dbPTM

PUM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PUM1_MOUSE
UniProt AC	Q80U78
Protein Name	Pumilio homolog 1 {ECO:0000305}
Gene Name	Pum1 {ECO:0000312\|MGI:MGI:1931749}
Organism	Mus musculus (Mouse).
Sequence Length	1189
Subcellular Localization	Cytoplasm . Cytoplasm, P-body . Cytoplasmic granule .
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. Following growth factor stimulation, phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a local conformational change that exposes miRNA-binding sites, promoting association of miR-221 and miR-222, efficient suppression of CDKN1B/p27 expression, and rapid entry to the cell cycle (By similarity). Acts as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation (By similarity). 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 (By similarity). Involved in neuronal functions by regulating ATXN1 mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts, leading to their down-regulation independently of the miRNA machinery. [PubMed: 25768905 In testis, acts as a post-transcriptional regulator of spermatogenesis by binding to the 3'-UTR of mRNAs coding for regulators of p53/TP53]
Protein Sequence	MSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNTSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIAGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSATQQSAPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPSNNLASSSFYGNNSLSSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAVANSNTGSGSRRDSLTGSSDLYKRTSSSLAPIGHSFYSSLSYSSSPGPVGMPLPSQGPGHSQTPPPSLSSHGSSSSLNLGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATAAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSHEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQVINEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVACVLKR ------CCHHHHEEC	29.71	-
17	Phosphorylation	KAVLWQDSFSPHLKH CEEEECCCCCHHHCC	16.72	23984901
19	Phosphorylation	VLWQDSFSPHLKHHP EEECCCCCHHHCCCC	18.50	23984901
63	Phosphorylation	LAAGTHSSPVPGSIG HHCCCCCCCCCCCEE	23.47	23649490
75	Phosphorylation	SIGVAGRSQDDAMVD CEEECCCCCCHHHHH	36.72	22817900
83	Phosphorylation	QDDAMVDYFFQRQHG CCHHHHHHHHHHHCC	8.55	22817900
98	Phosphorylation	EQLGGGGSGGGGYNT CCCCCCCCCCCCCCC	37.22	28066266
103	Phosphorylation	GGSGGGGYNTSKHRW CCCCCCCCCCCCCCC	20.67	28066266
105	Phosphorylation	SGGGGYNTSKHRWPT CCCCCCCCCCCCCCC	30.57	28066266
106	Phosphorylation	GGGGYNTSKHRWPTG CCCCCCCCCCCCCCC	23.87	28066266
112	Phosphorylation	TSKHRWPTGDNIHAE CCCCCCCCCCCCCHH	50.65	27087446
124 (in isoform 2)	Phosphorylation	-	31.56	19144319
124	Phosphorylation	HAEHQVRSMDELNHD CHHHHCCCHHHCCHH	31.56	25521595
159	Phosphorylation	FWETDESSKDGPKGI EECCCCCCCCCCCCE	32.49	-
197	Phosphorylation	VQRRPGQSFHVNSEV EEECCCCCEECCCHH	24.20	25619855
202	Phosphorylation	GQSFHVNSEVNSVLS CCCEECCCHHCCCCC	41.66	25619855
206	Phosphorylation	HVNSEVNSVLSPRSE ECCCHHCCCCCCCCC	29.61	25619855
209	Phosphorylation	SEVNSVLSPRSESGG CHHCCCCCCCCCCCC	18.99	26824392
212	Phosphorylation	NSVLSPRSESGGLGV CCCCCCCCCCCCCCE	39.23	25619855
214	Phosphorylation	VLSPRSESGGLGVSM CCCCCCCCCCCCEEE	39.13	21082442
220	Phosphorylation	ESGGLGVSMVEYVLS CCCCCCEEEEEHHHH	18.47	25168779
224	Phosphorylation	LGVSMVEYVLSSSPG CCEEEEEHHHHCCCC	8.69	25266776
227	Phosphorylation	SMVEYVLSSSPGDSC EEEEHHHHCCCCCCH	20.80	23984901
228	Phosphorylation	MVEYVLSSSPGDSCL EEEHHHHCCCCCCHH	36.07	27087446
229	Phosphorylation	VEYVLSSSPGDSCLR EEHHHHCCCCCCHHH	29.53	27087446
233	Phosphorylation	LSSSPGDSCLRKGGF HHCCCCCCHHHCCCC	22.44	26643407
247	Phosphorylation	FGPRDADSDENDKGE CCCCCCCCCCCCCCC	48.85	26643407
260	Phosphorylation	GEKKNKGTFDGDKLG CCCCCCCCCCCCCCC	21.84	23684622
305	Phosphorylation	TPGNCQNSANEVDLL CCCCCCCCCCCCCCC	13.44	-
515	Phosphorylation	GASQRPLTPNQNQQG CCCCCCCCCCCCCCC	23.91	25338131
710	Phosphorylation	GSGSRRDSLTGSSDL CCCCCCCCCCCCHHH	26.48	27087446
712	Phosphorylation	GSRRDSLTGSSDLYK CCCCCCCCCCHHHHH	38.68	27087446
714	Phosphorylation	RRDSLTGSSDLYKRT CCCCCCCCHHHHHHC	18.55	25619855
715	Phosphorylation	RDSLTGSSDLYKRTS CCCCCCCHHHHHHCC	32.74	25619855
718	Phosphorylation	LTGSSDLYKRTSSSL CCCCHHHHHHCCCCC	11.92	25619855
785	Phosphorylation	LTNGSGRYISAAPGA CCCCCCCEEECCCCC	11.62	29514104
795	Ubiquitination	AAPGAEAKYRSASSA CCCCCCHHHCCCCCC	32.47	-
796	Phosphorylation	APGAEAKYRSASSAS CCCCCHHHCCCCCCH	19.49	23984901
797	Methylation	PGAEAKYRSASSASS CCCCHHHCCCCCCHH	25.66	-
798	Phosphorylation	GAEAKYRSASSASSL CCCHHHCCCCCCHHH	29.43	23984901
800	Phosphorylation	EAKYRSASSASSLFS CHHHCCCCCCHHHCC	27.90	26745281
801	Phosphorylation	AKYRSASSASSLFSP HHHCCCCCCHHHCCC	31.70	26745281
803	Phosphorylation	YRSASSASSLFSPSS HCCCCCCHHHCCCCH	29.53	26745281
804	Phosphorylation	RSASSASSLFSPSST CCCCCCHHHCCCCHH	32.90	26745281
807	Phosphorylation	SSASSLFSPSSTLFS CCCHHHCCCCHHHCC	29.21	22942356
809	Phosphorylation	ASSLFSPSSTLFSSS CHHHCCCCHHHCCCC	34.45	26745281
810	Phosphorylation	SSLFSPSSTLFSSSR HHHCCCCHHHCCCCC	32.30	28066266
811	Phosphorylation	SLFSPSSTLFSSSRL HHCCCCHHHCCCCCH	35.84	28066266
814	Phosphorylation	SPSSTLFSSSRLRYG CCCHHHCCCCCHHCC	30.43	25777480
819	Methylation	LFSSSRLRYGMSDVM HCCCCCHHCCCCCCC	25.50	58856361
819	Dimethylation	LFSSSRLRYGMSDVM HCCCCCHHCCCCCCC	25.50	-
823	Phosphorylation	SRLRYGMSDVMPSGR CCHHCCCCCCCCCCH	23.77	-
969	Ubiquitination	GHVLKCVKDQNGNHV CCEEEEEECCCCCCH	64.17	-
1106	Phosphorylation	VLIDEVCTMNDGPHS EEEEEEECCCCCCCH	24.96	-
1113	Phosphorylation	TMNDGPHSALYTMMK CCCCCCCHHHHHHHH	24.09	-
1116	Phosphorylation	DGPHSALYTMMKDQY CCCCHHHHHHHHHHH	7.72	-
1117	Phosphorylation	GPHSALYTMMKDQYA CCCHHHHHHHHHHHH	16.19	-

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 PUM1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
715	S	Phosphorylation	-
Following growth factor stimulation phosphorylated at Ser-715, promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.
715	S	Phosphorylation	-
Phosphorylation at Ser-715 promotes RNA-binding activity.

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 PUM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PUM1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PUM1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-124, AND MASSSPECTROMETRY.	19144319 [Abstract]
"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-710, AND MASSSPECTROMETRY.	19367708 [Abstract]

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