ASCC2_HUMAN - dbPTM
ASCC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASCC2_HUMAN
UniProt AC Q9H1I8
Protein Name Activating signal cointegrator 1 complex subunit 2
Gene Name ASCC2
Organism Homo sapiens (Human).
Sequence Length 757
Subcellular Localization Nucleus .
Protein Description Enhances NF-kappa-B, SRF and AP1 transactivation..
Protein Sequence MPALPLDQLQITHKDPKTGKLRTSPALHPEQKADRYFVLYKPPPKDNIPALVEEYLERATFVANDLDWLLALPHDKFWCQVIFDETLQKCLDSYLRYVPRKFDEGVASAPEVVDMQKRLHRSVFLTFLRMSTHKESKDHFISPSAFGEILYNNFLFDIPKILDLCVLFGKGNSPLLQKMIGNIFTQQPSYYSDLDETLPTILQVFSNILQHCGLQGDGANTTPQKLEERGRLTPSDMPLLELKDIVLYLCDTCTTLWAFLDIFPLACQTFQKHDFCYRLASFYEAAIPEMESAIKKRRLEDSKLLGDLWQRLSHSRKKLMEIFHIILNQICLLPILESSCDNIQGFIEEFLQIFSSLLQEKRFLRDYDALFPVAEDISLLQQASSVLDETRTAYILQAVESAWEGVDRRKATDAKDPSVIEEPNGEPNGVTVTAEAVSQASSHPENSEEEECMGAAAAVGPAMCGVELDSLISQVKDLLPDLGEGFILACLEYYHYDPEQVINNILEERLAPTLSQLDRNLDREMKPDPTPLLTSRHNVFQNDEFDVFSRDSVDLSRVHKGKSTRKEENTRSLLNDKRAVAAQRQRYEQYSVVVEEVPLQPGESLPYHSVYYEDEYDDTYDGNQVGANDADSDDELISRRPFTIPQVLRTKVPREGQEEDDDDEEDDADEEAPKPDHFVQDPAVLREKAEARRMAFLAKKGYRHDSSTAVAGSPRGHGQSRETTQERRKKEANKATRANHNRRTMADRKRSKGMIPS
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
14UbiquitinationDQLQITHKDPKTGKL
HHCEEEECCCCCCCC		68.05-
23PhosphorylationPKTGKLRTSPALHPE
CCCCCCCCCCCCCHH		49.8823312004
24PhosphorylationKTGKLRTSPALHPEQ
CCCCCCCCCCCCHHH		11.1823312004
41UbiquitinationDRYFVLYKPPPKDNI
CCEEEEECCCCCCCC		47.06-
101UbiquitinationYLRYVPRKFDEGVAS
HHHHCCCCCCCCCCC		51.61-
117UbiquitinationPEVVDMQKRLHRSVF
HHHHHHHHHHHHHHH		50.73-
122PhosphorylationMQKRLHRSVFLTFLR
HHHHHHHHHHHHHHH		13.38-
131PhosphorylationFLTFLRMSTHKESKD
HHHHHHHHCCCCCCC		22.4122817900
136PhosphorylationRMSTHKESKDHFISP
HHHCCCCCCCCCCCH		48.4622817900
151PhosphorylationSAFGEILYNNFLFDI
HHHHHHHHHHHCCHH		17.4526657352
181 (in isoform 2)Ubiquitination-20.0621906983
189 (in isoform 2)Ubiquitination-32.1521906983
233PhosphorylationLEERGRLTPSDMPLL
HHHCCCCCCCCCCHH		21.2730266825
235PhosphorylationERGRLTPSDMPLLEL
HCCCCCCCCCCHHHH		41.1130266825
281PhosphorylationDFCYRLASFYEAAIP
CHHHHHHHHHHHHHH		32.7127811184
283PhosphorylationCYRLASFYEAAIPEM
HHHHHHHHHHHHHHH		11.3627811184
292PhosphorylationAAIPEMESAIKKRRL
HHHHHHHHHHHHHHH		33.7027811184
295 (in isoform 1)Ubiquitination-39.6921906983
295UbiquitinationPEMESAIKKRRLEDS
HHHHHHHHHHHHHHH		39.6921906983
296UbiquitinationEMESAIKKRRLEDSK
HHHHHHHHHHHHHHH		36.32-
303 (in isoform 1)Ubiquitination-61.1121906983
303UbiquitinationKRRLEDSKLLGDLWQ
HHHHHHHHHHHHHHH		61.112190698
313PhosphorylationGDLWQRLSHSRKKLM
HHHHHHHHHHHHHHH		22.93-
390PhosphorylationASSVLDETRTAYILQ
HHHHCHHHHHHHHHH		32.7420068231
447PhosphorylationASSHPENSEEEECMG
HHCCCCCCCHHHHHH		44.7324275569
513PhosphorylationLEERLAPTLSQLDRN
HHHHHHHHHHHHHHH		33.1721406692
515PhosphorylationERLAPTLSQLDRNLD
HHHHHHHHHHHHHHC		31.0421406692
530PhosphorylationREMKPDPTPLLTSRH
CCCCCCCCCCCCCCC		33.6727251275
534PhosphorylationPDPTPLLTSRHNVFQ
CCCCCCCCCCCCCCC		31.2524719451
535PhosphorylationDPTPLLTSRHNVFQN
CCCCCCCCCCCCCCC		31.3528348404
549PhosphorylationNDEFDVFSRDSVDLS
CCCCEECCCCCCCHH		34.7220873877
552PhosphorylationFDVFSRDSVDLSRVH
CEECCCCCCCHHHHC		19.2027251275
564PhosphorylationRVHKGKSTRKEENTR
HHCCCCCCCCHHHHH		49.61-
572PhosphorylationRKEENTRSLLNDKRA
CCHHHHHHHHHHHHH		34.8628555341
577UbiquitinationTRSLLNDKRAVAAQR
HHHHHHHHHHHHHHH		40.98-
577AcetylationTRSLLNDKRAVAAQR
HHHHHHHHHHHHHHH		40.9825953088
632PhosphorylationVGANDADSDDELISR
CCCCCCCCCHHHHHC		49.0026657352
638PhosphorylationDSDDELISRRPFTIP
CCCHHHHHCCCCCHH		34.5624719451
674UbiquitinationDADEEAPKPDHFVQD
CCCCCCCCCCCCCCC		70.85-
699MethylationRRMAFLAKKGYRHDS
HHHHHHHHCCCCCCC		49.21-
702PhosphorylationAFLAKKGYRHDSSTA
HHHHHCCCCCCCCCC		17.4127251275
706PhosphorylationKKGYRHDSSTAVAGS
HCCCCCCCCCCCCCC		24.3824732914
707PhosphorylationKGYRHDSSTAVAGSP
CCCCCCCCCCCCCCC		26.8324732914
708PhosphorylationGYRHDSSTAVAGSPR
CCCCCCCCCCCCCCC		29.1524732914
713PhosphorylationSSTAVAGSPRGHGQS
CCCCCCCCCCCCCCC		11.1629255136
715MethylationTAVAGSPRGHGQSRE
CCCCCCCCCCCCCHH		51.98-
720PhosphorylationSPRGHGQSRETTQER
CCCCCCCCHHHHHHH		36.3528111955
730AcetylationTTQERRKKEANKATR
HHHHHHHHHHHHHHH		61.316570101
744PhosphorylationRANHNRRTMADRKRS
HHHHHHCHHHHHHHH		17.30-
751PhosphorylationTMADRKRSKGMIPS-
HHHHHHHHCCCCCC-		36.2724719451
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:22388891
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASCC2_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 ASCC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUTC_HUMANCUTCphysical
16169070
CKAP4_HUMANCKAP4physical
16169070
DEAF1_HUMANDEAF1physical
16169070
RNZ2_HUMANELAC2physical
16169070
FAF1_HUMANFAF1physical
16169070
ALR_HUMANGFERphysical
16169070
TUTLA_HUMANIGSF9physical
16169070
LIPL_HUMANLPLphysical
16169070
GNL3_HUMANGNL3physical
16169070
PK3CD_HUMANPIK3CDphysical
16169070
URM1_HUMANURM1physical
16169070
RADIL_HUMANRADILphysical
16169070
TF3C1_HUMANGTF3C1physical
16169070
FUND2_HUMANFUNDC2physical
16169070
MIC60_HUMANIMMTphysical
16169070
MYH9_HUMANMYH9physical
16169070
PIN4_HUMANPIN4physical
16169070
PJA1_HUMANPJA1physical
16169070
PDIP2_HUMANPOLDIP2physical
16169070
RSMB_HUMANSNRPBphysical
16169070
TBC17_HUMANTBC1D17physical
16169070
KDM1A_HUMANKDM1Aphysical
16169070
ASSY_HUMANASS1physical
16169070
F16P1_HUMANFBP1physical
16169070
DPOA2_HUMANPOLA2physical
16169070
OLA1_HUMANOLA1physical
16169070
MED31_HUMANMED31physical
16169070
RFA1_HUMANRPA1physical
16169070
EF1D_HUMANEEF1Dphysical
16169070
RLA1_HUMANRPLP1physical
16169070
SNW1_HUMANSNW1physical
16169070
GA45A_HUMANGADD45Aphysical
21988832
ASCC3_HUMANASCC3physical
26344197
GPC4_HUMANGPC4physical
26344197
TRIP4_HUMANTRIP4physical
26344197
CSRP1_HUMANCSRP1physical
26924529
ASCC1_HUMANASCC1physical
26924529
TRIP4_HUMANTRIP4physical
26924529
TRIP4_HUMANTRIP4physical
28514442
ASCC3_HUMANASCC3physical
28514442
Drug and Disease Associations
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.
Regulatory Network of ASCC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND MASSSPECTROMETRY.

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