PUM2_MOUSE - dbPTM
PUM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUM2_MOUSE
UniProt AC Q80U58
Protein Name Pumilio homolog 2
Gene Name Pum2
Organism Mus musculus (Mouse).
Sequence Length 1066
Subcellular Localization Cytoplasm . Cytoplasmic granule . Cytoplasm, perinuclear region. The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS
Protein Description Sequence-specific RNA-binding protein that acts as a post-transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-UGUANAUA-3', that is related to the Nanos Response Element (NRE). Mediates post-transcriptional repression of transcripts via different mechanisms: acts via direct recruitment of the CCR4-POP2-NOT deadenylase leading to translational inhibition and mRNA degradation. Also mediates deadenylation-independent repression by promoting accessibility of miRNAs. Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation. Plays a role in cytoplasmic sensing of viral infection. Represses a program of genes necessary to maintain genomic stability such as key mitotic, DNA repair and DNA replication factors. Its ability to repress those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its high abundance and multitude of PUMILIO binding sites, is able to sequester a significant fraction of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels. May support proliferation and self-renewal of stem cells. Binds specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA MIR199A expression at a postranscriptional level (By similarity)..
Protein Sequence MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGTSHHSMSQPIMVQRRSGQSFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGTFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQDDEDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPSTNPPEGLGPLPNPTANKPLVEEFSNPETQNLDAMDQVGLDSLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTSALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAASNTANQQAASQAQPGQQQVLRPGAGQRPITPSQGQQGQQAESLAAAANPTLAFGQSLAAGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSTAAQAAAAAAAAGGTANSLTGSTNGLFRPIGTQPPQQQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSASLGFGSGSSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQIVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML
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
67PhosphorylationPIMVQRRSGQSFHGN
CEEEEECCCCCCCCC		43.2925619855
70PhosphorylationVQRRSGQSFHGNSEV
EEECCCCCCCCCCCC		23.8025619855
75PhosphorylationGQSFHGNSEVNAILS
CCCCCCCCCCCEEEC		47.7325619855
82PhosphorylationSEVNAILSPRSESGG
CCCCEEECCCCCCCC		16.5027087446
85PhosphorylationNAILSPRSESGGLGV
CEEECCCCCCCCCCH		39.2327087446
87PhosphorylationILSPRSESGGLGVSM
EECCCCCCCCCCHHH		39.1328066266
93PhosphorylationESGGLGVSMVEYVLS
CCCCCCHHHEEHHHH		18.4728066266
97PhosphorylationLGVSMVEYVLSSSPA
CCHHHEEHHHHCCCH		8.6927087446
100PhosphorylationSMVEYVLSSSPADKL
HHEEHHHHCCCHHHH		20.8026239621
101PhosphorylationMVEYVLSSSPADKLD
HEEHHHHCCCHHHHH		35.8626239621
102PhosphorylationVEYVLSSSPADKLDS
EEHHHHCCCHHHHHH		22.2627087446
109PhosphorylationSPADKLDSRFRKGTF
CCHHHHHHHHCCCCC		43.7023984901
115PhosphorylationDSRFRKGTFGTRDAE
HHHHCCCCCCCCCCC		23.1725338131
136PhosphorylationGDQKGKASPFEEDQN
CCCCCCCCCCHHHHC		33.3427087446
168GlutathionylationPNGMDADCKDFNRTP
CCCCCCCCCCCCCCC		4.9624333276
174PhosphorylationDCKDFNRTPGSRQAS
CCCCCCCCCCCCCCC		32.8627087446
177PhosphorylationDFNRTPGSRQASPTE
CCCCCCCCCCCCHHH		23.5627087446
181PhosphorylationTPGSRQASPTEVVER
CCCCCCCCHHHHHHH		24.8227087446
183PhosphorylationGSRQASPTEVVERLG
CCCCCCHHHHHHHHC		38.6325521595
395PhosphorylationGAGQRPITPSQGQQG
CCCCCCCCCCCCCCH		21.41-
587PhosphorylationSSATRRESLSTSSDL
CHHHHHHHCCCCHHH		26.3025521595
589PhosphorylationATRRESLSTSSDLYK
HHHHHHCCCCHHHHH		35.2125619855
590PhosphorylationTRRESLSTSSDLYKR
HHHHHCCCCHHHHHH		37.2325619855
591PhosphorylationRRESLSTSSDLYKRS
HHHHCCCCHHHHHHC		20.6225619855
592PhosphorylationRESLSTSSDLYKRSS
HHHCCCCHHHHHHCC		31.5525619855
595PhosphorylationLSTSSDLYKRSSSSL
CCCCHHHHHHCCCCC		14.8925619855
662PhosphorylationLTNGSGRYISAAPGA
CCCCCCCEEECCCCC		11.6229514104
672UbiquitinationAAPGAEAKYRSASST
CCCCCCEEECCCCCC		32.47-
674MethylationPGAEAKYRSASSTSS
CCCCEEECCCCCCHH		25.66-
684PhosphorylationSSTSSLFSSSSQLFP
CCCHHHCCCCCCCCC		34.30-
700PhosphorylationSRLRYNRSDIMPSGR
HHHCCCHHHCCCCCH		28.0522817900
739 (in isoform 2)Ubiquitination-44.48-
846UbiquitinationGHVLKCVKDQNGNHV
CCEEEEEECCCCCCH		64.17-
990PhosphorylationCQNDGPHSALYTMMK
CCCCCCCHHHHHHHH		24.09-
993PhosphorylationDGPHSALYTMMKDQY
CCCCHHHHHHHHHHH		7.72-
994PhosphorylationGPHSALYTMMKDQYA
CCCHHHHHHHHHHHH		16.19-
1052PhosphorylationEKYYLKNSPDLGPIG
HHHHHHCCCCCCCCC		20.4326643407
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 PUM2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUM2_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 PUM2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP6_MOUSERbbp6physical
15617101
NANO3_MOUSENanos3physical
18089289
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUM2_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 SER-136, AND MASSSPECTROMETRY.
"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-136 AND SER-587, ANDMASS SPECTROMETRY.

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