| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MQSPAVLV -------CCCCCEEE | 8.86 | 22814378 | |
| 3 | Phosphorylation | -----MQSPAVLVTS -----CCCCCEEEEC | 17.33 | 29255136 | |
| 9 | Phosphorylation | QSPAVLVTSRRLQNA CCCCEEEECHHCHHC | 16.62 | 20068231 | |
| 10 | Phosphorylation | SPAVLVTSRRLQNAH CCCEEEECHHCHHCC | 14.13 | 20068231 | |
| 18 | Phosphorylation | RRLQNAHTGLDLTVP HHCHHCCCCCCCCCC | 36.71 | 28857561 | |
| 23 | Phosphorylation | AHTGLDLTVPQHQEV CCCCCCCCCCCHHHH | 29.79 | 23312004 | |
| 69 | 2-Hydroxyisobutyrylation | VVQFLVSKKYSEIEE HHHHHHCCCHHHHHH | 48.53 | - | |
| 70 | Ubiquitination | VQFLVSKKYSEIEEF HHHHHCCCHHHHHHH | 46.64 | - | |
| 85 | Phosphorylation | YQKLSSRYAAASLPP HHHHHHHHHHHHCCC | 11.53 | 22817900 | |
| 89 | Phosphorylation | SSRYAAASLPPLPRK HHHHHHHHCCCCCCE | 36.36 | 28857561 | |
| 96 | Ubiquitination | SLPPLPRKVLFVGES HCCCCCCEEEEEECH | 41.15 | - | |
| 120 | Phosphorylation | NEILRCVSKDAELAG HHHHHHHHCCHHHCC | 28.57 | 25954137 | |
| 128 | Phosphorylation | KDAELAGSPELLEFL CCHHHCCCHHHHHHH | 15.03 | 20068231 | |
| 137 | Phosphorylation | ELLEFLGTRSPGAAG HHHHHHCCCCCCCCC | 30.07 | 28450419 | |
| 139 | Phosphorylation | LEFLGTRSPGAAGLT HHHHCCCCCCCCCCC | 27.76 | 29255136 | |
| 146 | Phosphorylation | SPGAAGLTSRDSSVL CCCCCCCCCCCCCCC | 22.31 | 28450419 | |
| 147 | Phosphorylation | PGAAGLTSRDSSVLD CCCCCCCCCCCCCCC | 38.85 | 28450419 | |
| 150 | Phosphorylation | AGLTSRDSSVLDGTD CCCCCCCCCCCCCCC | 22.64 | 20873877 | |
| 151 | Phosphorylation | GLTSRDSSVLDGTDS CCCCCCCCCCCCCCC | 30.87 | 20873877 | |
| 156 | Phosphorylation | DSSVLDGTDSQTGND CCCCCCCCCCCCCCC | 31.95 | 27251275 | |
| 158 | Phosphorylation | SVLDGTDSQTGNDEE CCCCCCCCCCCCCHH | 29.49 | 26657352 | |
| 160 | Phosphorylation | LDGTDSQTGNDEEAF CCCCCCCCCCCHHHH | 41.74 | 26657352 | |
| 185 | Phosphorylation | EEGPPVQSLKGEDAE HHCCCCCCCCCCCHH | 32.08 | 20873877 | |
| 194 | Phosphorylation | KGEDAEESLEEEEAL CCCCHHHHHHHHHHH | 32.36 | 29255136 | |
| 209 | Phosphorylation | DPLGIMRSKKPKKHP CHHHHCCCCCCCCCC | 27.87 | 26657352 | |
| 221 | Acetylation | KHPKVAVKAKPSPRL CCCCEEEECCCCCCE | 40.74 | 25953088 | |
| 229 | Phosphorylation | AKPSPRLTIFDEEVD CCCCCCEEEECCCCC | 22.37 | 22817900 | |
| 249 | Phosphorylation | FGPGRKLSPQDPSED CCCCCCCCCCCCCCC | 24.45 | 23927012 | |
| 254 | Phosphorylation | KLSPQDPSEDVSSVD CCCCCCCCCCCCCCC | 55.51 | 30266825 | |
| 258 | Phosphorylation | QDPSEDVSSVDPLKL CCCCCCCCCCCCCCC | 36.65 | 23403867 | |
| 259 | Phosphorylation | DPSEDVSSVDPLKLF CCCCCCCCCCCCCCC | 30.32 | 23403867 | |
| 280 | Phosphorylation | GAIPLGDSLLLPAAC CCCCCCCCCCHHHHH | 21.08 | 25159151 | |
| 289 | Phosphorylation | LLPAACESGGPTPSL CHHHHHHCCCCCCCC | 49.27 | 25159151 | |
| 293 | Phosphorylation | ACESGGPTPSLSHRD HHHCCCCCCCCCHHH | 28.87 | 21712546 | |
| 295 | Phosphorylation | ESGGPTPSLSHRDAS HCCCCCCCCCHHHHH | 45.01 | 27251275 | |
| 297 | Phosphorylation | GGPTPSLSHRDASKE CCCCCCCCHHHHHHH | 22.33 | 27251275 | |
| 302 | Phosphorylation | SLSHRDASKELFRVE CCCHHHHHHHHCCCH | 30.83 | 26657352 | |
| 337 | Acetylation | PKPPVAAKPVIPRKP CCCCCCCCCCCCCCC | 30.04 | 19608861 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H1BP3_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LSMD1_HUMAN | NAA38 | physical | 26344197 | |
| ABTB2_HUMAN | ABTB2 | physical | 28514442 | |
| PDXD1_HUMAN | PDXDC1 | physical | 28514442 | |
| RAD50_HUMAN | RAD50 | physical | 28514442 |
| 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. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "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 | |
| Reference | PubMed |
| "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. | |