WDR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: WDR1_MOUSE
• UniProt AC: O88342
• Protein Name: WD repeat-containing protein 1
• Gene Name: Wdr1
• Organism: Mus musculus (Mouse).
• Sequence Length: 606
• Subcellular Localization: Cytoplasm, cytoskeleton . Cell projection, podosome .
• Protein Description: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (By similarity). Enhances cofilin-mediated actin severing. [PubMed: 25915128 Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (By similarity Involved in myocardium sarcomere organization. Required for cardiomyocyte growth at the postnatal and maintenance at the adult stage]
• Protein Sequence: MPYEIKKVFASLPQVERGVSKILGGDPKGDHFLYTNGKCVILRNIDNPAIADIYTEHAHQVVVAKYAPSGFYIASGDISGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDTGSSVGEITGHNKVINSVDIKQTRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIFIYDGKTGEKVCALGESKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVNVNSVVSTFPMGSNVLDQQLGCLWQKDHLLSISLSGYINYLDKNNPSKPLRVIKGHSKSIQCLTVHRNGGKSYIYSGSHDGHINYWDSETGENDSFSGKGHTNQVSRMTVNESEQLVSCSMDDTVRYTNLTLRDYSGQGVVKLDVQPKCVAVGPGGYTVVVCIGQIVLLKDQKKCFSIDNPGYEPEVVAVHPGGDTVAVGGTDGNVRVYSILASTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETKVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY

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
3	Phosphorylation	-----MPYEIKKVFA -----CCHHHHHHHH	29.05	25367039
7	Acetylation	-MPYEIKKVFASLPQ -CCHHHHHHHHCCHH	48.52	23806337
7	Ubiquitination	-MPYEIKKVFASLPQ -CCHHHHHHHHCCHH	48.52	-
7	Succinylation	-MPYEIKKVFASLPQ -CCHHHHHHHHCCHH	48.52	23806337
21	Acetylation	QVERGVSKILGGDPK HHHHCHHHHHCCCCC	39.27	23806337
21	Succinylation	QVERGVSKILGGDPK HHHHCHHHHHCCCCC	39.27	23806337
28	Acetylation	KILGGDPKGDHFLYT HHHCCCCCCCEEEEE	80.06	23236377
38	Ubiquitination	HFLYTNGKCVILRNI EEEEECCEEEEEECC	27.65	22790023
72	Phosphorylation	KYAPSGFYIASGDIS EECCCCEEEEECCCC	10.09	26026062
81	Acetylation	ASGDISGKLRIWDTT EECCCCCCEEEEECC	28.00	23954790
81	Ubiquitination	ASGDISGKLRIWDTT EECCCCCCEEEEECC	28.00	22790023
90	Acetylation	RIWDTTQKEHLLKYE EEEECCCCHHHHEEE	45.04	23806337
90	Succinylation	RIWDTTQKEHLLKYE EEEECCCCHHHHEEE	45.04	23806337
95	Acetylation	TQKEHLLKYEYQPFA CCCHHHHEEECCCCC	42.25	23806337
95	Ubiquitination	TQKEHLLKYEYQPFA CCCHHHHEEECCCCC	42.25	22790023
96	Phosphorylation	QKEHLLKYEYQPFAG CCHHHHEEECCCCCC	21.60	28464351
98	Phosphorylation	EHLLKYEYQPFAGKI HHHHEEECCCCCCCC	20.56	21454597
104	Acetylation	EYQPFAGKIKDIAWT ECCCCCCCCEEEEEC	43.06	23806337
104	Ubiquitination	EYQPFAGKIKDIAWT ECCCCCCCCEEEEEC	43.06	-
104	Succinylation	EYQPFAGKIKDIAWT ECCCCCCCCEEEEEC	43.06	23806337
106	Ubiquitination	QPFAGKIKDIAWTED CCCCCCCEEEEECCC	46.71	22790023
111	Phosphorylation	KIKDIAWTEDSKRIA CCEEEEECCCCCEEE	22.38	21454597
114	Phosphorylation	DIAWTEDSKRIAVVG EEEECCCCCEEEEEE	20.01	21454597
115	Acetylation	IAWTEDSKRIAVVGE EEECCCCCEEEEEEC	61.21	23954790
115	Succinylation	IAWTEDSKRIAVVGE EEECCCCCEEEEEEC	61.21	23954790
170	S-nitrosocysteine	ATGSDDNCAAFFEGP CCCCCCCCHHHCCCC	3.58	-
170	S-nitrosylation	ATGSDDNCAAFFEGP CCCCCCCCHHHCCCC	3.58	21278135
180	Acetylation	FFEGPPFKFKFTIGD HCCCCCEEEEEEECC	54.11	22733758
182	Malonylation	EGPPFKFKFTIGDHS CCCCEEEEEEECCCC	42.03	26320211
182	Acetylation	EGPPFKFKFTIGDHS CCCCEEEEEEECCCC	42.03	22826441
219	Acetylation	QIFIYDGKTGEKVCA EEEEECCCCCCEEEE	50.92	23236377
223	Acetylation	YDGKTGEKVCALGES ECCCCCCEEEECCCE	43.91	23806337
223	Succinylation	YDGKTGEKVCALGES ECCCCCCEEEECCCE	43.91	23806337
225	Glutathionylation	GKTGEKVCALGESKA CCCCCEEEECCCEEC	3.71	24333276
225	S-nitrosylation	GKTGEKVCALGESKA CCCCCEEEECCCEEC	3.71	21278135
225	S-nitrosocysteine	GKTGEKVCALGESKA CCCCCEEEECCCEEC	3.71	-
238	Phosphorylation	KAHDGGIYAISWSPD ECCCCCEEEEEECCC	10.93	28418008
241	Phosphorylation	DGGIYAISWSPDSTH CCCEEEEEECCCCCC	17.21	20415495
243	Phosphorylation	GIYAISWSPDSTHLL CEEEEEECCCCCCEE	16.43	20415495
246	Phosphorylation	AISWSPDSTHLLSAS EEEECCCCCCEEECC	22.55	20415495
247	Phosphorylation	ISWSPDSTHLLSASG EEECCCCCCEEECCC	24.75	20415495
251	Phosphorylation	PDSTHLLSASGDKTS CCCCCEEECCCCCCC	27.09	20415495
253	Phosphorylation	STHLLSASGDKTSKI CCCEEECCCCCCCCE	44.12	20415495
256	Acetylation	LLSASGDKTSKIWDV EEECCCCCCCCEEEE	59.22	23806337
256	Ubiquitination	LLSASGDKTSKIWDV EEECCCCCCCCEEEE	59.22	22790023
321	Acetylation	RVIKGHSKSIQCLTV EEEECCCCEEEEEEE	46.00	22826441
325	S-palmitoylation	GHSKSIQCLTVHRNG CCCCEEEEEEEEECC	3.07	26165157
325	S-nitrosylation	GHSKSIQCLTVHRNG CCCCEEEEEEEEECC	3.07	21278135
325	Glutathionylation	GHSKSIQCLTVHRNG CCCCEEEEEEEEECC	3.07	24333276
325	S-nitrosocysteine	GHSKSIQCLTVHRNG CCCCEEEEEEEEECC	3.07	-
348	Phosphorylation	SHDGHINYWDSETGE CCCCCEEEEECCCCC	15.25	-
358	Phosphorylation	SETGENDSFSGKGHT CCCCCCCCCCCCCCC	32.66	23375375
382	S-nitrosocysteine	ESEQLVSCSMDDTVR CCHHEEEEECCCCEE	2.81	-
382	S-nitrosylation	ESEQLVSCSMDDTVR CCHHEEEEECCCCEE	2.81	21278135
399	Phosphorylation	NLTLRDYSGQGVVKL EEEEECCCCCCEEEE	29.00	29176673
405	Ubiquitination	YSGQGVVKLDVQPKC CCCCCEEEEEEECCE	36.24	22790023
438	Glutathionylation	LLKDQKKCFSIDNPG EECCCCCEEECCCCC	4.10	24333276
480	Acetylation	SILASTLKDEGKLLE EEEEEEECCCCCEEE	54.55	23806337
480	Ubiquitination	SILASTLKDEGKLLE EEEEEEECCCCCEEE	54.55	-
480	Succinylation	SILASTLKDEGKLLE EEEEEEECCCCCEEE	54.55	23954790

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of WDR1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of WDR1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of WDR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR61_MOUSE	Wdr61	physical	19345177
CDC73_MOUSE	Cdc73	physical	19345177
LEO1_MOUSE	Leo1	physical	19345177
SF3B4_MOUSE	Sf3b4	physical	19345177
RUVB2_MOUSE	Ruvbl2	physical	19345177
RUVB1_MOUSE	Ruvbl1	physical	19345177

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASSSPECTROMETRY.
PubMed: 18034455