Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heterochromatin protein 1-binding protein 3  

UniProtKB / Swiss-Prot ID :  HP1B3_HUMAN

Gene Name (Synonyms) : 
HP1BP3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Chromosome (By similarity). 

Protein Function :  Component of heterochromatin, may be involved in chromatin structure and function (By similarity). 

Protein Sequence MATDTSQGELVHPKALPLIVGAQLIHADKLGEKVEDSTMPIRRTVNSTRETPPKSKLAEGEEEKPEPDIS...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATDTS
---
17.74UniProtKB
Link-
3Phosphothreonine--MATDTSQ
--
38.21HPRD
Link-
3Phosphothreonine--MATDTSQ
--
38.21Phosphositeplus
Link-
6PhosphoserineATDTSQGEL
38.71HPRD
Link-
6PhosphoserineATDTSQGEL
38.71Phosphositeplus
Link-
6PhosphoserineATDTSQGEL
38.71SysPTM
Link-
6Phosphoserine.ATDTSQGEL
38.71UniProtKB
Link-
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVHPKALPL
47.91Phosphositeplus
Link-
47PhosphoserineRTVNSTRET
25.22HPRD
Link-
48PhosphothreonineTVNSTRETP
27.59HPRD
Link-
51PhosphothreonineSTRETPPKS
41.42HPRD
Link-
51PhosphothreonineSTRETPPKS
41.42Phosphositeplus
Link-
70PhosphoserineEPDISSEES
38.79HPRD
Link-
70PhosphoserineEPDISSEES
38.79Phosphositeplus
Link-
71PhosphoserinePDISSEESV
45.80HPRD
Link-
74PhosphoserineSSEESVSTV
19.81HPRD
Link-
76PhosphoserineEESVSTVEE
35.69HPRD
Link-
77PhosphothreonineESVSTVEEQ
29.76HPRD
Link-
85PhosphothreonineQENETPPAT
46.27HPRD
Link-
131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKVKKTIPS
55.46Phosphositeplus
Link-
132PhosphothreonineKVKKTIPSW
32.19HPRD
Link-
132Phosphothreonine.KVKKTIPSW
32.19UniProtKB
Link-
142PhosphoserineTLSASQLAR
23.50HPRD
Link-
142PhosphoserineTLSASQLAR
23.50Phosphositeplus
Link-
142Phosphoserine.TLSASQLAR
23.50UniProtKB
Link-
155PhosphoserineTPMASSPRP
34.32HPRD
Link
155PhosphoserineTPMASSPRP
34.32Phosphositeplus
Link
156PhosphoserinePMASSPRPK
18.52HPRD
Link
156PhosphoserinePMASSPRPK
18.52Phosphositeplus
Link
156Phosphoserine.PMASSPRPK
18.52UniProtKB
Link
176PhosphoserineCFQKSGASV
28.89HPRD
Link
176PhosphoserineCFQKSGASV
28.89Phosphositeplus
Link
190N6-acetyllysineYIIHKYPSL
48.74HPRD
Link
190N6-acetyllysineYIIHKYPSL
48.74Phosphositeplus
Link
190N6-acetyllysine.YIIHKYPSL
48.74UniProtKB
Link
248PhosphoserineRKNRSSAVD
31.85HPRD
Link-
248PhosphoserineRKNRSSAVD
31.85Phosphositeplus
Link-
248PhosphoserineRKNRSSAVD
31.85SysPTM
Link-
248Phosphoserine.RKNRSSAVD
31.85UniProtKB
Link-
249PhosphoserineKNRSSAVDP
29.13HPRD
Link-
249PhosphoserineKNRSSAVDP
29.13Phosphositeplus
Link-
249PhosphoserineKNRSSAVDP
29.13SysPTM
Link-
249Phosphoserine.KNRSSAVDP
29.13UniProtKB
Link-
288PhosphotyrosineYVSQYYPKL
17.77Phosphositeplus
Link-
289PhosphotyrosineVSQYYPKLR
6.05Phosphositeplus
Link-
291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QYYPKLRVD
32.57Phosphositeplus
Link-
379PhosphotyrosineTNSNYQMHL
13.66Phosphositeplus
Link-
431PhosphoserineEPDDSRDED
49.35Phosphositeplus
Link-
441PhosphoserineDEDESSEED
56.20HPRD
Link-
441PhosphoserineDEDESSEED
56.20Phosphositeplus
Link-
441Phosphoserine.DEDESSEED
56.20UniProtKB
Link-
442PhosphoserineEDESSEEDS
42.85HPRD
Link-
442PhosphoserineEDESSEEDS
42.85Phosphositeplus
Link-
442Phosphoserine.EDESSEEDS
42.85UniProtKB
Link-
446PhosphoserineSEEDSEDEE
50.67HPRD
Link-
446PhosphoserineSEEDSEDEE
50.67Phosphositeplus
Link-
446Phosphoserine.SEEDSEDEE
50.67UniProtKB
Link-
461PhosphothreonineLQKKTPAKS
35.20HPRD
Link-
461PhosphothreonineLQKKTPAKS
35.20Phosphositeplus
Link-
465PhosphoserineTPAKSPGKA
40.78HPRD
Link-
465PhosphoserineTPAKSPGKA
40.78Phosphositeplus
Link-
520PhosphoserineIKKPSGGSS
65.74Phosphositeplus
Link-
523PhosphoserinePSGGSSKKP
42.37Phosphositeplus
Link-
524PhosphoserineSGGSSKKPA
48.23Phosphositeplus
Link-
529PhosphothreonineKKPATSARK
31.29Phosphositeplus
Link-
530PhosphoserineKPATSARKE
28.34Phosphositeplus
Link-
548PhosphoserineTMKKSFRVK
16.87HPRD
Link-
548PhosphoserineTMKKSFRVK
16.87Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-190, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-441; SER-442 ANDSER-446, AND MASS SPECTROMETRY.
"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-142, 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-248 AND SER-249, ANDMASS 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 SER-6 AND SER-156, AND MASSSPECTROMETRY.
"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 THR-132 AND SER-142, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures