ASF1A_HUMAN - dbPTM
ASF1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASF1A_HUMAN
UniProt AC Q9Y294
Protein Name Histone chaperone ASF1A
Gene Name ASF1A
Organism Homo sapiens (Human).
Sequence Length 204
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 and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit..
Protein Sequence MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
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
120PhosphorylationVNNEYTETELRENPP
ECCCCCCCCHHHCCC
32.3019562805
129UbiquitinationLRENPPVKPDFSKLQ
HHHCCCCCCCHHHHH
44.6424816145
142PhosphorylationLQRNILASNPRVTRF
HHHHHHHCCCCEEEE
43.8726055452
157PhosphorylationHINWEDNTEKLEDAE
EEECCCCHHHHHHHH
46.9826657352
159UbiquitinationNWEDNTEKLEDAESS
ECCCCHHHHHHHHHC
55.9529967540
165PhosphorylationEKLEDAESSNPNLQS
HHHHHHHHCCCCHHH
36.8230266825
166PhosphorylationKLEDAESSNPNLQSL
HHHHHHHCCCCHHHH
48.0525159151
172PhosphorylationSSNPNLQSLLSTDAL
HCCCCHHHHHCCCCC
34.1530266825
175PhosphorylationPNLQSLLSTDALPSA
CCHHHHHCCCCCCCC
29.5430266825
176PhosphorylationNLQSLLSTDALPSAS
CHHHHHCCCCCCCCC
25.8430266825
181PhosphorylationLSTDALPSASKGWST
HCCCCCCCCCCCCCC
46.1323898821
183PhosphorylationTDALPSASKGWSTSE
CCCCCCCCCCCCCCC
35.7225159151
189PhosphorylationASKGWSTSENSLNVM
CCCCCCCCCHHHHHH
29.3027080861
192PhosphorylationGWSTSENSLNVMLES
CCCCCCHHHHHHHHH
19.7814680630

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
192SPhosphorylationKinaseTLK2Q86UE8
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
192SPhosphorylation

20016786

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 ASF1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAF1A_HUMANCHAF1Aphysical
11897662
CAF1B_HUMANCHAF1Bphysical
11897662
HIRA_HUMANHIRAphysical
16980972
HIRA_HUMANHIRAphysical
15621527
HTAI2_HUMANHTATIP2physical
15073177
H31T_HUMANHIST3H3physical
17242207
HIRA_HUMANHIRAphysical
17242207
TAF1_HUMANTAF1physical
20393127
H31_HUMANHIST1H3Aphysical
20393127
CDAN1_HUMANCDAN1physical
22407294
IPO4_HUMANIPO4physical
22407294
NASP_HUMANNASPphysical
22407294
RBBP7_HUMANRBBP7physical
22407294
RBBP4_HUMANRBBP4physical
22407294
H31_HUMANHIST1H3Aphysical
22407294
MCM2_HUMANMCM2physical
22407294
MCM4_HUMANMCM4physical
22407294
MCM6_HUMANMCM6physical
22407294
MCM7_HUMANMCM7physical
22407294
TONSL_HUMANTONSLphysical
22407294
ASF1B_HUMANASF1Bphysical
22407294
H31_HUMANHIST1H3Aphysical
15664198
NASP_HUMANNASPphysical
15664198
RBBP4_HUMANRBBP4physical
15664198
H4_XENLAhist1h4aphysical
23178455
H33_HUMANH3F3Aphysical
23075851
H31T_HUMANHIST3H3physical
24209620
H33_HUMANH3F3Aphysical
24209620
SYSC_HUMANSARSphysical
22863883
FBW1A_HUMANBTRCphysical
24700029
CUL1_HUMANCUL1physical
24700029
PRR3_HUMANPRR3physical
25416956
CENPB_HUMANCENPBphysical
26496610
COPB_HUMANCOPB1physical
26496610
NASP_HUMANNASPphysical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
RBBP4_HUMANRBBP4physical
26496610
RBBP7_HUMANRBBP7physical
26496610
SPTN2_HUMANSPTBN2physical
26496610
HIRA_HUMANHIRAphysical
26496610
HAT1_HUMANHAT1physical
26496610
TLK2_HUMANTLK2physical
26496610
ANKL2_HUMANANKLE2physical
26496610
CABIN_HUMANCABIN1physical
26496610
UBN1_HUMANUBN1physical
26496610
RIF1_HUMANRIF1physical
26496610
ASF1B_HUMANASF1Bphysical
26496610
IPO4_HUMANIPO4physical
26496610
ARFG2_HUMANARFGAP2physical
26496610
CO041_HUMANC15orf41physical
26496610
CDAN1_HUMANCDAN1physical
26496610
UBN2_HUMANUBN2physical
26496610
CO041_HUMANC15orf41physical
28514442
CDAN1_HUMANCDAN1physical
28514442
UBN2_HUMANUBN2physical
28514442
PAN3_HUMANPAN3physical
28514442
UBN1_HUMANUBN1physical
28514442
CABIN_HUMANCABIN1physical
28514442
HIRA_HUMANHIRAphysical
28514442
TLK1_HUMANTLK1physical
28514442
TLK2_HUMANTLK2physical
28514442
PAN2_HUMANPAN2physical
28514442
TONSL_HUMANTONSLphysical
28514442
NASP_HUMANNASPphysical
28514442
IPO4_HUMANIPO4physical
28514442
MCM2_HUMANMCM2physical
28514442
MCM4_HUMANMCM4physical
28514442
MCM6_HUMANMCM6physical
28514442
RBBP4_HUMANRBBP4physical
28514442
RIF1_HUMANRIF1physical
28514442
MCM7_HUMANMCM7physical
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 ASF1A_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-192 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-166 AND SER-172, ANDMASS SPECTROMETRY.

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