HIRA_HUMAN - dbPTM
HIRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIRA_HUMAN
UniProt AC P54198
Protein Name Protein HIRA
Gene Name HIRA
Organism Homo sapiens (Human).
Sequence Length 1017
Subcellular Localization Nucleus. Nucleus, PML body. Primarily, though not exclusively, localized to the nucleus. Localizes to PML bodies immediately prior to onset of senescence.
Protein Description Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit..
Protein Sequence MKLLKPTWVNHNGKPIFSVDIHPDGTKFATGGQGQDSGKVVIWNMSPVLQEDDEKDENIPKMLCQMDNHLACVNCVRWSNSGMYLASGGDDKLIMVWKRATYIGPSTVFGSSGKLANVEQWRCVSILRNHSGDVMDVAWSPHDAWLASCSVDNTVVIWNAVKFPEILATLRGHSGLVKGLTWDPVGKYIASQADDRSLKVWRTLDWQLETSITKPFDECGGTTHVLRLSWSPDGHYLVSAHAMNNSGPTAQIIEREGWKTNMDFVGHRKAVTVVKFNPKIFKKKQKNGSSAKPSCPYCCCAVGSKDRSLSVWLTCLKRPLVVIHELFDKSIMDISWTLNGLGILVCSMDGSVAFLDFSQDELGDPLSEEEKSRIHQSTYGKSLAIMTEAQLSTAVIENPEMLKYQRRQQQQQLDQKSAATREMGSATSVAGVVNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTGDFSTAFFNSIPLSGSLAGTMLSSHSSPQLLPLDSSTPNSFGASKPCTEPVVAASARPAGDSVNKDSMNATSTPAALSPSVLTTPSKIEPMKAFDSRFTERSKATPGAPALTSMTPTAVERLKEQNLVKELRPRDLLESSSDSDEKVPLAKASSLSKRKLELEVETVEKKKKGRPRKDSRLMPVSLSVQSPAALTAEKEAMCLSAPALALKLPIPSPQRAFTLQVSSDPSMYIEVENEVTVVGGVKLSRLKCNREGKEWETVLTSRILTAAGSCDVVCVACEKRMLSVFSTCGRRLLSPILLPSPISTLHCTGSYVMALTAAATLSVWDVHRQVVVVKEESLHSILAGSDMTVSQILLTQHGIPVMNLSDGKAYCFNPSLSTWNLVSDKQDSLAQCADFRSSLPSQDAMLCSGPLAIIQGRTSNSGRQAARLFSVPHVVQQETTLAYLENQVAAALTLQSSHEYRHWLLVYARYLVNEGFEYRLREICKDLLGPVHYSTGSQWESTVVGLRKRELLKELLPVIGQNLRFQRLFTECQEQLDILRDK
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
27 (in isoform 1)Ubiquitination-38.2321890473
27 (in isoform 2)Ubiquitination-38.2321890473
27UbiquitinationDIHPDGTKFATGGQG
EECCCCCCCCCCCCC		38.2321890473
111PhosphorylationGPSTVFGSSGKLANV
CCCHHCCCCCCCCCH		25.1825159151
112PhosphorylationPSTVFGSSGKLANVE
CCHHCCCCCCCCCHH		40.0825159151
114UbiquitinationTVFGSSGKLANVEQW
HHCCCCCCCCCHHHH		46.50-
114AcetylationTVFGSSGKLANVEQW
HHCCCCCCCCCHHHH		46.5023954790
178 (in isoform 2)Ubiquitination-53.9321890473
178UbiquitinationRGHSGLVKGLTWDPV
CCCCCCCCCCCCCCH		53.9322817900
178 (in isoform 1)Ubiquitination-53.9321890473
187 (in isoform 2)Ubiquitination-33.4521890473
187UbiquitinationLTWDPVGKYIASQAD
CCCCCHHHHHHHHCC		33.4522817900
187 (in isoform 1)Ubiquitination-33.4521890473
187AcetylationLTWDPVGKYIASQAD
CCCCCHHHHHHHHCC		33.4526051181
214UbiquitinationQLETSITKPFDECGG
HHCCCCCCCCHHCCC		41.85-
231O-linked_GlycosylationHVLRLSWSPDGHYLV
EEEEEEECCCCCEEE		15.1127217568
259UbiquitinationIIEREGWKTNMDFVG
HEEECCCCCCCCCCC		40.66-
269UbiquitinationMDFVGHRKAVTVVKF
CCCCCCCCEEEEEEC		41.3529967540
275UbiquitinationRKAVTVVKFNPKIFK
CCEEEEEECCHHHHH		34.78-
279UbiquitinationTVVKFNPKIFKKKQK
EEEECCHHHHHCCCC		62.9829967540
292UbiquitinationQKNGSSAKPSCPYCC
CCCCCCCCCCCCCCE		39.14-
292AcetylationQKNGSSAKPSCPYCC
CCCCCCCCCCCCCCE		39.1426051181
381UbiquitinationIHQSTYGKSLAIMTE
HHHHHHCHHHHHHCH		31.70-
393PhosphorylationMTEAQLSTAVIENPE
HCHHHHHHHHHCCHH		33.2722817900
404PhosphorylationENPEMLKYQRRQQQQ
CCHHHHHHHHHHHHH		11.8622817900
416UbiquitinationQQQQLDQKSAATREM
HHHHHHHHHHHHHHH		41.5529967540
425O-linked_GlycosylationAATREMGSATSVAGV
HHHHHHCCCHHHHCC		27.3627217568
437PhosphorylationAGVVNGESLEDIRKN
HCCCCCCCHHHHHHH		38.1621815630
448UbiquitinationIRKNLLKKQVETRTA
HHHHHHHHHHHHCCC		60.5924816145
506PhosphorylationPQLLPLDSSTPNSFG
CCEECCCCCCCCCCC		43.7426074081
507PhosphorylationQLLPLDSSTPNSFGA
CEECCCCCCCCCCCC		47.7726074081
508PhosphorylationLLPLDSSTPNSFGAS
EECCCCCCCCCCCCC		30.3726074081
511PhosphorylationLDSSTPNSFGASKPC
CCCCCCCCCCCCCCC		26.6826074081
515PhosphorylationTPNSFGASKPCTEPV
CCCCCCCCCCCCCCE		37.1926074081
519PhosphorylationFGASKPCTEPVVAAS
CCCCCCCCCCEEECC		52.4226074081
526PhosphorylationTEPVVAASARPAGDS
CCCEEECCCCCCCCC		18.3123090842
533PhosphorylationSARPAGDSVNKDSMN
CCCCCCCCCCCCCCC		27.0330108239
538PhosphorylationGDSVNKDSMNATSTP
CCCCCCCCCCCCCCC		18.6225159151
542PhosphorylationNKDSMNATSTPAALS
CCCCCCCCCCCCCCC		28.2930266825
543PhosphorylationKDSMNATSTPAALSP
CCCCCCCCCCCCCCC		29.9530266825
543O-linked_GlycosylationKDSMNATSTPAALSP
CCCCCCCCCCCCCCC		29.9527217568
544PhosphorylationDSMNATSTPAALSPS
CCCCCCCCCCCCCCC		16.7630266825
549PhosphorylationTSTPAALSPSVLTTP
CCCCCCCCCCCCCCC		15.4830266825
551PhosphorylationTPAALSPSVLTTPSK
CCCCCCCCCCCCCCC		26.7830266825
554PhosphorylationALSPSVLTTPSKIEP
CCCCCCCCCCCCCCC		34.2130266825
555PhosphorylationLSPSVLTTPSKIEPM
CCCCCCCCCCCCCCC		22.7730266825
557PhosphorylationPSVLTTPSKIEPMKA
CCCCCCCCCCCCCCH		44.1430266825
563AcetylationPSKIEPMKAFDSRFT
CCCCCCCCHHCCCHH		57.5325953088
567PhosphorylationEPMKAFDSRFTERSK
CCCCHHCCCHHCHHC		23.8820873877
570PhosphorylationKAFDSRFTERSKATP
CHHCCCHHCHHCCCC		29.4020873877
573PhosphorylationDSRFTERSKATPGAP
CCCHHCHHCCCCCCC		22.0222199227
576PhosphorylationFTERSKATPGAPALT
HHCHHCCCCCCCCCC		26.4525159151
583PhosphorylationTPGAPALTSMTPTAV
CCCCCCCCCCCHHHH		20.6829255136
584PhosphorylationPGAPALTSMTPTAVE
CCCCCCCCCCHHHHH		22.8529255136
586PhosphorylationAPALTSMTPTAVERL
CCCCCCCCHHHHHHH		19.7729255136
588PhosphorylationALTSMTPTAVERLKE
CCCCCCHHHHHHHHH		33.8829255136
594UbiquitinationPTAVERLKEQNLVKE
HHHHHHHHHCCHHHH		64.5729967540
600UbiquitinationLKEQNLVKELRPRDL
HHHCCHHHHHCHHHH		54.9529967540
600AcetylationLKEQNLVKELRPRDL
HHHCCHHHHHCHHHH		54.9526051181
610PhosphorylationRPRDLLESSSDSDEK
CHHHHHHCCCCCCCC		34.8025159151
611PhosphorylationPRDLLESSSDSDEKV
HHHHHHCCCCCCCCC		28.8725159151
612PhosphorylationRDLLESSSDSDEKVP
HHHHHCCCCCCCCCC		50.8725159151
614PhosphorylationLLESSSDSDEKVPLA
HHHCCCCCCCCCCHH		50.0125159151
630AcetylationASSLSKRKLELEVET
HHHHCHHCEEEEEEE		50.4826051181
637PhosphorylationKLELEVETVEKKKKG
CEEEEEEEHHHHHCC		38.8629214152
640AcetylationLEVETVEKKKKGRPR
EEEEEHHHHHCCCCC		66.6126051181
650PhosphorylationKGRPRKDSRLMPVSL
CCCCCCCCCCEEEEE		30.2823090842
656PhosphorylationDSRLMPVSLSVQSPA
CCCCEEEEEEECCCC		14.7321712546
658PhosphorylationRLMPVSLSVQSPAAL
CCEEEEEEECCCCCC		15.5926055452
661PhosphorylationPVSLSVQSPAALTAE
EEEEEECCCCCCCCH		17.8529255136
666PhosphorylationVQSPAALTAEKEAMC
ECCCCCCCCHHHHHH		28.2229255136
675PhosphorylationEKEAMCLSAPALALK
HHHHHHHCCCHHHHC		27.5525159151
687PhosphorylationALKLPIPSPQRAFTL
HHCCCCCCCCCEEEE		34.0930266825
697PhosphorylationRAFTLQVSSDPSMYI
CEEEEEECCCCCCEE		18.96-
711PhosphorylationIEVENEVTVVGGVKL
EEEECEEEEECCEEE		11.86-
728UbiquitinationLKCNREGKEWETVLT
EEECCCCCCCCHHHH		55.70-
754UbiquitinationVVCVACEKRMLSVFS
EEEEECCHHHHHHHH		42.88-
761PhosphorylationKRMLSVFSTCGRRLL
HHHHHHHHHCCHHHC		22.1922210691
762PhosphorylationRMLSVFSTCGRRLLS
HHHHHHHHCCHHHCC		13.9122210691
769PhosphorylationTCGRRLLSPILLPSP
HCCHHHCCCCCCCCC		17.9324043423
775PhosphorylationLSPILLPSPISTLHC
CCCCCCCCCCCCCCC		34.5324043423
778PhosphorylationILLPSPISTLHCTGS
CCCCCCCCCCCCCHH		28.4424043423
779PhosphorylationLLPSPISTLHCTGSY
CCCCCCCCCCCCHHH		22.6524043423
783PhosphorylationPISTLHCTGSYVMAL
CCCCCCCCHHHHHHH		20.5824043423
785PhosphorylationSTLHCTGSYVMALTA
CCCCCCHHHHHHHHH		9.0824043423
786PhosphorylationTLHCTGSYVMALTAA
CCCCCHHHHHHHHHH		8.7924043423
791PhosphorylationGSYVMALTAAATLSV
HHHHHHHHHHHHCHH		12.5224043423
795PhosphorylationMALTAAATLSVWDVH
HHHHHHHHCHHHHCC		18.1624043423
797PhosphorylationLTAAATLSVWDVHRQ
HHHHHHCHHHHCCCC		19.4624043423
812PhosphorylationVVVVKEESLHSILAG
EEEECHHHHHHHHCC		32.26-
815PhosphorylationVKEESLHSILAGSDM
ECHHHHHHHHCCCCC		25.29-
860UbiquitinationTWNLVSDKQDSLAQC
HHCCCCCCCCHHHHH		48.80-
876O-linked_GlycosylationDFRSSLPSQDAMLCS
HHHHCCCCCCCCCCC		46.0827217568
945PhosphorylationWLLVYARYLVNEGFE
HHHHHHHHHHHCCCH		13.56-
953PhosphorylationLVNEGFEYRLREICK
HHHCCCHHHHHHHHH		16.82-
988UbiquitinationLRKRELLKELLPVIG
HHHHHHHHHHHHHHC		59.96-
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
555TPhosphorylationKinaseCDK2P24941
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
555TPhosphorylation

11238922
555TPhosphorylation

11238922
687SPhosphorylation

11238922
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 HIRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2B1K_HUMANHIST1H2BKphysical
9710638
H2B1D_HUMANHIST1H2BDphysical
9710638
H2B1C_HUMANHIST1H2BDphysical
9710638
NFU1_HUMANNFU1physical
11342215
ASF1A_HUMANASF1Aphysical
16980972
ASF1B_HUMANASF1Bphysical
16980972
ASF1A_HUMANASF1Aphysical
15621527
ASF1A_HUMANASF1Aphysical
18378699
MEF2D_HUMANMEF2Dphysical
21414300
ASF1A_HUMANASF1Aphysical
21414300
CABIN_HUMANCABIN1physical
21414300
DNJA2_HUMANDNAJA2physical
17242198
UBN1_HUMANUBN1physical
22401310
H32_HUMANHIST2H3Cphysical
21724829
H2B1_YEASTHTB1physical
22885324
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 HIRA_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-549; SER-557; THR-576;THR-586 AND SER-661, AND MASS SPECTROMETRY.
"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-538; SER-549; SER-551;THR-555 AND SER-557, AND MASS SPECTROMETRY.
"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 THR-576; SER-584; THR-586;SER-610; SER-611; SER-612 AND SER-614, AND MASS SPECTROMETRY.
"HIRA, the human homologue of yeast Hir1p and Hir2p, is a novelcyclin-cdk2 substrate whose expression blocks S-phase progression.";
Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S.,Lipinski M., Adams P.D.;
Mol. Cell. Biol. 21:1854-1865(2001).
Cited for: INTERACTION WITH CCNA1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATTHR-555 AND SER-687, AND MUTAGENESIS OF THR-555 AND 628-LYS--LEU-631.

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