WAC_MOUSE - dbPTM
WAC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WAC_MOUSE
UniProt AC Q924H7
Protein Name WW domain-containing adapter protein with coiled-coil
Gene Name Wac
Organism Mus musculus (Mouse).
Sequence Length 646
Subcellular Localization Nucleus speckle . Nucleus . In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes.
Protein Description Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. Also acts as a negative regulator of basal autophagy. Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation. May negatively regulate the ubiquitin proteasome pathway..
Protein Sequence MVMYARKQQRLSDGCHDRRGDSQPFQALKYSSKSHPSSGDHRHEKMRDAADPSPPNKMLRRSNSPENKYSDSTGHNKAKNVHTQRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEANKLAVNSFPKDRDYRREVMQATATSGFTSGMEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKESAPGDKSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQSTIPPLLQDPNLFRQLLPALQATLQLNNSNVDISKINEVLTAAVTQASLQSIIHKFLTAGPSAFNITSLISQAAQLSTQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPMKPLISTPPVSSQPKVSTPVVKQGPVSHSATQQPVTADKQQSHDPVSPRSLQRLSSQRSPSPGPNHTCSSNASTATVVPQNASARPACSLTPTLAAHFNDNLIKHVQGWPADHAEKQASRLREEAHNMGSVHMSEICTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV
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
8 (in isoform 2)Phosphorylation-28.2425521595
12PhosphorylationARKQQRLSDGCHDRR
CCCCHHCCCCCCCCC
33.8627841257
22PhosphorylationCHDRRGDSQPFQALK
CCCCCCCCCCHHHHH
42.4528066266
53PhosphorylationMRDAADPSPPNKMLR
HHHCCCCCCCCHHHH
54.2425521595
62PhosphorylationPNKMLRRSNSPENKY
CCHHHHCCCCCCCCC
34.9127087446
64PhosphorylationKMLRRSNSPENKYSD
HHHHCCCCCCCCCCC
34.5327087446
69PhosphorylationSNSPENKYSDSTGHN
CCCCCCCCCCCCCCC
29.3225777480
70PhosphorylationNSPENKYSDSTGHNK
CCCCCCCCCCCCCCC
27.0526745281
72PhosphorylationPENKYSDSTGHNKAK
CCCCCCCCCCCCCCC
30.2830635358
73PhosphorylationENKYSDSTGHNKAKN
CCCCCCCCCCCCCCC
47.6630635358
93PhosphorylationVRERDGGTSYSPQEN
CCCCCCCCCCCCCCC
29.9825777480
94PhosphorylationRERDGGTSYSPQENS
CCCCCCCCCCCCCCC
27.2126643407
95PhosphorylationERDGGTSYSPQENSH
CCCCCCCCCCCCCCC
24.9825777480
96PhosphorylationRDGGTSYSPQENSHN
CCCCCCCCCCCCCCC
21.6327742792
101PhosphorylationSYSPQENSHNHSALH
CCCCCCCCCCCCCCC
25.5525777480
105PhosphorylationQENSHNHSALHSSNS
CCCCCCCCCCCCCCC
37.5325777480
109PhosphorylationHNHSALHSSNSHSSN
CCCCCCCCCCCCCCC
31.8725777480
110PhosphorylationNHSALHSSNSHSSNP
CCCCCCCCCCCCCCC
31.4425777480
112PhosphorylationSALHSSNSHSSNPSN
CCCCCCCCCCCCCCC
27.0525777480
114PhosphorylationLHSSNSHSSNPSNNP
CCCCCCCCCCCCCCC
31.4725777480
115PhosphorylationHSSNSHSSNPSNNPS
CCCCCCCCCCCCCCC
47.5425777480
118PhosphorylationNSHSSNPSNNPSKTS
CCCCCCCCCCCCCCC
54.1925777480
122PhosphorylationSNPSNNPSKTSDAPY
CCCCCCCCCCCCCCC
51.1725777480
131PhosphorylationTSDAPYDSADDWSEH
CCCCCCCCCCHHHHH
27.9625338131
136PhosphorylationYDSADDWSEHISSSG
CCCCCHHHHHHHHCC
26.7123684622
142PhosphorylationWSEHISSSGKKYYYN
HHHHHHHCCCEEEEE
48.09-
222PhosphorylationLLPQNILSQTSRHND
HCCHHHHHHHHCCCC
27.84-
225PhosphorylationQNILSQTSRHNDKDY
HHHHHHHHCCCCCCC
24.73-
265PhosphorylationATPSTVPSSPFTLQS
CCCCCCCCCCCCCCC
46.4326643407
266PhosphorylationTPSTVPSSPFTLQSD
CCCCCCCCCCCCCCC
20.2626643407
269PhosphorylationTVPSSPFTLQSDHQP
CCCCCCCCCCCCCCC
27.5429550500
272PhosphorylationSSPFTLQSDHQPKKS
CCCCCCCCCCCCCCC
39.9229550500
279PhosphorylationSDHQPKKSFDANGAS
CCCCCCCCCCCCCCC
34.1928973931
293PhosphorylationSTLSKLPTPTASLPA
CHHHCCCCCCCCCCC
43.6528833060
295PhosphorylationLSKLPTPTASLPAQK
HHCCCCCCCCCCCCC
31.2128833060
297PhosphorylationKLPTPTASLPAQKTE
CCCCCCCCCCCCCCC
37.0528833060
302AcetylationTASLPAQKTERKESA
CCCCCCCCCCCCCCC
55.2323806337
433PhosphorylationLSTQAQPSNQSPMSL
HHHHCCCCCCCCCCC
35.1123984901
436PhosphorylationQAQPSNQSPMSLTSD
HCCCCCCCCCCCCCC
27.1623984901
439PhosphorylationPSNQSPMSLTSDASS
CCCCCCCCCCCCCCC
31.7023984901
441PhosphorylationNQSPMSLTSDASSPR
CCCCCCCCCCCCCCC
19.7723984901
442PhosphorylationQSPMSLTSDASSPRS
CCCCCCCCCCCCCCC
36.1523984901
445PhosphorylationMSLTSDASSPRSYVS
CCCCCCCCCCCCCCC
45.9623984901
446PhosphorylationSLTSDASSPRSYVSP
CCCCCCCCCCCCCCC
26.5026824392
449PhosphorylationSDASSPRSYVSPRIS
CCCCCCCCCCCCCCC
33.0227717184
452PhosphorylationSSPRSYVSPRISTPQ
CCCCCCCCCCCCCCC
10.5423737553
456PhosphorylationSYVSPRISTPQTNTV
CCCCCCCCCCCCCCC
35.0021082442
457PhosphorylationYVSPRISTPQTNTVP
CCCCCCCCCCCCCCC
19.6226824392
460PhosphorylationPRISTPQTNTVPMKP
CCCCCCCCCCCCCCC
33.7826239621
462PhosphorylationISTPQTNTVPMKPLI
CCCCCCCCCCCCCCC
29.4026239621
470PhosphorylationVPMKPLISTPPVSSQ
CCCCCCCCCCCCCCC
42.4126239621
471PhosphorylationPMKPLISTPPVSSQP
CCCCCCCCCCCCCCC
25.3121082442
475PhosphorylationLISTPPVSSQPKVST
CCCCCCCCCCCCCCC
29.0926160508
476PhosphorylationISTPPVSSQPKVSTP
CCCCCCCCCCCCCCC
51.2226160508
482PhosphorylationSSQPKVSTPVVKQGP
CCCCCCCCCCEECCC
24.0822817900
491PhosphorylationVVKQGPVSHSATQQP
CEECCCCCCCCCCCC
18.1725777480
493PhosphorylationKQGPVSHSATQQPVT
ECCCCCCCCCCCCCC
26.0425777480
495PhosphorylationGPVSHSATQQPVTAD
CCCCCCCCCCCCCCC
30.6525777480
500PhosphorylationSATQQPVTADKQQSH
CCCCCCCCCCCHHCC
35.5025777480
506PhosphorylationVTADKQQSHDPVSPR
CCCCCHHCCCCCCHH
27.6223684622
511PhosphorylationQQSHDPVSPRSLQRL
HHCCCCCCHHHHHHH
21.7125521595
519PhosphorylationPRSLQRLSSQRSPSP
HHHHHHHHHCCCCCC
26.9826160508
520PhosphorylationRSLQRLSSQRSPSPG
HHHHHHHHCCCCCCC
33.9226160508
523PhosphorylationQRLSSQRSPSPGPNH
HHHHHCCCCCCCCCC
23.3023684622
525PhosphorylationLSSQRSPSPGPNHTC
HHHCCCCCCCCCCCC
43.6726824392
531PhosphorylationPSPGPNHTCSSNAST
CCCCCCCCCCCCCCC
22.2626160508
533PhosphorylationPGPNHTCSSNASTAT
CCCCCCCCCCCCCEE
27.9926160508
534PhosphorylationGPNHTCSSNASTATV
CCCCCCCCCCCCEEE
38.2626160508
537PhosphorylationHTCSSNASTATVVPQ
CCCCCCCCCEEECCC
23.8726160508
538PhosphorylationTCSSNASTATVVPQN
CCCCCCCCEEECCCC
24.7626160508
540PhosphorylationSSNASTATVVPQNAS
CCCCCCEEECCCCCC
23.3326160508
547PhosphorylationTVVPQNASARPACSL
EECCCCCCCCCCCCC
32.1525293948

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 WAC_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 WAC_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WAC_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WAC_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, AND MASSSPECTROMETRY.

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