PR40A_MOUSE - dbPTM
PR40A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PR40A_MOUSE
UniProt AC Q9R1C7
Protein Name Pre-mRNA-processing factor 40 homolog A
Gene Name Prpf40a
Organism Mus musculus (Mouse).
Sequence Length 953
Subcellular Localization Nucleus speckle. Nucleus matrix. Colocalizes with AKAP8L in the nuclear matrix.
Protein Description Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing..
Protein Sequence MRPGTGAERGGLMVSEMESQPPSRGPGDGERRLSGSNLCSSSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMSGMMMSHMSQASMQPALPPGVNSMDVAAGAASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGGLITKSNLHAMIKAEESSKQEECTTASTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAANANTSTTPTNTVGSVPVAPEPEVTSIVATAVDNENTVTVSTEEQAQLANTTAIQDLSGDISSNTGEEPAKQETVSDFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKTLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQATPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSESDDDDSHSKKKRQRSESHSASERSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDTEREKDKKEKDRDSEKDRSRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ
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
2Methylation------MRPGTGAER
------CCCCCCCCC		38.05-
5Phosphorylation---MRPGTGAERGGL
---CCCCCCCCCCCE		35.5829895711
9MethylationRPGTGAERGGLMVSE
CCCCCCCCCCEEEEE		43.9024129315
15PhosphorylationERGGLMVSEMESQPP
CCCCEEEEECCCCCC		19.7729895711
34PhosphorylationGDGERRLSGSNLCSS
CCCCCCCCCCCCCCC		38.0622942356
36PhosphorylationGERRLSGSNLCSSSW
CCCCCCCCCCCCCCC		24.2122942356
40PhosphorylationLSGSNLCSSSWVSAD
CCCCCCCCCCCCCCC		30.4925159016
41PhosphorylationSGSNLCSSSWVSADG
CCCCCCCCCCCCCCC		27.5025159016
42PhosphorylationGSNLCSSSWVSADGF
CCCCCCCCCCCCCCH		18.4025159016
45PhosphorylationLCSSSWVSADGFLRR
CCCCCCCCCCCHHHC		17.8725777480
55PhosphorylationGFLRRRPSMGHPGMH
CHHHCCCCCCCCCCC		35.2724719451
105PhosphorylationGQMPGMMSSVMSGMM
CCCCHHHHHHHHHHH		15.76-
106PhosphorylationQMPGMMSSVMSGMMM
CCCHHHHHHHHHHHH		12.16-
109PhosphorylationGMMSSVMSGMMMSHM
HHHHHHHHHHHHHHH		22.75-
114PhosphorylationVMSGMMMSHMSQASM
HHHHHHHHHHHHHHC		9.72-
151PhosphorylationSMWTEHKSPDGRTYY
CCCEECCCCCCCEEE		30.0825159016
192PhosphorylationCPWKEYKSDSGKPYY
CCCHHCCCCCCCCCC		35.7927149854
194PhosphorylationWKEYKSDSGKPYYYN
CHHCCCCCCCCCCCC		56.6727149854
196AcetylationEYKSDSGKPYYYNSQ
HCCCCCCCCCCCCCC		33.5223806337
196UbiquitinationEYKSDSGKPYYYNSQ
HCCCCCCCCCCCCCC		33.52-
198PhosphorylationKSDSGKPYYYNSQTK
CCCCCCCCCCCCCCC		23.2827149854
199PhosphorylationSDSGKPYYYNSQTKE
CCCCCCCCCCCCCCC		12.5127149854
200PhosphorylationDSGKPYYYNSQTKES
CCCCCCCCCCCCCCC		11.5127149854
202PhosphorylationGKPYYYNSQTKESRW
CCCCCCCCCCCCCCC		24.0927149854
204PhosphorylationPYYYNSQTKESRWAK
CCCCCCCCCCCCCCC		36.2827149854
205AcetylationYYYNSQTKESRWAKP
CCCCCCCCCCCCCCC		46.16156863
207PhosphorylationYNSQTKESRWAKPKE
CCCCCCCCCCCCCCH		34.3827149854
341PhosphorylationEQAQLANTTAIQDLS
HHHHHCCCCHHHHHC		16.40-
364PhosphorylationEEPAKQETVSDFTPK
CCCCCCCCCCCCCCC		23.8623684622
366PhosphorylationPAKQETVSDFTPKKE
CCCCCCCCCCCCCHH		34.1325159016
369PhosphorylationQETVSDFTPKKEEEE
CCCCCCCCCCHHHHC		38.9125521595
628UbiquitinationGQLHSMSSWMELYPT
CCCCCCCHHHHHCCC		23.0727667366
677UbiquitinationDEKKIIKDILKDKGF
CHHHHHHHHHHCCCE		40.8327667366
682UbiquitinationIKDILKDKGFVVEVN
HHHHHHCCCEEEEEE		53.3027667366
696UbiquitinationNTTFEDFVAIISSTK
ECCHHHHHHHHHCCC		6.0627667366
700UbiquitinationEDFVAIISSTKRSTT
HHHHHHHHCCCCCEE		26.3327667366
705PhosphorylationIISSTKRSTTLDAGN
HHHCCCCCEEECHHH		27.5722871156
706PhosphorylationISSTKRSTTLDAGNI
HHCCCCCEEECHHHH		35.1022871156
714UbiquitinationTLDAGNIKLAFNSLL
EECHHHHHHHHHHHH		37.45-
719PhosphorylationNIKLAFNSLLEKAEA
HHHHHHHHHHHHHHH		28.0722006019
720UbiquitinationIKLAFNSLLEKAEAR
HHHHHHHHHHHHHHH		8.2127667366
723UbiquitinationAFNSLLEKAEARERE
HHHHHHHHHHHHHHH		52.0427667366
724UbiquitinationFNSLLEKAEARERER
HHHHHHHHHHHHHHH		13.3027667366
731UbiquitinationAEAREREREKEEARK
HHHHHHHHHHHHHHH		67.5227667366
742UbiquitinationEARKMKRKESAFKSM
HHHHHHHHHHHHHHH		50.9727667366
745UbiquitinationKMKRKESAFKSMLKQ
HHHHHHHHHHHHHHH		19.5827667366
749UbiquitinationKESAFKSMLKQATPP
HHHHHHHHHHHCCCC		5.8127667366
754PhosphorylationKSMLKQATPPIELDA
HHHHHHCCCCCCHHH		27.4026643407
769UbiquitinationVWEDIRERFVKEPAF
HHHHHHHHHCCCCCC		31.6327667366
772UbiquitinationDIRERFVKEPAFEDI
HHHHHHCCCCCCCCC		56.0927667366
773UbiquitinationIRERFVKEPAFEDIT
HHHHHCCCCCCCCCC		36.2427667366
780PhosphorylationEPAFEDITLESERKR
CCCCCCCCCHHHHHH		36.4729472430
783PhosphorylationFEDITLESERKRIFK
CCCCCCHHHHHHHHH		45.9026824392
791UbiquitinationERKRIFKDFMHVLEH
HHHHHHHHHHHHHHH		35.0427667366
805PhosphorylationHECQHHHSKNKKHSK
HHHHHHHHCCHHCCH		33.3028418008
824PhosphorylationHHRKRSRSRSGSESD
HHHHHHHCCCCCCCC		31.8522817900
826PhosphorylationRKRSRSRSGSESDDD
HHHHHCCCCCCCCCC		48.1722817900
828PhosphorylationRSRSRSGSESDDDDS
HHHCCCCCCCCCCCC		34.8622817900
830PhosphorylationRSRSGSESDDDDSHS
HCCCCCCCCCCCCHH		48.3022817900
853PhosphorylationSHSASERSSSAESER
CCCHHHHHCHHHHHH		25.2929514104
854PhosphorylationHSASERSSSAESERS
CCHHHHHCHHHHHHH		39.5329514104
855PhosphorylationSASERSSSAESERSY
CHHHHHCHHHHHHHH		36.9829514104
879PhosphorylationSKKRRHKSDSPESDT
HHHHHCCCCCCCCHH		36.8825521595
881PhosphorylationKRRHKSDSPESDTER
HHHCCCCCCCCHHHH		37.3425521595
884PhosphorylationHKSDSPESDTEREKD
CCCCCCCCHHHHHHH		53.9025521595
886PhosphorylationSDSPESDTEREKDKK
CCCCCCHHHHHHHHH		46.3425521595
899PhosphorylationKKEKDRDSEKDRSRQ
HHHHHHHHHHHHHHH		47.6523684622
919PhosphorylationHKSPKKKTGKDSGNW
CCCCCCCCCCCCCCC		59.3420531401
923PhosphorylationKKKTGKDSGNWDTSG
CCCCCCCCCCCCCCC		37.2028833060
928PhosphorylationKDSGNWDTSGSELSE
CCCCCCCCCCCCCCH		26.9721082442
929PhosphorylationDSGNWDTSGSELSEG
CCCCCCCCCCCCCHH		37.5422942356
931PhosphorylationGNWDTSGSELSEGEL
CCCCCCCCCCCHHHH		34.8225521595
934PhosphorylationDTSGSELSEGELEKR
CCCCCCCCHHHHHHH		39.2325521595
944PhosphorylationELEKRRRTLLEQLDD
HHHHHHHHHHHHHCC		33.6125619855
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 PR40A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PR40A_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 PR40A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WASF2_MOUSEWasf2physical
14697212
WASF3_MOUSEWasf3physical
14697212
WASL_MOUSEWaslphysical
14697212
WASF1_MOUSEWasf1physical
14697212
FMN1_MOUSEFmn1physical
8605874
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PR40A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931AND SER-934, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824; SER-826; SER-828;SER-830; SER-879; SER-881 AND SER-884, AND MASS SPECTROMETRY.
"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-36 AND SER-934, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931AND SER-934, AND MASS SPECTROMETRY.

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