CAF1B_HUMAN - dbPTM
CAF1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAF1B_HUMAN
UniProt AC Q13112
Protein Name Chromatin assembly factor 1 subunit B
Gene Name CHAF1B
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Nucleus . Cytoplasm . DNA replication foci. Cytoplasmic in M phase.
Protein Description Complex that is thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer..
Protein Sequence MKVITCEIAWHNKEPVYSLDFQHGTAGRIHRLASAGVDTNVRIWKVEKGPDGKAIVEFLSNLARHTKAVNVVRFSPTGEILASGGDDAVILLWKVNDNKEPEQIAFQDEDEAQLNKENWTVVKTLRGHLEDVYDICWATDGNLMASASVDNTAIIWDVSKGQKISIFNEHKSYVQGVTWDPLGQYVATLSCDRVLRVYSIQKKRVAFNVSKMLSGIGAEGEARSYRMFHDDSMKSFFRRLSFTPDGSLLLTPAGCVESGENVMNTTYVFSRKNLKRPIAHLPCPGKATLAVRCCPVYFELRPVVETGVELMSLPYRLVFAVASEDSVLLYDTQQSFPFGYVSNIHYHTLSDISWSSDGAFLAISSTDGYCSFVTFEKDELGIPLKEKPVLNMRTPDTAKKTKSQTHRGSSPGPRPVEGTPASRTQDPSSPGTTPPQARQAPAPTVIRDPPSITPAVKSPLPGPSEEKTLQPSSQNTKAHPSRRVTLNTLQAWSKTTPRRINLTPLKTDTPPSSVPTSVISTPSTEEIQSETPGDAQGSPPELKRPRLDENKGGTESLDP
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
13AcetylationCEIAWHNKEPVYSLD
EEEEECCCCCEEEEE		50.9726051181
13UbiquitinationCEIAWHNKEPVYSLD
EEEEECCCCCEEEEE		50.97-
15UbiquitinationIAWHNKEPVYSLDFQ
EEECCCCCEEEEECC		31.7722817900
16UbiquitinationAWHNKEPVYSLDFQH
EECCCCCEEEEECCC		5.4922817900
24UbiquitinationYSLDFQHGTAGRIHR
EEEECCCCCHHHHHH		13.3821890473
34PhosphorylationGRIHRLASAGVDTNV
HHHHHHHHCCCCCCE		30.1023312004
39PhosphorylationLASAGVDTNVRIWKV
HHHCCCCCCEEEEEE		32.9623312004
45UbiquitinationDTNVRIWKVEKGPDG
CCCEEEEEEEECCCH		37.84-
47UbiquitinationNVRIWKVEKGPDGKA
CEEEEEEEECCCHHH		48.8721890473
48UbiquitinationVRIWKVEKGPDGKAI
EEEEEEEECCCHHHH		77.9222817900
53UbiquitinationVEKGPDGKAIVEFLS
EEECCCHHHHHHHHH		42.1721963094
60PhosphorylationKAIVEFLSNLARHTK
HHHHHHHHHHHHHCC		34.8124719451
66PhosphorylationLSNLARHTKAVNVVR
HHHHHHHCCCEEEEE		18.3624719451
67UbiquitinationSNLARHTKAVNVVRF
HHHHHHCCCEEEEEE		44.1821906983
94UbiquitinationDAVILLWKVNDNKEP
CEEEEEEEECCCCCH		31.0022817900
99UbiquitinationLWKVNDNKEPEQIAF
EEEECCCCCHHHCCC		76.9921906983
116UbiquitinationEDEAQLNKENWTVVK
HHHHHHCCCCEEEEH		62.1021906983
123UbiquitinationKENWTVVKTLRGHLE
CCCEEEEHHHHHCHH		37.1922817900
163UbiquitinationWDVSKGQKISIFNEH
EECCCCCEEEEECCC		47.2729967540
198UbiquitinationCDRVLRVYSIQKKRV
CCEEEEEEEECCCEE		8.1421890473
200UbiquitinationRVLRVYSIQKKRVAF
EEEEEEEECCCEEEE		3.6922817900
2022-HydroxyisobutyrylationLRVYSIQKKRVAFNV
EEEEEECCCEEEEEH		40.66-
202UbiquitinationLRVYSIQKKRVAFNV
EEEEEECCCEEEEEH		40.6621906983
202AcetylationLRVYSIQKKRVAFNV
EEEEEECCCEEEEEH		40.6625953088
203UbiquitinationRVYSIQKKRVAFNVS
EEEEECCCEEEEEHH		35.4122817900
211AcetylationRVAFNVSKMLSGIGA
EEEEEHHHHHHCCCC		39.3125953088
211UbiquitinationRVAFNVSKMLSGIGA
EEEEEHHHHHHCCCC		39.3121890473
212UbiquitinationVAFNVSKMLSGIGAE
EEEEHHHHHHCCCCC		2.5423503661
212SulfoxidationVAFNVSKMLSGIGAE
EEEEHHHHHHCCCCC		2.5421406390
213UbiquitinationAFNVSKMLSGIGAEG
EEEHHHHHHCCCCCC		4.9524816145
214PhosphorylationFNVSKMLSGIGAEGE
EEHHHHHHCCCCCCC		25.5122210691
215UbiquitinationNVSKMLSGIGAEGEA
EHHHHHHCCCCCCCH		20.5623503661
234UbiquitinationMFHDDSMKSFFRRLS
CCCCHHHHHHHHHHC		48.3322817900
235PhosphorylationFHDDSMKSFFRRLSF
CCCHHHHHHHHHHCC		22.4524719451
275UbiquitinationVFSRKNLKRPIAHLP
EEECCCCCCCCCCCC		66.5729967540
306PhosphorylationELRPVVETGVELMSL
EECCCCCCCCHHHCC		34.6128387310
307UbiquitinationLRPVVETGVELMSLP
ECCCCCCCCHHHCCC		9.4421890473
312PhosphorylationETGVELMSLPYRLVF
CCCCHHHCCCCEEEE		38.5328387310
364UbiquitinationDGAFLAISSTDGYCS
CCCEEEEECCCCCEE		22.9024816145
385UbiquitinationDELGIPLKEKPVLNM
CCCCCCCCCCCCCCC		59.3421906983
387UbiquitinationLGIPLKEKPVLNMRT
CCCCCCCCCCCCCCC		38.5522817900
394PhosphorylationKPVLNMRTPDTAKKT
CCCCCCCCCCCCHHC		18.1023401153
397PhosphorylationLNMRTPDTAKKTKSQ
CCCCCCCCCHHCCCC		41.3925159151
399UbiquitinationMRTPDTAKKTKSQTH
CCCCCCCHHCCCCCC		64.1723503661
400UbiquitinationRTPDTAKKTKSQTHR
CCCCCCHHCCCCCCC		59.7424816145
402UbiquitinationPDTAKKTKSQTHRGS
CCCCHHCCCCCCCCC		49.8223503661
403PhosphorylationDTAKKTKSQTHRGSS
CCCHHCCCCCCCCCC		45.6128985074
405PhosphorylationAKKTKSQTHRGSSPG
CHHCCCCCCCCCCCC		22.1925394399
407MethylationKTKSQTHRGSSPGPR
HCCCCCCCCCCCCCC		50.50-
409PhosphorylationKSQTHRGSSPGPRPV
CCCCCCCCCCCCCCC		33.0629255136
410PhosphorylationSQTHRGSSPGPRPVE
CCCCCCCCCCCCCCC		36.3829255136
419PhosphorylationGPRPVEGTPASRTQD
CCCCCCCCCCCCCCC		11.3725159151
422PhosphorylationPVEGTPASRTQDPSS
CCCCCCCCCCCCCCC		36.7423927012
424PhosphorylationEGTPASRTQDPSSPG
CCCCCCCCCCCCCCC		34.5223927012
428PhosphorylationASRTQDPSSPGTTPP
CCCCCCCCCCCCCCC		58.4129255136
429PhosphorylationSRTQDPSSPGTTPPQ
CCCCCCCCCCCCCCC		32.5119664994
432PhosphorylationQDPSSPGTTPPQARQ
CCCCCCCCCCCCHHC		39.2429255136
433PhosphorylationDPSSPGTTPPQARQA
CCCCCCCCCCCHHCC		38.6029255136
444PhosphorylationARQAPAPTVIRDPPS
HHCCCCCEEECCCCC		30.5824732914
451PhosphorylationTVIRDPPSITPAVKS
EEECCCCCCCCCCCC		44.4725159151
453PhosphorylationIRDPPSITPAVKSPL
ECCCCCCCCCCCCCC		14.9925159151
457AcetylationPSITPAVKSPLPGPS
CCCCCCCCCCCCCCC		48.7625953088
458PhosphorylationSITPAVKSPLPGPSE
CCCCCCCCCCCCCCC		25.6829255136
464PhosphorylationKSPLPGPSEEKTLQP
CCCCCCCCCCCCCCC		65.3930266825
468PhosphorylationPGPSEEKTLQPSSQN
CCCCCCCCCCCCCCC		33.6328111955
472PhosphorylationEEKTLQPSSQNTKAH
CCCCCCCCCCCCCCC		31.4320068231
473PhosphorylationEKTLQPSSQNTKAHP
CCCCCCCCCCCCCCC		33.8525159151
476PhosphorylationLQPSSQNTKAHPSRR
CCCCCCCCCCCCCCC		23.2120068231
477UbiquitinationQPSSQNTKAHPSRRV
CCCCCCCCCCCCCCE		52.8529967540
481PhosphorylationQNTKAHPSRRVTLNT
CCCCCCCCCCEEHHH		23.8923882029
485PhosphorylationAHPSRRVTLNTLQAW
CCCCCCEEHHHHHHH		16.6925159151
488PhosphorylationSRRVTLNTLQAWSKT
CCCEEHHHHHHHHCC		24.3023312004
493PhosphorylationLNTLQAWSKTTPRRI
HHHHHHHHCCCCCEE		24.1224719451
494AcetylationNTLQAWSKTTPRRIN
HHHHHHHCCCCCEEE		45.8019608861
494UbiquitinationNTLQAWSKTTPRRIN
HHHHHHHCCCCCEEE		45.8023000965
495PhosphorylationTLQAWSKTTPRRINL
HHHHHHCCCCCEEEC		36.2028111955
496PhosphorylationLQAWSKTTPRRINLT
HHHHHCCCCCEEECC		20.6626278961
503PhosphorylationTPRRINLTPLKTDTP
CCCEEECCCCCCCCC		23.3025159151
507PhosphorylationINLTPLKTDTPPSSV
EECCCCCCCCCCCCC		53.4322199227
509PhosphorylationLTPLKTDTPPSSVPT
CCCCCCCCCCCCCCC		42.1825159151
512PhosphorylationLKTDTPPSSVPTSVI
CCCCCCCCCCCCCEE		45.2125159151
513PhosphorylationKTDTPPSSVPTSVIS
CCCCCCCCCCCCEEE		37.5822199227
516PhosphorylationTPPSSVPTSVISTPS
CCCCCCCCCEEECCC		33.2130266825
517PhosphorylationPPSSVPTSVISTPST
CCCCCCCCEEECCCH		16.0430266825
520PhosphorylationSVPTSVISTPSTEEI
CCCCCEEECCCHHHH		31.9130266825
521PhosphorylationVPTSVISTPSTEEIQ
CCCCEEECCCHHHHH		15.3330266825
523PhosphorylationTSVISTPSTEEIQSE
CCEEECCCHHHHHCC		48.8430266825
524PhosphorylationSVISTPSTEEIQSET
CEEECCCHHHHHCCC		38.5530266825
529PhosphorylationPSTEEIQSETPGDAQ
CCHHHHHCCCCCCCC		49.4530266825
531PhosphorylationTEEIQSETPGDAQGS
HHHHHCCCCCCCCCC		37.5130266825
538PhosphorylationTPGDAQGSPPELKRP
CCCCCCCCCCCCCCC		25.7925159151
551UbiquitinationRPRLDENKGGTESLD
CCCCCCCCCCCCCCC		57.5824816145
554PhosphorylationLDENKGGTESLDP--
CCCCCCCCCCCCC--		30.9423663014
556PhosphorylationENKGGTESLDP----
CCCCCCCCCCC----		37.6023663014
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 CAF1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAF1B_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 CAF1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX5_HUMANCBX5physical
12697822
CAF1A_HUMANCHAF1Aphysical
9614144
ASF1A_HUMANASF1Aphysical
11897662
ASF1B_HUMANASF1Bphysical
11897662
ASF1A_HUMANASF1Aphysical
16980972
ASF1B_HUMANASF1Bphysical
16980972
SETB1_HUMANSETDB1physical
19498464
CBX5_HUMANCBX5physical
15882967
CAF1A_HUMANCHAF1Aphysical
21724829
H32_HUMANHIST2H3Cphysical
21724829
A4_HUMANAPPphysical
21832049
PCNA_HUMANPCNAphysical
22939629
H31_HUMANHIST1H3Aphysical
15664198
CAF1A_HUMANCHAF1Aphysical
26344197
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 CAF1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND SER-538, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-429; THR-432;THR-433; THR-524; SER-529 AND SER-538, AND MASS SPECTROMETRY.
"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-409; THR-419; SER-429;THR-433; THR-503; THR-524 AND SER-538, AND MASS SPECTROMETRY.
"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-458, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND SER-538, ANDMASS SPECTROMETRY.
"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 THR-485, AND MASSSPECTROMETRY.

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