| UniProt ID | PABP_YEAST | |
|---|---|---|
| UniProt AC | P04147 | |
| Protein Name | Polyadenylate-binding protein, cytoplasmic and nuclear | |
| Gene Name | PAB1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 577 | |
| Subcellular Localization | Cytoplasm. Nucleus. Predominantly cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm. Can be exported from the nucleus through at least 2 distinct pathways, the main being dependent on the exportin CRM1, and the second requiring MEX6 | |
| Protein Description | Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.. | |
| Protein Sequence | MADITDKTAEQLENLNIQDDQKQAATGSESQSVENSSASLYVGDLEPSVSEAHLYDIFSPIGSVSSIRVCRDAITKTSLGYAYVNFNDHEAGRKAIEQLNYTPIKGRLCRIMWSQRDPSLRKKGSGNIFIKNLHPDIDNKALYDTFSVFGDILSSKIATDENGKSKGFGFVHFEEEGAAKEAIDALNGMLLNGQEIYVAPHLSRKERDSQLEETKAHYTNLYVKNINSETTDEQFQELFAKFGPIVSASLEKDADGKLKGFGFVNYEKHEDAVKAVEALNDSELNGEKLYVGRAQKKNERMHVLKKQYEAYRLEKMAKYQGVNLFVKNLDDSVDDEKLEEEFAPYGTITSAKVMRTENGKSKGFGFVCFSTPEEATKAITEKNQQIVAGKPLYVAIAQRKDVRRSQLAQQIQARNQMRYQQATAAAAAAAAGMPGQFMPPMFYGVMPPRGVPFNGPNPQQMNPMGGMPKNGMPPQFRNGPVYGVPPQGGFPRNANDNNQFYQQKQRQALGEQLYKKVSAKTSNEEAAGKITGMILDLPPQEVFPLLESDELFEQHYKEASAAYESFKKEQEQQTEQA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MADITDKTA ------CCCCCHHHH | 19.53 | 9298649 | |
| 5 | Phosphorylation | ---MADITDKTAEQL ---CCCCCHHHHHHH | 31.80 | 24961812 | |
| 7 | Acetylation | -MADITDKTAEQLEN -CCCCCHHHHHHHHC | 40.77 | 23572591 | |
| 7 | Ubiquitination | -MADITDKTAEQLEN -CCCCCHHHHHHHHC | 40.77 | 22106047 | |
| 8 | Phosphorylation | MADITDKTAEQLENL CCCCCHHHHHHHHCC | 37.93 | 28889911 | |
| 22 | Ubiquitination | LNIQDDQKQAATGSE CCCCCHHHHHHCCCC | 49.23 | 17644757 | |
| 26 | Phosphorylation | DDQKQAATGSESQSV CHHHHHHCCCCCCCC | 44.23 | 30377154 | |
| 63 | Phosphorylation | DIFSPIGSVSSIRVC HCCCCCCCCCHHEEC | 21.39 | 28889911 | |
| 76 | Ubiquitination | VCRDAITKTSLGYAY ECHHHCCCCCCEEEE | 29.97 | 23749301 | |
| 94 | Ubiquitination | NDHEAGRKAIEQLNY CCHHHHHHHHHHCCC | 53.44 | 23749301 | |
| 94 | Acetylation | NDHEAGRKAIEQLNY CCHHHHHHHHHHCCC | 53.44 | 24489116 | |
| 101 | Phosphorylation | KAIEQLNYTPIKGRL HHHHHCCCCCCCCEE | 23.61 | 30377154 | |
| 102 | Phosphorylation | AIEQLNYTPIKGRLC HHHHCCCCCCCCEEH | 19.91 | 22369663 | |
| 105 | Ubiquitination | QLNYTPIKGRLCRIM HCCCCCCCCEEHHHH | 38.90 | 23749301 | |
| 105 | Succinylation | QLNYTPIKGRLCRIM HCCCCCCCCEEHHHH | 38.90 | 23954790 | |
| 105 | Acetylation | QLNYTPIKGRLCRIM HCCCCCCCCEEHHHH | 38.90 | 24489116 | |
| 105 | 2-Hydroxyisobutyrylation | QLNYTPIKGRLCRIM HCCCCCCCCEEHHHH | 38.90 | - | |
| 107 | Methylation | NYTPIKGRLCRIMWS CCCCCCCEEHHHHHH | 26.13 | 23865587 | |
| 114 | Phosphorylation | RLCRIMWSQRDPSLR EEHHHHHHCCCHHHH | 9.65 | 22369663 | |
| 119 | Phosphorylation | MWSQRDPSLRKKGSG HHHCCCHHHHCCCCC | 45.13 | 22369663 | |
| 125 | Phosphorylation | PSLRKKGSGNIFIKN HHHHCCCCCCEEEEC | 37.23 | 22369663 | |
