H1BP3_HUMAN - dbPTM
H1BP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H1BP3_HUMAN
UniProt AC Q53T59
Protein Name HCLS1-binding protein 3
Gene Name HS1BP3
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization
Protein Description May be a modulator of IL-2 signaling..
Protein Sequence MQSPAVLVTSRRLQNAHTGLDLTVPQHQEVRGKMMSGHVEYQILVVTRLAAFKSAKHRPEDVVQFLVSKKYSEIEEFYQKLSSRYAAASLPPLPRKVLFVGESDIRERRAVFNEILRCVSKDAELAGSPELLEFLGTRSPGAAGLTSRDSSVLDGTDSQTGNDEEAFDFFEEQDQVAEEGPPVQSLKGEDAEESLEEEEALDPLGIMRSKKPKKHPKVAVKAKPSPRLTIFDEEVDPDEGLFGPGRKLSPQDPSEDVSSVDPLKLFDDPDLGGAIPLGDSLLLPAACESGGPTPSLSHRDASKELFRVEEDLDQILNLGAEPKPKPQLKPKPPVAAKPVIPRKPAVPPKAGPAEAVAGQQKPQEQIQAMDEMDILQYIQDHDTPAQAAPSLF
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
1Acetylation-------MQSPAVLV
-------CCCCCEEE
8.8622814378
3Phosphorylation-----MQSPAVLVTS
-----CCCCCEEEEC
17.3329255136
9PhosphorylationQSPAVLVTSRRLQNA
CCCCEEEECHHCHHC
16.6220068231
10PhosphorylationSPAVLVTSRRLQNAH
CCCEEEECHHCHHCC
14.1320068231
18PhosphorylationRRLQNAHTGLDLTVP
HHCHHCCCCCCCCCC
36.7128857561
23PhosphorylationAHTGLDLTVPQHQEV
CCCCCCCCCCCHHHH
29.7923312004
692-HydroxyisobutyrylationVVQFLVSKKYSEIEE
HHHHHHCCCHHHHHH
48.53-
70UbiquitinationVQFLVSKKYSEIEEF
HHHHHCCCHHHHHHH
46.64-
85PhosphorylationYQKLSSRYAAASLPP
HHHHHHHHHHHHCCC
11.5322817900
89PhosphorylationSSRYAAASLPPLPRK
HHHHHHHHCCCCCCE
36.3628857561
96UbiquitinationSLPPLPRKVLFVGES
HCCCCCCEEEEEECH
41.15-
120PhosphorylationNEILRCVSKDAELAG
HHHHHHHHCCHHHCC
28.5725954137
128PhosphorylationKDAELAGSPELLEFL
CCHHHCCCHHHHHHH
15.0320068231
137PhosphorylationELLEFLGTRSPGAAG
HHHHHHCCCCCCCCC
30.0728450419
139PhosphorylationLEFLGTRSPGAAGLT
HHHHCCCCCCCCCCC
27.7629255136
146PhosphorylationSPGAAGLTSRDSSVL
CCCCCCCCCCCCCCC
22.3128450419
147PhosphorylationPGAAGLTSRDSSVLD
CCCCCCCCCCCCCCC
38.8528450419
150PhosphorylationAGLTSRDSSVLDGTD
CCCCCCCCCCCCCCC
22.6420873877
151PhosphorylationGLTSRDSSVLDGTDS
CCCCCCCCCCCCCCC
30.8720873877
156PhosphorylationDSSVLDGTDSQTGND
CCCCCCCCCCCCCCC
31.9527251275
158PhosphorylationSVLDGTDSQTGNDEE
CCCCCCCCCCCCCHH
29.4926657352
160PhosphorylationLDGTDSQTGNDEEAF
CCCCCCCCCCCHHHH
41.7426657352
185PhosphorylationEEGPPVQSLKGEDAE
HHCCCCCCCCCCCHH
32.0820873877
194PhosphorylationKGEDAEESLEEEEAL
CCCCHHHHHHHHHHH
32.3629255136
209PhosphorylationDPLGIMRSKKPKKHP
CHHHHCCCCCCCCCC
27.8726657352
221AcetylationKHPKVAVKAKPSPRL
CCCCEEEECCCCCCE
40.7425953088
229PhosphorylationAKPSPRLTIFDEEVD
CCCCCCEEEECCCCC
22.3722817900
249PhosphorylationFGPGRKLSPQDPSED
CCCCCCCCCCCCCCC
24.4523927012
254PhosphorylationKLSPQDPSEDVSSVD
CCCCCCCCCCCCCCC
55.5130266825
258PhosphorylationQDPSEDVSSVDPLKL
CCCCCCCCCCCCCCC
36.6523403867
259PhosphorylationDPSEDVSSVDPLKLF
CCCCCCCCCCCCCCC
30.3223403867
280PhosphorylationGAIPLGDSLLLPAAC
CCCCCCCCCCHHHHH
21.0825159151
289PhosphorylationLLPAACESGGPTPSL
CHHHHHHCCCCCCCC
49.2725159151
293PhosphorylationACESGGPTPSLSHRD
HHHCCCCCCCCCHHH
28.8721712546
295PhosphorylationESGGPTPSLSHRDAS
HCCCCCCCCCHHHHH
45.0127251275
297PhosphorylationGGPTPSLSHRDASKE
CCCCCCCCHHHHHHH
22.3327251275
302PhosphorylationSLSHRDASKELFRVE
CCCHHHHHHHHCCCH
30.8326657352
337AcetylationPKPPVAAKPVIPRKP
CCCCCCCCCCCCCCC
30.0419608861

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 H1BP3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H1BP3_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 H1BP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSMD1_HUMANNAA38physical
26344197
ABTB2_HUMANABTB2physical
28514442
PDXD1_HUMANPDXDC1physical
28514442
RAD50_HUMANRAD50physical
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 H1BP3_HUMAN

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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 MET-1, 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-337, AND MASS SPECTROMETRY.
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 TYR-85; SER-139 AND SER-194,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 SER-194, AND MASSSPECTROMETRY.
"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 SER-139, AND MASSSPECTROMETRY.

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