| UniProt ID | PAN2_HUMAN | |
|---|---|---|
| UniProt AC | Q504Q3 | |
| Protein Name | PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000255|HAMAP-Rule:MF_03182} | |
| Gene Name | PAN2 {ECO:0000255|HAMAP-Rule:MF_03182} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1202 | |
| Subcellular Localization | Cytoplasm . Cytoplasm, P-body . Nucleus . Shuttles between nucleus and cytoplasm. | |
| Protein Description | Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation.. | |
| Protein Sequence | MNFEGLDPGLAEYAPAMHSALDPVLDAHLNPSLLQNVELDPEGVALEALPVQESVHIMEGVYSELHSVVAEVGVPVSVSHFDLHEEMLWVGSHGGHATSFFGPALERYSSFQVNGSDDIRQIQSLENGILFLTKNNLKYMARGGLIIFDYLLDENEDMHSLLLTDSSTLLVGGLQNHIIEIDLNTVQETQKYAVETPGVTIMRQTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVHGNLLAACGFSSRLTGLACDRFLKVYDLRMMRAITPLQVHVDPAFLRFIPTYTSRLAIISQSGQCQFCEPTGLANPADIFHVNPVGPLLMTFDVSASKQALAFGDSEGCVHLWTDSPEPSFNPYSRETEFALPCLVDSLPPLDWSQDLLPLSLIPVPLTTDTLLSDWPAANSAPAPRRAPPVDAEILRTMKKVGFIGYAPNPRTRLRNQIPYRLKESDSEFDSFSQVTESPVGREEEPHLHMVSKKYRKVTIKYSKLGLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHLCQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASALGLILADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQAYRGAGGSSFCSSGDSVIGQLFSCEMENCSLCRCGSETVRASSTLLFTLSYPDGSKSDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSKEADFWRMQAEVAFKMAVKKHGGEISKNKEFALADWKELGSPEGVLVCPSIEELKNVWLPFSIRMKMTKNKGLDVCNWTDGDEMQWGPARAEEEHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHQRKEGVTHQQWYLFNDFLIEPIDKHEAVQFDMNWKVPAILYYVKRNLNSRYNLNIKNPIEASVLLAEASLARKQRKTHTTFIPLMLNEMPQIGDLVGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKISSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETHDSIEDARTALQLYRKYLELSKNGTEPESFHKVLKGLYEKGRKMDWKVPEPEGQTSPKNAAVFSSVLAL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 134 | Ubiquitination | NGILFLTKNNLKYMA CCEEEEECCCHHHHH | 46.08 | - | |
| 259 | Phosphorylation | CGFSSRLTGLACDRF CCCCHHHHHHHHHHH | 29.10 | 23312004 | |
| 265 | Methylation | LTGLACDRFLKVYDL HHHHHHHHHHHHHHH | 38.39 | 115919649 | |
| 268 | Ubiquitination | LACDRFLKVYDLRMM HHHHHHHHHHHHHHH | 35.72 | - | |
| 422 | Methylation | NSAPAPRRAPPVDAE CCCCCCCCCCCCCHH | 50.84 | 115919653 | |
| 432 | Methylation | PVDAEILRTMKKVGF CCCHHHHHHHHHHCC | 38.13 | 115919657 | |
| 433 | Phosphorylation | VDAEILRTMKKVGFI CCHHHHHHHHHHCCE | 29.87 | 28555341 | |
| 436 | Ubiquitination | EILRTMKKVGFIGYA HHHHHHHHHCCEEEC | 36.45 | - | |
| 459 | Ubiquitination | NQIPYRLKESDSEFD CCCCCCCCCCCCCCC | 46.29 | - | |
