UniProt ID | UNK_HUMAN | |
---|---|---|
UniProt AC | Q9C0B0 | |
Protein Name | RING finger protein unkempt homolog | |
Gene Name | UNK | |
Organism | Homo sapiens (Human). | |
Sequence Length | 810 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes. [PubMed: 25737280] | |
Protein Sequence | MSKGPGPGGSAASSAPPAATAQVLQAQPEKPQHYTYLKEFRTEQCPLFVQHKCTQHRPYTCFHWHFVNQRRRRSIRRRDGTFNYSPDVYCTKYDEATGLCPEGDECPFLHRTTGDTERRYHLRYYKTGICIHETDSKGNCTKNGLHCAFAHGPHDLRSPVYDIRELQAMEALQNGQTTVEGSIEGQSAGAASHAMIEKILSEEPRWQETAYVLGNYKTEPCKKPPRLCRQGYACPYYHNSKDRRRSPRKHKYRSSPCPNVKHGDEWGDPGKCENGDACQYCHTRTEQQFHPEIYKSTKCNDMQQSGSCPRGPFCAFAHVEQPPLSDDLQPSSAVSSPTQPGPVLYMPSAAGDSVPVSPSSPHAPDLSALLCRNSSLGSPSNLCGSPPGSIRKPPNLEGIVFPGESGLAPGSYKKAPGFEREDQVGAEYLKNFKCQAKLKPHSLEPRSQEQPLLQPKQDMLGILPAGSPLTSSISSSITSSLAATPPSPVGTSSVPGMNANALPFYPTSDTVESVIESALDDLDLNEFGVAALEKTFDNSTVPHPGSITIGGSLLQSSAPVNIPGSLGSSASFHSASPSPPVSLSSHFLQQPQGHLSQSENTFLGTSASHGSLGLNGMNSSIWEHFASGSFSPGTSPAFLSGPGAAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAGPEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKAVFHMQSVKCLKCQEQKRAVLPCQHAALCELCAEGSECPICQPGRAHTLQS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | O-linked_Glycosylation | ------MSKGPGPGG ------CCCCCCCCC | 46.44 | 23301498 | |
13 | Phosphorylation | GPGGSAASSAPPAAT CCCCCCCCCCCCHHH | 27.09 | 24275569 | |
14 | Phosphorylation | PGGSAASSAPPAATA CCCCCCCCCCCHHHH | 39.82 | 24275569 | |
20 | Phosphorylation | SSAPPAATAQVLQAQ CCCCCHHHHHHHHCC | 21.52 | 28152594 | |
20 | O-linked_Glycosylation | SSAPPAATAQVLQAQ CCCCCHHHHHHHHCC | 21.52 | 23301498 | |
30 | Ubiquitination | VLQAQPEKPQHYTYL HHHCCCCCCCCEEEH | 57.57 | - | |
34 | Phosphorylation | QPEKPQHYTYLKEFR CCCCCCCEEEHHHHC | 7.57 | 28152594 | |
35 | Phosphorylation | PEKPQHYTYLKEFRT CCCCCCEEEHHHHCC | 21.91 | 28152594 | |
36 | Phosphorylation | EKPQHYTYLKEFRTE CCCCCEEEHHHHCCC | 14.49 | 28152594 | |
38 | Ubiquitination | PQHYTYLKEFRTEQC CCCEEEHHHHCCCCC | 44.38 | - | |
38 | Acetylation | PQHYTYLKEFRTEQC CCCEEEHHHHCCCCC | 44.38 | 26051181 | |
85 | Phosphorylation | RDGTFNYSPDVYCTK CCCCCCCCCCEEEEC | 18.74 | 28674419 | |
134 | Phosphorylation | TGICIHETDSKGNCT CCEEEEECCCCCCCC | 31.26 | 28348404 | |
136 | Phosphorylation | ICIHETDSKGNCTKN EEEEECCCCCCCCCC | 50.29 | 28985074 | |
158 | Phosphorylation | HGPHDLRSPVYDIRE CCCCCCCCCCCCHHH | 26.47 | 21815630 | |
201 | Phosphorylation | AMIEKILSEEPRWQE HHHHHHHCCCCCHHH | 43.30 | 24719451 | |
232 | Phosphorylation | PRLCRQGYACPYYHN CHHCCCCCCCCCCCC | 9.19 | 28152594 | |
236 | Phosphorylation | RQGYACPYYHNSKDR CCCCCCCCCCCCCCC | 19.76 | 25884760 | |
237 | Phosphorylation | QGYACPYYHNSKDRR CCCCCCCCCCCCCCC | 4.62 | 23927012 | |
240 | Phosphorylation | ACPYYHNSKDRRRSP CCCCCCCCCCCCCCC | 23.71 | 23401153 | |
246 | Phosphorylation | NSKDRRRSPRKHKYR CCCCCCCCCCCCCCC | 27.52 | 17081983 | |
252 | Phosphorylation | RSPRKHKYRSSPCPN CCCCCCCCCCCCCCC | 18.56 | 28985074 | |
254 | Phosphorylation | PRKHKYRSSPCPNVK CCCCCCCCCCCCCCC | 35.23 | 28450419 | |
255 | Phosphorylation | RKHKYRSSPCPNVKH CCCCCCCCCCCCCCC | 22.86 | 28450419 | |
295 | Ubiquitination | QFHPEIYKSTKCNDM CCCHHHHHCCCCCCC | 58.26 | - | |
295 | Acetylation | QFHPEIYKSTKCNDM CCCHHHHHCCCCCCC | 58.26 | 26051181 | |
353 | Phosphorylation | MPSAAGDSVPVSPSS CCCCCCCCCCCCCCC | 27.66 | 26074081 | |
357 | Phosphorylation | AGDSVPVSPSSPHAP CCCCCCCCCCCCCCC | 17.00 | 26074081 | |
359 | Phosphorylation | DSVPVSPSSPHAPDL CCCCCCCCCCCCCCH | 49.33 | 26074081 | |
360 | Phosphorylation | SVPVSPSSPHAPDLS CCCCCCCCCCCCCHH | 24.88 | 26074081 | |
374 | Phosphorylation | SALLCRNSSLGSPSN HHHHCCCCCCCCHHH | 13.95 | 23927012 | |
375 | Phosphorylation | ALLCRNSSLGSPSNL HHHCCCCCCCCHHHC | 40.06 | 25159151 | |
378 | Phosphorylation | CRNSSLGSPSNLCGS CCCCCCCCHHHCCCC | 30.37 | 23927012 | |
380 | Phosphorylation | NSSLGSPSNLCGSPP CCCCCCHHHCCCCCC | 44.10 | 30278072 | |
385 | Phosphorylation | SPSNLCGSPPGSIRK CHHHCCCCCCCCCCC | 27.25 | 19664994 | |
389 | Phosphorylation | LCGSPPGSIRKPPNL CCCCCCCCCCCCCCC | 25.62 | 22167270 | |
392 | Ubiquitination | SPPGSIRKPPNLEGI CCCCCCCCCCCCCCC | 64.26 | - | |
405 | Phosphorylation | GIVFPGESGLAPGSY CCCCCCCCCCCCCCC | 45.05 | 23312004 | |
411 | Phosphorylation | ESGLAPGSYKKAPGF CCCCCCCCCCCCCCC | 32.49 | 30576142 | |
412 | Phosphorylation | SGLAPGSYKKAPGFE CCCCCCCCCCCCCCC | 23.56 | 16094384 | |
413 | Ubiquitination | GLAPGSYKKAPGFER CCCCCCCCCCCCCCC | 44.12 | - | |
413 | Acetylation | GLAPGSYKKAPGFER CCCCCCCCCCCCCCC | 44.12 | 25953088 | |
414 | Ubiquitination | LAPGSYKKAPGFERE CCCCCCCCCCCCCCC | 52.13 | - | |
428 | Phosphorylation | EDQVGAEYLKNFKCQ CHHHCHHHHHHCCCC | 23.57 | 29978859 | |
430 | Ubiquitination | QVGAEYLKNFKCQAK HHCHHHHHHCCCCEE | 60.48 | - | |
439 | Ubiquitination | FKCQAKLKPHSLEPR CCCCEECCCCCCCCC | 39.72 | - | |
442 | Phosphorylation | QAKLKPHSLEPRSQE CEECCCCCCCCCCCC | 42.85 | 28555341 | |
447 | Phosphorylation | PHSLEPRSQEQPLLQ CCCCCCCCCCCCCCC | 49.11 | 28450419 | |
565 | O-linked_Glycosylation | APVNIPGSLGSSASF CCCCCCCCCCCCCCC | 24.97 | 23301498 | |
576 | O-linked_Glycosylation | SASFHSASPSPPVSL CCCCCCCCCCCCCCC | 29.00 | 23301498 | |
596 | Phosphorylation | QQPQGHLSQSENTFL HCCCCCCCCCCCCEE | 26.45 | 26074081 | |
598 | Phosphorylation | PQGHLSQSENTFLGT CCCCCCCCCCCEECC | 29.45 | 26074081 | |
605 | Phosphorylation | SENTFLGTSASHGSL CCCCEECCCCCCCCC | 24.22 | 26074081 | |
606 | Phosphorylation | ENTFLGTSASHGSLG CCCEECCCCCCCCCC | 26.44 | 26074081 | |
608 | Phosphorylation | TFLGTSASHGSLGLN CEECCCCCCCCCCCC | 28.31 | 26074081 | |
611 | Phosphorylation | GTSASHGSLGLNGMN CCCCCCCCCCCCCCC | 17.53 | 26074081 | |
627 | Phosphorylation | SIWEHFASGSFSPGT HHHHHHHCCCCCCCC | 33.74 | 26074081 | |
629 | Phosphorylation | WEHFASGSFSPGTSP HHHHHCCCCCCCCCC | 21.76 | 26074081 | |
631 | Phosphorylation | HFASGSFSPGTSPAF HHHCCCCCCCCCCHH | 24.90 | 26074081 | |
634 | Phosphorylation | SGSFSPGTSPAFLSG CCCCCCCCCCHHHCC | 34.62 | 26074081 | |
635 | Phosphorylation | GSFSPGTSPAFLSGP CCCCCCCCCHHHCCC | 21.83 | 26074081 | |
669 | Ubiquitination | KQWEESWKQAKQACD HHHHHHHHHHHHHHH | 50.05 | - | |
669 | Acetylation | KQWEESWKQAKQACD HHHHHHHHHHHHHHH | 50.05 | 25953088 | |
672 | Ubiquitination | EESWKQAKQACDAWK HHHHHHHHHHHHHHH | 35.61 | - | |
744 | Phosphorylation | ALSLSTLYSLQKQLR HHCHHHHHHHHHHHH | 13.86 | - |
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 UNK_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UNK_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 UNK_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-374; SER-375; SER-378AND SER-385, AND MASS SPECTROMETRY. | |
"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-378 AND SER-385, ANDMASS SPECTROMETRY. | |
"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-385, AND MASSSPECTROMETRY. | |
"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-385, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-412, AND MASSSPECTROMETRY. |