PHF5A_HUMAN - dbPTM
PHF5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF5A_HUMAN
UniProt AC Q7RTV0
Protein Name PHD finger-like domain-containing protein 5A
Gene Name PHF5A
Organism Homo sapiens (Human).
Sequence Length 110
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. [PubMed: 27720643]
Protein Sequence MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
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
3Malonylation-----MAKHHPDLIF
-----CCCCCCCEEE		40.9426320211
3Ubiquitination-----MAKHHPDLIF
-----CCCCCCCEEE		40.9419608861
32-Hydroxyisobutyrylation-----MAKHHPDLIF
-----CCCCCCCEEE		40.94-
3Acetylation-----MAKHHPDLIF
-----CCCCCCCEEE		40.9419608861
13UbiquitinationPDLIFCRKQAGVAIG
CCEEEEEHHCCCHHH		45.76-
132-HydroxyisobutyrylationPDLIFCRKQAGVAIG
CCEEEEEHHCCCHHH		45.76-
25AcetylationAIGRLCEKCDGKCVI
HHHHHHHHCCCEEEE		36.3123749302
252-HydroxyisobutyrylationAIGRLCEKCDGKCVI
HHHHHHHHCCCEEEE		36.31-
29AcetylationLCEKCDGKCVICDSY
HHHHCCCEEEEECCC		16.4525953088
35PhosphorylationGKCVICDSYVRPCTL
CEEEEECCCCCCCEE		22.5528152594
36PhosphorylationKCVICDSYVRPCTLV
EEEEECCCCCCCEEE		6.2928152594
41PhosphorylationDSYVRPCTLVRICDE
CCCCCCCEEEEECCC		30.8528152594
51PhosphorylationRICDECNYGSYQGRC
EECCCCCCCCCCCEE		21.0728152594
53PhosphorylationCDECNYGSYQGRCVI
CCCCCCCCCCCEEEE		12.1528152594
54PhosphorylationDECNYGSYQGRCVIC
CCCCCCCCCCEEEEC		15.6028152594
67PhosphorylationICGGPGVSDAYYCKE
ECCCCCCCCEEEEEC		23.5728152594
70PhosphorylationGPGVSDAYYCKECTI
CCCCCCEEEEECCCC		17.8728152594
71PhosphorylationPGVSDAYYCKECTIQ
CCCCCEEEEECCCCC		9.9628152594
73UbiquitinationVSDAYYCKECTIQEK
CCCEEEEECCCCCEE		39.44-
73AcetylationVSDAYYCKECTIQEK
CCCEEEEECCCCCEE		39.4423749302
80AcetylationKECTIQEKDRDGCPK
ECCCCCEECCCCCCC		41.5125953088
87UbiquitinationKDRDGCPKIVNLGSS
ECCCCCCCEEEECCC		64.46-
87AcetylationKDRDGCPKIVNLGSS
ECCCCCCCEEEECCC		64.4626051181
93PhosphorylationPKIVNLGSSKTDLFY
CCEEEECCCCHHHHH		31.6528450419
94PhosphorylationKIVNLGSSKTDLFYE
CEEEECCCCHHHHHH		37.4628450419
95MalonylationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.9926320211
95SumoylationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.99-
95AcetylationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.9926051181
95UbiquitinationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.9921890473
952-HydroxyisobutyrylationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.99-
95SumoylationIVNLGSSKTDLFYER
EEEECCCCHHHHHHH		47.99-
96PhosphorylationVNLGSSKTDLFYERK
EEECCCCHHHHHHHH		39.6228450419
100PhosphorylationSSKTDLFYERKKYGF
CCCHHHHHHHHHHCC		23.3228796482
105PhosphorylationLFYERKKYGFKKR--
HHHHHHHHCCCCC--		30.7226074081
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 PHF5A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF5A_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 PHF5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B1_HUMANSF3B1physical
22939629
SF3B3_HUMANSF3B3physical
22939629
RU2A_HUMANSNRPA1physical
22939629
SF3B4_HUMANSF3B4physical
22939629
RU2B_HUMANSNRPB2physical
22939629
SF3B6_HUMANSF3B6physical
22939629
SF3B5_HUMANSF3B5physical
22939629
SF3B2_HUMANSF3B2physical
22939629
YBOX1_HUMANYBX1physical
22939629
ROA1_HUMANHNRNPA1physical
22939629
SFPQ_HUMANSFPQphysical
22939629
PRP31_HUMANPRPF31physical
22939629
RBM25_HUMANRBM25physical
22939629
S10AA_HUMANS100A10physical
22939629
PRP31_HUMANPRPF31physical
22365833
SF3B4_HUMANSF3B4physical
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 PHF5A_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-3, AND MASS SPECTROMETRY.

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