HIRP3_HUMAN - dbPTM
HIRP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIRP3_HUMAN
UniProt AC Q9BW71
Protein Name HIRA-interacting protein 3
Gene Name HIRIP3
Organism Homo sapiens (Human).
Sequence Length 556
Subcellular Localization Nucleus . Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis.
Protein Description May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones..
Protein Sequence MAREKEMQEFTRSFFRGRPDLSTLTHSIVRRRYLAHSGRSHLEPEEKQALKRLVEEELLKMQVDEAASREDKLDLTKKGKRPPTPCSDPERKRFRFNSESESGSEASSPDYFGPPAKNGVAAEVSPAKEENPRRASKAVEESSDEERQRDLPAQRGEESSEEEEKGYKGKTRKKPVVKKQAPGKASVSRKQAREESEESEAEPVQRTAKKVEGNKGTKSLKESEQESEEEILAQKKEQREEEVEEEEKEEDEEKGDWKPRTRSNGRRKSAREERSCKQKSQAKRLLGDSDSEEEQKEAASSGDDSGRDREPPVQRKSEDRTQLKGGKRLSGSSEDEEDSGKGEPTAKGSRKMARLGSTSGEESDLEREVSDSEAGGGPQGERKNRSSKKSSRKGRTRSSSSSSDGSPEAKGGKAGSGRRGEDHPAVMRLKRYIRACGAHRNYKKLLGSCCSHKERLSILRAELEALGMKGTPSLGKCRALKEQREEAAEVASLDVANIISGSGRPRRRTAWNPLGEAAPPGELYRRTLDSDEERPRPAPPDWSHMRGIISSDGESN
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
5Acetylation---MAREKEMQEFTR
---CCCHHHHHHHHH		53.5925953088
5Ubiquitination---MAREKEMQEFTR
---CCCHHHHHHHHH		53.59-
13PhosphorylationEMQEFTRSFFRGRPD
HHHHHHHHHHCCCCC		26.1924719451
22PhosphorylationFRGRPDLSTLTHSIV
HCCCCCHHHHHHHHH		28.8427135362
23PhosphorylationRGRPDLSTLTHSIVR
CCCCCHHHHHHHHHH		42.8624732914
25PhosphorylationRPDLSTLTHSIVRRR
CCCHHHHHHHHHHHH		17.4228464451
27PhosphorylationDLSTLTHSIVRRRYL
CHHHHHHHHHHHHHH		19.9726055452
37PhosphorylationRRRYLAHSGRSHLEP
HHHHHHHCCCCCCCH		30.2329214152
40PhosphorylationYLAHSGRSHLEPEEK
HHHHCCCCCCCHHHH		35.6329214152
47UbiquitinationSHLEPEEKQALKRLV
CCCCHHHHHHHHHHH		38.9333845483
51UbiquitinationPEEKQALKRLVEEEL
HHHHHHHHHHHHHHH		46.8624816145
72UbiquitinationEAASREDKLDLTKKG
HHHHHHHHHCCHHCC		38.8629967540
72AcetylationEAASREDKLDLTKKG
HHHHHHHHHCCHHCC		38.8625953088
76PhosphorylationREDKLDLTKKGKRPP
HHHHHCCHHCCCCCC		30.3126074081
84PhosphorylationKKGKRPPTPCSDPER
HCCCCCCCCCCCHHH		39.3429255136
87PhosphorylationKRPPTPCSDPERKRF
CCCCCCCCCHHHHCC		58.3629255136
87 (in isoform 3)Phosphorylation-58.3629116813
98PhosphorylationRKRFRFNSESESGSE
HHCCCCCCCCCCCCC		39.5220164059
100PhosphorylationRFRFNSESESGSEAS
CCCCCCCCCCCCCCC		36.5625159151
102PhosphorylationRFNSESESGSEASSP
CCCCCCCCCCCCCCC		57.8220164059
104PhosphorylationNSESESGSEASSPDY
CCCCCCCCCCCCCCC		38.9923927012
107PhosphorylationSESGSEASSPDYFGP
CCCCCCCCCCCCCCC		38.0523927012
108PhosphorylationESGSEASSPDYFGPP
CCCCCCCCCCCCCCC		28.9223927012
111PhosphorylationSEASSPDYFGPPAKN
CCCCCCCCCCCCCCC		17.5123927012
125PhosphorylationNGVAAEVSPAKEENP
CCCCCCCCCCCCCCH		15.6229255136
136PhosphorylationEENPRRASKAVEESS
CCCHHHHHHHHHHCC		21.2429978859
142PhosphorylationASKAVEESSDEERQR
HHHHHHHCCHHHHHH		29.5929255136
143PhosphorylationSKAVEESSDEERQRD
HHHHHHCCHHHHHHC		52.9329255136
159PhosphorylationPAQRGEESSEEEEKG
CHHHCCCCCHHHHCC		38.4529255136
160PhosphorylationAQRGEESSEEEEKGY
HHHCCCCCHHHHCCC		52.9229255136
167PhosphorylationSEEEEKGYKGKTRKK
CHHHHCCCCCCCCCC		27.8622167270
179UbiquitinationRKKPVVKKQAPGKAS
CCCCCCCCCCCCCHH		39.83-
184AcetylationVKKQAPGKASVSRKQ
CCCCCCCCHHCCHHH		36.1125953088
184UbiquitinationVKKQAPGKASVSRKQ
CCCCCCCCHHCCHHH		36.1124816145
186PhosphorylationKQAPGKASVSRKQAR
CCCCCCHHCCHHHHH		24.9028348404
188O-linked_GlycosylationAPGKASVSRKQAREE
CCCCHHCCHHHHHHH		31.1230379171
188PhosphorylationAPGKASVSRKQAREE
CCCCHHCCHHHHHHH		31.1228348404
196PhosphorylationRKQAREESEESEAEP
HHHHHHHHHHHCCHH		41.7429255136
199PhosphorylationAREESEESEAEPVQR
HHHHHHHHCCHHHHH		37.7529255136
207PhosphorylationEAEPVQRTAKKVEGN
CCHHHHHHHHHHHCC		26.2428985074
219PhosphorylationEGNKGTKSLKESEQE
HCCCCCCCHHHHHHH		44.5023927012
223PhosphorylationGTKSLKESEQESEEE
CCCCHHHHHHHHHHH		42.8919664994
227PhosphorylationLKESEQESEEEILAQ
HHHHHHHHHHHHHHH		50.4219664994
261PhosphorylationKGDWKPRTRSNGRRK
CCCCCCCCCCCCCCH		47.1522210691
269PhosphorylationRSNGRRKSAREERSC
CCCCCCHHHHHHHHH		30.65-
275PhosphorylationKSAREERSCKQKSQA
HHHHHHHHHHHHHHH		29.0126074081
280PhosphorylationERSCKQKSQAKRLLG
HHHHHHHHHHHHHHC		32.6426074081
289PhosphorylationAKRLLGDSDSEEEQK
HHHHHCCCCCHHHHH		41.0429255136
291PhosphorylationRLLGDSDSEEEQKEA
HHHCCCCCHHHHHHH		51.3529255136
300PhosphorylationEEQKEAASSGDDSGR
HHHHHHHHCCCCCCC		41.7325159151
301PhosphorylationEQKEAASSGDDSGRD
HHHHHHHCCCCCCCC		41.3325159151
305PhosphorylationAASSGDDSGRDREPP
HHHCCCCCCCCCCCC		40.2325159151
317PhosphorylationEPPVQRKSEDRTQLK
CCCCCCCCCCCCCCC		47.0928985074
324AcetylationSEDRTQLKGGKRLSG
CCCCCCCCCCCCCCC		56.667966171
324UbiquitinationSEDRTQLKGGKRLSG
CCCCCCCCCCCCCCC		56.6624816145
327UbiquitinationRTQLKGGKRLSGSSE
CCCCCCCCCCCCCCC		59.8524816145
330PhosphorylationLKGGKRLSGSSEDEE
CCCCCCCCCCCCCCC		40.4329255136
332PhosphorylationGGKRLSGSSEDEEDS
CCCCCCCCCCCCCCC		27.4629255136
333PhosphorylationGKRLSGSSEDEEDSG
CCCCCCCCCCCCCCC		53.2229255136
339PhosphorylationSSEDEEDSGKGEPTA
CCCCCCCCCCCCCCH		45.7625159151
345PhosphorylationDSGKGEPTAKGSRKM
CCCCCCCCHHHHHHH		36.3828102081
357PhosphorylationRKMARLGSTSGEESD
HHHHHHCCCCCCCHH		24.8029255136
358PhosphorylationKMARLGSTSGEESDL
HHHHHCCCCCCCHHH		38.6629255136
359PhosphorylationMARLGSTSGEESDLE
HHHHCCCCCCCHHHH		46.0029255136
363PhosphorylationGSTSGEESDLEREVS
CCCCCCCHHHHHHCC		43.1029255136
370PhosphorylationSDLEREVSDSEAGGG
HHHHHHCCCCCCCCC		30.5729255136
372PhosphorylationLEREVSDSEAGGGPQ
HHHHCCCCCCCCCCC		23.1129255136
398PhosphorylationSRKGRTRSSSSSSDG
CCCCCCCCCCCCCCC		33.6830576142
399PhosphorylationRKGRTRSSSSSSDGS
CCCCCCCCCCCCCCC		30.8330576142
400PhosphorylationKGRTRSSSSSSDGSP
CCCCCCCCCCCCCCC		35.1725072903
401PhosphorylationGRTRSSSSSSDGSPE
CCCCCCCCCCCCCCC		35.4925072903
402PhosphorylationRTRSSSSSSDGSPEA
CCCCCCCCCCCCCCC		34.1025072903
403PhosphorylationTRSSSSSSDGSPEAK
CCCCCCCCCCCCCCC		48.1925072903
406PhosphorylationSSSSSDGSPEAKGGK
CCCCCCCCCCCCCCC		25.2625072903
416PhosphorylationAKGGKAGSGRRGEDH
CCCCCCCCCCCCCCC		33.7024719451
448PhosphorylationNYKKLLGSCCSHKER
CHHHHHHHHCCHHHH		16.3625159151
451PhosphorylationKLLGSCCSHKERLSI
HHHHHHCCHHHHHHH		41.7529449344
453UbiquitinationLGSCCSHKERLSILR
HHHHCCHHHHHHHHH		28.3829967540
468SulfoxidationAELEALGMKGTPSLG
HHHHHCCCCCCCCHH		3.6321406390
469AcetylationELEALGMKGTPSLGK
HHHHCCCCCCCCHHH		58.8125953088
469UbiquitinationELEALGMKGTPSLGK
HHHHCCCCCCCCHHH		58.8124816145
471PhosphorylationEALGMKGTPSLGKCR
HHCCCCCCCCHHHHH		12.2722617229
473PhosphorylationLGMKGTPSLGKCRAL
CCCCCCCCHHHHHHH		49.9822617229
476UbiquitinationKGTPSLGKCRALKEQ
CCCCCHHHHHHHHHH		26.3229967540
476AcetylationKGTPSLGKCRALKEQ
CCCCCHHHHHHHHHH		26.327692245
492PhosphorylationEEAAEVASLDVANII
HHHHHHHCCCHHHHH		30.2230576142
500PhosphorylationLDVANIISGSGRPRR
CCHHHHHCCCCCCCC		24.1021712546
502PhosphorylationVANIISGSGRPRRRT
HHHHHCCCCCCCCCC		25.4928555341
509PhosphorylationSGRPRRRTAWNPLGE
CCCCCCCCCCCCCCC		33.9228555341
524PhosphorylationAAPPGELYRRTLDSD
CCCCCCCCCCCCCCC		8.1826074081
527PhosphorylationPGELYRRTLDSDEER
CCCCCCCCCCCCCCC		26.3930266825
530PhosphorylationLYRRTLDSDEERPRP
CCCCCCCCCCCCCCC		50.4629255136
543PhosphorylationRPAPPDWSHMRGIIS
CCCCCCHHHHCCCCC		18.1323927012
550PhosphorylationSHMRGIISSDGESN-
HHHCCCCCCCCCCC-		22.0628102081
551PhosphorylationHMRGIISSDGESN--
HHCCCCCCCCCCC--		38.9526055452
555PhosphorylationIISSDGESN------
CCCCCCCCC------		54.0626055452
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 HIRP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIRP3_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 HIRP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIRA_HUMANHIRAphysical
9710638
CSK2B_HUMANCSNK2Bphysical
17391060
CSK21_HUMANCSNK2A1physical
17391060
A4_HUMANAPPphysical
21832049
SYCC_HUMANCARSphysical
22863883
RANB3_HUMANRANBP3physical
22863883
SF01_HUMANSF1physical
22863883
XPO7_HUMANXPO7physical
22863883
RL8_HUMANRPL8physical
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 HIRP3_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-27; SER-125; SER-196;SER-199; SER-223; SER-227 AND SER-372, 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 THR-84; SER-87; SER-125;SER-159; SER-160; SER-196; SER-219; SER-223; SER-227; SER-289 ANDSER-291, 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-84; SER-87; SER-98;SER-100; SER-104; SER-125; SER-159; SER-160; SER-196; SER-199;SER-223; SER-227; SER-330; SER-332; SER-333; SER-357; THR-358;SER-359; SER-363; SER-370 AND SER-372, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-136; SER-196;SER-199; SER-223; SER-227; SER-300; SER-301; SER-305; SER-330; SER-332AND SER-333, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND TYR-167, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-87; SER-159;SER-160; SER-196; SER-199; SER-227 AND SER-370, AND MASS SPECTROMETRY.
"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 THR-84; SER-87; SER-98;SER-100; SER-102; SER-104; SER-107; TYR-111; SER-125; SER-142;SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227;SER-289; SER-291; SER-357; THR-358; SER-359; SER-363 AND SER-370, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 AND SER-199, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-125; SER-199;SER-223; SER-227 AND SER-370, AND MASS SPECTROMETRY.

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