dbPTM

PUM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PUM2_HUMAN
UniProt AC	Q8TB72
Protein Name	Pumilio homolog 2
Gene Name	PUM2
Organism	Homo sapiens (Human).
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 NANO
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) (, PubMed:21397187). 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. [PubMed: 22955276 Also mediates deadenylation-independent repression by promoting accessibility of miRNAs]
Protein Sequence	MNHDFQALALESRGMGELLPTKKFWEPDDSTKDGQKGIFLGDDEWRETAWGASHHSMSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQVISEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	GMGELLPTKKFWEPD CCCCCCCCCCCCCCC	47.00	22964224
22	Acetylation	MGELLPTKKFWEPDD CCCCCCCCCCCCCCC	43.99	26051181
32	Ubiquitination	WEPDDSTKDGQKGIF CCCCCCCCCCCCCEE	64.91	-
53	Phosphorylation	RETAWGASHHSMSQP HHHCCCCCCCCCCCC	20.14	27080861
56	Phosphorylation	AWGASHHSMSQPIMV CCCCCCCCCCCCEEE	18.07	27080861
58	Phosphorylation	GASHHSMSQPIMVQR CCCCCCCCCCEEEEE	35.50	27732954
58 (in isoform 3)	Phosphorylation	-	35.50	24719451
67	Phosphorylation	PIMVQRRSGQGFHGN CEEEEECCCCCCCCC	37.34	30266825
67 (in isoform 3)	Phosphorylation	-	37.34	24719451
75	Phosphorylation	GQGFHGNSEVNAILS CCCCCCCCCCCEEEC	47.73	30266825
75 (in isoform 3)	Phosphorylation	-	47.73	27251275
82	Phosphorylation	SEVNAILSPRSESGG CCCCEEECCCCCCCC	16.50	22167270
82 (in isoform 3)	Phosphorylation	-	16.50	24719451
85	O-linked_Glycosylation	NAILSPRSESGGLGV CEEECCCCCCCCCCH	39.23	30059200
85	Phosphorylation	NAILSPRSESGGLGV CEEECCCCCCCCCCH	39.23	22167270
87	Phosphorylation	ILSPRSESGGLGVSM EECCCCCCCCCCHHH	39.13	22167270
87 (in isoform 3)	Phosphorylation	-	39.13	27251275
93	Phosphorylation	ESGGLGVSMVEYVLS CCCCCCHHHEEHHHH	18.47	22167270
97	Phosphorylation	LGVSMVEYVLSSSPA CCHHHEEHHHHCCCH	8.69	22167270
100	Phosphorylation	SMVEYVLSSSPADKL HHEEHHHHCCCHHHH	20.80	22167270
101	Phosphorylation	MVEYVLSSSPADKLD HEEHHHHCCCHHHHH	35.86	22167270
101 (in isoform 3)	Phosphorylation	-	35.86	24719451
102	Phosphorylation	VEYVLSSSPADKLDS EEHHHHCCCHHHHHH	22.26	22167270
102 (in isoform 3)	Phosphorylation	-	22.26	27251275
109	Phosphorylation	SPADKLDSRFRKGNF CCHHHHHHHHCCCCC	43.70	30278072
128	Acetylation	AETDGPEKGDQKGKA CCCCCCCCCCCCCCC	71.56	26051181
136	Phosphorylation	GDQKGKASPFEEDQN CCCCCCCCCCCCHHC	33.34	29255136
136 (in isoform 3)	Phosphorylation	-	33.34	24719451
175	Phosphorylation	DCKDFNRTPGSRQAS CCCCCCCCCCCCCCC	32.86	23401153
175 (in isoform 3)	Phosphorylation	-	32.86	24719451
178	Phosphorylation	DFNRTPGSRQASPTE CCCCCCCCCCCCHHH	23.56	25159151
178 (in isoform 3)	Phosphorylation	-	23.56	24719451
182	Phosphorylation	TPGSRQASPTEVVER CCCCCCCCHHHHHHH	24.82	19664994
182 (in isoform 3)	Phosphorylation	-	24.82	24719451
184	Phosphorylation	GSRQASPTEVVERLG CCCCCCHHHHHHHHC	38.63	22167270
184 (in isoform 3)	Phosphorylation	-	38.63	-
396	Phosphorylation	GAGQRPLTPNQGQQG CCCCCCCCCCCCCHH	23.91	27273156
408	Phosphorylation	QQGQQAESLAAAAAA CHHHHHHHHHHHHHH	26.73	26074081
432	Phosphorylation	LATGMPGYQVLAPTA HHCCCCCCEEECCEE	6.92	28464451
454	Methylation	LVVGPGARTGLGAPV EEECCCCCCCCCCCC	34.93	81452739
462	Methylation	TGLGAPVRLMAPTPV CCCCCCCEEECCCCE	20.07	26493963
540	Ubiquitination	SQSSSLFSHGPGQPG CCCCCCCCCCCCCCC	32.59	-
587	Phosphorylation	SSATRRESLSTSSDL CHHHHHHHCCCCHHH	26.30	29255136
587 (in isoform 3)	Phosphorylation	-	26.30	24719451
589	Phosphorylation	ATRRESLSTSSDLYK HHHHHHCCCCHHHHH	35.21	29255136
590	Phosphorylation	TRRESLSTSSDLYKR HHHHHCCCCHHHHHH	37.23	29255136
591	Phosphorylation	RRESLSTSSDLYKRS HHHHCCCCHHHHHHC	20.62	23403867
592	Phosphorylation	RESLSTSSDLYKRSS HHHCCCCHHHHHHCC	31.55	23927012
593 (in isoform 2)	Ubiquitination	-	54.51	21890473
595	Phosphorylation	LSTSSDLYKRSSSSL CCCCHHHHHHCCCCC	14.89	-
596	Ubiquitination	STSSDLYKRSSSSLA CCCHHHHHHCCCCCC	53.77	21906983
596 (in isoform 1)	Ubiquitination	-	53.77	21890473
596 (in isoform 3)	Ubiquitination	-	53.77	21890473
616	Acetylation	FYNSLGFSSSPSPIG CHHCCCCCCCCCCCC	28.27	19608861
616	Phosphorylation	FYNSLGFSSSPSPIG CHHCCCCCCCCCCCC	28.27	26074081
616	Ubiquitination	FYNSLGFSSSPSPIG CHHCCCCCCCCCCCC	28.27	19608861
617	Phosphorylation	YNSLGFSSSPSPIGM HHCCCCCCCCCCCCC	43.96	26074081
618	Phosphorylation	NSLGFSSSPSPIGMP HCCCCCCCCCCCCCC	28.35	26074081
620	Phosphorylation	LGFSSSPSPIGMPLP CCCCCCCCCCCCCCC	30.97	26074081
628	Phosphorylation	PIGMPLPSQTPGHSL CCCCCCCCCCCCCCC	55.13	26074081
630	Phosphorylation	GMPLPSQTPGHSLTP CCCCCCCCCCCCCCC	35.26	26074081
634	Phosphorylation	PSQTPGHSLTPPPSL CCCCCCCCCCCCCCC	39.59	26074081
636	Phosphorylation	QTPGHSLTPPPSLSS CCCCCCCCCCCCCCC	36.44	26074081
640	Phosphorylation	HSLTPPPSLSSHGSS CCCCCCCCCCCCCCC	46.81	26074081
642	Phosphorylation	LTPPPSLSSHGSSSS CCCCCCCCCCCCCCC	25.32	26074081
643	Phosphorylation	TPPPSLSSHGSSSSL CCCCCCCCCCCCCCE	36.84	26074081
646	Phosphorylation	PSLSSHGSSSSLHLG CCCCCCCCCCCEECC	22.94	26074081
647	Phosphorylation	SLSSHGSSSSLHLGG CCCCCCCCCCEECCC	28.65	26074081
648	Phosphorylation	LSSHGSSSSLHLGGL CCCCCCCCCEECCCC	38.32	26074081
649	Phosphorylation	SSHGSSSSLHLGGLT CCCCCCCCEECCCCC	23.04	26074081
662	Phosphorylation	LTNGSGRYISAAPGA CCCCCCCEEECCCCC	11.62	28152594
664	Phosphorylation	NGSGRYISAAPGAEA CCCCCEEECCCCCCE	14.94	28442448
672	Ubiquitination	AAPGAEAKYRSASST CCCCCCEEECCCCCC	32.47	21890473
672	Acetylation	AAPGAEAKYRSASST CCCCCCEEECCCCCC	32.47	19608861
672	Ubiquitination	AAPGAEAKYRSASST CCCCCCEEECCCCCC	32.47	19608861
672 (in isoform 1)	Ubiquitination	-	32.47	21890473
672 (in isoform 3)	Acetylation	-	32.47	-
672 (in isoform 3)	Ubiquitination	-	32.47	21890473
673	Phosphorylation	APGAEAKYRSASSTS CCCCCEEECCCCCCH	19.49	-
674	Methylation	PGAEAKYRSASSTSS CCCCEEECCCCCCHH	25.66	-
675	Phosphorylation	GAEAKYRSASSTSSL CCCEEECCCCCCHHH	29.43	23186163
677	Phosphorylation	EAKYRSASSTSSLFS CEEECCCCCCHHHCC	35.08	23186163
678	Phosphorylation	AKYRSASSTSSLFSS EEECCCCCCHHHCCC	31.83	23186163
679	Phosphorylation	KYRSASSTSSLFSSS EECCCCCCHHHCCCC	21.60	23186163
680	Phosphorylation	YRSASSTSSLFSSSS ECCCCCCHHHCCCCC	27.30	23186163
681	Phosphorylation	RSASSTSSLFSSSSQ CCCCCCHHHCCCCCC	33.26	28555341
684	Phosphorylation	SSTSSLFSSSSQLFP CCCHHHCCCCCCCCC	34.30	23186163
685	Phosphorylation	STSSLFSSSSQLFPP CCHHHCCCCCCCCCH	27.03	28985074
686	Phosphorylation	TSSLFSSSSQLFPPS CHHHCCCCCCCCCHH	22.39	23186163
687	Phosphorylation	SSLFSSSSQLFPPSR HHHCCCCCCCCCHHH	32.62	23917254
691	Ubiquitination	SSSSQLFPPSRLRYN CCCCCCCCHHHHCCC	34.25	-
