| UniProt ID | CDC73_HUMAN | |
|---|---|---|
| UniProt AC | Q6P1J9 | |
| Protein Name | Parafibromin | |
| Gene Name | CDC73 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 531 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors.. | |
| Protein Sequence | MADVLSVLRQYNIQKKEIVVKGDEVIFGEFSWPKNVKTNYVVWGTGKEGQPREYYTLDSILFLLNNVHLSHPVYVRRAATENIPVVRRPDRKDLLGYLNGEASTSASIDRSAPLEIGLQRSTQVKRAADEVLAEAKKPRIEDEECVRLDKERLAARLEGHKEGIVQTEQIRSLSEAMSVEKIAAIKAKIMAKKRSTIKTDLDDDITALKQRSFVDAEVDVTRDIVSRERVWRTRTTILQSTGKNFSKNIFAILQSVKAREEGRAPEQRPAPNAAPVDPTLRTKQPIPAAYNRYDQERFKGKEETEGFKIDTMGTYHGMTLKSVTEGASARKTQTPAAQPVPRPVSQARPPPNQKKGSRTPIIIIPAATTSLITMLNAKDLLQDLKFVPSDEKKKQGCQRENETLIQRRKDQMQPGGTAISVTVPYRVVDQPLKLMPQDWDRVVAVFVQGPAWQFKGWPWLLPDGSPVDIFAKIKAFHLKYDEVRLDPNVQKWDVTVLELSYHKRHLDRPVFLRFWETLDRYMVKHKSHLRF | |
| 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 | ------MADVLSVLR ------CHHHHHHHH | 18.67 | 22223895 | |
| 6 | Phosphorylation | --MADVLSVLRQYNI --CHHHHHHHHHCCC | 20.96 | 21406692 | |
| 11 | Phosphorylation | VLSVLRQYNIQKKEI HHHHHHHCCCCCCEE | 14.06 | 27762562 | |
| 34 | Sumoylation | FGEFSWPKNVKTNYV EEECCCCCCCCCCEE | 69.02 | - | |
| 34 | Ubiquitination | FGEFSWPKNVKTNYV EEECCCCCCCCCCEE | 69.02 | 29967540 | |
| 47 | Ubiquitination | YVVWGTGKEGQPREY EEEECCCCCCCCCEE | 59.51 | - | |
| 47 | Acetylation | YVVWGTGKEGQPREY EEEECCCCCCCCCEE | 59.51 | 26051181 | |
| 80 | Phosphorylation | VYVRRAATENIPVVR HHHHCCCCCCCCEEC | 28.69 | - | |
| 105 | Phosphorylation | LNGEASTSASIDRSA HCCCCCCCCCCCCCC | 19.95 | 18452278 | |
| 136 | Ubiquitination | DEVLAEAKKPRIEDE HHHHHHHCCCCCCCH | 55.61 | 33845483 | |
| 136 | Sumoylation | DEVLAEAKKPRIEDE HHHHHHHCCCCCCCH | 55.61 | - | |
| 137 | Acetylation | EVLAEAKKPRIEDEE HHHHHHCCCCCCCHH | 46.72 | 25953088 | |
| 137 | Ubiquitination | EVLAEAKKPRIEDEE HHHHHHCCCCCCCHH | 46.72 | - | |
| 150 | Acetylation | EECVRLDKERLAARL HHHHHCCHHHHHHHH | 49.69 | 26051181 | |
| 150 | Ubiquitination | EECVRLDKERLAARL HHHHHCCHHHHHHHH | 49.69 | - | |
| 161 | Sumoylation | AARLEGHKEGIVQTE HHHHHHHHCCCCCHH | 69.37 | - | |
| 161 | Sumoylation | AARLEGHKEGIVQTE HHHHHHHHCCCCCHH | 69.37 | - | |
| 161 | Ubiquitination | AARLEGHKEGIVQTE HHHHHHHHCCCCCHH | 69.37 | 21963094 | |
| 161 | Acetylation | AARLEGHKEGIVQTE HHHHHHHHCCCCCHH | 69.37 | 26051181 | |
| 172 | Phosphorylation | VQTEQIRSLSEAMSV CCHHHHHHHHHCCCH | 37.57 | 20068231 | |
| 174 | Phosphorylation | TEQIRSLSEAMSVEK HHHHHHHHHCCCHHH | 25.26 | 20068231 | |
| 178 | Phosphorylation | RSLSEAMSVEKIAAI HHHHHCCCHHHHHHH | 33.89 | 25159151 | |
| 181 | Ubiquitination | SEAMSVEKIAAIKAK HHCCCHHHHHHHHHH | 35.17 | 21906983 | |
| 186 | Ubiquitination | VEKIAAIKAKIMAKK HHHHHHHHHHHHHHC | 38.61 | 22817900 | |
| 198 | Sumoylation | AKKRSTIKTDLDDDI HHCCCCCCCCCCCHH | 35.75 | 28112733 | |
| 198 | Ubiquitination | AKKRSTIKTDLDDDI HHCCCCCCCCCCCHH | 35.75 | 29967540 | |
| 198 | Sumoylation | AKKRSTIKTDLDDDI HHCCCCCCCCCCCHH | 35.75 | - | |
| 198 | Acetylation | AKKRSTIKTDLDDDI HHCCCCCCCCCCCHH | 35.75 | 26051181 | |
| 209 | Ubiquitination | DDDITALKQRSFVDA CCHHHHHHHHHCCCC | 41.00 | 23000965 | |
| 209 | 2-Hydroxyisobutyrylation | DDDITALKQRSFVDA CCHHHHHHHHHCCCC | 41.00 | - | |
| 212 | Phosphorylation | ITALKQRSFVDAEVD HHHHHHHHCCCCEEE | 27.42 | 30266825 | |
| 221 | Phosphorylation | VDAEVDVTRDIVSRE CCCEEEEHHHHHHHH | 20.40 | 29396449 | |
| 234 | Methylation | RERVWRTRTTILQST HHHHHHHHHHHHHHC | 22.69 | - | |
| 235 | Phosphorylation | ERVWRTRTTILQSTG HHHHHHHHHHHHHCC | 19.99 | 20068231 | |
| 236 | Phosphorylation | RVWRTRTTILQSTGK HHHHHHHHHHHHCCC | 19.19 | 20068231 | |
| 240 | Phosphorylation | TRTTILQSTGKNFSK HHHHHHHHCCCCHHH | 35.36 | 20068231 | |
| 241 | Phosphorylation | RTTILQSTGKNFSKN HHHHHHHCCCCHHHH | 38.93 | 20068231 | |
| 243 | Ubiquitination | TILQSTGKNFSKNIF HHHHHCCCCHHHHHH | 55.71 | 23000965 | |
| 243 | Acetylation | TILQSTGKNFSKNIF HHHHHCCCCHHHHHH | 55.71 | 25953088 | |
| 246 | Phosphorylation | QSTGKNFSKNIFAIL HHCCCCHHHHHHHHH | 33.90 | - | |
| 247 | Ubiquitination | STGKNFSKNIFAILQ HCCCCHHHHHHHHHH | 50.34 | 23000965 | |
| 255 | Phosphorylation | NIFAILQSVKAREEG HHHHHHHHHHHHHCC | 23.34 | 24173317 | |
| 257 | Ubiquitination | FAILQSVKAREEGRA HHHHHHHHHHHCCCC | 47.15 | 21963094 | |
| 282 | Phosphorylation | PVDPTLRTKQPIPAA CCCCCCCCCCCCCCC | 36.82 | 22210691 | |
| 283 | Sumoylation | VDPTLRTKQPIPAAY CCCCCCCCCCCCCCC | 47.87 | - | |
| 283 | Sumoylation | VDPTLRTKQPIPAAY CCCCCCCCCCCCCCC | 47.87 | - | |
| 283 | Methylation | VDPTLRTKQPIPAAY CCCCCCCCCCCCCCC | 47.87 | - | |
| 283 | Ubiquitination | VDPTLRTKQPIPAAY CCCCCCCCCCCCCCC | 47.87 | 24816145 | |
| 290 | Phosphorylation | KQPIPAAYNRYDQER CCCCCCCCHHHCHHH | 11.41 | 21726809 | |
| 293 | Phosphorylation | IPAAYNRYDQERFKG CCCCCHHHCHHHHCC | 20.52 | 21726809 | |
| 299 | Ubiquitination | RYDQERFKGKEETEG HHCHHHHCCCCCCCC | 75.25 | 29967540 | |
| 301 | Ubiquitination | DQERFKGKEETEGFK CHHHHCCCCCCCCCE | 53.63 | 33845483 | |
| 301 | Sumoylation | DQERFKGKEETEGFK CHHHHCCCCCCCCCE | 53.63 | - | |
| 301 | Sumoylation | DQERFKGKEETEGFK CHHHHCCCCCCCCCE | 53.63 | 28112733 | |
| 308 | Sumoylation | KEETEGFKIDTMGTY CCCCCCCEEECCEEE | 50.99 | 28112733 | |
| 314 | O-linked_Glycosylation | FKIDTMGTYHGMTLK CEEECCEEECCEEEE | 11.09 | 30379171 | |
| 315 | Phosphorylation | KIDTMGTYHGMTLKS EEECCEEECCEEEEH | 7.22 | 25159151 | |
| 319 | Phosphorylation | MGTYHGMTLKSVTEG CEEECCEEEEHHHCC | 35.31 | 22985185 | |
| 321 | Ubiquitination | TYHGMTLKSVTEGAS EECCEEEEHHHCCCC | 33.44 | 32015554 | |
| 321 | Sumoylation | TYHGMTLKSVTEGAS EECCEEEEHHHCCCC | 33.44 | 28112733 | |
| 331 | Ubiquitination | TEGASARKTQTPAAQ HCCCCCCCCCCCCCC | 44.71 | 24816145 | |
| 331 | Methylation | TEGASARKTQTPAAQ HCCCCCCCCCCCCCC | 44.71 | - | |
| 332 | Phosphorylation | EGASARKTQTPAAQP CCCCCCCCCCCCCCC | 31.93 | 23312004 | |
| 334 | Phosphorylation | ASARKTQTPAAQPVP CCCCCCCCCCCCCCC | 21.81 | 23312004 | |
| 345 | Phosphorylation | QPVPRPVSQARPPPN CCCCCCHHHCCCCCC | 22.32 | 28555341 | |
| 354 | Ubiquitination | ARPPPNQKKGSRTPI CCCCCCCCCCCCCCE | 66.78 | 29967540 | |
| 357 | Phosphorylation | PPNQKKGSRTPIIII CCCCCCCCCCCEEEE | 41.69 | 22210691 | |
| 359 | Phosphorylation | NQKKGSRTPIIIIPA CCCCCCCCCEEEEEC | 22.12 | 22210691 | |
| 385 | Sumoylation | KDLLQDLKFVPSDEK HHHHHHCCCCCCHHH | 53.24 | - | |
| 385 | Ubiquitination | KDLLQDLKFVPSDEK HHHHHHCCCCCCHHH | 53.24 | 29967540 | |
| 385 | Acetylation | KDLLQDLKFVPSDEK HHHHHHCCCCCCHHH | 53.24 | 26051181 | |
| 392 | 2-Hydroxyisobutyrylation | KFVPSDEKKKQGCQR CCCCCHHHHHHCCCH | 70.97 | - | |
| 392 | Acetylation | KFVPSDEKKKQGCQR CCCCCHHHHHHCCCH | 70.97 | 25953088 | |
| 393 | Acetylation | FVPSDEKKKQGCQRE CCCCHHHHHHCCCHH | 48.56 | 25953088 | |
| 420 | O-linked_Glycosylation | QPGGTAISVTVPYRV CCCCEEEEEEEEEEE | 14.85 | 30379171 | |
| 422 | Phosphorylation | GGTAISVTVPYRVVD CCEEEEEEEEEEECC | 14.69 | 22210691 | |
| 425 | Phosphorylation | AISVTVPYRVVDQPL EEEEEEEEEECCCCH | 16.23 | 22210691 | |
| 433 | Acetylation | RVVDQPLKLMPQDWD EECCCCHHCCCCCHH | 49.80 | 26051181 | |
| 455 | Sumoylation | QGPAWQFKGWPWLLP ECCCCCCCCCCCCCC | 44.99 | - | |
| 465 | Phosphorylation | PWLLPDGSPVDIFAK CCCCCCCCCCCHHHE | 29.18 | 28348404 | |
| 479 | Acetylation | KIKAFHLKYDEVRLD EEEEEECCCCEEECC | 41.93 | 27452117 | |
| 479 | Ubiquitination | KIKAFHLKYDEVRLD EEEEEECCCCEEECC | 41.93 | 29967540 | |
| 495 | Phosphorylation | NVQKWDVTVLELSYH CCCCEEEEEEEHHHH | 19.53 | 20068231 | |
| 500 | Phosphorylation | DVTVLELSYHKRHLD EEEEEEHHHHHHHCC | 18.80 | 20068231 | |
| 501 | Phosphorylation | VTVLELSYHKRHLDR EEEEEHHHHHHHCCC | 24.80 | 20068231 | |
| 520 | Methylation | RFWETLDRYMVKHKS HHHHHHHHHHHHCHH | 25.26 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC73_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 CDC73_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 145000 | Familial isolated hyperparathyroidism (FIHP) | |||||
| 145001 | Hyperparathyroidism-jaw tumor syndrome (HPT-JT) | |||||
| 608266 | Parathyroid carcinoma (PRTC) | |||||
| 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 |
| "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-212, AND MASSSPECTROMETRY. | |
| "Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-178, ANDMASS SPECTROMETRY. | |
