ASXL1_HUMAN - dbPTM
ASXL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASXL1_HUMAN
UniProt AC Q8IXJ9
Protein Name Putative Polycomb group protein ASXL1
Gene Name ASXL1
Organism Homo sapiens (Human).
Sequence Length 1541
Subcellular Localization Nucleus .
Protein Description Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1)..
Protein Sequence MKDKQKKKKERTWAEAARLVLENYSDAPMTPKQILQVIEAEGLKEMRSGTSPLACLNAMLHSNSRGGEGLFYKLPGRISLFTLKKDALQWSRHPATVEGEEPEDTADVESCGSNEASTVSGENDVSLDETSSNASCSTESQSRPLSNPRDSYRASSQANKQKKKTGVMLPRVVLTPLKVNGAHVESASGFSGCHADGESGSPSSSSSGSLALGSAAIRGQAEVTQDPAPLLRGFRKPATGQMKRNRGEEIDFETPGSILVNTNLRALINSRTFHALPSHFQQQLLFLLPEVDRQVGTDGLLRLSSSALNNEFFTHAAQSWRERLADGEFTHEMQVRIRQEMEKEKKVEQWKEKFFEDYYGQKLGLTKEESLQQNVGQEEAEIKSGLCVPGESVRIQRGPATRQRDGHFKKRSRPDLRTRARRNLYKKQESEQAGVAKDAKSVASDVPLYKDGEAKTDPAGLSSPHLPGTSSAAPDLEGPEFPVESVASRIQAEPDNLARASASPDRIPSLPQETVDQEPKDQKRKSFEQAASASFPEKKPRLEDRQSFRNTIESVHTEKPQPTKEEPKVPPIRIQLSRIKPPWVVKGQPTYQICPRIIPTTESSCRGWTGARTLADIKARALQVRGARGHHCHREAATTAIGGGGGPGGGGGGATDEGGGRGSSSGDGGEACGHPEPRGGPSTPGKCTSDLQRTQLLPPYPLNGEHTQAGTAMSRARREDLPSLRKEESCLLQRATVGLTDGLGDASQLPVAPTGDQPCQALPLLSSQTSVAERLVEQPQLHPDVRTECESGTTSWESDDEEQGPTVPADNGPIPSLVGDDTLEKGTGQALDSHPTMKDPVNVTPSSTPESSPTDCLQNRAFDDELGLGGSCPPMRESDTRQENLKTKALVSNSSLHWIPIPSNDEVVKQPKPESREHIPSVEPQVGEEWEKAAPTPPALPGDLTAEEGLDPLDSLTSLWTVPSRGGSDSNGSYCQQVDIEKLKINGDSEALSPHGESTDTASDFEGHLTEDSSEADTREAAVTKGSSVDKDEKPNWNQSAPLSKVNGDMRLVTRTDGMVAPQSWVSRVCAVRQKIPDSLLLASTEYQPRAVCLSMPGSSVEATNPLVMQLLQGSLPLEKVLPPAHDDSMSESPQVPLTKDQSHGSLRMGSLHGLGKNSGMVDGSSPSSLRALKEPLLPDSCETGTGLARIEATQAPGAPQKNCKAVPSFDSLHPVTNPITSSRKLEEMDSKEQFSSFSCEDQKEVRAMSQDSNSNAAPGKSPGDLTTSRTPRFSSPNVISFGPEQTGRALGDQSNVTGQGKKLFGSGNVAATLQRPRPADPMPLPAEIPPVFPSGKLGPSTNSMSGGVQTPREDWAPKPHAFVGSVKNEKTFVGGPLKANAENRKATGHSPLELVGHLEGMPFVMDLPFWKLPREPGKGLSEPLEPSSLPSQLSIKQAFYGKLSKLQLSSTSFNYSSSSPTFPKGLAGSVVQLSHKANFGASHSASLSLQMFTDSSTVESISLQCACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLVVR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
30PhosphorylationNYSDAPMTPKQILQV
HCCCCCCCHHHHHHH
26.69-
48PhosphorylationEGLKEMRSGTSPLAC
CCHHHHHCCCCHHHH
45.1527080861
50PhosphorylationLKEMRSGTSPLACLN
HHHHHCCCCHHHHHH
28.5527080861
51PhosphorylationKEMRSGTSPLACLNA
HHHHCCCCHHHHHHH
22.8022199227
164AcetylationQANKQKKKTGVMLPR
HHHHHHHCCCCCCCE
58.5112433735
175PhosphorylationMLPRVVLTPLKVNGA
CCCEEEEEEEEECCE
18.2421815630
186PhosphorylationVNGAHVESASGFSGC
ECCEEEECCCCCCCC
27.0124275569
188PhosphorylationGAHVESASGFSGCHA
CEEEECCCCCCCCCC
50.0424275569
