YYAP1_HUMAN - dbPTM
YYAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YYAP1_HUMAN
UniProt AC Q9H869
Protein Name YY1-associated protein 1 {ECO:0000303|PubMed:14744866}
Gene Name YY1AP1 {ECO:0000312|HGNC:HGNC:30935}
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus .
Protein Description Associates with the INO80 chromatin remodeling complex, which is responsible for transcriptional regulation, DNA repair, and replication. [PubMed: 27939641 Enhances transcription activation by YY1]
Protein Sequence MEEEASRSAAATNPGSRLTRWPPPDKREGSAVDPGKRRSLAATPSSSLPCTLIALGLRHEKEANELMEDLFETFQDEMGFSNMEDDGPEEEERVAEPQANFNTPQALRFEELLANLLNEQHQIAKELFEQLKMKKPSAKQQKEVEKVKPQCKEVHQTLILDPAQRKRLQQQMQQHVQLLTQIHLLATCNPNLNPEASSTRICLKELGTFAQSSIALHHQYNPKFQTLFQPCNLMGAMQLIEDFSTHVSIDCSPHKTVKKTANEFPCLPKQVAWILATSKVFMYPELLPVCSLKAKNPQDKILFTKAEDNKYLLTCKTARQLTVRIKNLNMNRAPDNIIKFYKKTKQLPVLGKCCEEIQPHQWKPPIEREEHRLPFWLKASLPSIQEELRHMADGAREVGNMTGTTEINSDQGLEKDNSELGSETRYPLLLPKGVVLKLKPVADRFPKKAWRQKRSSVLKPLLIQPSPSLQPSFNPGKTPAQSTHSEAPPSKMVLRIPHPIQPATVLQTVPGVPPLGVSGGESFESPAALPAMPPEARTSFPLSESQTLLSSAPVPKVMMPSPASSMFRKPYVRRRPSKRRGARAFRCIKPAPVIHPASVIFTVPATTVKIVSLGGGCNMIQPVNAAVAQSPQTIPIATLLVNPTSFPCPLNQPLVASSVSPLIVSGNSVNLPIPSTPEDKAHMNVDIACAVADGENAFQGLEPKLEPQELSPLSATVFPKVEHSPGPPPVDKQCQEGLSENSAYRWTVVKTEEGRQALEPLPQGIQESLNNSSPGDLEEVVKMEPEDATEEISGFL
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
7 (in isoform 9)Phosphorylation-37.0525072903
7 (in isoform 8)Phosphorylation-37.0525072903
12PhosphorylationASRSAAATNPGSRLT
HHHHHHCCCCCCCCC		36.90-
16PhosphorylationAAATNPGSRLTRWPP
HHCCCCCCCCCCCCC		25.93-
19PhosphorylationTNPGSRLTRWPPPDK
CCCCCCCCCCCCCCC		29.58-
30PhosphorylationPPDKREGSAVDPGKR
CCCCCCCCCCCCCCC		21.99-
39PhosphorylationVDPGKRRSLAATPSS
CCCCCCCCCCCCCCC		26.79-
51PhosphorylationPSSSLPCTLIALGLR
CCCCCCHHHHHHHCC		21.18-
103PhosphorylationEPQANFNTPQALRFE
CCCCCCCCHHHHHHH		16.7925159151
132UbiquitinationKELFEQLKMKKPSAK
HHHHHHHHCCCCCHH		48.66-
137PhosphorylationQLKMKKPSAKQQKEV
HHHCCCCCHHHHHHH		57.9120860994
146UbiquitinationKQQKEVEKVKPQCKE
HHHHHHHHHHHHHHH		61.81-
148UbiquitinationQKEVEKVKPQCKEVH
HHHHHHHHHHHHHHH		40.20-
152UbiquitinationEKVKPQCKEVHQTLI
HHHHHHHHHHHHHHC		58.48-
252PhosphorylationTHVSIDCSPHKTVKK
CCEEEECCCCCCCCC		26.7025627689
259UbiquitinationSPHKTVKKTANEFPC
CCCCCCCCCCCCCCC		48.83-
293UbiquitinationLLPVCSLKAKNPQDK
HHHHCCCCCCCCCCE		40.81-
300UbiquitinationKAKNPQDKILFTKAE
CCCCCCCEEEEEECC		35.74-
305UbiquitinationQDKILFTKAEDNKYL
CCEEEEEECCCCCEE		42.30-
310UbiquitinationFTKAEDNKYLLTCKT
EEECCCCCEEEEECC		49.99-
314PhosphorylationEDNKYLLTCKTARQL
CCCCEEEEECCCCHH		14.9030301811
316UbiquitinationNKYLLTCKTARQLTV
CCEEEEECCCCHHHH		39.73-
317PhosphorylationKYLLTCKTARQLTVR
CEEEEECCCCHHHHE		29.2630301811
326UbiquitinationRQLTVRIKNLNMNRA
CHHHHEEECCCCCCC		44.83-
339UbiquitinationRAPDNIIKFYKKTKQ
CCCCCHHHHHHHHCC		38.55-
345UbiquitinationIKFYKKTKQLPVLGK
HHHHHHHCCCCCCHH		59.73-
352UbiquitinationKQLPVLGKCCEEIQP
CCCCCCHHHHCCCCC		31.39-
378UbiquitinationHRLPFWLKASLPSIQ
CCCCHHHHCCCHHHH		26.90-
404PhosphorylationEVGNMTGTTEINSDQ
HCCCCCCCCEECCCC		16.4622798277
418PhosphorylationQGLEKDNSELGSETR
CCCCCCCCCCCCCCC		44.3122798277
422PhosphorylationKDNSELGSETRYPLL
CCCCCCCCCCCCCEE		48.7120873877
424PhosphorylationNSELGSETRYPLLLP
CCCCCCCCCCCEECC		36.8822798277
426PhosphorylationELGSETRYPLLLPKG
CCCCCCCCCEECCCC		12.9720873877
432UbiquitinationRYPLLLPKGVVLKLK
CCCEECCCCEEEEEE		65.39-
437UbiquitinationLPKGVVLKLKPVADR
CCCCEEEEEECCHHH		42.74-
455PhosphorylationKAWRQKRSSVLKPLL
HHHHHHHHHCCHHEE		31.6627080861
456PhosphorylationAWRQKRSSVLKPLLI
HHHHHHHHCCHHEEE		35.1927080861
459SumoylationQKRSSVLKPLLIQPS
HHHHHCCHHEEECCC		31.31-
459UbiquitinationQKRSSVLKPLLIQPS
HHHHHCCHHEEECCC		31.31-
459SumoylationQKRSSVLKPLLIQPS
HHHHHCCHHEEECCC		31.31-
466PhosphorylationKPLLIQPSPSLQPSF
HHEEECCCCCCCCCC		15.6725159151
468PhosphorylationLLIQPSPSLQPSFNP
EEECCCCCCCCCCCC		43.9325627689
491UbiquitinationHSEAPPSKMVLRIPH
CCCCCCCCEEEECCC		38.51-
491SumoylationHSEAPPSKMVLRIPH
CCCCCCCCEEEECCC		38.51-
491SumoylationHSEAPPSKMVLRIPH
CCCCCCCCEEEECCC		38.51-
504PhosphorylationPHPIQPATVLQTVPG
CCCCCCCEEEEECCC		28.5620068231
508PhosphorylationQPATVLQTVPGVPPL
CCCEEEEECCCCCCC		25.2220068231
518PhosphorylationGVPPLGVSGGESFES
CCCCCCCCCCCCCCC		39.0020068231
522PhosphorylationLGVSGGESFESPAAL
CCCCCCCCCCCCCCC		37.2720068231
525PhosphorylationSGGESFESPAALPAM
CCCCCCCCCCCCCCC		20.1620068231
538PhosphorylationAMPPEARTSFPLSES
CCCCCHHCCCCCCHH		41.5920068231
539PhosphorylationMPPEARTSFPLSESQ
CCCCHHCCCCCCHHH		21.2220068231
543PhosphorylationARTSFPLSESQTLLS
HHCCCCCCHHHHHHH		35.1323186163
545PhosphorylationTSFPLSESQTLLSSA
CCCCCCHHHHHHHCC		25.7020068231
547PhosphorylationFPLSESQTLLSSAPV
CCCCHHHHHHHCCCC		38.6624719451
550PhosphorylationSESQTLLSSAPVPKV
CHHHHHHHCCCCCCC		27.8020068231
551PhosphorylationESQTLLSSAPVPKVM
HHHHHHHCCCCCCCC		36.2420068231
561PhosphorylationVPKVMMPSPASSMFR
CCCCCCCCCHHHHCC		18.4020068231
564PhosphorylationVMMPSPASSMFRKPY
CCCCCCHHHHCCCCC		26.2220068231
565PhosphorylationMMPSPASSMFRKPYV
CCCCCHHHHCCCCCC		24.8520068231
589UbiquitinationARAFRCIKPAPVIHP
CCCEEECCCCCCCCC		38.46-
598PhosphorylationAPVIHPASVIFTVPA
CCCCCCCEEEEEECC		21.8724043423
602PhosphorylationHPASVIFTVPATTVK
CCCEEEEEECCCEEE		17.9224043423
606PhosphorylationVIFTVPATTVKIVSL
EEEEECCCEEEEEEE		26.5024043423
607PhosphorylationIFTVPATTVKIVSLG
EEEECCCEEEEEEEC		23.1624043423
612PhosphorylationATTVKIVSLGGGCNM
CCEEEEEEECCCCCC		25.4420068231
653PhosphorylationFPCPLNQPLVASSVS
CCCCCCCCCEECCCC		27.9424719451
665PhosphorylationSVSPLIVSGNSVNLP
CCCCEEEECCCCCCC		25.8419664995
704SumoylationAFQGLEPKLEPQELS
CCCCCCCCCCHHHCC		56.99-
711PhosphorylationKLEPQELSPLSATVF
CCCHHHCCCCEEEEC		24.0429255136
714PhosphorylationPQELSPLSATVFPKV
HHHCCCCEEEECCCC		25.8530266825
716PhosphorylationELSPLSATVFPKVEH
HCCCCEEEECCCCCC		21.2123927012
720SumoylationLSATVFPKVEHSPGP
CEEEECCCCCCCCCC		49.11-
724PhosphorylationVFPKVEHSPGPPPVD
ECCCCCCCCCCCCCC		20.3223401153
732SumoylationPGPPPVDKQCQEGLS
CCCCCCCHHHHHCCC		53.89-
732UbiquitinationPGPPPVDKQCQEGLS
CCCCCCCHHHHHCCC		53.89-
739PhosphorylationKQCQEGLSENSAYRW
HHHHHCCCCCCCCCE		45.6623927012
750SumoylationAYRWTVVKTEEGRQA
CCCEEEEECHHHHHH		45.97-
750SumoylationAYRWTVVKTEEGRQA
CCCEEEEECHHHHHH		45.97-
750UbiquitinationAYRWTVVKTEEGRQA
CCCEEEEECHHHHHH		45.97-
768PhosphorylationLPQGIQESLNNSSPG
CCHHHHHHHHCCCCC		21.7427732954
772PhosphorylationIQESLNNSSPGDLEE
HHHHHHCCCCCCHHH		36.5230278072
773PhosphorylationQESLNNSSPGDLEEV
HHHHHCCCCCCHHHH		34.7230278072
782SumoylationGDLEEVVKMEPEDAT
CCHHHHHCCCHHHCH		42.60-
816Phosphorylation---------------------------
---------------------------		24719451
865Phosphorylation----------------------------------------------------------------------------
----------------------------------------------------------------------------		27251275
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 YYAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YYAP1_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 YYAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD2L2_HUMANMAD2L2physical
17541814
CEBPA_HUMANCEBPAphysical
23769673
ZFAT_HUMANZFATphysical
21988832
S18L2_HUMANSS18L2physical
28514442
ZN579_HUMANZNF579physical
28514442
BAG1_HUMANBAG1physical
28514442
ZN496_HUMANZNF496physical
28514442
HIC2_HUMANHIC2physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
ZMYM4_HUMANZMYM4physical
28514442
B3GL2_HUMANB3GALNT2physical
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 YYAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-724, AND MASSSPECTROMETRY.

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