| 131 | Acetylation | GSGNIFIKNLHPDID CCCCEEEECCCCCCC | 42.58 | 24489116 | |
| 164 | Ubiquitination | IATDENGKSKGFGFV EEECCCCCCCCEEEE | 61.65 | 23749301 | |
| 166 | Ubiquitination | TDENGKSKGFGFVHF ECCCCCCCCEEEEEE | 62.84 | 22817900 | |
| 203 | Phosphorylation | IYVAPHLSRKERDSQ EEECCCCCHHHHHHH | 37.97 | 21440633 | |
| 209 | Phosphorylation | LSRKERDSQLEETKA CCHHHHHHHHHHHHH | 42.77 | 27214570 | |
| 215 | 2-Hydroxyisobutyrylation | DSQLEETKAHYTNLY HHHHHHHHHHHHHEE | 36.12 | - | |
| 215 | Acetylation | DSQLEETKAHYTNLY HHHHHHHHHHHHHEE | 36.12 | 24489116 | |
| 215 | Ubiquitination | DSQLEETKAHYTNLY HHHHHHHHHHHHHEE | 36.12 | 24961812 | |
| 224 | Acetylation | HYTNLYVKNINSETT HHHHEEEECCCCCCC | 38.25 | 24489116 | |
| 224 | Ubiquitination | HYTNLYVKNINSETT HHHHEEEECCCCCCC | 38.25 | 17644757 | |
| 241 | Ubiquitination | QFQELFAKFGPIVSA HHHHHHHHHCCCEEE | 43.44 | 17644757 | |
| 247 | Phosphorylation | AKFGPIVSASLEKDA HHHCCCEEEEECCCC | 16.92 | 27214570 | |
| 249 | Phosphorylation | FGPIVSASLEKDADG HCCCEEEEECCCCCC | 29.56 | 21440633 | |
| 252 | Ubiquitination | IVSASLEKDADGKLK CEEEEECCCCCCCCE | 64.61 | 23749301 | |
| 252 | Acetylation | IVSASLEKDADGKLK CEEEEECCCCCCCCE | 64.61 | 24489116 | |
| 257 | 2-Hydroxyisobutyrylation | LEKDADGKLKGFGFV ECCCCCCCCEEEEEE | 47.80 | - | |
| 257 | Acetylation | LEKDADGKLKGFGFV ECCCCCCCCEEEEEE | 47.80 | 24489116 | |
| 259 | 2-Hydroxyisobutyrylation | KDADGKLKGFGFVNY CCCCCCCEEEEEECC | 56.53 | - | |
| 259 | Acetylation | KDADGKLKGFGFVNY CCCCCCCEEEEEECC | 56.53 | 24489116 | |
| 268 | Ubiquitination | FGFVNYEKHEDAVKA EEEECCCCHHHHHHH | 41.77 | 24961812 | |
| 268 | Acetylation | FGFVNYEKHEDAVKA EEEECCCCHHHHHHH | 41.77 | 24489116 | |
| 274 | Acetylation | EKHEDAVKAVEALND CCHHHHHHHHHHCCC | 48.73 | 24489116 | |
| 288 | Ubiquitination | DSELNGEKLYVGRAQ CHHCCCCEEECCCHH | 46.66 | 23749301 | |
| 288 | Acetylation | DSELNGEKLYVGRAQ CHHCCCCEEECCCHH | 46.66 | 24489116 | |
| 305 | Ubiquitination | NERMHVLKKQYEAYR HHHHHHHHHHHHHHH | 36.42 | 22817900 | |
| 306 | Ubiquitination | ERMHVLKKQYEAYRL HHHHHHHHHHHHHHH | 54.68 | 23749301 | |
| 315 | Acetylation | YEAYRLEKMAKYQGV HHHHHHHHHHHHHCC | 49.07 | 24489116 | |
| 318 | Ubiquitination | YRLEKMAKYQGVNLF HHHHHHHHHHCCCEE | 34.31 | 23749301 | |
| 318 | Acetylation | YRLEKMAKYQGVNLF HHHHHHHHHHCCCEE | 34.31 | 24489116 | |
| 327 | Acetylation | QGVNLFVKNLDDSVD HCCCEEEECCCCCCC | 44.45 | 24489116 | |
| 332 | Phosphorylation | FVKNLDDSVDDEKLE EEECCCCCCCHHHHH | 27.41 | 22369663 | |
| 337 | Ubiquitination | DDSVDDEKLEEEFAP CCCCCHHHHHHHHCC | 69.10 | 23749301 | |
| 337 | Acetylation | DDSVDDEKLEEEFAP CCCCCHHHHHHHHCC | 69.10 | 24489116 | |
| 345 | Phosphorylation | LEEEFAPYGTITSAK HHHHHCCCCEEEEEE | 24.38 | 22369663 | |
| 347 | Phosphorylation | EEFAPYGTITSAKVM HHHCCCCEEEEEEEE | 18.42 | 22369663 | |
| 349 | Phosphorylation | FAPYGTITSAKVMRT HCCCCEEEEEEEEEC | 23.59 | 22369663 | |
| 350 | Phosphorylation | APYGTITSAKVMRTE CCCCEEEEEEEEECC | 23.42 | 22369663 | |
| 352 | Acetylation | YGTITSAKVMRTENG CCEEEEEEEEECCCC | 36.01 | 24489116 | |
| 362 | Acetylation | RTENGKSKGFGFVCF ECCCCCCCCEEEEEE | 62.84 | 24489116 | |
| 368 | Glutathionylation | SKGFGFVCFSTPEEA CCCEEEEEECCHHHH | 1.76 | 22833525 | |
| 376 | Phosphorylation | FSTPEEATKAITEKN ECCHHHHHHHHHHHH | 25.04 | 21551504 | |
| 377 | Acetylation | STPEEATKAITEKNQ CCHHHHHHHHHHHHH | 44.85 | 24489116 | |
| 380 | Phosphorylation | EEATKAITEKNQQIV HHHHHHHHHHHHHHH | 45.85 | 21551504 | |
| 382 | Acetylation | ATKAITEKNQQIVAG HHHHHHHHHHHHHCC | 51.94 | 24489116 | |
| 382 | Ubiquitination | ATKAITEKNQQIVAG HHHHHHHHHHHHHCC | 51.94 | 17644757 | |
| 390 | Acetylation | NQQIVAGKPLYVAIA HHHHHCCCCEEEEEE | 23.32 | 24489116 | |
| 390 | Succinylation | NQQIVAGKPLYVAIA HHHHHCCCCEEEEEE | 23.32 | 23954790 | |
| 390 | Ubiquitination | NQQIVAGKPLYVAIA HHHHHCCCCEEEEEE | 23.32 | 17644757 | |
| 393 | Phosphorylation | IVAGKPLYVAIAQRK HHCCCCEEEEEECCH | 9.07 | 21082442 | |
| 400 | Ubiquitination | YVAIAQRKDVRRSQL EEEEECCHHHCHHHH | 48.79 | 17644757 | |
| 405 | Phosphorylation | QRKDVRRSQLAQQIQ CCHHHCHHHHHHHHH | 20.98 | 22369663 | |
| 469 | Ubiquitination | NPMGGMPKNGMPPQF CCCCCCCCCCCCCCC | 58.19 | 23749301 | |
| 504 | Acetylation | NNQFYQQKQRQALGE CCHHHHHHHHHHHHH | 31.74 | 22865919 | |
| 504 | Succinylation | NNQFYQQKQRQALGE CCHHHHHHHHHHHHH | 31.74 | 23954790 | |
| 504 | Ubiquitination | NNQFYQQKQRQALGE CCHHHHHHHHHHHHH | 31.74 | 23749301 | |
| 515 | Ubiquitination | ALGEQLYKKVSAKTS HHHHHHHHHHHCCCC | 56.12 | 22817900 | |
| 515 | Acetylation | ALGEQLYKKVSAKTS HHHHHHHHHHHCCCC | 56.12 | 24489116 | |
| 515 | Succinylation | ALGEQLYKKVSAKTS HHHHHHHHHHHCCCC | 56.12 | 23954790 | |
| 516 | Ubiquitination | LGEQLYKKVSAKTSN HHHHHHHHHHCCCCC | 28.06 | 22817900 | |
| 520 | Ubiquitination | LYKKVSAKTSNEEAA HHHHHHCCCCCHHHH | 45.00 | 23749301 | |
| 522 | Phosphorylation | KKVSAKTSNEEAAGK HHHHCCCCCHHHHHH | 41.35 | 23749301 | |
| 560 | Phosphorylation | EQHYKEASAAYESFK HHHHHHHHHHHHHHH | 17.96 | 23749301 | |
| 565 | Phosphorylation | EASAAYESFKKEQEQ HHHHHHHHHHHHHHH | 29.68 | 23749301 | |
| 567 | Ubiquitination | SAAYESFKKEQEQQT HHHHHHHHHHHHHHH | 65.76 | 24961812 | |
| 567 | Acetylation | SAAYESFKKEQEQQT HHHHHHHHHHHHHHH | 65.76 | 24489116 | |
| 567 | Succinylation | SAAYESFKKEQEQQT HHHHHHHHHHHHHHH | 65.76 | 23954790 | |
| 568 | Ubiquitination | AAYESFKKEQEQQTE HHHHHHHHHHHHHHH | 63.72 | 23749301 |
| 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 PABP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PABP_YEAST !! | ||||||
* 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 PABP_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT ALA-2. | |
| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-125; SER-249 ANDSER-405, AND MASS SPECTROMETRY. | |
