| UniProt ID | NU145_YEAST | |
|---|---|---|
| UniProt AC | P49687 | |
| Protein Name | Nucleoporin NUP145 | |
| Gene Name | NUP145 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1317 | |
| Subcellular Localization |
Nucleoporin NUP145C: Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein Cytoplasmic side. Nucleus membrane Peripheral membrane protein Nucleoplasmic side. Symmetrically distributed on the cytoplasmic and nucleoplasmic sid |
|
| Protein Description | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization.. | |
| Protein Sequence | MFNKSVNSGFTFGNQNTSTPTSTPAQPSSSLQFPQKSTGLFGNVNVNANTSTPSPSGGLFNANSNANSISQQPANNSLFGNKPAQPSGGLFGATNNTTSKSAGSLFGNNNATANSTGSTGLFSGSNNIASSTQNGGLFGNSNNNNITSTTQNGGLFGKPTTTPAGAGGLFGNSSSTNSTTGLFGSNNTQSSTGIFGQKPGASTTGGLFGNNGASFPRSGETTGTMSTNPYGINISNVPMAVADMPRSITSSLSDVNGKSDAEPKPIENRRTYSFSSSVSGNAPLPLASQSSLVSRLSTRLKATQKSTSPNEIFSPSYSKPWLNGAGSAPLVDDFFSSKMTSLAPNENSIFPQNGFNFLSSQRADLTELRKLKIDSNRSAAKKLKLLSGTPAITKKHMQDEQDSSENEPIANADSVTNIDRKENRDNNLDNTYLNGKEQSNNLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAAVSNFVIGRRGYGCITFQHDVDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKKTKKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFSIWGLVNEEDAEIDEDDLSKQEDGGEQPLRKVRTLAQSKPSDKEVILKTDGTFGTLSGKDDSIVEEKAYEPDLSDADFEGIEASPKLDVSKDWVEQLILAGSSLRSVFATSKEFDGPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEIEKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVSQIGPEIEEKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSIDKNISKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKFSLPYDDPIGVIFQLYAANENTEKLYKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMREITLLRASTNDHILNRLKIPSQLIFNAQALKDRYEGNYLSEVQNLLLGSSYDLAEMAIVTSLGPRLLLSNNPVQNNELKTLREILNEFPDSERDKWSVSINVFEVYLKLVLDNVETQETIDSLISGMKIFYDQYKHCREVAACCNVMSQEIVSKILEKNNPSIGDSKAKLLELPLGQPEKAYLRGEFAQDLMKCTYKI | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MFNKSVNSGFTF ---CCCCCCCCCCCC | 27.86 | 21551504 | |
| 8 | Phosphorylation | MFNKSVNSGFTFGNQ CCCCCCCCCCCCCCC | 32.88 | 21551504 | |
| 17 | Phosphorylation | FTFGNQNTSTPTSTP CCCCCCCCCCCCCCC | 24.98 | 28889911 | |
| 18 | Phosphorylation | TFGNQNTSTPTSTPA CCCCCCCCCCCCCCC | 39.68 | 21440633 | |
| 21 | Phosphorylation | NQNTSTPTSTPAQPS CCCCCCCCCCCCCCC | 45.37 | 21440633 | |
| 22 | Phosphorylation | QNTSTPTSTPAQPSS CCCCCCCCCCCCCCC | 33.33 | 21551504 | |
| 23 | Phosphorylation | NTSTPTSTPAQPSSS CCCCCCCCCCCCCCC | 25.73 | 28132839 | |
| 218 | Phosphorylation | NGASFPRSGETTGTM CCCCCCCCCCCCCCC | 41.02 | 19779198 | |
| 222 | Phosphorylation | FPRSGETTGTMSTNP CCCCCCCCCCCCCCC | 26.76 | 19779198 | |
| 224 | Phosphorylation | RSGETTGTMSTNPYG CCCCCCCCCCCCCCC | 13.07 | 19779198 | |
| 247 | Phosphorylation | AVADMPRSITSSLSD EECCCCCCHHHCHHC | 25.09 | 28889911 | |
| 249 | Phosphorylation | ADMPRSITSSLSDVN CCCCCCHHHCHHCCC | 17.32 | 22369663 | |
| 250 | Phosphorylation | DMPRSITSSLSDVNG CCCCCHHHCHHCCCC | 27.84 | 22369663 | |
| 251 | Phosphorylation | MPRSITSSLSDVNGK CCCCHHHCHHCCCCC | 24.20 | 22369663 | |
| 253 | Phosphorylation | RSITSSLSDVNGKSD CCHHHCHHCCCCCCC | 41.27 | 22369663 | |
| 271 | Phosphorylation | KPIENRRTYSFSSSV CCCCCCCEEEECCCC | 21.93 | 22369663 | |
| 272 | Phosphorylation | PIENRRTYSFSSSVS CCCCCCEEEECCCCC | 13.10 | 22369663 | |
| 273 | Phosphorylation | IENRRTYSFSSSVSG CCCCCEEEECCCCCC | 20.31 | 22369663 | |
| 275 | Phosphorylation | NRRTYSFSSSVSGNA CCCEEEECCCCCCCC | 18.76 | 22369663 | |
| 276 | Phosphorylation | RRTYSFSSSVSGNAP CCEEEECCCCCCCCC | 32.52 | 22369663 | |
| 277 | Phosphorylation | RTYSFSSSVSGNAPL CEEEECCCCCCCCCC | 21.07 | 22369663 | |
| 279 | Phosphorylation | YSFSSSVSGNAPLPL EEECCCCCCCCCCCC | 28.42 | 21440633 | |
| 288 | Phosphorylation | NAPLPLASQSSLVSR CCCCCCCCHHHHHHH | 37.97 | 22369663 | |
| 290 | Phosphorylation | PLPLASQSSLVSRLS CCCCCCHHHHHHHHH | 24.12 | 22369663 | |
| 291 | Phosphorylation | LPLASQSSLVSRLST CCCCCHHHHHHHHHH | 25.75 | 22369663 | |
| 294 | Phosphorylation | ASQSSLVSRLSTRLK CCHHHHHHHHHHHHH | 32.56 | 22369663 | |
| 306 | Phosphorylation | RLKATQKSTSPNEIF HHHHHCCCCCCCCCC | 25.05 | 22369663 | |
| 307 | Phosphorylation | LKATQKSTSPNEIFS HHHHCCCCCCCCCCC | 56.06 | 22369663 | |
| 308 | Phosphorylation | KATQKSTSPNEIFSP HHHCCCCCCCCCCCC | 32.59 | 22369663 | |
| 314 | Phosphorylation | TSPNEIFSPSYSKPW CCCCCCCCCCCCCCC | 20.71 | 22369663 | |
| 316 | Phosphorylation | PNEIFSPSYSKPWLN CCCCCCCCCCCCCCC | 40.62 | 22369663 | |
| 317 | Phosphorylation | NEIFSPSYSKPWLNG CCCCCCCCCCCCCCC | 24.89 | 28889911 | |
| 318 | Phosphorylation | EIFSPSYSKPWLNGA CCCCCCCCCCCCCCC | 36.26 | 22369663 | |
| 327 | Phosphorylation | PWLNGAGSAPLVDDF CCCCCCCCCCCHHHH | 26.61 | 21551504 | |
| 359 | Phosphorylation | QNGFNFLSSQRADLT CCCCCHHHHCCCCHH | 21.93 | 30377154 | |
| 387 | Phosphorylation | AKKLKLLSGTPAITK HHHHHHHHCCCCHHH | 51.57 | 21440633 | |
| 389 | Phosphorylation | KLKLLSGTPAITKKH HHHHHHCCCCHHHHH | 13.23 | 21440633 | |
| 394 | Acetylation | SGTPAITKKHMQDEQ HCCCCHHHHHCCCCC | 34.27 | 25381059 | |
| 403 | Phosphorylation | HMQDEQDSSENEPIA HCCCCCCCCCCCCCC | 38.97 | 19823750 | |
| 404 | Phosphorylation | MQDEQDSSENEPIAN CCCCCCCCCCCCCCC | 53.37 | 25521595 | |
| 414 | Phosphorylation | EPIANADSVTNIDRK CCCCCCCCCCCCCCC | 28.56 | 25704821 | |
| 416 | Phosphorylation | IANADSVTNIDRKEN CCCCCCCCCCCCCCC | 30.34 | 24961812 | |
| 431 | Phosphorylation | RDNNLDNTYLNGKEQ CCCCCCCCCCCCHHH | 29.11 | 21440633 | |
| 439 | Phosphorylation | YLNGKEQSNNLNKQD CCCCHHHCCCCCCCC | 28.86 | 28889911 | |
| 450 | Phosphorylation | NKQDGENTLQHEKSS CCCCCCCCCCCCCCC | 24.40 | 25704821 | |
