wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair protein RAD51 homolog 1 (P37383)
Organism: Gallus gallus (Chicken)
Function: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Also involved in interstrand cross-link repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Chromosome {ECO:0000250|UniProtKB:Q06609}. Note=Accumulated at sites of DNA damage. Recruited to stalled replication forks during replication stress. {ECO:0000250|UniProtKB:Q06609}.
Interaction partners:
- Tower domain-containing protein.
- DNA repair protein RAD52 homolog
- Uncharacterized protein.
- Uncharacterized protein.
- DNA repair and recombination protein RAD54-like
- Partner and localizer of BRCA2
- Uncharacterized protein.
- DNA repair protein
- Uncharacterized protein.
- Fanconi anemia group M protein
Sequence:
MAMQVQFEASTDTSAEEESFGPEPISRLEQCGINANDVKKLEEAGYHTVESVAHAPKKELLNIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARGFNTDHQTQLLYQASAMMAESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKE
Protein: Cell cycle response regulator CtrA (Q7APB9)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MRVLLIEDDSATAQSIELMLKSESFNVYTTDLGEEGVDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLSKVKTPILILSGMAGIEDKVRGLGFGADDYMTKPFHKDELVARIHAIVRRSKGHAQSVISTGELIVNLDAKTVEVGGQRVHLTGKEYQMLELLSLRKGTTLTKEMFLNHLYGGMDEPELKIIDVFICKLRKKLANAAGGANYIETVWGRGYVLREPEGSDYLETA
Protein: Probable PhiRv1 integrase (O06604)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible phage PhiRv1 protein
- Partial REP13E12 repeat protein
- Probable PhiRv1 phage protein
- Possible PhiRv1 phage protein
- Probable PhiRv1 phage protein
- Possible oxidoreductase
- Uncharacterized protein Rv1588c
Sequence:
MRYTTPVRAAVYLRISEDRSGEQLGVARQREDCLKLCGQRKWVPVEYLDNDVSASTGKRRPAYEQMLADITAGKIAAVVAWDLDRLHRRPIELEAFMSLADEKRLALATVAGDVDLATPQGRLVARLKGSVAAHETEHKKARQRRAARQKAERGHPNWSKAFGYLPGPNGPEPDPRTAPLVKQAYADILAGASLGDVCRQWNDAGAFTITGRPWTTTTLSKFLRKPRNAGLRAYKGARYGPVDRDAIVGKAQWSPLVDEATFWAAQAVLDAPGRAPGRKSVRRHLLTGLAGCGKCGNHLAGSYRTDGQVVYVCKACHGVAILADNIEPILYHIVAERLAMPDAVDLLRREIHDAAEAETIRLELETLYGELDRLAVERAEGLLTARQVKISTDIVNAKITKLQARQQDQERLRVFDGIPLGTPQVAGMIAELSPDRFRAVLDVLAEVVVQPVGKSGRIFNPERVQVNWR
Protein: Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (Inosine phosphorylase) (Thymidine phosphorylase) (Uridine phosphorylase) (Xanthosine phosphorylase) (P0C037)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. Is not able to produce D-ribose 1-phosphate from D-ribose and phosphate.
Interaction partners:
- Uridine phosphorylase
- Thymidine phosphorylase
- Adenosine deaminase
- Uridine kinase
- Purine nucleoside phosphorylase 2
- Guanosine-inosine kinase
- Adenine phosphoribosyltransferase
- Purine nucleoside phosphorylase DeoD-type
- Cytidine deaminase
- FMN reductase RutF
Sequence:
MLQSNEYFSGKVKSIGFSSSSTGRASVGVMVEGEYTFSTAEPEEMTVISGALNVLLPDATDWQVYEAGSVFNVPGHSEFHLQVAEPTSYLCRYL
Protein: TPX2 (Targeting protein for Xklp2) protein family (F4K773)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Similarity to unknown protein protein family)
- Cell cycle regulated microtubule associated protein
- At4g11990
- Cell cycle regulated microtubule associated protein
- At4g22860
- Protein WVD2-like 6
- Protein WVD2-like 4
Sequence:
MCTGKSSYTKSSPKFGKTSPTSSVLSLGSNGKGMTKVEPLKERAHDKTKAATTKNITKAPAKENKKPLEFKLHSGERAVKRAMFNYSVATNYYIQKLQKKQEERLQKMIEEEEIRMLRKEMVPKAQLMPFFDRPFLPQRSSRPLTMPKEPSFGNVNSTCWTCVFNNQHYLYHINHAHA
Protein: Amelogenin, X isoform (Class I amelogenin) (P02817)
Organism: Bos taurus (Bovine)
Function: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99217}.
Interaction partners:
- Ameloblastin
- Tuftelin
- Proproteinase E
- Peripherin-2
- Neuropeptide Y receptor type 2
- Short palate, lung and nasal epithelium carcinoma-associated protein 2A
- Chondroadherin
- Somatoliberin
- Somatotropin
- Killer cell immunoglobulin-like receptor, two domains, long cytoplasmic tail, 5A
Sequence:
MGTWILFACLLGAAFSMPLPPHPGHPGYINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPVVSQQTPQNHALQPHHHIPMVPAQQPVVPQQPMMPVPGQHSMTPTQHHQPNLPLPAQQPFQPQSIQPQPHQPLQPHQPLQPMQPMQPLQPLQPLQPQPPVHPIQPLPPQPPLPPIFPMQPLPPMLPDLPLEAWPATDKTKREEVD
Protein: DNA mismatch repair protein MLH3 (MutL protein homolog 3) (Q12083)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLbeta heterodimer, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in promoting meiotic crossing-over and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein MLH1
- MutS protein homolog 4
- MutS protein homolog 5
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MSH2
- Exodeoxyribonuclease 1
- DNA mismatch repair protein PMS1
- ATP-dependent helicase SGS1
- DNA mismatch repair protein MSH1, mitochondrial
Sequence:
MSQHIRKLDSDVSERLKSQACTVSLASAVREIVQNSVDAHATTIDVMIDLPNLSFAVYDDGIGLTRSDLNILATQNYTSKIRKMNDLVTMKTYGYRGDALYSISNVSNLFVCSKKKDYNSAWMRKFPSKSVMLSENTILPIDPFWKICPWSRTKSGTVVIVEDMLYNLPVRRRILKEEPPFKTFNTIKADMLQILVMHPMISLNVQYTDKLRINTEVLFRSKNITEGLTKHQQMSQVLRNVFGAIIPPDMLKKVSLKFNEYQIEGIISKMPVGLKDLQFIYINGRRYADSAFQGYVDSLFQAQDFGEKGMSLLKTKSVGKPYRSHPVFILDVRCPQTIDDLLQDPAKKIVKPSHIRTIEPLIVKTIRSFLTFQGYLTPDKSDSSFEIVNCSQKTATLPDSRIQISKRNQVLNSKMKIARINSYIGKPAVNGCRINNSTINYEKIKNIRIDGQKSRLRNKLSSRPYDSGFTEDYDSIGKTITDFSISRSVLAKYEVINQVDKKFILIRCLDQSIHNCPLLVLVDQHACDERIRLEELFYSLLTEVVTGTFVARDLKDCCIEVDRTEADLFKHYQSEFKKWGIGYETIEGTMETSLLEIKTLPEMLTSKYNGDKDYLKMVLLQHAHDLKDFKKLPMDLSHFENYTSVDKLYWWKYSSCVPTVFHEILNSKACRSAVMFGDELTRQECIILISKLSRCHNPFECAHGRPSMVPIAELK
Protein: GLI family zinc finger 1 (Zinc finger protein GLI1) (F1QAC4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Suppressor of fused homolog.
- Protein patched homolog 1
- Kinesin-like protein kif7
- Protein smoothened
- Protein patched homolog 1
- Sonic hedgehog protein
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
Sequence:
MPVDMQPHQGLYHYDNTSNQPSRGLAPSVRSPYSSEASSVCVALSGGQSVNSREMYNPSMAPGACMEPYMRPPHAPPPHSMMGHRGMPPPEGMSGAPYCNQNMMTSHHNLPHNQHTSELMASGDASCFSTPRSMLKLSKKRALSISPLSDASVDLQTVIRTSPNSLVAFVNSRCGPNNPSSYGHLSVGTMSPSLGFSSSINYSRPQGNIYSHPVPSCIGAPARLPPHNPRLHTPAKHTHLKTEPVLGSVMDSINIKGLEDHSEGDVASPSSTGTQDPLLGLLEGRDDLDKEEKPEPEAIYETNCHWESCSKEFDTQEQLVHHINNEHIHGEKKEFVCHWKDCSREQRPFKAQYMLVVHMRRHTGEKPHKCTFEGCNKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPEAHITKKHRGDTGPRPPGLTTAGQSSELLIEKEERNREDCKLLAPDNTLKSQPSPGGQSSCSSERSPLGSANNNDSGVEMNLNAAGSLEDLTTQEDSGNAGVSESSATISSGGMCMSVQALKRLENLKIDKLKQIRRPTPPGRNAGNKLPALSATGEMMSMCAPSPLLSNRRVMELSAPDMGGVTGMSCPPNDRRGSGTSSLSSAYTVSRRSSMVSPYLSSRRSSDVSHCQSVMGGEVPGDPLSPQNSQRAGLCQNSGGLPGLPSLTPAQQYSLKAKYAAATGGPPPTPLPNMDQAGTPARHVGFLRECQGQPLPPFLQQGGTRRHSANAEYGTGVIYPHQAPGNNTRRASDPVRSAADPQGLPKVQRFNSLSNVSLMSRRNALQQCGSDAALSRHMYSPRPPSITENVMMEAMGMDGNTEGRQQGNMIPGGDRSYMGYQHNPHQASQLSPGQESLGCIDQVYQSQMQGQYQREESCSTGVMGQTDIANNLLQQAEYGMSTCQLSPSGPHYPSQGDGSGPWGQTNQLHSPGMQYQGAGMQGQHYTQQGIYDPTSNPNLQRVTVKPEQFHPSMGGSSSCQNTKALHQNRHNANMQTYPLQGQGIMNRSSSASCDFHHSQMGTQPNQGGSFQSGTGINLALAESRRSQTPMHQMKEMMVRNYVQSQQALLWEQQQEQSVSEKPDGMDMGQTQMMQHSPQHQQANQNLYPGNTYQGYPNQNLMSPQQNRVPGSVKEQMQSSCYGPDMIPRPPQVRKSLSRQNSLSQQAGGAYLGSPPHLSPVHSTASPRRGVRLPPVQQQQQQQQQHSENFNNNNNPMYYSGQIHMHHDLEKTPEGPCLAQQHLTSSDPTTKPTSISYPDPAPMSNALEHLDLENAQIDFTSIIDDQEPSSYSPINAPIGHNQCSSQTSSRLTTPQNSITLPSGLSNMAIGDMSSMLTSLAGENKYLNTLS
Protein: Sodium/potassium-transporting ATPase subunit alpha (A0A060D574)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004415}. Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
Interaction partners:
Sequence:
KQMFGGFSMLLWTGALLCFLAYGIQAAMEDEPANDNLYLGVVLSAVVIVTGCFSYYQEAKSSKIMDSFKNLVPQQALVVRDGEKMNINAQQVVVGDLVEVKGGDRIPADLRIISASGCKVDNSSLTGESEPQTRTPDYSNDNPLETRNIAFFSTNCVEGTARGIVINTGDRTVMGRIATLASGLEVGRTPISIEIEHFIHIITGVAVFLGMSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGTSFDRSSATWAALARVAGLCNRAVFLAEQSGIPILKRDVAGDASESALLKCIELCCGSVQGMRDQYTKVAEIPFNSTNKYQLSVHLNKNEGESKHLLVMKGAPERILDRCSTILIQGKEQPLDDEMKDSFQNAYMELGGLGERVLGFCHFQLPDDQFAEGFQFDCEEVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNEVDPRDAKACVVHGGDLKDLSAEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLFFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSKTDKLVNERLISIAYGQIGMIQALAGFFTYFVILAENGFLPSRLLGIRVDWDNKFCNDLEDSYGQQWTYEQRKIVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMRNKILIFGLFEETALAAFL
Protein: MHC Class I antigen (B60) (Q9MY60)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
SHSMRYFHTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRESLRNLRGYYNQSEAGSHTLQRMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQISQRKWEAAREAEQRRAYLEGECVEWLRRYLENGKDKLERA
Protein: Solute carrier family 15 member 2 (Kidney H(+)/peptide cotransporter) (Oligopeptide transporter, kidney isoform) (Peptide transporter 2) (Q16348)
Organism: Homo sapiens (Human)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity). Also able to transport carnosine. Involved in innate immunity by promoting the detection of microbial pathogens by NOD-like receptors (NLRs) (By similarity). Probably acts by mediating transport of bacterial peptidoglycans across the plasma membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q63424}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:20406817}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20406817}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with the cell membrane in resting macrophages and enriched in phagocytic cups and phagosomes after particle internalization. {ECO:0000269|PubMed:20406817}.
Interaction partners:
Sequence:
MNPFQKNESKETLFSPVSIEEVPPRPPSPPKKPSPTICGSNYPLSIAFIVVNEFCERFSYYGMKAVLILYFLYFLHWNEDTSTSIYHAFSSLCYFTPILGAAIADSWLGKFKTIIYLSLVYVLGHVIKSLGALPILGGQVVHTVLSLIGLSLIALGTGGIKPCVAAFGGDQFEEKHAEERTRYFSVFYLSINAGSLISTFITPMLRGDVQCFGEDCYALAFGVPGLLMVIALVVFAMGSKIYNKPPPEGNIVAQVFKCIWFAISNRFKNRSGDIPKRQHWLDWAAEKYPKQLIMDVKALTRVLFLYIPLPMFWALLDQQGSRWTLQAIRMNRNLGFFVLQPDQMQVLNPLLVLIFIPLFDFVIYRLVSKCGINFSSLRKMAVGMILACLAFAVAAAVEIKINEMAPAQPGPQEVFLQVLNLADDEVKVTVVGNENNSLLIESIKSFQKTPHYSKLHLKTKSQDFHFHLKYHNLSLYTEHSVQEKNWYSLVIREDGNSISSMMVKDTESRTTNGMTTVRFVNTLHKDVNISLSTDTSLNVGEDYGVSAYRTVQRGEYPAVHCRTEDKNFSLNLGLLDFGAAYLFVITNNTNQGLQAWKIEDIPANKMSIAWQLPQYALVTAGEVMFSVTGLEFSYSQAPSSMKSVLQAAWLLTIAVGNIIVLVVAQFSGLVQWAEFILFSCLLLVICLIFSIMGYYYVPVKTEDMRGPADKHIPHIQGNMIKLETKKTKL
Protein: LD39455p (Q9VAR0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMINKFYSSAVQTVSTLSGVLPGNNVTREYEVLEQVCTAGVGLMWKVYNGHKKSTKQEVSVFVFEKKSLERWSKDDRETMLETLRRGVQQLTKIRHPHVLTVQHPLEESRDSLAFATEPVFASLANVVGDNVRSEKKLYDVEIRHGLLQLFDGLQFLHQDAKIVHRNISAETIVINKNRSWKLFGFDFCIANQPATDGTPHWPFREYTTSLHVLAQPSLEYTAPELALNSVNTPDSDLFSLGVLIFTIYAGKPLKMFGSDYSSFRRYANDLNQRKYPPMNAVPSELTESLKALLHPSANLRPKLHELKQIAYFQDVGVKTLSYLDSLYQWDNLQKSKFYKGLPQIIPTLPHRVNLHSILPYLVKEFVNSPMIPFVLPNVLLIAEMSSQREYCDHILPHLKPIFKLTDPIQILLIFMQKMDLLLKLTPAEEVKQSVLPLLYRSLECDMPQIQDLCLAVLPTFSTLIDYNAMKNSVLPRIKKLCLQSSNVSVKVNCLISIGKLLENLDKWLVLDEILPFLQQIQSREPAIIMGIIGIYKIAMTNTKLGITKDVMAHKCIPYLVPLSVENGLTIAQFNTIISLIKEMMGRVEQEQREKLQQLSTIQRDNKPKDASEILANELENSTLSPYGSINGNKINDDMFSGFTVGQPKAAIGAAIAPAKAREQLKISHNTISAPPAARPDILSSMMQSNLTGLGTITVAAAPPPTTTQMPSNNGWHSANPLVMNHQLASPQASNNNSFSLDDLDPFAGGRPSVGAPKANNTNGANMYTVQQPTVNYIYPTGYSLNSIQQHQQQQLLGKPSQAPTLQPQTQPLLPTDNQNLNALSQQDILNFLN
Protein: Cutinase (EC 3.1.1.74) (Q2UIR7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361263}.
Interaction partners:
Sequence:
MHLAIKSLFVSLLGASVLASPLPSNALVERNAPLNEFLSALLSHLPAIDGTIDAVSGVITDFDQLLADLTGARTTQNGYIGVCTDYTVLFARGTSEPGNVGVLVGPPLSEAFEQAVGAKALSFQGVNGYNADVAGYLAGGDAAGSKSMASLASEVLSKCPDTKLVMSGYSQGCQIVHNAVEQLPAADASKISSVLLFGDPYAGKAFPNVDASRVHTVCHAGDTICNNSVVILPPHLTYAVDVTNAVQFAVAAAN
Protein: Tail spike protein (TSP) (Endo-N-acetylneuraminidase) (Endo-N) (Endo-alpha-sialidase) (EC 3.2.1.129) (EndoNF) (G102) [Cleaved into: Mature tail spike protein; Intramolecular chaperone] (Q04830)
Organism: Escherichia phage K1F (Bacteriophage K1F)
Function: Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.
Subcellular location: [Mature tail spike protein]: Virion {ECO:0000269|PubMed:8331067}. Note=Tail spike. {ECO:0000269|PubMed:8331067}.
Interaction partners:
Sequence:
MSTITQFPSGNTQYRIEFDYLARTFVVVTLVNSSNPTLNRVLEVGRDYRFLNPTMIEMLVDQSGFDIVRIHRQTGTDLVVDFRNGSVLTASDLTTAELQAIHIAEEGRDQTVDLAKEYADAAGSSAGNAKDSEDEARRIAESIRAAGLIGYMTRRSFEKGYNVTTWSEVLLWEEDGDYYRWDGTLPKNVPAGSTPETSGGIGLGAWVSVGDAALRSQISNPEGAILYPELHRARWLDEKDARGWGAKGDGVTDDTAALTSALNDTPVGQKINGNGKTYKVTSLPDISRFINTRFVYERIPGQPLYYASEEFVQGELFKITDTPYYNAWPQDKAFVYENVIYAPYMGSDRHGVSRLHVSWVKSGDDGQTWSTPEWLTDLHPDYPTVNYHCMSMGVCRNRLFAMIETRTLAKNALTNCALWDRPMSRSLHLTGGITKAANQRYATIHVPDHGLFVGDFVNFSNSAVTGVSGDMTVATVIDKDNFTVLTPNQQTSDLNNAGKNWHMGTSFHKSPWRKTDLGLIPSVTEVHSFATIDNNGFAMGYHQGDVAPREVGLFYFPDAFNSPSNYVRRQIPSEYEPDASEPCIKYYDGVLYLITRGTRGDRLGSSLHRSRDIGQTWESLRFPHNVHHTTLPFAKVGDDLIMFGSERAENEWEAGAPDDRYKASYPRTFYARLNVNNWNADDIEWVNITDQIYQGGIVNSGVGVGSVVVKDNYIYYMFGGEDHFNPWTYGDNSAKDPFKSDGHPSDLYCYKMKIGPDNRVSRDFRYGAVPNRAVPVFFDTNGVRTVPAPMEFTGDLGLGHVTIRASTSSNIRSEVLMEGEYGFIGKSIPTDNPAGQRIIFCGGEGTSSTTGAQITLYGANNTDSRRIVYNGDEHLFQSADVKPYNDNVTALGGPSNRFTTAYLGSNPIVTSNGERKTEPVVFDDAFLDAWGDVHYIMYQWLDAVQLKGNDARIHFGVIAQQIRDVFIAHGLMDENSTNCRYAVLCYDKYPRMTDTVFSHNEIVEHTDEEGNVTTTEEPVYTEVVIHEEGEEWGVRPDGIFFAEAAYQRRKLERIEARLSALEQK
Protein: Transmembrane protein (Q388G2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSPSQLSREEFTCAYQGYHGRLIVSFHNLAFNSEQLNVDFPWEYVKHIKVTTKHLKEVPTTMLEIKVSRNKQQPSQKPQIDGKQYFYGFEDIVVVEREIQKFRNAASTADHANDDSAPVGADKNANTTSALMSNAKTNATGPRNGHQVGTSSFVQCDRATNGDAAAASPGSPMEDGDYVHGVSRSRQGAHTAREGEEDRRSNLFAPNATGNPLFLLTKSRPPDREHNSPGYGQQNQQLQPKHEKRQKCRAVSFLRRLLPLNSAYISDSGLQVIIGFLLVIVPVLFILVTSMEGRWESPSEGKLEKVIRDLESLQRWRKGQQQQKHGGTVSQTSEAPVHVTLSDLAEGVKELTRRFVDRQHELTALRLRHLQREVPNDVSPLTGMGGVTLSELNAAVDEGAKEEDIENGNGKTSTVETEQQRQQQTRRFSLARVKHDLYRAASLVQKILSFAHWIITGGGKVKQNSYDVPRATPWFFGILGGGGNAAHHHKKRKFVRYVERLPNGQSVTEYVDEEELEERRTCIRLTRSLVASADLLDGVLLQYMGVVMMPQYEAYLNLMQASTGVSFASSLDSNGASPSPSSSSRPSAGQGDTVGSEATGEQGPRLLKTIALRRHASLLLEMEPLSSWGHGYNSQGWKGQPDPSNHGSKNEGYEVPQSVAGNKSISKILNEFLLATQNKLLSGVDTSTPRLMFRNILKEVRYWSRHEEDWQTLVLWQLNRTNTNITNSNHTHERLEAETLKAMDDMPLFRGQWCFLEKPIASPLDSASGRRNTDRTEDHDTRSVESAPREAVYSSHNSKGKETQGEDGLACSAEAVASFPRGIHSSFLPNIKAVGCQKRGSGSVENPGEDLKYGSKGDALGREEETGESHPLDDAADDGRARLRNAEYISREVQLRWKNALELFFSAHNPEKDQWHERDARQKWTSAGRGGTDSWWEREGVINDENTDGQDDGMSAEERDMVKIRRRLLQLFVYVGRRYDQYLFVPASSYPWSAAAFRKCTSEDFGCHFWLRSSLFSFFWPSLWFHTEWLSHPMHEWLRRIKGRDPVIRHLFRELLHIPLGEVEDVSWVLLNTMTTSQELLEVKHNICALMYRLVFVLTAVIVATVAFFRCSH
Protein: histidine kinase (EC 2.7.13.3) (Q1CVV2)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- Response regulator/GGDEF domain protein
- Response regulator
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MSQGLRLSRRSGVLAAGALLLLCGLFAMGRPWATSDNDRYRSALRHLRVASGDLEMDVLRERMGLRTLHGSDPEDFAALRARADALRQFPSFLSAMDRRTMNAALDLFVSALEESAALLERARAADARGEKEAADAAVQALLEGTVSTRAERLINTYLELYERTQARNERSRIIFFIVSLALVAYVLVVMVRLSRATADLATLNTDLERRVEERTKALSAANDGLRASEARKAAILEASPDGILLLDGGGDLLELNPSAQKTFQVVAADVVGRDFLSVALPAELPDGARQKVLAAGRNTASGQATRLESPCLRRDGSTFPAELTIVRVPGEGPPRYTVFVRDITERKAVERMKNEFISTVSHELRTPLTSIRGSLGLLEGGIVGDIPPQALDMVRIARTNTERLIRLINDILDLEKMEAGKLELKVSTPECADLVESAFASVRGMADGAGVSLHAEVTGTPQVKADRDRLVQVLTNLVSNAVKFSPQGAGVTVRVGEEEDGRVRFSVVDQGPGISQEQRARLFGRFQQLDSSDTRSKGGTGLGLAISQAIVEQHGSRITVESEEGRGSTFTFTLESARPASVTPPPVIPEDVSRHEVLVTTADAELASLLGGLLAHEGYRVVRATSLIEAAKHLDTALPDALVVDMRLPEGHALDWVRRLREQPRTHELPVLALSGRSEDAEGVPHWVDWMPRPLEESRLLKSLRYATRQPGQARVLVVDDDASTRRTLCAQMERLGVQVFEAADGESAVELARETTPDLIVLDVGLPRLDGFEVVDILRQGKGRATPLIVFTGRDLTRMDERQLTLGITRHFTKSRASEEELVSSVRDLLNGLLARKAHPS
Protein: Uncharacterized protein (Q381D6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCLPIIRLRNVDLNASTVADDPINASCTLYSFLRPVPTPTECEAAMEVFKCAVRSKGSSGVLSCNNARVVNLINASVQDGVLRNPPKVVPSVARSSQVWRTFLRGKRRNAGAHGQVAETEAEGLGTGSSNILSTGGDNTQIQAERSHTPSIRFEGSRGHSRHEHAESQIDSSHVEVVRETVSMSAARFRTPYEPVGVETEEYTVACYLSPDTTQDVGSDIRNDRKSEMGVENLKDVERSSGTGNDEECISESERIYKPHPVLSHLLEQIRTTLPVEEDELDRREREFSTLMESKAASLHTKLESALSSVPPEETETVAFLQHLKTRVTVAEKLFQVERHEEETIQIAHCTLMIEVEAMRRTLKGIMALVQKAEERLQREGPRAPYHAEELHFMAMLQRALEGTVNP
Protein: L-rhamnose-proton symporter (L-rhamnose-H(+) transport protein) (P27125)
Organism: Escherichia coli (strain K12)
Function: Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-mannose and L-lyxose, but at reduced rates.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2283027, ECO:0000269|PubMed:8262918}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01532, ECO:0000269|PubMed:8262918}.
Interaction partners:
- HTH-type transcriptional activator RhaR
- L-Rhamnulokinase
- HTH-type transcriptional activator RhaS
- L-rhamnose isomerase
- L-rhamnose mutarotase
- Rhamnulose-1-phosphate aldolase
Sequence:
MSNAITMGIFWHLIGAASAACFYAPFKKVKKWSWETMWSVGGIVSWIILPWAISALLLPNFWAYYSSFSLSTRLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIVGTLMTPIINGNFDVLISTEGGRMTLLGVLVALIGVGIVTRAGQLKERKMGIKAEEFNLKKGLVLAVMCGIFSAGMSFAMNAAKPMHEAAAALGVDPLYVALPSYVVIMGGGAIINLGFCFIRLAKVKDLSLKADFSLAKSLIIHNVLLSTLGGLMWYLQFFFYAWGHARIPAQYDYISWMLHMSFYVLCGGIVGLVLKEWNNAGRRPVTVLSLGCVVIIVAANIVGIGMAN
Protein: Transcriptional regulatory protein PdtaR (P9WGM3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system PdtaR/PdtaS. This two-component system plays an essential role in mycobacterial adaptation to poor nutrient conditions. PdtaR probably acts at the level of transcriptional antitermination rather than transcriptional initiation.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:34003742}.
Interaction partners:
- Sensor histidine kinase PdtaS
- Small ribosomal subunit protein bS1
- Probable transcriptional regulatory protein
- ATP synthase subunit beta
- Uncharacterized protein Rv2239c
- Transcriptional regulatory protein
Sequence:
MTGPTTDADAAVPRRVLIAEDEALIRMDLAEMLREEGYEIVGEAGDGQEAVELAELHKPDLVIMDVKMPRRDGIDAASEIASKRIAPIVVLTAFSQRDLVERARDAGAMAYLVKPFSISDLIPAIELAVSRFREITALEGEVATLSERLETRKLVERAKGLLQTKHGMTEPDAFKWIQRAAMDRRTTMKRVAEVVLETLGTPKDT
Protein: Dehydrogenase/reductase SDR family member 2, mitochondrial (EC 1.1.1.-) (Dicarbonyl reductase HEP27) (Protein D) (Short chain dehydrogenase/reductase family 25C member 1) (Protein SDR25C1) (Q13268)
Organism: Homo sapiens (Human)
Function: NADPH-dependent oxidoreductase which catalyzes the reduction of dicarbonyl compounds. Displays reductase activity in vitro with 3,4-hexanedione, 2,3-heptanedione and 1-phenyl-1,2-propanedione as substrates. May function as a dicarbonyl reductase in the enzymatic inactivation of reactive carbonyls involved in covalent modification of cellular components. Also displays a minor hydroxysteroid dehydrogenase activity toward bile acids such as ursodeoxycholic acid (UDCA) and isoursodeoxycholic acid (isoUDCA), which makes it unlikely to control hormone levels. Doesn't show any activity in vitro with retinoids and sugars as substrates. Attenuates MDM2-mediated p53/TP53 degradation, leading to p53/TP53 stabilization and increased transcription activity, resulting in the accumulation of MDM2 and CDKN1A/p21. Reduces proliferation, migration and invasion of cancer cells and well as the production of ROS in cancer.
Subcellular location: Mitochondrion matrix. Nucleus. Note=A minor fraction of the protein is translocated from the mitochondria to the nucleus, after cleavage of the targeting signal.
Interaction partners:
- E3 ubiquitin-protein ligase DZIP3
- E3 ubiquitin-protein ligase TTC3
- SH2 domain-containing adapter protein B
- SH2 domain-containing adapter protein D
- Glucocorticoid modulatory element-binding protein 1
- Prolyl 3-hydroxylase 3
Sequence:
MLSAVARGYQGWFHPCARLSVRMSSTGIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVFHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYSTRL
Protein: Non-specific lipid transfer protein GPI-anchored 16 (AtLTPG-16) (Protein LTP-GPI-ANCHORED 16) (Protein EMBRYO SAC DEVELOPMENT ARREST 4) (Xylogen like protein 6) (AtXYP6) (Q94AX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein involved in female gametophyte development. Probable lipid transfer protein (By similarity).
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- GDSL esterase/lipase At4g30140
- GDSL esterase/lipase At1g74460
- GDSL esterase/lipase At2g23540
- Cytochrome b561 and DOMON domain-containing protein At4g17280
- GDSL esterase/lipase At5g37690
- Glycerol-3-phosphate acyltransferase 5
- Omega-hydroxypalmitate O-feruloyl transferase
- Casparian strip membrane protein 1
- Peroxidase 23
- CASP-like protein 1A1
Sequence:
MEGLTLIVVMMSSFMLGGQGQQISTPCTSSMISTFTPCLNFITGSSGGSVTPTAGCCDSLKTLTNTGMGCACLILTANVPLPTGFINRTLALALPRACKMGGVPIQCQAAGTPLPAPGQVPFLIAPPPQVSAFSPGASKAAGTTPTQAPAPDTPADGPTGPTTKSGIRPVDQPMQPTGLAQSSTSPFLPLLFISLILLNL