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 | ||
|
* 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. |