YAF2_HUMAN - dbPTM
YAF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YAF2_HUMAN
UniProt AC Q8IY57
Protein Name YY1-associated factor 2
Gene Name YAF2
Organism Homo sapiens (Human).
Sequence Length 180
Subcellular Localization Nucleus .
Protein Description Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling..
Protein Sequence MGDKKSPTRPKRQPKPSSDEGYWDCSVCTFRNSAEAFKCMMCDVRKGTSTRKPRPVSQLVAQQVTQQFVPPTQSKKEKKDKVEKEKSEKETTSKKNSHKKTRPRLKNVDRSSAQHLEVTVGDLTVIITDFKEKTKSPPASSAASADQHSQSGSSSDNTERGMSRSSSPRGEASSLNGESH
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
6Phosphorylation--MGDKKSPTRPKRQ
--CCCCCCCCCCCCC		36.9317081983
8PhosphorylationMGDKKSPTRPKRQPK
CCCCCCCCCCCCCCC		67.6920068231
18PhosphorylationKRQPKPSSDEGYWDC
CCCCCCCCCCCCCCC		48.4828555341
38UbiquitinationRNSAEAFKCMMCDVR
ECCHHHHHHHCCCCC		28.412189047
38 (in isoform 1)Ubiquitination-28.4121890473
38UbiquitinationRNSAEAFKCMMCDVR
ECCHHHHHHHCCCCC		28.4121890473
52UbiquitinationRKGTSTRKPRPVSQL
CCCCCCCCCCCHHHH		45.53-
57PhosphorylationTRKPRPVSQLVAQQV
CCCCCCHHHHHHHHH		22.0830576142
65PhosphorylationQLVAQQVTQQFVPPT
HHHHHHHHHHCCCCC		16.5929978859
72PhosphorylationTQQFVPPTQSKKEKK
HHHCCCCCCCHHHHH		39.1328555341
74PhosphorylationQFVPPTQSKKEKKDK
HCCCCCCCHHHHHHH		48.4428555341
94MethylationSEKETTSKKNSHKKT
HHHHHHCCCCCCCCC		54.61-
94TrimethylationSEKETTSKKNSHKKT
HHHHHHCCCCCCCCC		54.61-
97PhosphorylationETTSKKNSHKKTRPR
HHHCCCCCCCCCCCC		45.63-
99TrimethylationTSKKNSHKKTRPRLK
HCCCCCCCCCCCCCC		56.51-
99MethylationTSKKNSHKKTRPRLK
HCCCCCCCCCCCCCC		56.51-
111PhosphorylationRLKNVDRSSAQHLEV
CCCCCCHHHHHCEEE		26.0927080861
112PhosphorylationLKNVDRSSAQHLEVT
CCCCCHHHHHCEEEE		32.6127080861
134PhosphorylationITDFKEKTKSPPASS
EEEHHHHHCCCCCCC		37.5323927012
135UbiquitinationTDFKEKTKSPPASSA
EEHHHHHCCCCCCCC		72.53-
136PhosphorylationDFKEKTKSPPASSAA
EHHHHHCCCCCCCCC		41.1523927012
140PhosphorylationKTKSPPASSAASADQ
HHCCCCCCCCCCCCC		26.7025159151
141PhosphorylationTKSPPASSAASADQH
HCCCCCCCCCCCCCC		29.9325159151
141O-linked_GlycosylationTKSPPASSAASADQH
HCCCCCCCCCCCCCC		29.9329351928
144PhosphorylationPPASSAASADQHSQS
CCCCCCCCCCCCCCC		31.9023927012
149O-linked_GlycosylationAASADQHSQSGSSSD
CCCCCCCCCCCCCCC		22.0229351928
149PhosphorylationAASADQHSQSGSSSD
CCCCCCCCCCCCCCC		22.0217525332
151PhosphorylationSADQHSQSGSSSDNT
CCCCCCCCCCCCCCC		43.5923927012
153PhosphorylationDQHSQSGSSSDNTER
CCCCCCCCCCCCCCC		31.7323927012
154PhosphorylationQHSQSGSSSDNTERG
CCCCCCCCCCCCCCC		45.2825159151
155PhosphorylationHSQSGSSSDNTERGM
CCCCCCCCCCCCCCC		36.2625159151
158PhosphorylationSGSSSDNTERGMSRS
CCCCCCCCCCCCCCC		31.8625159151
163PhosphorylationDNTERGMSRSSSPRG
CCCCCCCCCCCCCCC		31.6630576142
165PhosphorylationTERGMSRSSSPRGEA
CCCCCCCCCCCCCCH		28.0623401153
166PhosphorylationERGMSRSSSPRGEAS
CCCCCCCCCCCCCHH		43.1621955146
167PhosphorylationRGMSRSSSPRGEASS
CCCCCCCCCCCCHHH		21.6225159151
173PhosphorylationSSPRGEASSLNGESH
CCCCCCHHHCCCCCC		30.9321955146
174PhosphorylationSPRGEASSLNGESH-
CCCCCHHHCCCCCC-		32.6625159151
177PhosphorylationGEASSLNGESH----
CCHHHCCCCCC----		42.9727251275
179PhosphorylationASSLNGESH------
HHHCCCCCC------		35.5821712546
190Phosphorylation-----------------
-----------------		27251275
191Phosphorylation------------------
------------------		24719451
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 YAF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YAF2_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 YAF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYY1_HUMANYY1physical
9016636
RING2_HUMANRNF2physical
22325352
PCGF1_HUMANPCGF1physical
22325352
PCGF2_HUMANPCGF2physical
22325352
PCGF3_HUMANPCGF3physical
22325352
BMI1_HUMANBMI1physical
22325352
PCGF5_HUMANPCGF5physical
22325352
PCGF6_HUMANPCGF6physical
22325352
RING1_HUMANRING1physical
22325352
LMBL2_HUMANL3MBTL2physical
22325352
CBX3_HUMANCBX3physical
22325352
E2F6_HUMANE2F6physical
22325352
TFDP1_HUMANTFDP1physical
22325352
WDR5_HUMANWDR5physical
22325352
MGAP_HUMANMGAphysical
22325352
HDAC2_HUMANHDAC2physical
22325352
SKP1_HUMANSKP1physical
22325352
BCOR_HUMANBCORphysical
22325352
BCORL_HUMANBCORL1physical
22325352
KDM2B_HUMANKDM2Bphysical
22325352
UBP7_HUMANUSP7physical
22325352
FBRS_HUMANFBRSphysical
22325352
CSK21_HUMANCSNK2A1physical
22325352
CSK22_HUMANCSNK2A2physical
22325352
SETBP_HUMANSETBP1physical
25416956
RING1_HUMANRING1physical
21516116
PCGF2_HUMANPCGF2physical
28514442
PCGF6_HUMANPCGF6physical
28514442
PCGF1_HUMANPCGF1physical
28514442
PCGF3_HUMANPCGF3physical
28514442
KDM2B_HUMANKDM2Bphysical
28514442
BMI1_HUMANBMI1physical
28514442
FBRS_HUMANFBRSphysical
28514442
AGGF1_HUMANAGGF1physical
28514442
MORC4_HUMANMORC4physical
28514442
BCOR_HUMANBCORphysical
28514442
BCORL_HUMANBCORL1physical
28514442
RING2_HUMANRNF2physical
28514442
RING1_HUMANRING1physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
AUTS2_HUMANAUTS2physical
28514442
ZN622_HUMANZNF622physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
LMBL2_HUMANL3MBTL2physical
28514442
CHD8_HUMANCHD8physical
28514442
ENL_HUMANMLLT1physical
28514442
FBX7_HUMANFBXO7physical
28514442
TRI26_HUMANTRIM26physical
28514442
DCAF7_HUMANDCAF7physical
28514442
UBXN1_HUMANUBXN1physical
28514442
MGAP_HUMANMGAphysical
28514442
E2F6_HUMANE2F6physical
28514442
MCAF1_HUMANATF7IPphysical
28514442
PAF1_HUMANPAF1physical
28514442
FBSL_HUMANFBRSL1physical
28514442
RYBP_HUMANRYBPphysical
28514442
UBE2S_HUMANUBE2Sphysical
28514442
MDM2_HUMANMDM2physical
28514442
TFDP1_HUMANTFDP1physical
28514442
ARI4B_HUMANARID4Bphysical
28514442
UBP7_HUMANUSP7physical
28514442
ARF6_HUMANARF6physical
28514442
CO1A1_HUMANCOL1A1physical
28514442
CTR9_HUMANCTR9physical
28514442
CSK2B_HUMANCSNK2Bphysical
28514442
DCAF6_HUMANDCAF6physical
28514442
CO1A2_HUMANCOL1A2physical
28514442
UBB_HUMANUBBphysical
28514442
PDCD5_HUMANPDCD5physical
25603536
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 YAF2_HUMAN

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Related Literatures of Post-Translational Modification
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-167, 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-167, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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-6, AND MASSSPECTROMETRY.

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