693	Phosphorylation	SSQLFPPSRLRYNRS CCCCCCHHHHCCCHH	44.15	28985074
694	Methylation	SQLFPPSRLRYNRSD CCCCCHHHHCCCHHH	29.02	81452747
697	Phosphorylation	FPPSRLRYNRSDIMP CCHHHHCCCHHHCCC	21.37	28555341
700	Phosphorylation	SRLRYNRSDIMPSGR HHHCCCHHHCCCCCH	28.05	28348404
700 (in isoform 3)	Phosphorylation	-	28.05	24719451
705	Phosphorylation	NRSDIMPSGRSRLLE CHHHCCCCCHHHHHH	29.47	23186163
747	Ubiquitination	GSRFIQQKLERATPA HHHHHHHHHHHCCHH	35.62	-
762	Ubiquitination	ERQMVFNEILQAAYQ HHHHHHHHHHHHHHH	33.34	-
768	Phosphorylation	NEILQAAYQLMTDVF HHHHHHHHHHHHHHH	12.75	24043423
772	Phosphorylation	QAAYQLMTDVFGNYV HHHHHHHHHHHHHHH	37.29	24043423
778	Phosphorylation	MTDVFGNYVIQKFFE HHHHHHHHHHHHHHH	10.18	24043423
792	Ubiquitination	EFGSLDQKLALATRI HCCCHHHHHHHHHHH	35.08	-
818 (in isoform 3)	Ubiquitination	-	43.76	-
843	Ubiquitination	ELDGHVLKCVKDQNG HHCCCEEEEEECCCC	35.57	-
846	Ubiquitination	GHVLKCVKDQNGNHV CCEEEEEECCCCCCH	64.17	-
856	Ubiquitination	NGNHVVQKCIECVQP CCCCHHHHHHHHHCC	26.10	-
885 (in isoform 2)	Ubiquitination	-	22.66	21890473
906	Ubiquitination	AEQTLPILEELHQHT HHHHHHHHHHHHHHH	3.85	-
940	Acetylation	GRPEDKSKIVSEIRG CCCCCHHHHHHHHHH	53.52	25953088
956	Acetylation	VLALSQHKFASNVVE HHHHHHHHHHHHHHH	34.68	26051181
962 (in isoform 3)	Ubiquitination	-	7.33	21890473
964	Ubiquitination	FASNVVEKCVTHASR HHHHHHHHHHHHHHH	23.54	2190698
964 (in isoform 1)	Ubiquitination	-	23.54	21890473
988	Ubiquitination	VCCQNDGPHSALYTM HHCCCCCCCHHHHHH	22.56	-
990	Phosphorylation	CQNDGPHSALYTMMK CCCCCCCHHHHHHHH	24.09	27732954
993	Phosphorylation	DGPHSALYTMMKDQY CCCCHHHHHHHHHHH	7.72	27732954
994	Phosphorylation	GPHSALYTMMKDQYA CCCHHHHHHHHHHHH	16.19	27732954
1000	Phosphorylation	YTMMKDQYANYVVQK HHHHHHHHHHHHHHH	13.62	-
1003	Phosphorylation	MKDQYANYVVQKMID HHHHHHHHHHHHHHH	8.20	28152594
1023	Acetylation	QRKIIMHKIRPHITT HHHHHHHHHHCCHHH	24.03	25953088
1029	Phosphorylation	HKIRPHITTLRKYTY HHHHCCHHHCHHHCC	19.42	23312004
1030	Phosphorylation	KIRPHITTLRKYTYG HHHCCHHHCHHHCCH	24.78	23312004
1034	Phosphorylation	HITTLRKYTYGKHIL CHHHCHHHCCHHHHH	9.96	-
1036	Phosphorylation	TTLRKYTYGKHILAK HHCHHHCCHHHHHHH	22.53	-
1046	Ubiquitination	HILAKLEKYYLKNSP HHHHHHHHHHHHCCC	50.02	-
1047	Phosphorylation	ILAKLEKYYLKNSPD HHHHHHHHHHHCCCC	12.49	27690223
1048	Phosphorylation	LAKLEKYYLKNSPDL HHHHHHHHHHCCCCC	23.44	27690223
1050 (in isoform 3)	Phosphorylation	-	38.98	24719451
1052	Phosphorylation	EKYYLKNSPDLGPIG HHHHHHCCCCCCCCC	20.43	25159151

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PUM2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PUM2_HUMAN	PUM2	physical	12690449
NANO1_HUMAN	NANOS1	physical	12690449
AURKA_HUMAN	AURKA	physical	21589936
DAZL_HUMAN	DAZL	physical	12511597
NANO3_HUMAN	NANOS3	physical	18089289

Drug and Disease Associations

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

Regulatory Network of PUM2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-672, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136; SER-182 ANDTHR-184, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-182, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136; SER-178;SER-182; THR-184 AND SER-587, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.	15302935 [Abstract]