HOB2 / YPR117W Protein
Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval
for
various strains, sequence-based physico-chemical properties, protein modification sites, and external
identifiers for the protein.
Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval for various strains, sequence-based physico-chemical properties, protein modification sites, and external identifiers for the protein.
- Feature Type
- ORF , Verified
AlphaFold Protein Structure
AlphaFold, developed by DeepMind, is an AI program that accurately predicts protein structures from amino acid sequences, enabling visualization of protein conformations. The predicted structures can be accessed through the Protein Data Bank (PDB) and AlphaFold Protein Structure Database.
Experimental Data
Contains experimentally-derived protein half-life data obtained using stable isotope labeling by amino acids (SILAC) coupled with mass spectrometry. This section also contains protein abundance data for both untreated and treated cells obtained from over 20 studies. These data have been normalized and converted to a common unit of molecules per cell.
Protein Half Life
Protein Abundance
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Abundance (molecules/cell) | Media | Treatment | Treatment time | Fold Change | Visualization | Strain background | Original Reference | Reference |
|---|---|---|---|---|---|---|---|---|
| 1237 | SD | untreated | confocal microscopy evidence | S288C | Breker M, et al. (2013) | Ho B, et al. (2018) | ||
| 437 | YEPD | untreated | quantitative mass spectrometry evidence | S288C | Kulak NA, et al. (2014) | Ho B, et al. (2018) | ||
| 138 | SC | untreated | quantitative mass spectrometry evidence | S288C | Peng M, et al. (2012) | Ho B, et al. (2018) |
Domains and Classification - S288C
Collection of computationally identified domains and motifs, as determined by InterProScan analysis; includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain.
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Evidence ID | Analyze ID | Gene | Gene Systematic Name | Protein Coordinates | Accession ID | Description | Source | No. of Genes with Domain |
|---|
Domain Locations
Visual representation of the locations of the domains within the protein, as listed in the Domains and Classification table. Each row displays the domain(s) derived from a different Source, with domains color-coded according to this Source.
Scroll over a domain to view its exact coordinates and its Description.
Alleles
Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.
View all HOB2 alleles in SGD search
Sequence
Protein sequence for the given gene in S288C and other strains, when available. Use the pull-down menu under "Strain" to select the sequence for a specific strain. The displayed sequence can be downloaded in FASTA format as a .txt file. Amino acids displayed in blue represent modification sites. More detailed evidence for these modification sites is presented in the Post-translational Modifications table, located just below the protein sequence.
This locus is not translated into a protein.
1 MSMLPWSQIR DVSKLLLGFM LFIISIQKIA SILMSWILML RHSTIRKISF GYFFGTSIRR
61 AFILTDFAQI YIGKITLRIG WKPGIVFHNV DLKLFGKDSH ITAHSTKDSR TYFNPRDQTF
121 TFVINRRVLS ILKLVFSFST FFHTLALTVP NGKQYKLNIG SITISHPHDD TIKLEAFLHD
181 FTHPETKDTL NHTGFFMVCK IGKEDDTGSN CTKVILKNWK SSLKISDVCW HLPEKKGKNL
241 HSEPVEPFSA GDDAEMLTSY RKMLKPFHYP LKTLNILDLK VENVKLIYKK KFTIRISSAQ
301 LYLESISILN NVSALELLPL NKPTWGDFEL SLSANAVVVD IDGNTAVRIP FGNVILTSDI
361 LLFLLDNVPL RRTKVSSILN IINPSVFLTI HQVLEVLHLV DKFDSPETSS CTNTNDRSLN
421 ILDLDIDRLP SFNFELLMSN FISRLHISDE ENVTFKVFST HALFSRNNLS MTPKKGQVMQ
481 IRPDWPFAKT ALVSDQLSNY IKIVGTSLSY LRIPTEQDAN PVSIPVCGFE RLDTFLDEFS
541 NSKLIVQSTL RHSYVSLENI EVLHTLSRAF DKIYLLISSR TKRNAAHKAN GGKLGDLNEA
601 KKTFNWSLKL RMKDISCSLL VAGFLPKNLD PVEAENFNLS DVTRGAKVVF TESILLADSQ
661 EKNFTIIDAS VYRFMDGTTY KPSPEVIIQF TNLLLSFNDS DEIHFSLPKI KFKMDVNIIW
721 LWFYIRSIWI KFRPNSKLSR NSVSSVKSVN VLDRLRVDIG KMIIELTLPH NTEVLLIFER
781 IGLSSSTKNL TIASLSAYVV SVYVKHIKVY VSLLNINDFE LDTEELICKK SAVINTSLIH
841 FHAEYHFRFY MITDNIVTLY KSFKQIKLAF SNLNEFKRLY PQQQFPKKVP NLHICCQDFL
901 IDIEEDPFEQ ELGLILKVGV LEQRERLKKL EEFKEKLSTY EDMNVRLRSL YDTSRGQSFF
961 PEFYANDQEY EQKAYLRLLE NFSTSWIARY RKAKLSFYGM PYRVISREEL GTKYHLFTRQ
1021 KTSTVANLVV KDLDFKLGSP SFPLDNYMDF VYQYGKKVPK STEYTLLIIL GLKIKSALWE
1081 LRLRDYPIPA ISFPDTFTTG DVVFAEKMPA PCALHTVYVP FVSSAQRSPY NDANTIYGLH
1141 IIRTINSVKT YFNIRSMVTS SSSARITWGK SLQPGYESLM LWFDFLTKPL IDPSKKLGFW
1201 DKFRYLVHGK WIYEFSEESE IHLNIKGSHD PYKITDDGAG LAFCWSGGTT IYVHNSTDPK
1261 EFLKIESQRF QLAVPDFAKV SKFDKVFMKL DGRVIWTLGL LFEQGDISKA GDEERFLPNR
1321 PHYEIQLMNP DGVADLDHHD TYKGFRTSFI HMSFGVYSSE HGSINSLYLA PYALTHFFKW
1381 WNLFHTYTSG PIRQGRLFTD VLQNKTKFGR SLFTIAYQLH LKRLMVTHIY RHITTQYDLE
1441 KDRKITFTGL KGRFDSLKID LHQKRVKLTH TNQKLNKSKP VWKFKMSRGE IDCAEADIRI
1501 LSTLFDQEAV KEILTSGLDG ILEDEPSRPI TPQDVEYLRE SDWYDYEDYI DLNQVPLGSS
1561 LPLKLEAIPL LYSPRISYFR KINDDGYVLA YPFGTEESHN CLIGKNHPEL TQEKLATERK
1621 REIEEQLKLL HITLSELQSN KGGGSVSGNS ERYARELKAE VAELNHRLHT VNTILSDLKI
1681 SETIPGGNTD GDSSSSLSDT DVNLENAPPI QNRISLLRTN TVESFVSMRK ASTMQVESTY
1741 DNRFMVHNIE LKIDNKIRHH LLEYASSAFE RKSMRFAVTY KSVTILKELL GNVLTGVRTS
1801 VEDYGSILED DLASNSEFIE HFEKLIREVP SDDFDYVDNY LFRLISPQVQ IKSDVERNAA
1861 VILAARDIEM GIIDIVQVYG KSGKRIPVDV DTIVETRYSA VSKDIQLFTL FKKDLEGPEG
1921 RFFHKNGYGS DKESDIWPPW IPLEMCFDGS LLDKHVFLKR RSMFLTYVAP NPLFFSANDT
1981 SAFSYDSRFR IAFPGLVLTS DCQQYCAVYA IAEDLLSFGS SLDEKVEKLS RILFTDEVRN
2041 NLENLDVSVV TALQERIKEL YYTRAYLKLH EPRLFMKSGQ ELTFDIQTST LKLTLLMTAI
2101 KKTYDRMGSG NRVIQKRLRW QVGTDELIWE LYDESKTPFV TIGLGPSTFI RSETSDGTNS
2161 NKVSISSLQC FNQQENPVYT ELLAPFYENS SYNKNAPMVE IFWILGPSVG GISDLQDLIV
2221 SLQPLIFKMD HKTSEKLMNY LFPKIEQTSI EPNSPELVPR SSTSSFFSSS PVLRHSLSNG
2281 SLSVYDAKDV DSWDLRSIQS KEGIKKHKGD HRKLSASLFV QPDYNINEMV KRSGTFFNVK
2341 SIIIRKTLMS VCYKGSHSLL TDVNNLIVRV PVLKYHNKLW SREEFFTALK RDVVRIVLQH
2401 LGNIIGNKFL PHKKENKKKT SMEIHRLLSP DSQNRDNSHI LEVEGHNSFY SSTHSSDIRS
2461 INSDETYNEN DGNGVKPFYP VTSEFSKNK*
* Blue amino acids indicate modification sites. More information below.
Post-translational Modifications - S288C
Modification sites for the protein in the selected strain, based on the presence of a residue in the specific strain, as inferred from experimental evidence.
35 entries for 25 sitesIncrease the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Site | Modification | Modifier | Reference |
|---|---|---|---|
| S13 | phosphorylated residue | Leutert M, et al. (2023) PMID: 37845410 | |
| T148 | phosphorylated residue | Leutert M, et al. (2023) PMID: 37845410 | |
| S1163 | phosphorylated residue | Leutert M, et al. (2023) PMID: 37845410 | |
| S1527 | phosphorylated residue | Holt LJ, et al. (2009) PMID: 19779198 | |
| T1531 | phosphorylated residue | Lanz MC, et al. (2021) PMID: 33491328 | |
| T1531 | phosphorylated residue | Holt LJ, et al. (2009) PMID: 19779198 | |
| T1633 | phosphorylated residue | Leutert M, et al. (2023) PMID: 37845410 | |
| T1721 | phosphorylated residue | Lanz MC, et al. (2021) PMID: 33491328 | |
| T1721 | phosphorylated residue | Albuquerque CP, et al. (2008) PMID: 18407956 | |
| T1733 | phosphorylated residue | Zhou X, et al. (2021) PMID: 33481703 |
Sequence-Based Physico-chemical Properties - S288C
Calculated protein properties, including amino acid composition, length, coding region calculations, and atomic composition.
Amino Acid Composition
Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.
| Amino Acid | Frequency | Percentage |
|---|---|---|
| A | 89 | 3.58 |
| C | 18 | 0.72 |
| D | 149 | 5.99 |
| E | 144 | 5.79 |
| F | 147 | 5.91 |
| G | 107 | 4.30 |
| H | 70 | 2.81 |
| I | 184 | 7.39 |
| K | 184 | 7.39 |
| L | 279 | 11.21 |
| M | 43 | 1.73 |
| N | 127 | 5.10 |
| P | 100 | 4.02 |
| Q | 67 | 2.69 |
| R | 121 | 4.86 |
| S | 241 | 9.68 |
| T | 148 | 5.95 |
| V | 149 | 5.99 |
| W | 30 | 1.21 |
| Y | 92 | 3.70 |
Physical Details
| Length (a.a): | 2489 |
| Molecular Weight (Da): | 285918.3 |
| Isoelectric Point (pl): | 8.5 |
| Formula: | C12978H20284N3400O3751S61 |
| Aliphatic Index: | 88.66 |
| Instability Index: | 41.72 |
Coding Region Translation Calculations
| Codon Bias: | -0.03 |
| Codon Adaptation Index: | 0.12 |
| Frequence of Optimal Codons: | 0.41 |
| Hydropathicity of Protein: | -0.25 |
| Aromaticity Score: | 0.11 |
Extinction Coefficients at 280nm
| ALL Cys residues appear as half cystines: | 303205.0 |
| NO Cys residues appear as half cystines: | 302080.0 |
Atomic Composition
Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.
| Atom | Frequency | Percentage |
|---|
Data not found or not available for S288C
External Identifiers
List of external identifiers for the protein from various database sources.
15 entries for 8 sourcesIncrease the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| External ID | Source |
|---|---|
| orf19.1240 | CGD |
| 6325374 | GenBank/EMBL/DDBJ |
| AAB68087.1 | GenBank/EMBL/DDBJ |
| U32445 | GenBank/EMBL/DDBJ |
| 74676385 | GenBank/EMBL/DDBJ |
| 914988 | GenBank/EMBL/DDBJ |
| 6608 | LoQAtE |
| DAA11532.1 | NCBI |
| NM_001184214.1 | NCBI |
| 856233 | NCBI |
Resources
Homologs
AGD | AnalogYeast | BLASTP at NCBI | CGD | FungiDB | PhylomeDB | PomBase | YGOB | YOGY
Protein Databases
AlphaFold Protein Structure | GPMDB | ModelArchive | Pfam domains | SUPERFAMILY | TopologYeast | UniProtKB
Localization
CYCLoPs | dHITS | LoQAtE | YeastGFP | YeastRGB | YPL+