| 474 | Phosphorylation | PEQLERLSLKQLAAV HHHHHHCCHHHHHHH | 39.48 | 27738172 | |
| 590 | Phosphorylation | MREMNYISYNPFGGT HHHCCCEEECCCCCE | 14.43 | 28889911 | |
| 591 | Phosphorylation | REMNYISYNPFGGTW HHCCCEEECCCCCEE | 19.80 | 28889911 | |
| 597 | Phosphorylation | SYNPFGGTWTFKVNH EECCCCCEEEEEECE | 23.01 | 28889911 | |
| 599 | Phosphorylation | NPFGGTWTFKVNHFS CCCCCEEEEEECEEE | 17.26 | 28889911 | |
| 639 | Phosphorylation | QPLRKVRTLAQSKPS CCHHHHHHHHHCCCC | 29.45 | 21440633 | |
| 643 | Phosphorylation | KVRTLAQSKPSDKEV HHHHHHHCCCCCCEE | 40.71 | 19823750 | |
| 646 | Phosphorylation | TLAQSKPSDKEVILK HHHHCCCCCCEEEEE | 66.12 | 19823750 | |
| 654 | Phosphorylation | DKEVILKTDGTFGTL CCEEEEEECCCCCCC | 35.89 | 19795423 | |
| 657 | Phosphorylation | VILKTDGTFGTLSGK EEEEECCCCCCCCCC | 23.00 | 28152593 | |
| 660 | Phosphorylation | KTDGTFGTLSGKDDS EECCCCCCCCCCCCC | 17.35 | 23749301 | |
| 662 | Phosphorylation | DGTFGTLSGKDDSIV CCCCCCCCCCCCCHH | 43.57 | 22369663 | |
| 664 | Ubiquitination | TFGTLSGKDDSIVEE CCCCCCCCCCCHHHH | 55.79 | 23749301 | |
| 667 | Phosphorylation | TLSGKDDSIVEEKAY CCCCCCCCHHHHHHC | 38.37 | 22369663 | |
| 674 | Phosphorylation | SIVEEKAYEPDLSDA CHHHHHHCCCCCCCC | 38.78 | 22369663 | |
| 679 | Phosphorylation | KAYEPDLSDADFEGI HHCCCCCCCCCCCCC | 37.83 | 22369663 | |
| 689 | Phosphorylation | DFEGIEASPKLDVSK CCCCCCCCCCCCCCH | 15.13 | 25521595 | |
| 695 | Phosphorylation | ASPKLDVSKDWVEQL CCCCCCCCHHHHHHH | 25.27 | 20377248 | |
| 751 | Phosphorylation | IMKERRFTASYTFAK HHHHCCEEEEEEEEE | 16.94 | 22369663 | |
| 754 | Phosphorylation | ERRFTASYTFAKFST HCCEEEEEEEEEECC | 11.92 | 19779198 | |
| 755 | Phosphorylation | RRFTASYTFAKFSTG CCEEEEEEEEEECCC | 18.02 | 19779198 | |
| 763 | Phosphorylation | FAKFSTGSMLLTKDI EEEECCCCEEEEECC | 13.32 | 21440633 | |
| 855 | Acetylation | DPVSYPYKTDNDQVK CCCCCCCCCCCHHHH | 44.92 | 24489116 | |
| 1068 | Phosphorylation | QTLRFNGTRVFSKET HHHCCCCEEEECCCC | 25.43 | 28889911 | |
| 1198 | Ubiquitination | PVQNNELKTLREILN CCCCCHHHHHHHHHH | 39.06 | 23749301 | |
| 1299 | Acetylation | LPLGQPEKAYLRGEF CCCCCHHHHHHCHHH | 49.35 | 24489116 | |
| 1299 | Ubiquitination | LPLGQPEKAYLRGEF CCCCCHHHHHHCHHH | 49.35 | 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 NU145_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NU145_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 NU145_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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-247; SER-251; THR-271;SER-273; SER-403; SER-404; SER-667; SER-679; SER-689 AND THR-751, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-404 ANDSER-667, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND SER-689, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND MASSSPECTROMETRY. | |