199PhosphorylationGCHADGESGSPSSSS
CCCCCCCCCCCCCCC
50.5324275569
199O-linked_GlycosylationGCHADGESGSPSSSS
CCCCCCCCCCCCCCC
50.5321740066
201PhosphorylationHADGESGSPSSSSSG
CCCCCCCCCCCCCCC
30.7827050516
204PhosphorylationGESGSPSSSSSGSLA
CCCCCCCCCCCCCCH
37.3124275569
205PhosphorylationESGSPSSSSSGSLAL
CCCCCCCCCCCCCHH
32.6222817900
304PhosphorylationTDGLLRLSSSALNNE
CCHHHHCCHHHHCCH
18.80-
351 (in isoform 1)Ubiquitination-51.2021890473
351 (in isoform 2)Ubiquitination-51.2021890473
351UbiquitinationEKKVEQWKEKFFEDY
HHHHHHHHHHHHHHH
51.2021906983
353UbiquitinationKVEQWKEKFFEDYYG
HHHHHHHHHHHHHHH
52.18-
362UbiquitinationFEDYYGQKLGLTKEE
HHHHHHHHHCCCHHH
39.9121890473
362 (in isoform 1)Ubiquitination-39.9121890473
362 (in isoform 2)Ubiquitination-39.9121890473
367UbiquitinationGQKLGLTKEESLQQN
HHHHCCCHHHHHHHH
65.6121906983
367 (in isoform 1)Ubiquitination-65.6121890473
367 (in isoform 2)Ubiquitination-65.6121890473
401PhosphorylationRIQRGPATRQRDGHF
EEEECCCHHCCCCCC
30.3923403867
449PhosphorylationVASDVPLYKDGEAKT
HHCCCCCCCCCCCCC
10.85-
456PhosphorylationYKDGEAKTDPAGLSS
CCCCCCCCCCCCCCC
55.0227080861
462PhosphorylationKTDPAGLSSPHLPGT
CCCCCCCCCCCCCCC
40.6927080861
463PhosphorylationTDPAGLSSPHLPGTS
CCCCCCCCCCCCCCC
22.7528450419
469PhosphorylationSSPHLPGTSSAAPDL
CCCCCCCCCCCCCCC
19.9828450419
470PhosphorylationSPHLPGTSSAAPDLE
CCCCCCCCCCCCCCC
24.7227080861
471PhosphorylationPHLPGTSSAAPDLEG
CCCCCCCCCCCCCCC
28.4327080861
501PhosphorylationPDNLARASASPDRIP
CCCHHHCCCCCCCCC
24.5930266825
503PhosphorylationNLARASASPDRIPSL
CHHHCCCCCCCCCCC
25.4930266825
509PhosphorylationASPDRIPSLPQETVD
CCCCCCCCCCHHHCC
50.7630266825
514PhosphorylationIPSLPQETVDQEPKD
CCCCCHHHCCCCCHH
24.9223403867
526PhosphorylationPKDQKRKSFEQAASA
CHHHHHHHHHHHHHC
37.7422199227
532PhosphorylationKSFEQAASASFPEKK
HHHHHHHHCCCCCCC
27.7128985074
557PhosphorylationNTIESVHTEKPQPTK
HHHHHHHCCCCCCCC
43.48-
577PhosphorylationPPIRIQLSRIKPPWV
CCEEEEEEECCCCEE
18.6524719451
606MethylationPTTESSCRGWTGART
CCCCCCCCCCCCCCC
45.70-
723PhosphorylationARREDLPSLRKEESC
HHHHHCHHHCHHHHH
48.3724719451
844PhosphorylationMKDPVNVTPSSTPES
CCCCCCCCCCCCCCC
16.55-
909UbiquitinationPSNDEVVKQPKPESR
CCCCCCCCCCCCCCC
67.09-
936PhosphorylationEWEKAAPTPPALPGD
HHHHHCCCCCCCCCC
36.8628348404
989PhosphorylationKLKINGDSEALSPHG
ECEECCCCCCCCCCC
26.6022210691
999PhosphorylationLSPHGESTDTASDFE
CCCCCCCCCCHHHHC
32.8222210691
1010PhosphorylationSDFEGHLTEDSSEAD
HHHCCCCCCCCCCCH
31.8822210691
1025AcetylationTREAAVTKGSSVDKD
HHHHHHHCCCCCCCC
50.6318527295
1056PhosphorylationDMRLVTRTDGMVAPQ
CEEEEECCCCCCCCH
27.7823403867
1064PhosphorylationDGMVAPQSWVSRVCA
CCCCCCHHHHHHHHH
28.52-
1067PhosphorylationVAPQSWVSRVCAVRQ
CCCHHHHHHHHHHHH
16.8523403867
1143PhosphorylationVPLTKDQSHGSLRMG
CCCCCCCCCCCEECC
39.6920815410
1151PhosphorylationHGSLRMGSLHGLGKN
CCCEECCCCCCCCCC
14.0923532336
1159PhosphorylationLHGLGKNSGMVDGSS
CCCCCCCCCCCCCCC
31.5823532336
1165PhosphorylationNSGMVDGSSPSSLRA
CCCCCCCCCHHHHHH
34.3125627689
1166PhosphorylationSGMVDGSSPSSLRAL
CCCCCCCCHHHHHHH
34.0425627689
1168PhosphorylationMVDGSSPSSLRALKE
CCCCCCHHHHHHHCC
43.9122964224
1169PhosphorylationVDGSSPSSLRALKEP
CCCCCHHHHHHHCCC
25.8422964224
1174UbiquitinationPSSLRALKEPLLPDS
HHHHHHHCCCCCCCC
57.19-
1194PhosphorylationGLARIEATQAPGAPQ
CCEEEEECCCCCCCC
16.69-
1209PhosphorylationKNCKAVPSFDSLHPV
CCCCCCCCCCCCCCC
34.78-
1250PhosphorylationQKEVRAMSQDSNSNA
HHHHHHHHCCCCCCC
29.83-
1253PhosphorylationVRAMSQDSNSNAAPG
HHHHHCCCCCCCCCC
34.22-
1262PhosphorylationSNAAPGKSPGDLTTS
CCCCCCCCCCCCCCC
39.78-
1276PhosphorylationSRTPRFSSPNVISFG
CCCCCCCCCCEEECC
20.13-
1302AcetylationSNVTGQGKKLFGSGN
CCCCCCCCCCCCCCC
38.1126051181
1341PhosphorylationPSGKLGPSTNSMSGG
CCCCCCCCCCCCCCC
38.12-
1344PhosphorylationKLGPSTNSMSGGVQT
CCCCCCCCCCCCCCC
17.89-
1371UbiquitinationVGSVKNEKTFVGGPL
ECCCCCCEEEECCCC
57.57-
1379UbiquitinationTFVGGPLKANAENRK
EEECCCCCCCCCCCC
42.61-
1419UbiquitinationKLPREPGKGLSEPLE
CCCCCCCCCCCCCCC
68.35-
1437 (in isoform 1)Ubiquitination-32.0021890473
1437UbiquitinationLPSQLSIKQAFYGKL
CCCCHHHHHHHHHCC
32.002190698
1443UbiquitinationIKQAFYGKLSKLQLS
HHHHHHHCCCCCEEE
37.90-
1446UbiquitinationAFYGKLSKLQLSSTS
HHHHCCCCCEEECCC
51.17-
1494PhosphorylationSLSLQMFTDSSTVES
EEEEEECCCCCCCCH
29.63-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 ASXL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASXL1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 ASXL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKT1_HUMANAKT1physical
18624398
BAP1_HUMANBAP1physical
21642991
A4_HUMANAPPphysical
21832049
EZH2_HUMANEZH2physical
22897849
EED_HUMANEEDphysical
22897849
STAT3_HUMANSTAT3physical
21988832
OGT1_HUMANOGTphysical
26416890
HCFC1_HUMANHCFC1physical
26416890
FOXK1_HUMANFOXK1physical
26416890
FOXK2_HUMANFOXK2physical
26416890

Drug and Disease Associations
Kegg Disease
OMIM Disease
605039Bohring-Opitz syndrome (BOPS)
614286Myelodysplastic syndrome (MDS)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASXL1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP