UniProt ID | SP130_HUMAN | |
---|---|---|
UniProt AC | Q9H0E3 | |
Protein Name | Histone deacetylase complex subunit SAP130 | |
Gene Name | SAP130 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1048 | |
Subcellular Localization | Nucleus . | |
Protein Description | Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes.. | |
Protein Sequence | MGPPRHPQAGEIEAGGAGGGRRLQVEMSSQQFPRLGAPSTGLSQAPSQIANSGSAGLINPAATVNDESGRDSEVSAREHMSSSSSLQSREEKQEPVVVRPYPQVQMLSTHHAVASATPVAVTAPPAHLTPAVPLSFSEGLMKPPPKPTMPSRPIAPAPPSTLSLPPKVPGQVTVTMESSIPQASAIPVATISGQQGHPSNLHHIMTTNVQMSIIRSNAPGPPLHIGASHLPRGAAAAAVMSSSKVTTVLRPTSQLPNAATAQPAVQHIIHQPIQSRPPVTTSNAIPPAVVATVSATRAQSPVITTTAAHATDSALSRPTLSIQHPPSAAISIQRPAQSRDVTTRITLPSHPALGTPKQQLHTMAQKTIFSTGTPVAAATVAPILATNTIPSATTAGSVSHTQAPTSTIVTMTVPSHSSHATAVTTSNIPVAKVVPQQITHTSPRIQPDYPAERSSLIPISGHRASPNPVAMETRSDNRPSVPVQFQYFLPTYPPSAYPLAAHTYTPITSSVSTIRQYPVSAQAPNSAITAQTGVGVASTVHLNPMQLMTVDASHARHIQGIQPAPISTQGIQPAPIGTPGIQPAPLGTQGIHSATPINTQGLQPAPMGTQQPQPEGKTSAVVLADGATIVANPISNPFSAAPAATTVVQTHSQSASTNAPAQGSSPRPSILRKKPATDGAKPKSEIHVSMATPVTVSMETVSNQNNDQPTIAVPPTAQQPPPTIPTMIAAASPPSQPAVALSTIPGAVPITPPITTIAAAPPPSVTVGGSLSSVLGPPVPEIKVKEEVEPMDIMRPVSAVPPLATNTVSPSLALLANNLSMPTSDLPPGASPRKKPRKQQHVISTEEGDMMETNSTDDEKSTAKSLLVKAEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYSDVRVKEEKKAMLQEIANQKGVSCRAQGWKVHLCAAQLLQLTNLEHDVYERLTNLQEGIIPKKKAATDDDLHRINELIQGNMQRCKLVMDQISEARDSMLKVLDHKDRVLKLLNKNGTVKKVSKLKRKEKV | |
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 |
---|---|---|---|---|---|
5 | Methylation | ---MGPPRHPQAGEI ---CCCCCCCCCCCE | 58.20 | 115493277 | |
29 | Phosphorylation | RLQVEMSSQQFPRLG EEEEEECCCCCCCCC | 27.04 | 22798277 | |
34 | Methylation | MSSQQFPRLGAPSTG ECCCCCCCCCCCCCC | 47.22 | 115388623 | |
63 | Phosphorylation | GLINPAATVNDESGR CCCCCCCCCCCCCCC | 23.19 | - | |
72 | Phosphorylation | NDESGRDSEVSAREH CCCCCCCCHHHHHHH | 38.24 | - | |
75 | Phosphorylation | SGRDSEVSAREHMSS CCCCCHHHHHHHHCC | 19.98 | 28985074 | |
83 | Phosphorylation | AREHMSSSSSLQSRE HHHHHCCCHHHCCHH | 19.35 | 28985074 | |
108 | O-linked_Glycosylation | YPQVQMLSTHHAVAS CCCCEECCCCCCHHC | 21.98 | 30059200 | |
122 | O-linked_Glycosylation | SATPVAVTAPPAHLT CCCCEEEECCCCCCC | 24.57 | 30059200 | |
129 | O-linked_Glycosylation | TAPPAHLTPAVPLSF ECCCCCCCCCCCCCC | 10.19 | 30059200 | |
148 | Phosphorylation | MKPPPKPTMPSRPIA CCCCCCCCCCCCCCC | 48.08 | 29449344 | |
151 | Phosphorylation | PPKPTMPSRPIAPAP CCCCCCCCCCCCCCC | 39.61 | 29449344 | |
226 (in isoform 2) | Phosphorylation | - | 15.41 | 21815630 | |
232 | Methylation | IGASHLPRGAAAAAV ECCCCCCHHHHHHHH | 54.46 | 24129315 | |
235 (in isoform 2) | Phosphorylation | - | 10.64 | 28176443 | |
236 (in isoform 2) | Phosphorylation | - | 8.74 | 28176443 | |
237 (in isoform 2) | Phosphorylation | - | 8.89 | 25849741 | |
239 (in isoform 2) | Phosphorylation | - | 3.07 | 26055452 | |
300 | Phosphorylation | VSATRAQSPVITTTA ECCCCCCCCEEEEEC | 21.83 | 29255136 | |
304 | Phosphorylation | RAQSPVITTTAAHAT CCCCCEEEEECCHHC | 20.51 | 30108239 | |
305 | O-linked_Glycosylation | AQSPVITTTAAHATD CCCCEEEEECCHHCC | 11.87 | 30059200 | |
305 | Phosphorylation | AQSPVITTTAAHATD CCCCEEEEECCHHCC | 11.87 | 30108239 | |
306 | O-linked_Glycosylation | QSPVITTTAAHATDS CCCEEEEECCHHCCC | 17.13 | 30059200 | |
306 | Phosphorylation | QSPVITTTAAHATDS CCCEEEEECCHHCCC | 17.13 | 30108239 | |
311 | Phosphorylation | TTTAAHATDSALSRP EEECCHHCCCHHCCC | 22.18 | 27251275 | |
313 | Phosphorylation | TAAHATDSALSRPTL ECCHHCCCHHCCCEE | 27.10 | 27251275 | |
316 | Phosphorylation | HATDSALSRPTLSIQ HHCCCHHCCCEEECC | 35.61 | 27251275 | |
319 | Phosphorylation | DSALSRPTLSIQHPP CCHHCCCEEECCCCC | 31.84 | 27251275 | |
321 | Phosphorylation | ALSRPTLSIQHPPSA HHCCCEEECCCCCCC | 23.76 | 27251275 | |
327 | O-linked_Glycosylation | LSIQHPPSAAISIQR EECCCCCCCEEEEEC | 34.48 | 30059200 | |
331 | O-linked_Glycosylation | HPPSAAISIQRPAQS CCCCCEEEEECCCCC | 14.14 | 30059200 | |
344 | Methylation | QSRDVTTRITLPSHP CCCCCCCEEECCCCC | 15.55 | 115493269 | |
346 | O-linked_Glycosylation | RDVTTRITLPSHPAL CCCCCEEECCCCCCC | 29.35 | 30059200 | |
346 | Phosphorylation | RDVTTRITLPSHPAL CCCCCEEECCCCCCC | 29.35 | 27251275 | |
349 | O-linked_Glycosylation | TTRITLPSHPALGTP CCEEECCCCCCCCCC | 45.26 | 30059200 | |
349 | Phosphorylation | TTRITLPSHPALGTP CCEEECCCCCCCCCC | 45.26 | 20068231 | |
355 | Phosphorylation | PSHPALGTPKQQLHT CCCCCCCCCHHHHHH | 28.32 | 21712546 | |
439 | Phosphorylation | KVVPQQITHTSPRIQ EECCCCCCCCCCCCC | 18.11 | 23927012 | |
441 | Phosphorylation | VPQQITHTSPRIQPD CCCCCCCCCCCCCCC | 31.60 | 30266825 | |
442 | Phosphorylation | PQQITHTSPRIQPDY CCCCCCCCCCCCCCC | 12.46 | 30266825 | |
444 | Methylation | QITHTSPRIQPDYPA CCCCCCCCCCCCCCC | 39.68 | 115493289 | |
453 | Methylation | QPDYPAERSSLIPIS CCCCCCHHCCCCCCC | 33.38 | 80702559 | |
454 | Phosphorylation | PDYPAERSSLIPISG CCCCCHHCCCCCCCC | 22.47 | 23927012 | |
455 | Phosphorylation | DYPAERSSLIPISGH CCCCHHCCCCCCCCC | 36.22 | 23927012 | |
460 | O-linked_Glycosylation | RSSLIPISGHRASPN HCCCCCCCCCCCCCC | 24.16 | 30059200 | |
460 | Phosphorylation | RSSLIPISGHRASPN HCCCCCCCCCCCCCC | 24.16 | 23927012 | |
463 | Methylation | LIPISGHRASPNPVA CCCCCCCCCCCCCEE | 40.04 | 115493281 | |
465 | Phosphorylation | PISGHRASPNPVAME CCCCCCCCCCCEEEE | 25.76 | 23401153 | |
471 | Sulfoxidation | ASPNPVAMETRSDNR CCCCCEEEEECCCCC | 5.71 | 21406390 | |
473 | Phosphorylation | PNPVAMETRSDNRPS CCCEEEEECCCCCCC | 23.53 | 23927012 | |
480 | O-linked_Glycosylation | TRSDNRPSVPVQFQY ECCCCCCCCCEEEEE | 35.50 | 30059200 | |
491 | O-linked_Glycosylation | QFQYFLPTYPPSAYP EEEEECCCCCCCCCC | 51.30 | 30059200 | |
495 | O-linked_Glycosylation | FLPTYPPSAYPLAAH ECCCCCCCCCCCCCE | 35.61 | 30059200 | |
503 | O-linked_Glycosylation | AYPLAAHTYTPITSS CCCCCCEECCCCCCC | 25.10 | 30059200 | |
505 | O-linked_Glycosylation | PLAAHTYTPITSSVS CCCCEECCCCCCCCC | 14.90 | 30059200 | |
508 | O-linked_Glycosylation | AHTYTPITSSVSTIR CEECCCCCCCCCCHH | 19.02 | 30059200 | |
509 | O-linked_Glycosylation | HTYTPITSSVSTIRQ EECCCCCCCCCCHHC | 29.48 | 30059200 | |
510 | O-linked_Glycosylation | TYTPITSSVSTIRQY ECCCCCCCCCCHHCC | 16.07 | 30059200 | |
512 | O-linked_Glycosylation | TPITSSVSTIRQYPV CCCCCCCCCHHCCCC | 21.77 | 30059200 | |
513 | O-linked_Glycosylation | PITSSVSTIRQYPVS CCCCCCCCHHCCCCC | 20.30 | 30059200 | |
635 | O-linked_Glycosylation | TIVANPISNPFSAAP EEEECCCCCCCCCCC | 39.44 | 30059200 | |
639 | O-linked_Glycosylation | NPISNPFSAAPAATT CCCCCCCCCCCCCEE | 25.44 | 30059200 | |
646 | O-linked_Glycosylation | SAAPAATTVVQTHSQ CCCCCCEEEEEECCC | 17.60 | 30059200 | |
650 | Phosphorylation | AATTVVQTHSQSAST CCEEEEEECCCCCCC | 16.34 | 28348404 | |
652 | Phosphorylation | TTVVQTHSQSASTNA EEEEEECCCCCCCCC | 29.26 | 28348404 | |
654 | Phosphorylation | VVQTHSQSASTNAPA EEEECCCCCCCCCCC | 27.48 | 28348404 | |
656 | Phosphorylation | QTHSQSASTNAPAQG EECCCCCCCCCCCCC | 27.69 | 28348404 | |
657 | O-linked_Glycosylation | THSQSASTNAPAQGS ECCCCCCCCCCCCCC | 34.81 | 30059200 | |
657 | Phosphorylation | THSQSASTNAPAQGS ECCCCCCCCCCCCCC | 34.81 | 28348404 | |
664 | Phosphorylation | TNAPAQGSSPRPSIL CCCCCCCCCCCCHHH | 25.70 | 28348404 | |
665 | Phosphorylation | NAPAQGSSPRPSILR CCCCCCCCCCCHHHC | 31.58 | 28348404 | |
677 | Phosphorylation | ILRKKPATDGAKPKS HHCCCCCCCCCCCCC | 43.42 | - | |
696 (in isoform 3) | Phosphorylation | - | 5.37 | 21815630 | |
705 (in isoform 3) | Phosphorylation | - | 59.29 | 28176443 | |
706 (in isoform 3) | Phosphorylation | - | 39.26 | 28176443 | |
707 (in isoform 3) | Phosphorylation | - | 64.48 | 25849741 | |
709 (in isoform 3) | Phosphorylation | - | 28.74 | 26055452 | |
783 | Sumoylation | GPPVPEIKVKEEVEP CCCCCCCEECCCCCC | 45.66 | - | |
785 | Sumoylation | PVPEIKVKEEVEPMD CCCCCEECCCCCCCC | 43.06 | - | |
785 | Sumoylation | PVPEIKVKEEVEPMD CCCCCEECCCCCCCC | 43.06 | 28112733 | |
798 | Phosphorylation | MDIMRPVSAVPPLAT CCCCCCCCCCCCCCC | 26.65 | 20068231 | |
805 | Phosphorylation | SAVPPLATNTVSPSL CCCCCCCCCCCCHHH | 38.82 | 20068231 | |
807 | Phosphorylation | VPPLATNTVSPSLAL CCCCCCCCCCHHHHH | 20.29 | 20068231 | |
809 | Phosphorylation | PLATNTVSPSLALLA CCCCCCCCHHHHHHH | 13.51 | 20068231 | |
811 | Phosphorylation | ATNTVSPSLALLANN CCCCCCHHHHHHHCC | 20.83 | 20068231 | |
820 | Phosphorylation | ALLANNLSMPTSDLP HHHHCCCCCCCCCCC | 25.49 | 20068231 | |
823 | Phosphorylation | ANNLSMPTSDLPPGA HCCCCCCCCCCCCCC | 26.65 | 20068231 | |
824 | Phosphorylation | NNLSMPTSDLPPGAS CCCCCCCCCCCCCCC | 31.14 | 20068231 | |
831 | Phosphorylation | SDLPPGASPRKKPRK CCCCCCCCCCCCCCC | 31.02 | 20068231 | |
844 | Phosphorylation | RKQQHVISTEEGDMM CCCCCEEECCCCCCC | 28.78 | 23663014 | |
845 | Phosphorylation | KQQHVISTEEGDMME CCCCEEECCCCCCCC | 27.25 | 23927012 | |
853 | Phosphorylation | EEGDMMETNSTDDEK CCCCCCCCCCCCCHH | 19.30 | 23927012 | |
855 | Phosphorylation | GDMMETNSTDDEKST CCCCCCCCCCCHHHH | 40.40 | 23927012 | |
856 | Phosphorylation | DMMETNSTDDEKSTA CCCCCCCCCCHHHHH | 49.92 | 23927012 | |
861 | Phosphorylation | NSTDDEKSTAKSLLV CCCCCHHHHHHHHHH | 31.39 | 23927012 | |
862 | Phosphorylation | STDDEKSTAKSLLVK CCCCHHHHHHHHHHH | 49.53 | 25219547 | |
864 | Sumoylation | DDEKSTAKSLLVKAE CCHHHHHHHHHHHHH | 41.55 | 28112733 | |
865 | Phosphorylation | DEKSTAKSLLVKAEK CHHHHHHHHHHHHHH | 25.19 | 26074081 | |
869 | Sumoylation | TAKSLLVKAEKRKSP HHHHHHHHHHHCCCC | 51.28 | - | |
869 | Acetylation | TAKSLLVKAEKRKSP HHHHHHHHHHHCCCC | 51.28 | 25953088 | |
869 | Methylation | TAKSLLVKAEKRKSP HHHHHHHHHHHCCCC | 51.28 | - | |
869 | Sumoylation | TAKSLLVKAEKRKSP HHHHHHHHHHHCCCC | 51.28 | 28112733 | |
875 | Phosphorylation | VKAEKRKSPPKEYID HHHHHCCCCCHHHCC | 50.93 | 23401153 | |
880 | Phosphorylation | RKSPPKEYIDEEGVR CCCCCHHHCCCCCCE | 21.57 | 30576142 | |
937 | Ubiquitination | LQEIANQKGVSCRAQ HHHHHHCCCCCHHHC | 62.17 | - | |
972 (in isoform 3) | Ubiquitination | - | 4.06 | - | |
979 | Ubiquitination | LQEGIIPKKKAATDD CCCCCCCCCCCCCHH | 57.40 | - | |
981 | Ubiquitination | EGIIPKKKAATDDDL CCCCCCCCCCCHHHH | 49.75 | - | |
999 | Sulfoxidation | NELIQGNMQRCKLVM HHHHHHHHHHHHHHH | 3.21 | 21406390 | |
1023 | 2-Hydroxyisobutyrylation | MLKVLDHKDRVLKLL HHHHHCHHHHHHHHH | 47.07 | - | |
1023 | Ubiquitination | MLKVLDHKDRVLKLL HHHHHCHHHHHHHHH | 47.07 | - | |
1028 | Ubiquitination | DHKDRVLKLLNKNGT CHHHHHHHHHCCCCC | 48.33 | - | |
1040 | Phosphorylation | NGTVKKVSKLKRKEK CCCCCHHHHHCCHHC | 40.94 | 25599653 |
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 SP130_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SP130_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 SP130_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SIN3A_HUMAN | SIN3A | physical | 12724404 | |
HDAC1_HUMAN | HDAC1 | physical | 12724404 | |
HDAC2_HUMAN | HDAC2 | physical | 12724404 | |
SDS3_HUMAN | SUDS3 | physical | 12724404 | |
CUL2_HUMAN | CUL2 | physical | 18173839 | |
SF3B1_HUMAN | SF3B1 | physical | 18173839 | |
CUL1_HUMAN | CUL1 | physical | 18173839 | |
CUL4A_HUMAN | CUL4A | physical | 18173839 | |
VHL_HUMAN | VHL | physical | 18173839 | |
ELOB_HUMAN | TCEB2 | physical | 18173839 | |
TAF10_HUMAN | TAF10 | physical | 22939629 | |
CUL4B_HUMAN | CUL4B | physical | 25189618 | |
DDB1_HUMAN | DDB1 | physical | 25189618 | |
SIN3A_HUMAN | SIN3A | physical | 26344197 |
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 |
"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 THR-355; SER-442 ANDSER-875, AND MASS SPECTROMETRY. | |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND SER-455, ANDMASS SPECTROMETRY. |