MCAF1_MOUSE - dbPTM
MCAF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCAF1_MOUSE
UniProt AC Q7TT18
Protein Name Activating transcription factor 7-interacting protein 1
Gene Name Atf7ip
Organism Mus musculus (Mouse).
Sequence Length 1306
Subcellular Localization Nucleus .
Protein Description Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). May have ATPase activity..
Protein Sequence MDSVEEPQKKVFKARKTMRASDRQQLDAVHRVKGELLRADGKLLNGSHENGDLDPTSPLENTDCIQDREEVNGIDGICFQSEESTTEWKETPCMPNVAVKNKQEDLNSEALSPSITCDLSSRVTTEPGSGSPASDNPGCGTPVSDNPASDNPASDNPASDNPDSGDLAAGELATTVQATGDSACEEPPSSDPSSSDPTSSEPSSSEPTCSEPISGDPVSEEAASHDLVSGDSTCSEPVSGEPVSHEAASSEPATSEPASDEPVARVVAACELAPGESALDDCAPSGDSQSDEPPSSEDSLPRSVCSGLASGELTPGELSVEPATDTVKPSSSAVCEAGPDPDKTEPSSNNSDDCPGKSEDDEHLDQIQSKDSCDEGNKVNSNVVEKEEPLETHSAIICSDLPPENTTKIAEDPIAEPALEEEAISSSMEVDQSEKDEHKSPAEPVAAVSEDPAEEDKEDTVVDNTDSMETDEIIPILEKLAPTEDELSCFSKASLLPVETSQDLEDKMEGSFGSPSKQESSENLPKEAFLVLSDEEDLSCGKDESEAVAQSKMSTPEGEKSEKDGKAEEEERVPAEEQPPVRNEFSRRKRSKSEDMDSVESKRRRYMDEEYEAEFQVKITAKGDINQKLQKVIQWLLQEKLCALQCAVFDKTLAELKTRVEKIECNKRHKAVLTELQAKIARLTKRFGAAKDDLKKRQESPPNPPISPGKPANDTNSNNNMTYRNAGTVRQLLESKRNVSEGPPPSFQTPVNTVSSASHATSTAVVSSQPKLQTSATSGSLPAAPLLPAPSTATVVATTQVPSGTPQPTISLQPLPVILHVPVAVTSQPQLLQSHPGTLVTNQPSGNVEFISVQSQPTVSGLTKNPVSLPPLPNPTKPNIPSVPSPSSIQRNSSTTAAPLGTTLAVQAVPTAHSIVQATRTSLPTVGPSGLYSSSSSRGPIQMKIPISTFSPPSSAEQNSSATPRIVTENQTNKTVDSSINKKAADSTSQSGKASSSDSSGVIDLTMDDEESGTTQDPKKISPPSSSTVSTSQPMSRPLQPILPAPPLQPSGVPTSGPSQATIHVLPTAPTTVNVTHRPVTQVTTRLPVPRAPANHQVVYTTLPAPTTQAPLRGTVMQAPAVRQVNPQNSVTVRVPQTTTYVVNNGLTLGSAGPQLTVHHRPPQVHNEPPRPLHPAPLPEAPQPQRLPPEAASTSLPQKPHLKLARVQSQNGIVLSWSVLEVDRSCATVDSYHLYAYHEEPSATVPSQWKKIGEVKALPLPMACTLTQFVSGSKYYFAVRAKDIYGRFGPFCDPQSTDVISSSQNS
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
1Acetylation-------MDSVEEPQ
-------CCCCCHHH		38.99-
21PhosphorylationARKTMRASDRQQLDA
HHHHHCHHHHHHHHH		23.9825338131
56PhosphorylationENGDLDPTSPLENTD
CCCCCCCCCCCCCCC		42.5225619855
57PhosphorylationNGDLDPTSPLENTDC
CCCCCCCCCCCCCCC		32.6421082442
108PhosphorylationNKQEDLNSEALSPSI
CCCHHCCCCCCCCCE		31.3825619855
112PhosphorylationDLNSEALSPSITCDL
HCCCCCCCCCEEEEC		24.5325521595
114PhosphorylationNSEALSPSITCDLSS
CCCCCCCCEEEECCC		27.4425619855
116PhosphorylationEALSPSITCDLSSRV
CCCCCCEEEECCCCE		12.3325619855
120PhosphorylationPSITCDLSSRVTTEP
CCEEEECCCCEECCC		11.6625619855
121PhosphorylationSITCDLSSRVTTEPG
CEEEECCCCEECCCC		37.7625619855
124PhosphorylationCDLSSRVTTEPGSGS
EECCCCEECCCCCCC		25.08-
277PhosphorylationCELAPGESALDDCAP
