ASF1B_HUMAN - dbPTM
ASF1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASF1B_HUMAN
UniProt AC Q9NVP2
Protein Name Histone chaperone ASF1B
Gene Name ASF1B
Organism Homo sapiens (Human).
Sequence Length 202
Subcellular Localization Nucleus .
Protein Description Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for spermatogenesis..
Protein Sequence MAKVSVLNVAVLENPSPFHSPFRFEISFECSEALADDLEWKIIYVGSAESEEFDQILDSVLVGPVPAGRHMFVFQADAPNPSLIPETDAVGVTVVLITCTYHGQEFIRVGYYVNNEYLNPELRENPPMKPDFSQLQRNILASNPRVTRFHINWDNNMDRLEAIETQDPSLGCGLPLNCTPIKGLGLPGCIPGLLPENSMDCI
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
3Ubiquitination-----MAKVSVLNVA
-----CCCEEEEEEE		33.47-
111PhosphorylationQEFIRVGYYVNNEYL
CEEEEEEEEECCCCC		11.0328152594
112PhosphorylationEFIRVGYYVNNEYLN
EEEEEEEEECCCCCC		7.2628152594
117PhosphorylationGYYVNNEYLNPELRE
EEEECCCCCCHHHHH		17.5728152594
128SulfoxidationELRENPPMKPDFSQL
HHHHCCCCCCCHHHH		11.8221406390
129SumoylationLRENPPMKPDFSQLQ
HHHCCCCCCCHHHHH		47.40-
129UbiquitinationLRENPPMKPDFSQLQ
HHHCCCCCCCHHHHH		47.4021890473
129SumoylationLRENPPMKPDFSQLQ
HHHCCCCCCCHHHHH		47.40-
142PhosphorylationLQRNILASNPRVTRF
HHHHHHHCCCCEEEE		43.8726055452
165PhosphorylationDRLEAIETQDPSLGC
HHHHHHHCCCCCCCC		31.9625850435
169PhosphorylationAIETQDPSLGCGLPL
HHHCCCCCCCCCCCC		45.7630266825
179PhosphorylationCGLPLNCTPIKGLGL
CCCCCCCEECCCCCC		27.2930266825
198PhosphorylationPGLLPENSMDCI---
CCCCCCCCCCCC---		17.8425159151
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
198SPhosphorylationKinaseTLK2Q86UE8
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASF1B_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 ASF1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IPO4_HUMANIPO4physical
17353931
CDAN1_HUMANCDAN1physical
17353931
TLK2_HUMANTLK2physical
17353931
TLK1_HUMANTLK1physical
17353931
CAF1B_HUMANCHAF1Bphysical
17353931
RS3A_HUMANRPS3Aphysical
17353931
DOK2_HUMANDOK2physical
17353931
CO041_HUMANC15orf41physical
17353931
MMS22_HUMANMMS22Lphysical
17353931
RBBP4_HUMANRBBP4physical
17353931
CAF1A_HUMANCHAF1Aphysical
17353931
TITIN_HUMANTTNphysical
17353931
TONSL_HUMANTONSLphysical
17353931
UBXN1_HUMANUBXN1physical
17353931
DYL1_HUMANDYNLL1physical
17353931
SERB_HUMANPSPHphysical
17353931
RL31_HUMANRPL31physical
17353931
RT07_HUMANMRPS7physical
17353931
CAF1A_HUMANCHAF1Aphysical
11897662
CAF1B_HUMANCHAF1Bphysical
11897662
H31T_HUMANHIST3H3physical
20953179
HAT1_HUMANHAT1physical
20953179
RBBP7_HUMANRBBP7physical
20953179
MCM2_HUMANMCM2physical
20227376
MCM6_HUMANMCM6physical
20227376
CDAN1_HUMANCDAN1physical
22407294
IPO4_HUMANIPO4physical
22407294
FUBP2_HUMANKHSRPphysical
22939629
IDHC_HUMANIDH1physical
22939629
H31_HUMANHIST1H3Aphysical
15664198
H33_HUMANH3F3Aphysical
23075851
MMS22_HUMANMMS22Lphysical
21055984
MCM6_HUMANMCM6physical
21055984
H31T_HUMANHIST3H3physical
21055984
H31T_HUMANHIST3H3physical
24209620
H33_HUMANH3F3Aphysical
24209620
HAT1_HUMANHAT1physical
26344197
MCM2_HUMANMCM2physical
26527279
MCM3_HUMANMCM3physical
26527279
MCM4_HUMANMCM4physical
26527279
MCM5_HUMANMCM5physical
26527279
MCM6_HUMANMCM6physical
26527279
MCM7_HUMANMCM7physical
26527279
CAF1A_HUMANCHAF1Aphysical
26527279
CAF1B_HUMANCHAF1Bphysical
26527279
HIRA_HUMANHIRAphysical
26527279
CDAN1_HUMANCDAN1physical
28514442
CO041_HUMANC15orf41physical
28514442
CABIN_HUMANCABIN1physical
28514442
UBN1_HUMANUBN1physical
28514442
UBN2_HUMANUBN2physical
28514442
HIRA_HUMANHIRAphysical
28514442
PAN3_HUMANPAN3physical
28514442
TLK1_HUMANTLK1physical
28514442
PAN2_HUMANPAN2physical
28514442
TONSL_HUMANTONSLphysical
28514442
TLK2_HUMANTLK2physical
28514442
NASP_HUMANNASPphysical
28514442
MMS22_HUMANMMS22Lphysical
28514442
MCM2_HUMANMCM2physical
28514442
CAF1A_HUMANCHAF1Aphysical
28514442
IPO4_HUMANIPO4physical
28514442
MCM4_HUMANMCM4physical
28514442
PPTC7_HUMANPPTC7physical
28514442
RBBP4_HUMANRBBP4physical
28514442
MCM6_HUMANMCM6physical
28514442
MCM7_HUMANMCM7physical
28514442
CAF1B_HUMANCHAF1Bphysical
28514442
RBBP7_HUMANRBBP7physical
28514442
HAT1_HUMANHAT1physical
28514442
RIF1_HUMANRIF1physical
28514442
RECO_HUMANRCVRNphysical
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 ASF1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation-mediated control of histone chaperone ASF1 levels byTousled-like kinases.";
Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M.;
PLoS ONE 4:E8328-E8328(2009).
Cited for: PHOSPHORYLATION AT SER-198 BY TLK2.
"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-198, AND MASSSPECTROMETRY.
"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-142, AND MASSSPECTROMETRY.
"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 THR-179, AND MASSSPECTROMETRY.

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