UniProt ID | SCML1_HUMAN | |
---|---|---|
UniProt AC | Q9UN30 | |
Protein Name | Sex comb on midleg-like protein 1 | |
Gene Name | SCML1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 329 | |
Subcellular Localization | Nucleus . | |
Protein Description | Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. May be involved in spermatogenesis during sexual maturation (By similarity).. | |
Protein Sequence | MMSNSSSEIDVIKTRIPTYDEDDNTILYAYETKPEFVNKEPNIVSDASCNTEEQLKTVDDVLIHCQVIYDALQNLDKKIDVIRRKVSKIQRFHARSLWTNHKRYGYKKHSYRLVKKLKLQKMKKNEVYETFSYPESYSPTLPVSRRENNSPSNLPRPSFCMEEYQRAELEEDPILSRTPSPVHPSDFSEHNCQPYYASDGATYGSSSGLCLGNPRADSIHNTYSTDHASAAPPSVTRSPVENDGYIEEGSITKHPSTWSVEAVVLFLKQTDPLALCPLVDLFRSHEIDGKALLLLTSDVLLKHLGVKLGTAVKLCYYIDRLKQGKCFEN | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | EIDVIKTRIPTYDED CCEEEECCCCCCCCC | 28.08 | 18669648 | |
17 | Phosphorylation | DVIKTRIPTYDEDDN EEEECCCCCCCCCCC | 22.93 | 18452278 | |
18 | Phosphorylation | VIKTRIPTYDEDDNT EEECCCCCCCCCCCE | 41.03 | - | |
19 | Phosphorylation | IKTRIPTYDEDDNTI EECCCCCCCCCCCEE | 16.39 | - | |
55 | Phosphorylation | SCNTEEQLKTVDDVL CCCHHHHHCCHHHHH | 5.93 | 18452278 | |
117 | Phosphorylation | SYRLVKKLKLQKMKK HHHHHHHHCHHHCCC | 5.77 | 18452278 | |
128 | Phosphorylation | KMKKNEVYETFSYPE HCCCCCCEECCCCCC | 11.76 | 29978859 | |
130 | Phosphorylation | KKNEVYETFSYPESY CCCCCEECCCCCCCC | 10.53 | 28348404 | |
132 | Phosphorylation | NEVYETFSYPESYSP CCCEECCCCCCCCCC | 47.39 | 28348404 | |
133 | Phosphorylation | EVYETFSYPESYSPT CCEECCCCCCCCCCC | 13.56 | 29978859 | |
136 | Phosphorylation | ETFSYPESYSPTLPV ECCCCCCCCCCCCCC | 26.80 | 28387310 | |
137 | Phosphorylation | TFSYPESYSPTLPVS CCCCCCCCCCCCCCC | 19.60 | 24626860 | |
138 | Phosphorylation | FSYPESYSPTLPVSR CCCCCCCCCCCCCCC | 22.23 | 21082442 | |
140 | Phosphorylation | YPESYSPTLPVSRRE CCCCCCCCCCCCCCC | 37.44 | 22496350 | |
144 | Phosphorylation | YSPTLPVSRRENNSP CCCCCCCCCCCCCCC | 24.55 | 22496350 | |
150 | Phosphorylation | VSRRENNSPSNLPRP CCCCCCCCCCCCCCC | 41.09 | 23663014 | |
152 | Phosphorylation | RRENNSPSNLPRPSF CCCCCCCCCCCCCCC | 51.31 | 23663014 | |
176 | Phosphorylation | LEEDPILSRTPSPVH HHCCCCCCCCCCCCC | 34.52 | 29255136 | |
218 | Phosphorylation | LGNPRADSIHNTYST CCCCCHHHCCCCCCC | 25.43 | 25002506 | |
222 | Phosphorylation | RADSIHNTYSTDHAS CHHHCCCCCCCCCCC | 12.51 | 25002506 | |
223 | Phosphorylation | ADSIHNTYSTDHASA HHHCCCCCCCCCCCC | 18.19 | 25002506 | |
224 | Phosphorylation | DSIHNTYSTDHASAA HHCCCCCCCCCCCCC | 25.89 | 25002506 | |
225 | Phosphorylation | SIHNTYSTDHASAAP HCCCCCCCCCCCCCC | 22.76 | 25002506 | |
229 | Phosphorylation | TYSTDHASAAPPSVT CCCCCCCCCCCCCCC | 22.88 | 25002506 | |
234 | Phosphorylation | HASAAPPSVTRSPVE CCCCCCCCCCCCCCC | 34.75 | 22496350 | |
236 | Phosphorylation | SAAPPSVTRSPVEND CCCCCCCCCCCCCCC | 29.75 | 19060867 | |
238 | Phosphorylation | APPSVTRSPVENDGY CCCCCCCCCCCCCCC | 24.75 | 21082442 | |
245 | Phosphorylation | SPVENDGYIEEGSIT CCCCCCCCCCCCCCC | 14.18 | 25002506 | |
250 | Phosphorylation | DGYIEEGSITKHPST CCCCCCCCCCCCCCC | 30.29 | 25002506 | |
252 | Phosphorylation | YIEEGSITKHPSTWS CCCCCCCCCCCCCCE | 25.62 | 25002506 | |
259 | Phosphorylation | TKHPSTWSVEAVVLF CCCCCCCEEEEEEEH | 15.35 | 24260401 | |
284 | Phosphorylation | PLVDLFRSHEIDGKA HHHHHHHHCCCCCHH | 20.38 | 24260401 | |
296 | Phosphorylation | GKALLLLTSDVLLKH CHHHHHHCHHHHHHH | 23.89 | 30301811 | |
297 | Phosphorylation | KALLLLTSDVLLKHL HHHHHHCHHHHHHHH | 26.20 | 30301811 |
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 SCML1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SCML1_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 SCML1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CDAC1_HUMAN | CDADC1 | physical | 27173435 | |
UH1BL_HUMAN | UHRF1BP1L | physical | 27173435 |
Kegg Disease | ||||||
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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 |
"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-138, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY. |