HEECCCCCCHHHCCC		39.7930635358
285PhosphorylationALDDCAPSGDSQSDE
CHHHCCCCCCCCCCC		36.3925293948
288PhosphorylationDCAPSGDSQSDEPPS
HCCCCCCCCCCCCCC		34.8025293948
290PhosphorylationAPSGDSQSDEPPSSE
CCCCCCCCCCCCCCC		48.1425293948
295PhosphorylationSQSDEPPSSEDSLPR
CCCCCCCCCCCCCCH		58.0125293948
296PhosphorylationQSDEPPSSEDSLPRS
CCCCCCCCCCCCCHH		51.7225293948
299PhosphorylationEPPSSEDSLPRSVCS
CCCCCCCCCCHHHHC		35.9025293948
344PhosphorylationAGPDPDKTEPSSNNS
CCCCCCCCCCCCCCC		61.5827087446
358PhosphorylationSDDCPGKSEDDEHLD
CCCCCCCCCCHHHHH		52.7727087446
369PhosphorylationEHLDQIQSKDSCDEG
HHHHHHHCCCCCCCC		39.8129550500
372PhosphorylationDQIQSKDSCDEGNKV
HHHHCCCCCCCCCCC		27.4929550500
440PhosphorylationSEKDEHKSPAEPVAA
HHCCCCCCCCCCCEE		31.1125521595
449PhosphorylationAEPVAAVSEDPAEED
CCCCEECCCCCCCCC		31.3923375375
467PhosphorylationTVVDNTDSMETDEII
CCCCCCCCCCHHHHH		19.2425338131
488PhosphorylationAPTEDELSCFSKASL
CCCCCHHHHHHHCCC		15.8627566939
491PhosphorylationEDELSCFSKASLLPV
CCHHHHHHHCCCCCC		31.4727566939
494PhosphorylationLSCFSKASLLPVETS
HHHHHHCCCCCCCCC		33.8925777480
500PhosphorylationASLLPVETSQDLEDK
CCCCCCCCCCCHHHH		31.7428833060
501PhosphorylationSLLPVETSQDLEDKM
CCCCCCCCCCHHHHH		14.2725521595
511PhosphorylationLEDKMEGSFGSPSKQ
HHHHHCCCCCCCCHH		17.0923375375
514PhosphorylationKMEGSFGSPSKQESS
HHCCCCCCCCHHHCC		24.8025521595
516PhosphorylationEGSFGSPSKQESSEN
CCCCCCCCHHHCCCC		48.9823684622
520PhosphorylationGSPSKQESSENLPKE
CCCCHHHCCCCCCCC		40.2225619855
521PhosphorylationSPSKQESSENLPKEA
CCCHHHCCCCCCCCE		29.7425619855
533PhosphorylationKEAFLVLSDEEDLSC
CCEEEEECCHHHHCC		35.1826824392
539PhosphorylationLSDEEDLSCGKDESE
ECCHHHHCCCCCHHH		32.9023984901
545PhosphorylationLSCGKDESEAVAQSK
HCCCCCHHHHHHHHH		40.7823649490
591PhosphorylationEFSRRKRSKSEDMDS
HHHHHHCCCCCCCHH		43.5027087446
593PhosphorylationSRRKRSKSEDMDSVE
HHHHCCCCCCCHHHH		39.8227087446
598PhosphorylationSKSEDMDSVESKRRR
CCCCCCHHHHHHHHH		22.5828833060
601PhosphorylationEDMDSVESKRRRYMD
CCCHHHHHHHHHHCC		29.3428833060
602UbiquitinationDMDSVESKRRRYMDE
CCHHHHHHHHHHCCH		36.1027667366
605UbiquitinationSVESKRRRYMDEEYE
HHHHHHHHHCCHHHH		34.8527667366
613UbiquitinationYMDEEYEAEFQVKIT
HCCHHHHEEEEEEEE		23.2327667366
631UbiquitinationDINQKLQKVIQWLLQ
CHHHHHHHHHHHHHH		52.31-
657UbiquitinationDKTLAELKTRVEKIE
HHHHHHHHHHHHHHH		26.2822790023
691AcetylationTKRFGAAKDDLKKRQ
HHHHCCCHHHHHHHC		51.767617961
700PhosphorylationDLKKRQESPPNPPIS
HHHHHCCCCCCCCCC		37.0023375375
707PhosphorylationSPPNPPISPGKPAND
CCCCCCCCCCCCCCC		33.1127087446
715PhosphorylationPGKPANDTNSNNNMT
CCCCCCCCCCCCCCE		40.1125619855
717PhosphorylationKPANDTNSNNNMTYR
CCCCCCCCCCCCEEC		42.9225619855
722PhosphorylationTNSNNNMTYRNAGTV
CCCCCCCEECCHHHH		22.8125619855
723PhosphorylationNSNNNMTYRNAGTVR
CCCCCCEECCHHHHH		7.3625619855
868PhosphorylationGLTKNPVSLPPLPNP
CCCCCCCCCCCCCCC		36.0925619855
876PhosphorylationLPPLPNPTKPNIPSV
CCCCCCCCCCCCCCC		66.8125619855
882PhosphorylationPTKPNIPSVPSPSSI
CCCCCCCCCCCCHHH		42.7525619855
885PhosphorylationPNIPSVPSPSSIQRN
CCCCCCCCCHHHCCC		34.9522942356
887PhosphorylationIPSVPSPSSIQRNSS
CCCCCCCHHHCCCCC		44.4025619855
888PhosphorylationPSVPSPSSIQRNSST
CCCCCCHHHCCCCCC		26.5625619855
894PhosphorylationSSIQRNSSTTAAPLG
HHHCCCCCCCCCCCC		33.0727600695
933PhosphorylationVGPSGLYSSSSSRGP
CCCCCCCCCCCCCCC		28.87-
948PhosphorylationIQMKIPISTFSPPSS
EEEEEEEECCCCCCH		20.3225619855
949PhosphorylationQMKIPISTFSPPSSA
EEEEEEECCCCCCHH		28.9325619855
951PhosphorylationKIPISTFSPPSSAEQ
EEEEECCCCCCHHHC		35.6723527152
954PhosphorylationISTFSPPSSAEQNSS
EECCCCCCHHHCCCC		45.6325619855
955PhosphorylationSTFSPPSSAEQNSSA
ECCCCCCHHHCCCCC		41.4125619855
960PhosphorylationPSSAEQNSSATPRIV
CCHHHCCCCCCCCEE		22.5025619855
961PhosphorylationSSAEQNSSATPRIVT
CHHHCCCCCCCCEEC		43.6525619855
963PhosphorylationAEQNSSATPRIVTEN
HHCCCCCCCCEECCC		18.3025619855
975PhosphorylationTENQTNKTVDSSINK
CCCCCCCEECHHHHH		31.4525338131
978PhosphorylationQTNKTVDSSINKKAA
CCCCEECHHHHHHHC		28.8725338131
1025PhosphorylationPKKISPPSSSTVSTS
CCCCCCCCCCCCCCC		40.0617203969
1026PhosphorylationKKISPPSSSTVSTSQ
CCCCCCCCCCCCCCC		35.4817203969
1035OxidationTVSTSQPMSRPLQPI
CCCCCCCCCCCCCCC		4.0417203969
1209PhosphorylationLKLARVQSQNGIVLS
EEEEEEECCCCEEEE		23.8225159016
1216PhosphorylationSQNGIVLSWSVLEVD
CCCCEEEEEEEEEEC		13.3525159016
1218PhosphorylationNGIVLSWSVLEVDRS
CCEEEEEEEEEECCC		17.2825159016
1303PhosphorylationSTDVISSSQNS----
CCCCCCCCCCC----		26.9625293948
1306PhosphorylationVISSSQNS-------
CCCCCCCC-------		33.6825293948
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 MCAF1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCAF1_MOUSE !!
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 MCAF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATF7_MOUSEAtf7physical
10777215
ERCC3_MOUSEErcc3physical
10777215
TF2H1_MOUSEGtf2h1physical
10777215
CDK7_MOUSECdk7physical
10777215
CCNH_MOUSECcnhphysical
10777215
T2EB_MOUSEGtf2e2physical
10777215
TF2H3_MOUSEGtf2h3physical
10777215
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCAF1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory