKHTGPITC
EEEEECCCCCCCEEE		37.35-
280AcetylationKVAVLDGKHTGPITC
EEEEECCCCCCCEEE		37.3525953088
282PhosphorylationAVLDGKHTGPITCLQ
EEECCCCCCCEEEEE		48.41-
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 WDR82_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR82_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 WDR82_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SET1A_HUMANSETD1Aphysical
17355966
SET1B_HUMANSETD1Bphysical
17355966
KMT2C_HUMANKMT2Cphysical
20516061
KMT2B_HUMANKMT2Bphysical
20516061
SET1B_HUMANSETD1Bphysical
20516061
SET1A_HUMANSETD1Aphysical
20516061
RPB1_HUMANPOLR2Aphysical
20516061
PYDC1_HUMANPYDC1physical
20516061
KDM6A_HUMANKDM6Aphysical
20516061
RPB2_HUMANPOLR2Bphysical
20516061
HCFC1_HUMANHCFC1physical
20516061
PAXI1_HUMANPAXIP1physical
20516061
PP1RA_HUMANPPP1R10physical
20516061
TOX4_HUMANTOX4physical
20516061
RBM10_HUMANRBM10physical
20516061
ASH2L_HUMANASH2Lphysical
20516061
CXXC1_HUMANCXXC1physical
20516061
RBBP5_HUMANRBBP5physical
20516061
HSP7C_HUMANHSPA8physical
20516061
HSP74_HUMANHSPA4physical
20516061
TCPA_HUMANTCP1physical
20516061
TCPG_HUMANCCT3physical
20516061
TCPH_HUMANCCT7physical
20516061
TCPE_HUMANCCT5physical
20516061
WDR5_HUMANWDR5physical
20516061
PP1A_HUMANPPP1CAphysical
20516061
PP1B_HUMANPPP1CBphysical
20516061
PP1G_HUMANPPP1CCphysical
20516061
BAP18_HUMANC17orf49physical
20516061
KMT2D_HUMANKMT2Dphysical
20516061
CXXC1_HUMANCXXC1physical
23870121
ASH2L_HUMANASH2Lphysical
23870121
RBBP5_HUMANRBBP5physical
23870121
WDR5_HUMANWDR5physical
23870121
SET1A_HUMANSETD1Aphysical
23870121
SET1B_HUMANSETD1Bphysical
23870121
DPY30_HUMANDPY30physical
23870121
GLOD4_HUMANGLOD4physical
26344197
GMPPB_HUMANGMPPBphysical
26344197
AATC_HUMANGOT1physical
26344197
PPIL3_HUMANPPIL3physical
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 WDR82_HUMAN

loading...

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-98 AND LYS-181, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory