HP1B3_MOUSE - dbPTM
HP1B3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HP1B3_MOUSE
UniProt AC Q3TEA8
Protein Name Heterochromatin protein 1-binding protein 3
Gene Name Hp1bp3
Organism Mus musculus (Mouse).
Sequence Length 554
Subcellular Localization Nucleus . Chromosome . localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S).
Protein Description Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. May play a role in hypoxia-induced oncogenesis..
Protein Sequence MATDMSQGELIHPKALPLIVGAQLIHADKLGEKAEDTTMPIRRAVNSTRETPPKSKLAEGEEEKPEPDGSSEESISTVEEQENETPPATSSEAEQPKGEPESGEKEENNNKSAEEPKKDEKDQSKEKEKKVKKTIPAWATLSASQLARAQRQTPMASSPRPKMDAILTEAIKACFQKTGASVVAIRKYIIHKYPSLGLERRGYLLKQALKRELNRGVIRQVKGKGASGSFVVVQKSKPPQKSKNRKKGSALDPEPQVKLEDVLPLAFTRLCEPKEASYSLIRKYVSQYYPKLRVDIRPQLLKNALQRAVERGQLEQITGKGASGTFQLKKSGEKPLLGGSLMEYAILSAIAAMNEPKTCSTTALKKYVLENHPGANSNYQMHLLKKTLQKCEKNGWLEQISGKGFSGTFQLSFPYYPSPGVLFPKKESGGSDDEDEDDDDDESSEDSEDEEPPPKRSLQKKTPAKSQGKTASMKQRGSKPARKVPAAQRGKVRPLPKKAPPKAKTPARKARPSPSVIKKPSGSSSRKPIASARKEAKLPGKGKSAMKKSFKTKK
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
2Acetylation------MATDMSQGE
------CCCCCCCCC
16.59-
3Phosphorylation-----MATDMSQGEL
-----CCCCCCCCCC
30.8220531401
6Phosphorylation--MATDMSQGELIHP
--CCCCCCCCCCCCC
37.5325266776
14AcetylationQGELIHPKALPLIVG
CCCCCCCCHHHHHEE
48.6822826441
29AcetylationAQLIHADKLGEKAED
EEEEEHHHCCCCCCC
60.2123236377
37PhosphorylationLGEKAEDTTMPIRRA
CCCCCCCCCCHHHHH
19.2522418434
38PhosphorylationGEKAEDTTMPIRRAV
CCCCCCCCCHHHHHH
33.0220469934
47PhosphorylationPIRRAVNSTRETPPK
HHHHHHHCCCCCCCH
23.4223684622
48PhosphorylationIRRAVNSTRETPPKS
HHHHHHCCCCCCCHH
27.5926824392
51PhosphorylationAVNSTRETPPKSKLA
HHHCCCCCCCHHHCC
41.4226824392
54UbiquitinationSTRETPPKSKLAEGE
CCCCCCCHHHCCCCC
62.5227667366
55 (in isoform 2)Phosphorylation-38.3825266776
55PhosphorylationTRETPPKSKLAEGEE
CCCCCCHHHCCCCCC
38.3824453211
67UbiquitinationGEEEKPEPDGSSEES
CCCCCCCCCCCCHHH
60.8427667366
70PhosphorylationEKPEPDGSSEESIST
CCCCCCCCCHHHCCH
41.7921659605
71PhosphorylationKPEPDGSSEESISTV
CCCCCCCCHHHCCHH
51.4125521595
72 (in isoform 2)Phosphorylation-58.4225521595
74PhosphorylationPDGSSEESISTVEEQ
CCCCCHHHCCHHHHH
20.1426643407
76PhosphorylationGSSEESISTVEEQEN
CCCHHHCCHHHHHCC
35.3626643407
76 (in isoform 2)Phosphorylation-35.3627742792
77 (in isoform 2)Phosphorylation-30.2127742792
77PhosphorylationSSEESISTVEEQENE
CCHHHCCHHHHHCCC
30.2125521595
78 (in isoform 2)Phosphorylation-6.4327742792
82UbiquitinationISTVEEQENETPPAT
CCHHHHHCCCCCCCC
61.3827667366
85PhosphorylationVEEQENETPPATSSE
HHHHCCCCCCCCCCC
46.2722802335
89PhosphorylationENETPPATSSEAEQP
CCCCCCCCCCCCCCC
38.2626643407
90PhosphorylationNETPPATSSEAEQPK
CCCCCCCCCCCCCCC
28.4326643407
91PhosphorylationETPPATSSEAEQPKG
CCCCCCCCCCCCCCC
36.1526643407
92UbiquitinationTPPATSSEAEQPKGE
CCCCCCCCCCCCCCC
56.8627667366
95UbiquitinationATSSEAEQPKGEPES
CCCCCCCCCCCCCCC
52.6427667366
105UbiquitinationGEPESGEKEENNNKS
CCCCCCCCCCCCCCC
74.0727667366
112PhosphorylationKEENNNKSAEEPKKD
CCCCCCCCCCCCCCC
42.9323375375
119UbiquitinationSAEEPKKDEKDQSKE
CCCCCCCCHHHHHHH
74.4427667366
120UbiquitinationAEEPKKDEKDQSKEK
CCCCCCCHHHHHHHH
68.3727667366
132UbiquitinationKEKEKKVKKTIPAWA
HHHHHHHHHHHHHHH
53.7527667366
133UbiquitinationEKEKKVKKTIPAWAT
HHHHHHHHHHHHHHH
55.4627667366
140PhosphorylationKTIPAWATLSASQLA
HHHHHHHHCCHHHHH
15.5626643407
142PhosphorylationIPAWATLSASQLARA
HHHHHHCCHHHHHHH
22.8626643407
144PhosphorylationAWATLSASQLARAQR
HHHHCCHHHHHHHHH
23.5026745281
147UbiquitinationTLSASQLARAQRQTP
HCCHHHHHHHHHHCC
9.3427667366
157PhosphorylationQRQTPMASSPRPKMD
HHHCCCCCCCCHHHH
34.3225159016
158PhosphorylationRQTPMASSPRPKMDA
HHCCCCCCCCHHHHH
18.5226824392
160UbiquitinationTPMASSPRPKMDAIL
CCCCCCCCHHHHHHH
45.4827667366
192AcetylationIRKYIIHKYPSLGLE
EHHHHHHHCCCCCHH
48.7423806337
227PhosphorylationQVKGKGASGSFVVVQ
HHCCCCCCCCEEEEE
43.5728833060
229PhosphorylationKGKGASGSFVVVQKS
CCCCCCCCEEEEECC
16.6328833060
249PhosphorylationSKNRKKGSALDPEPQ
CCCCCCCCCCCCCCC
34.2428833060
268UbiquitinationDVLPLAFTRLCEPKE
HHHHHHHHHHCCCHH
19.6827667366
269UbiquitinationVLPLAFTRLCEPKEA
HHHHHHHHHCCCHHH
30.7827667366
274AcetylationFTRLCEPKEASYSLI
HHHHCCCHHHHHHHH
43.5522826441
279PhosphorylationEPKEASYSLIRKYVS
CCHHHHHHHHHHHHH
18.1529176673
282UbiquitinationEASYSLIRKYVSQYY
HHHHHHHHHHHHHHC
29.5527667366
286PhosphorylationSLIRKYVSQYYPKLR
HHHHHHHHHHCHHHC
14.9124759943
307UbiquitinationLLKNALQRAVERGQL
HHHHHHHHHHHHCCH
41.2627667366
319UbiquitinationGQLEQITGKGASGTF
CCHHHHCCCCCCCCE
28.2027667366
320UbiquitinationQLEQITGKGASGTFQ
CHHHHCCCCCCCCEE
42.5322790023
323PhosphorylationQITGKGASGTFQLKK
HHCCCCCCCCEEECC
47.2129176673
330UbiquitinationSGTFQLKKSGEKPLL
CCCEEECCCCCCCCC
72.75-
334UbiquitinationQLKKSGEKPLLGGSL
EECCCCCCCCCCHHH
44.4827667366
346UbiquitinationGSLMEYAILSAIAAM
HHHHHHHHHHHHHHH
2.8227667366
347UbiquitinationSLMEYAILSAIAAMN
HHHHHHHHHHHHHHC
1.8427667366
348PhosphorylationLMEYAILSAIAAMNE
HHHHHHHHHHHHHCC
16.1222802335
358PhosphorylationAAMNEPKTCSTTALK
HHHCCCCCCCHHHHH
23.5428576409
361PhosphorylationNEPKTCSTTALKKYV
CCCCCCCHHHHHHHH
20.4528576409
362PhosphorylationEPKTCSTTALKKYVL
CCCCCCHHHHHHHHH
17.4428576409
377PhosphorylationENHPGANSNYQMHLL
HCCCCCCCHHHHHHH
36.0625367039
379PhosphorylationHPGANSNYQMHLLKK
CCCCCCHHHHHHHHH
13.6625195567
415PhosphorylationTFQLSFPYYPSPGVL
EEEEECCCCCCCCEE
26.4626745281
416PhosphorylationFQLSFPYYPSPGVLF
EEEECCCCCCCCEEC
9.4726745281
418PhosphorylationLSFPYYPSPGVLFPK
EECCCCCCCCEECCC
20.4026643407
428PhosphorylationVLFPKKESGGSDDED
EECCCCCCCCCCCCC
58.2825159016
431PhosphorylationPKKESGGSDDEDEDD
CCCCCCCCCCCCCCC
45.4725159016
443PhosphorylationEDDDDDESSEDSEDE
CCCCCCCCCCCCCCC
46.1225159016
444PhosphorylationDDDDDESSEDSEDEE
CCCCCCCCCCCCCCC
43.2925159016
447PhosphorylationDDESSEDSEDEEPPP
CCCCCCCCCCCCCCC
42.7825159016
462PhosphorylationKRSLQKKTPAKSQGK
CCCCCCCCCCCCCCC
35.2025266776
469AcetylationTPAKSQGKTASMKQR
CCCCCCCCCCHHHHC
33.0323806337
513PhosphorylationPARKARPSPSVIKKP
CCHHCCCCCCCCCCC
25.0125521595
515PhosphorylationRKARPSPSVIKKPSG
HHCCCCCCCCCCCCC
40.5924068923

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 HP1B3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HP1B3_MOUSE !!

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 HP1B3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HP1B3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HP1B3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-443; SER-444AND SER-447, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND MASSSPECTROMETRY.

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