wanglab/gogpt-training-data huggingface dataset:
Protein: GH01974p (Q95U74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MASQPLGLLLGAILFSICAIDASVPHPLAANYSIDILRLAKAAHIKAYMGDEKEQACNNFYNYACANWPRLHPARKSKTRTNYLEELQELYIRKSADMLKSATRGAENSADRQLKYFYGSCRLQTNDTRSALNTLQNVTDFRGGWPEIRVASWYQYEYDWLQVVANLKRKLGVDIFIGLEVILDYKEEKMHRLKIGAPQFPMSRRHYLHPHFEGTREIYERSIENKLKLYFPEQSEHWRQEVASQVVQIEQQLAKGLPHNPALTLAQTTRQRTAAEMKTAYGSYVDVTRYLQLIFNDNLYMDLYETPEDYMSNLVDVIRETPKLQLANYTMWKALEALDIARVPASQRADIWCVQLAQQFFPHQLESLFHRNYNHMQMINELQSTWSDIKRVFREDLQASERLLWLTLETRQKAITKLEALKLHFRTHDDNKLIRQMHGLILNMDRFYPNLVSVLQWKTQRGLAKLMTEPVAEDEVHKLPHYEIQKNRIQVPITFLQARFFWDPAYPNGLKYATLGVLLARQMLHGFDGVGRRYDAYGYKNNWWDHTSESSYSRRTQCFQEQYAIFVEYKGKPVQDKDLLRRIVADNGALDIAYRAYQQWLKNAAETPVIYQRERLPLLDHDHNQIFYLGYAQLYCTDYPETVERFDELPEQLRVNTALSNSQQFANAYGCSMEEKLNARFKCTLY
Protein: KH homology domain-containing protein 4 (Brings lots of money 7) (Pre-mRNA splicing factor protein Khdc4) (Q3TCX3)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein involved in pre-mRNA splicing. Interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. Involved in regulating splice site selection. Binds preferentially RNA with A/C rich sequences and poly-C stretches.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7Z7F0}. Cytoplasm {ECO:0000250|UniProtKB:Q7Z7F0}.
Interaction partners:
Sequence:
MSAGSATHPAAGGRRSKWDQPAPAPLLFLPPTAPGGEVAGSGASPGGATTAAAPSGALDAAAAVAAKINAMLMAKGKLKPSQNAAEKLQAPGKSLTSNKSKDDLVVAEVEINDVPLTCRNLLTRGQTQDEISRLSGAAVSTRGRFMTTEEKAKVGPGDRPLYLHVQGQTRELVDRAVNRIKEIITNGVVKAATGTSPTFNGATVTVYHQPAPIAQLSPAINQKPSFQSGMHYVQDKLFVGLEHAVPTFNVKEKVEGPGCSYLQHIQIETGAKVFLRGKGSGCIEPASGREAFEPMYIYISHPKPEGLAAAKKLCENLLQTVHAEYSRFVNQINTAVPLPGYTQPSAISSIPPQPPYYPSNGYQSGYPVVPPPQQPVQPPYGVPSIVPPAVSLAPGVLPALPTGVPPVPTQYPITQVQPPASTGQSPISAPFIPAAPVKTALPTGPQPQPQLPAQPQSQKRRFTEELPDERDSGLLGYQHGPIHMTNLGTGFSSQNEIEGAGSKPASSSGKERERDRQLMPPPAFPVTGIKTESDERNGSGALAGSHDYPAKKMKTAEKGFGLVAYAADSSDEEEEHGGHKNASSFPQGWSLGYQYPSSQPRAKQQMPFWMAP
Protein: UDP-N-acetylglucosamine transferase subunit ALG14 (Asparagine-linked glycosylation protein 14) (P38242)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:16100110, ECO:0000269|PubMed:17686769}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:15282802}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- GDP-Man:Man
- Dol-P-Man:Man
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichol-phosphate mannosyltransferase
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Protein FMP52, mitochondrial
Sequence:
MKTAYLASLVLIVSTAYVIRLIAILPFFHTQAGTEKDTKDGVNLLKIRKSSKKPLKIFVFLGSGGHTGEMIRLLENYQDLLLGKSIVYLGYSDEASRQRFAHFIKKFGHCKVKYYEFMKAREVKATLLQSVKTIIGTLVQSFVHVVRIRFAMCGSPHLFLLNGPGTCCIISFWLKIMELLLPLLGSSHIVYVESLARINTPSLTGKILYWVVDEFIVQWQELRDNYLPRSKWFGILV
Protein: Glutathione-specific gamma-glutamylcyclotransferase 1 (Gamma-GCG 1) (EC 4.3.2.7) (Blocks Notch protein) (Botch) (Cation transport regulator-like protein 1) (Q9BUX1)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Glutathione depletion is an important factor for apoptosis initiation and execution. Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Notch in an immature inactive form, thereby promoting neurogenesis in embryos.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19109178}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8R3J5}.
Interaction partners:
- Tribbles homolog 3
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Gamma-glutamylcyclotransferase
- 5-oxoprolinase
- Glutathione hydrolase 6
- Glutathione hydrolase 5 proenzyme
- Glutathione peroxidase 3
- Glutathione synthetase
- Glutathione hydrolase 1 proenzyme
- Glutathione peroxidase 2
Sequence:
MKQESAAPNTPPTSQSPTPSAQFPRNDGDPQALWIFGYGSLVWRPDFAYSDSRVGFVRGYSRRFWQGDTFHRGSDKMPGRVVTLLEDHEGCTWGVAYQVQGEQVSKALKYLNVREAVLGGYDTKEVTFYPQDAPDQPLKALAYVATPQNPGYLGPAPEEAIATQILACRGFSGHNLEYLLRLADFMQLCGPQAQDEHLAAIVDAVGTMLPCFCPTEQALALV
Protein: Probable eukaryotic initiation factor 4A (ATP-dependent RNA helicase eIF4A) (Q38AX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Sas10 C-terminal domain-containing protein
- ESF1 RRM domain-containing protein
- RNA helicase
- BING4 C-terminal domain-containing protein
- KRR1 small subunit processome component
- rRNA biogenesis protein, putative
- Nop14-like protein
- Probable eukaryotic initiation factor 4A
- DDB1- and CUL4-associated factor 13
- CCAAT-binding factor domain-containing protein
Sequence:
MVKEKLAGGKKRPREESLRTIPPNQSIGSELLDNEESKDVTFKSLGLCEELIGACKEAGWRMPTRIQVATIPVVSEGRDIIGVAQTGSGKTGAYVLPLVNWLLTQAKVPYLSILVMVPTRELAQQVAAQFVMLGSSVGLRVATLVGGADMVDQACELSRRPHVVVGTPGRVKDHLNNTKGFQLVKLHALVLDEADKMLEMDYEKEINAILEHLPHNRQTLLFSATLSTKIDRLQNASLNDPVLLEVHRKNTTVDTLKQYYVFAPFAQMLPYLHLYLTRESGNHILVFCRSAALVHRITLTLRVLGHQALPLMGRMDQKNRNIALTKFKEGRVRILVCTDVAQRGLDIPRTDVVVNFALPDRVEDYIHRVGRTARAGAQGKAVNIISQYDIVLLQKVEASTGVKCEEWPISDGDVAAVLQRVEDAEQEAVKEMRESDQEAKFEREARQLTTARRAKRERGDNDMGYDDAKHGTADFSTLRLRREHESVFQMTKKQQHKSLWAKRREVRKQMKS
Protein: Protein GL2-INTERACTING REPRESSOR 1 (Q9FNI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of root hair development redundantly with GIR2. GIR1 and GIR2 may function as adapter proteins that associate with GL2 and participate in the control of root hair formation. GIR1 and GIR2 may function as adapter proteins that associate with TPL and participate in the repression of root gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:28526410, ECO:0000269|PubMed:28526412}.
Interaction partners:
- Homeobox-leucine zipper protein GLABRA 2
- Serine/threonine-protein kinase-like protein CCR4
Sequence:
MSRRSPKLELKLNLSPPTSSQRRMVRSPSRSATTSPTSPPSSCVSSEMNQDEPSVRYSTSPETTSMVLVGCPRCLMYVMLSEDDPKCPKCKSTVLLDFLHENATNANANAAAASSGRKTRRN
Protein: Protein BANP (B4DE54)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMSEHDLADVVQIAVEDLSPDHPVVLENHVVTDEDEPALKRQRLEINCQDPSIKSFLYSINQTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENVISNAVPGRRQNTIVVKVPGQEDSHHEDGESGSEASDSVSSCGQAGSQSIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPNSSSYCPSEPMMSTPPPASELPQPQPQPQALHYALANAQQVQIHQIGEDGQVQVGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQVLQGAQLIAVASSDPAAAGVDGSPLQGSDIQVQYVQLAPVSDHTAGAQTAEALQPTLQPEMQLEHGAIQIQ
Protein: Phospholipase A2 group V (EC 3.1.1.4) (PLA2-10) (Phosphatidylcholine 2-acylhydrolase 5) (P39877)
Organism: Homo sapiens (Human)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), preferentially releasing fatty acyl groups with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl (C18:2) groups. Hydrolyzes low-density lipoprotein (LDL) phospholipids releasing unsaturated fatty acids that drive macrophage polarization toward an M2 phenotype (By similarity). May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes at different subcellular locations and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a major component of the inner membrane of mitochondria and bacterial membranes. Promotes phagocytosis of bacteria in macrophages through production of lysophosphatidylethanolamines. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Promotes phagocytosis and killing of ingested fungi likely through controlling phagosome-lysosome fusion and phagosome maturation (By similarity). Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells. In eosinophils, triggers perinuclear arachidonate release and LTC4 synthesis in a PLA2G4A-independent way. In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A. Promotes immune complex clearance in macrophages via stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger phagocytosis (By similarity). May regulate antigen processing in antigen-presenting cells (By similarity). In pulmonary macrophages regulates IL33 production required for activation of group 2 innate lymphoid cells (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines.
Subcellular location: Secreted {ECO:0000269|PubMed:8300559}. Cell membrane {ECO:0000250|UniProtKB:P97391}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P97391}. Recycling endosome {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P97391}.
Interaction partners:
- Cytosolic phospholipase A2 delta
- Cytosolic phospholipase A2 beta
- Group 3 secretory phospholipase A2
- Phospholipase A and acyltransferase 3
- Lysosomal phospholipase A and acyltransferase
- Group XIIA secretory phospholipase A2
- Platelet-activating factor acetylhydrolase
- Prostaglandin G/H synthase 2
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Polyunsaturated fatty acid 5-lipoxygenase
Sequence:
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGTDWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKRNLRSYNPQYQYFPNILCS
Protein: SET domain-containing protein (Q57WW4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLNAGGAFSGFWEWCAQNGIVSKKLFIRQSMQGLMPLLSLHADQPIGAGDVVLSVPYLSTLNAQTVRGDLRPVAVPSIRVMCRFLQRRGVDISTARALWLASCLACATRLVAQGHEVGFAPLLSSSLLPKLPSPFVEAYVGGYPAISDALAGVADEPVRRAYLKDFETQVRSQLRATHAILRFNQRRHPSRIPLTLLPTVDELCAAYRTVLQRSVMLPVDCVPSSPGDLADLLEEKQGIDVLPSLVPGIDIIRSPTGYPPVTSVAGNSSGTPIAGDESNAANCSLHTCVQSDFISPGTRRRVLLETEPLSNRRVVVCSTKEIKVGEELFLSYGS
Protein: Estradiol 17-beta-dehydrogenase 11 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 11) (17-beta-HSD 11) (17bHSD11) (17betaHSD11) (17-beta-hydroxysteroid dehydrogenase XI) (17-beta-HSD XI) (17betaHSDXI) (Cutaneous T-cell lymphoma-associated antigen HD-CL-03) (CTCL-associated antigen HD-CL-03) (Dehydrogenase/reductase SDR family member 8) (Retinal short-chain dehydrogenase/reductase 2) (retSDR2) (Short chain dehydrogenase/reductase family 16C member 2) (Q8NBQ5)
Organism: Homo sapiens (Human)
Function: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor-associated antigen in cutaneous T-cell lymphoma.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9EQ06}. Lipid droplet {ECO:0000250|UniProtKB:Q9EQ06}. Note=Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation. {ECO:0000250|UniProtKB:Q9EQ06}.
Interaction partners:
Sequence:
MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLKSKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKVKAEIGDVSILVNNAGVVYTSDLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMTKNNHGHIVTVASAAGHVSVPFLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPEEVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKRKISVKFDAVIGYKMKAQ
Protein: Zinc finger protein 618 (Q5T7W0)
Organism: Homo sapiens (Human)
Function: Regulates UHRF2 function as a specific 5-hydroxymethylcytosine (5hmC) reader by regulating its chromatin localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:27129234}. Chromosome {ECO:0000269|PubMed:27129234}. Note=Localizes at genomic loci that are enriched for 5-hydroxymethylcytosine (5hmC). {ECO:0000269|PubMed:27129234}.
Interaction partners:
Sequence:
MNQPGGAAAPQADGASAAGRKSTASRERLKRSQKSTKVEGPEPVPAEASLSAEQGTMTEVKVKTELPDDYIQEVIWQGEAKEEKKAVSKDGTSDVPAEICVVIGGVRNQQTLDGKAPEGSPHGGSVRSRYSGTWIFDQALRYASGSYECGICGKKYKYYNCFQTHVRAHRDTEATSGEGASQSNNFRYTCDICGKKYKYYSCFQEHRDLHAVDVFSVEGAPENRADPFDQGVVATDEVKEEPPEPFQKIGPKTGNYTCEFCGKQYKYYTPYQEHVALHAPISTAPGWEPPDDPDTGSECSHPEVSPSPRFVAAKTQTNQSGKKAPASVVRCATLLHRTPPATQTQTFRTPNSGSPASKATAAESAFSRRVEGKAQNHFEETNSSSQNSSEPYTCGACGIQFQFYNNLLEHMQSHAADNENNIASNQSRSPPAVVEEKWKPQAQRNSANNTTTSGLTPNSMIPEKERQNIAERLLRVMCADLGALSVVSGKEFLKLAQTLVDSGARYGAFSVTEILGNFNTLALKHLPRMYNQVKVKVTCALGSNACLGIGVTCHSQSVGPDSCYILTAYQAEGNHIKSYVLGVKGADIRDSGDLVHHWVQNVLSEFVMSEIRTVYVTDCRVSTSAFSKAGMCLRCSACALNSVVQSVLSKRTLQARSMHEVIELLNVCEDLAGSTGLAKETFGSLEETSPPPCWNSVTDSLLLVHERYEQICEFYSRAKKMNLIQSLNKHLLSNLAAILTPVKQAVIELSNESQPTLQLVLPTYVRLEKLFTAKANDAGTVSKLCHLFLEALKENFKVHPAHKVAMILDPQQKLRPVPPYQHEEIIGKVCELINEVKESWAEEADFEPAAKKPRSAAVENPAAQEDDRLGKNEVYDYLQEPLFQATPDLFQYWSCVTQKHTKLAKLAFWLLAVPAVGARSGCVNMCEQALLIKRRRLLSPEDMNKLMFLKSNML
Protein: carbonic anhydrase (EC 4.2.1.1) (Q55136)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Carboxysome assembly protein CcmM
- Carbonic anhydrase
- Cyanate hydratase
- Low affinity sulfate transporter
- Bicarbonate transporter BicA
- Bifunctional pantoate ligase/cytidylate kinase
- Methyl-accepting chemotaxis protein
Sequence:
MMGKIEKFALTQNTSVFLVVLPDTQLNYPMAKIPTIDRRQLIQYGGAFLGTSLMATILGNQMAGNPAAQAQSANQTPQQLLTELMEGNGRFAAQKRVKANQDLYRLAEVAQGQNPFAAILSCADSRVPPEIIFDQGLGDLFICRIAGNVATPQEVGSLEFGTLVLGAKVLMVLGHQGCGAVKAAMDGGDLPGQIGSVIKKIDIGSVTDDSSNAASVVMATKANVEHQMAVLIQSPVLSQLIAEERLLIMGAYYNLESGIVTLL
Protein: Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) (Acetohydroxy-acid synthase I small subunit) (AHAS-I) (ALS-I) (P0ADF8)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Acetolactate synthase isozyme 1 large subunit
- Ketol-acid reductoisomerase
- Acetolactate synthase isozyme 2 small subunit
- Acetolactate synthase isozyme 3 large subunit
- L-threonine dehydratase biosynthetic IlvA
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase
- D-malate dehydrogenase [decarboxylating]
- Acetolactate synthase isozyme 3 small subunit
- L-threonine dehydratase catabolic TdcB
Sequence:
MQNTTHDNVILELTVRNHPGVMTHVCGLFARRAFNVEGILCLPIQDSDKSHIWLLVNDDQRLEQMISQIDKLEDVVKVQRNQSDPTMFNKIAVFFQ
Protein: Aldo-keto reductase Rv2971 (AKR) (EC 1.1.1.-) (P9WQA5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein
- Electron transfer flavoprotein subunit alpha
- OXPP cycle protein OpcA
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- Methionine synthase
- Carboxylic ester hydrolase LipN
- Possible conserved membrane or secreted protein
Sequence:
MTGESGAAAAPSITLNDEHTMPVLGLGVAELSDDETERAVSAALEIGCRLIDTAYAYGNEAAVGRAIAASGVAREELFVTTKLATPDQGFTRSQEACRASLDRLGLDYVDLYLIHWPAPPVGKYVDAWGGMIQSRGEGHARSIGVSNFTAENIENLIDLTFVTPAVNQIELHPLLNQDELRKANAQHTVVTQSYCPLALGRLLDNPTVTSIASEYVKTPAQVLLRWNLQLGNAVVVRSARPERIASNFDVFDFELAAEHMDALGGLNDGTRVREDPLTYAGT
Protein: RNA helicase (EC 3.6.4.13) (Q5JR04)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLYGMKIANLAYVTKTRVRFFRLDRWADVRFPEKRRMKLGSDISKHHKSLLAKIFYDRAEYLHGKHGVDVEVQGPHEARDGQLLIRLDLNRKEVLTLRLRNGGTQSVTLTHLFPLCRTPQFAFYNEDQELPCPLGPGECYELHVHCKTSFVGYFPATVLWELLGPGESGSEGAGTFYIARFLAAVAHSPLAAQLKPMTPFKRTRITGNPVVTNRIEEGERPDRAKGYDLELSMALGTYYPPPRLRQLLPMLLQGTSIFTAPKEIAEIKAQLETALKWRNYEVKLRLLLHLEELQMEHDIRHYDLESVPMTWDPVDQNPRLLTLEVPGVTESRPSVLRGDHLFALLSSETHQEDPITYKGFVHKVELDRVKLSFSMSLLSRFVDGLTFKVNFTFNRQPLRVQHRALELTGRWLLWPMLFPVAPRDVPLLPSDVKLKLYDRSLESNPEQLQAMRHIVTGTTRPAPYIIFGPPGTGKTVTLVEAIKQVVKHLPKAHILACAPSNSGADLLCQRLRVHLPSSIYRLLAPSRDIRMVPEDIKPCCNWDAKKGEYVFPAKKKLQEYRVLITTLITAGRLVSAQFPIDHFTHIFIDEAGHCMEPESLVAIAGLMEVKETGDPGGQLVLAGDPRQLGPVLRSPLTQKHGLGYSLLERLLTYNSLYKKGPDGYDPQFITKLLRNYRSHPTILDIPNQLYYEGELQACADVVDRERFCRWAGLPRQGFPIIFHGVMGKDEREGNSPSFFNPEEAATVTSYLKLLLAPSSKKGKARLSPRSVGVISPYRKQVEKIRYCITKLDRELRGLDDIKDLKVGSVEEFQGQERSVILISTVRSSQSFVQLDLDFNLGFLKNPKRFNVAVTRAKALLIIVGNPLLLGHDPDWKVFLEFCKENGGYTGCPFPAKLDLQQGQNLLQGLSKLSPSTSGPHSHDYLPQEREGEGGLSLQVEPEWRNEL
Protein: CysB (HTH-type transcriptional regulator CysB) (O05926)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MKLQQLRYIWEVAHHDLNVSATAQSLYTSQPGISKQIRLLEDELGVEVFARSGKHLTRVTPAGERIIHTAGEILRKVESIKQIAQEFSNEKKGTLSIATTHTQARYALPNVISGFIKQYPDVSLHMHQGTPMQIAEMAADGTVDFAIATEALELFGDLIMMPCYRWNRCVIVPHGHPLTKLPKLTLEALAEQPIVTYVFGFTGRSKLDEAFSQRGLVPKVVFTAADADVIKTYVRLGLGVGIVAHMAVDPKLDNDLVILDASHLFESSVTKIGFRRGTFLRGFMCDFIEKFAPHLTRELLAKAVQCHNKAELDELFDGIELPVY
Protein: Cytochrome b-245 chaperone 1 (Essential for reactive oxygen species protein) (Eros) (Q9BQA9)
Organism: Homo sapiens (Human)
Function: Functions as a chaperone necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 heterodimer. Controls the phagocyte respiratory burst and is essential for innate immunity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28351984}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MYLQVETRTSSRLHLKRAPGIRSWSLLVGILSIGLAAAYYSGDSLGWKLFYVTGCLFVAVQNLEDWEEAIFDKSTGKVVLKTFSLYKKLLTLFRAGHDQVVVLLHDVRDVSVEEEKVRYFGKGYMVVLRLATGFSHPLTQSAVMGHRSDVEAIAKLITSFLELHCLESPTELSQSSDSEAGDPASQS
Protein: GDSL esterase/lipase At5g14450 (EC 3.1.1.-) (Extracellular lipase At5g14450) (Q9LY84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein kinase superfamily protein
- GDSL esterase/lipase At5g62930
- At1g62510
- Glutaminyl-peptide cyclotransferase
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- CHY-type/CTCHY-type/RING-type Zinc finger protein
- At2g10940/F15K19.1
- Non-specific lipid transfer protein GPI-anchored 31
- Protein PHLOEM PROTEIN 2-LIKE A9
- At2g45180
Sequence:
MKDNLERAKLMVSSTVFSWLLLCLFAVTTSVSVQPTCTFPAIYNFGDSNSDTGGISAAFEPIRDPYGQGFFHRPTGRDSDGRLTIDFIAERLGLPYLSAYLNSLGSNFRHGANFATGGSTIRRQNETIFQYGISPFSLDMQIAQFDQFKARSALLFTQIKSRYDREKLPRQEEFAKALYTFDIGQNDLSVGFRTMSVDQLKATIPDIVNHLASAVRNIYQQGGRTFWVHNTGPFGCLPVNMFYMGTPAPGYLDKSGCVKAQNEMAMEFNRKLKETVINLRKELTQAAITYVDVYTAKYEMMSNPKKLGFANPLKVCCGYHEKYDHIWCGNKGKVNNTEIYGGSCPNPVMAVSWDGVHYTEAANKHVADRTLNGLLTDPPVPITRACYRQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9FZI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MYHLPTSCLVIFFLLSLFHPLPCDSSNQGLGWCETLFQCGNITAGFPFSGGNRHKECGHPSLELHCNKNNITSLFISNQKYSVLRIDQTSNTLTLAKQNLLGSFCSSVFTNTTLPPETFELSRTYKSVTIFYQCSSVLPNLSSYTCPEIGPISVSESPEKYPESCRSSFTVKVPTSFDTKEKELNVTNLESVLRKGFEVTVVINENTCQECLSSLGRCHVFNENLTPGVKCRPPSDSEGSCGYNQTSSTFLCYCKDPYSLSCSSGKSNIRWIIGGVLILILIVSGIIVSLVFLCLCCRAKIVRKKKSSDALEVPPRPIKESPTLSEDIKART
Protein: Fatty acid-binding protein, adipocyte (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (AFABP) (Fatty acid-binding protein 4) (A0A0K0MJN3)
Organism: Pygoscelis papua (Gentoo penguin)
Function: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Has the highest binding affinity for linoleic acid and decreasing relative affinity for eicosapentaenoic acid (EPA), alpha-linolenic acid (ALA), docosahexaenoic acid (DHA), oleic acid, palmitic acid and stearic acid, respectively.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P04117}.
Interaction partners:
Sequence:
MCDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA
Protein: L-arabinolactonase (EC 3.1.1.15) (Q1JUP5)
Organism: Azospirillum brasilense
Function: Catalyzes the cleavage of L-arabino-gamma-lactone to L-arabonate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Can also use D-galactono-1,4-lactone as substrate in vitro; however, the enzyme is probably not involved in the metabolism of D-galactose in vivo.
Interaction partners:
Sequence:
MQQIHPAGQATLLADTRNTLGEGATWCDRTRALYWVDIEGAQLWRCRADGSDLTPWPMPERLACFALTDDPDVLLVGLATHLAFFDLRSGAFTRIVEVEPELPTRLNDGRCDGSGAFVFGMKDEGAEPPRAVGGFYRLNADLTLERLALPPAAIANSIGFSPDGSKMYFCDSLVREIFVCDYRPGGEVANVRPFARLTDPDGDPDGSIVDRDGGLWNAQWGGRRVVRYGPDGVETDRVAVPTAQPSCTALDGEGRLYVTSARVGLSDDALADDPHAGGVFVAQTRHAGMATARFAGTPRG
Protein: K4 (F5HFL9)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDTKGILLVAVLTALLCLQSGDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKDWVKKLMQQLPVTAR
Protein: DNA repair and recombination protein rad22 (P36592)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Active in the repair of DNA damage and in mating-type switching. Probably involved in the repair of DNA double-strands breaks. Has a role in promoting S phase completion.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA repair protein rhp51
- DNA repair protein rhp54
- Replication factor A protein 1
- DNA repair protein rhp55
- DNA repair protein rhp57
- ATP-dependent DNA helicase srs2
- Crossover junction endonuclease mus81
- DNA repair and recombination protein rti1
- Exodeoxyribonuclease 1
- ATP-dependent DNA helicase II subunit 1
Sequence:
MSFEQKQHVASEDQGHFNTAYSHEEFNFLQSSLTRKLGPEYVSRRSGPGGFSVSYIESWKAIELANEIFGFNGWSSSIRSINVDFMDENKENGRISLGLSVIVRVTIKDGAYHEDIGYGSIDNCRGKASAFEKCKKEGTTDALKRALRNFGNSLGNCMYDKYYLREVGKMKPPTYHFDSGDLFRKTDPAARESFIKKQKTLNSTRTVNNQPLVNKGEQLAPRRAAELNDEQTREIEMYADEELDNIFVEDDIIAHLAVAEDTAHPAANNHHSEKAGTQINNKDKGSHNSAKPVQRSHTYPVAVPQNTSDSVGNAVTDTSPKTLFDPLKPNTGTPSPKFISARAAAAAEGVVSAPFTNNFNPRLDSPSIRKTSIIDHSKSLPVQRASVLPIIKQSSQTSPVSNNSMIRDSESIINERKENIGLIGVKRSLHDSTTSHNKSDLMRTNSDPQSAMRSRENYDATVDKKAKKG
Protein: Lipoprotein (Q9HTJ9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable outer membrane protein
- Probable Resistance-Nodulation-Cell Division
Sequence:
MLNRFRCRPCGRRTLHLKTQERDAMNRIHLALGLALALPAFAALAQETVAPATEKDGVLVDGKGMTLYTYDKDSEGQSACSGQCAKNWPPLAAAQGAQASGDWSLVAREDGTQQWAYYGKPLYTFIQDKKPGDKNGDGKMGAWHVAQPDMD