| 461 | Phosphorylation | IPYRLKESDSEFDSF CCCCCCCCCCCCCCC | 44.86 | 20873877 | |
| 463 | Phosphorylation | YRLKESDSEFDSFSQ CCCCCCCCCCCCCCC | 49.82 | 20873877 | |
| 467 | Phosphorylation | ESDSEFDSFSQVTES CCCCCCCCCCCCCCC | 31.92 | 20873877 | |
| 469 | Phosphorylation | DSEFDSFSQVTESPV CCCCCCCCCCCCCCC | 27.91 | 30266825 | |
| 472 | Phosphorylation | FDSFSQVTESPVGRE CCCCCCCCCCCCCCC | 24.10 | 30266825 | |
| 474 | Phosphorylation | SFSQVTESPVGREEE CCCCCCCCCCCCCCC | 18.60 | 25849741 | |
| 488 | Phosphorylation | EPHLHMVSKKYRKVT CCCCHHCCCCCCEEE | 18.82 | - | |
| 500 | Ubiquitination | KVTIKYSKLGLEDFD EEEEEEHHCCCCCCC | 43.41 | - | |
| 509 | Ubiquitination | GLEDFDFKHYNKTLF CCCCCCCCCCCCCHH | 47.20 | - | |
| 637 | Phosphorylation | ELEIPQAYRGAGGSS HCCCCCHHCCCCCCC | 12.34 | 27642862 | |
| 671 | Phosphorylation | CSLCRCGSETVRASS CCCCCCCCCEECCCC | 33.45 | - | |
| 673 | Phosphorylation | LCRCGSETVRASSTL CCCCCCCEECCCCEE | 19.59 | - | |
| 677 | Phosphorylation | GSETVRASSTLLFTL CCCEECCCCEEEEEE | 17.19 | 29396449 | |
| 678 | Phosphorylation | SETVRASSTLLFTLS CCEECCCCEEEEEEE | 23.30 | 29396449 | |
| 679 | Phosphorylation | ETVRASSTLLFTLSY CEECCCCEEEEEEEC | 25.61 | 29396449 | |
| 683 | Phosphorylation | ASSTLLFTLSYPDGS CCCEEEEEEECCCCC | 18.11 | 29396449 | |
| 685 | Phosphorylation | STLLFTLSYPDGSKS CEEEEEEECCCCCCC | 31.40 | 29396449 | |
| 690 | Phosphorylation | TLSYPDGSKSDKTGK EEECCCCCCCCCCCC | 36.04 | 29396449 | |
| 699 | Phosphorylation | SDKTGKNYDFAQVLK CCCCCCCCCHHHHHH | 18.87 | 25159151 | |
| 702 | Ubiquitination | TGKNYDFAQVLKRSI CCCCCCHHHHHHHHH | 8.82 | 21890473 | |
| 702 (in isoform 2) | Ubiquitination | - | 8.82 | 21890473 | |
| 705 | Ubiquitination | NYDFAQVLKRSICLD CCCHHHHHHHHHHCC | 2.25 | 21890473 | |
| 705 (in isoform 3) | Ubiquitination | - | 2.25 | 21890473 | |
| 706 (in isoform 1) | Ubiquitination | - | 45.29 | 21890473 | |
| 706 | Ubiquitination | YDFAQVLKRSICLDQ CCHHHHHHHHHHCCC | 45.29 | 22817900 | |
| 724 | Ubiquitination | AWCDTCEKYQPTIQT HHHHHHHHHCCCCCC | 51.86 | - | |
| 728 | Phosphorylation | TCEKYQPTIQTRNIR HHHHHCCCCCCCCCC | 15.36 | - | |
| 731 | Phosphorylation | KYQPTIQTRNIRHLP HHCCCCCCCCCCCCC | 23.10 | - | |
| 765 | Ubiquitination | MQAEVAFKMAVKKHG HHHHHHHHHHHHHCC | 19.06 | - | |
| 769 | Ubiquitination | VAFKMAVKKHGGEIS HHHHHHHHHCCCCCC | 29.52 | - | |
| 779 | Ubiquitination | GGEISKNKEFALADW CCCCCCCCCEEECCH | 58.93 | - | |
| 787 | Ubiquitination | EFALADWKELGSPEG CEEECCHHHHCCCCC | 43.54 | - | |
| 791 | Phosphorylation | ADWKELGSPEGVLVC CCHHHHCCCCCEEEC | 32.19 | 25159151 | |
| 800 | Phosphorylation | EGVLVCPSIEELKNV CCEEECCCHHHHHCC | 37.19 | 29396449 | |
| 816 | Acetylation | LPFSIRMKMTKNKGL ECCEEEEECCCCCCC | 33.30 | 7494163 | |
| 862 | Phosphorylation | TVVHILDSRTGGSLV EEEHHHHCCCCCEEE | 28.44 | 24275569 | |
| 882 | Acetylation | GETYHQRKEGVTHQQ CCCCCCCCCCCCHHH | 52.85 | 7960969 | |
| 935 | Ubiquitination | SRYNLNIKNPIEASV CCCCCCCCCHHHHHH | 56.44 | - | |
| 956 | Phosphorylation | LARKQRKTHTTFIPL HHHHHCCCCCCHHHH | 27.00 | 27174698 | |
| 958 | Phosphorylation | RKQRKTHTTFIPLML HHHCCCCCCHHHHHH | 28.74 | 27174698 | |
| 959 | Phosphorylation | KQRKTHTTFIPLMLN HHCCCCCCHHHHHHH | 16.38 | 27174698 | |
| 983 | Phosphorylation | GLDAEFVTLNEEEAE CCCCEEEECCHHHHH | 29.23 | 27174698 | |
| 993 | Ubiquitination | EEEAELRSDGTKSTI HHHHHHHCCCCCCCC | 53.68 | 24816145 | |
| 996 | Ubiquitination | AELRSDGTKSTIKPS HHHHCCCCCCCCCHH | 27.15 | 24816145 | |
| 997 | Ubiquitination | ELRSDGTKSTIKPSQ HHHCCCCCCCCCHHH | 51.65 | 24816145 | |
| 1001 | Ubiquitination | DGTKSTIKPSQMSVA CCCCCCCCHHHCEEE | 38.41 | - | |
| 1003 | Phosphorylation | TKSTIKPSQMSVARI CCCCCCHHHCEEEEE | 33.25 | 24719451 | |
| 1011 | Phosphorylation | QMSVARITCVRGQGP HCEEEEEEEECCCCC | 10.21 | 24719451 | |
| 1028 | Phosphorylation | GIPFIDDYISTQEQV CCCCHHHHCCCHHHH | 7.94 | 18083107 | |
| 1038 | Phosphorylation | TQEQVVDYLTQYSGI CHHHHHHHHHHCCCC | 10.47 | 18083107 | |
| 1042 | Phosphorylation | VVDYLTQYSGIKPGD HHHHHHHCCCCCCCC | 12.02 | 18083107 | |
| 1057 | Ubiquitination | LDAKISSKHLTTLKS CCHHHCCCCHHHCHH | 35.52 | - | |
| 1063 | Ubiquitination | SKHLTTLKSTYLKLR CCCHHHCHHHHHHHH | 38.36 | - | |
| 1116 | Phosphorylation | MPRKRMISLRFLAWY CCCHHHHHHHHHHHH | 12.26 | 22210691 | |
| 1149 | Ubiquitination | TALQLYRKYLELSKN HHHHHHHHHHHHHCC | 40.40 | - | |
| 1168 | Ubiquitination | ESFHKVLKGLYEKGR HHHHHHHHHHHHCCC | 50.27 | - | |
| 1185 | Phosphorylation | DWKVPEPEGQTSPKN CCCCCCCCCCCCCCH | 63.37 | 32142685 | |
| 1188 | Phosphorylation | VPEPEGQTSPKNAAV CCCCCCCCCCCHHHH | 58.83 | 29255136 | |
| 1189 | Phosphorylation | PEPEGQTSPKNAAVF CCCCCCCCCCHHHHH | 26.45 | 23401153 |
| 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 PAN2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PAN2_HUMAN !! | ||||||
* 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 PAN2_HUMAN !! | ||||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-1189, AND MASSSPECTROMETRY. | |
| "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-791, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189, AND MASSSPECTROMETRY. | |
