wanglab/gogpt-training-data huggingface dataset:
Protein: Rap guanine nucleotide exchange factor 4 (Exchange factor directly activated by cAMP 2) (Exchange protein directly activated by cAMP 2) (EPAC 2) (cAMP-regulated guanine nucleotide exchange factor II) (cAMP-GEFII) (Q9Z1C7)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2 (By similarity).
Subcellular location: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- ATP-binding cassette sub-family C member 8
- Regulating synaptic membrane exocytosis protein 2
- Protein piccolo
- Ras-related protein Rap-1A
- Adenylate cyclase type 8
- Adenylate cyclase type 6
- Adenylate cyclase type 7
- Adenylate cyclase type 1
- Adenylate cyclase type 5
Sequence:
RVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARMMVAFKEQLAELEKTVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLFKVYCIDHTDTTIRVPVAASVKEVISAVADKLGSGEGLIIVKMNSGGEKVVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTTGTVGTFELMSSKDLAYQMTTYDWELFNCVLELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKCIKIAAHCKEYKNLNSFFGIVMGLSNVAESRLALTWEKLPSKFKKFYAEFESLMDPSRNHKAYRLTAAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
Protein: Parathyroid hormone-related protein (PTH-rP) (PTHrP) [Cleaved into: Osteostatin (PTHrP[107-139])] (P17251)
Organism: Gallus gallus (Chicken)
Function: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone
- Indian hedgehog protein
- Karyopherin subunit beta 1
- Runt-related transcription factor
- Collagen alpha-1
- Collagen alpha-1
- TNF_2 domain-containing protein
- Transcription factor SOX-9
- Aggrecan core protein
Sequence:
MMFTKLFQQWSFAVFLLSYSVPSYGRSVEGISRRLKRAVSEHQLLHDKGKSIQDLRRRIFLQNLIEGVNTAEIRATSEVSPNPKPATNTKNYPVRFGSEDEGRYLTQETNKSQTYKEQPLKVSGKKKKAKPGKRKEQEKKKRRARSAWLNSGMYGSNVTESPVLDNSVTTHNHILR
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (O62602)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mitogen-activated protein kinase p38b
- Mitogen-activated protein kinase p38a
- Mitogen-activated protein kinase kinase kinase 7
- Apoptotic signal-regulating kinase 1, isoform C
- FI16976p1
- Mitogen-activated protein kinase kinase kinase 4
- Mitogen-activated protein kinase kinase kinase
- Putative mitogen-activated protein kinase 14C
- Putative mitogen-activated protein kinase kinase kinase 7-like
- Extracellular signal-regulated kinase 7
Sequence:
MSKRHRLTPFTIAKEPEAAIVPPRNLDSRATIQIGDRTFDIDADSLEKICDLGRGAYGIVDKMRHKQTDTVLAVKRIPMTVNIREQHRLVMDLDISMRSSDCPYTVHFYGAMYREGDVWICMEVMSTSLDKFYPKVFLHDLRMEESVLGKIAMSVVSALHYLHAQLKVIHRDVKPSNILINRAGQVKICDFGISGYLVDSIAKTIDAGCKPYMAPERIDPQGNPAQYDIRSDVWSLGIGMIEMATGRYPYDNWRTPFEQLRQVVEDSPPRLPEGTFSPEFEDFIAVCLQKEYMARPNYEQLLKHSFIVEHLQRNTDISEFVARILDLPDAQPAQ
Protein: Extracellular fatty acid-binding protein (Ex-FABP) (Protein Ch21) (Quiescence-specific protein) (p20K) (P21760)
Organism: Gallus gallus (Chicken)
Function: Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein D
- Uncharacterized protein.
- Ovotransferrin
- Putative glutamine amidotransferase like class 1 domain containing 3A-like1
- Ovotransferrin
- Ovotransferrin
- Ovoinhibitor
Sequence:
MRTLALSLALALLCLLHTEAAATVPDRSEVAGKWYIVALASNTDFFLREKGKMKMVMARISFLGEDELEVSYAAPSPKGCRKWETTFKKTSDDGELYYSEEAEKTVEVLDTDYKSYAVIFATRVKDGRTLHMMRLYSRSREVSPTAMAIFRKLARERNYTDEMVAVLPSQEECSVDEV
Protein: Bcl-2-modifying factor (Q91ZE9)
Organism: Mus musculus (Mouse)
Function: May play a role in apoptosis.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 2
- Bcl-2-related protein A1
- Bcl-2-like protein 1
- Dynein light chain 2, cytoplasmic
- Induced myeloid leukemia cell differentiation protein Mcl-1 homolog
- Dynein light chain
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-interacting killer
- Activator of apoptosis harakiri
Sequence:
MEPPQCVEELEDDVFQSEDGEPGTQPGGLLSADLFAQSQLDCPLSRLQLFPLTHCCGPGLRPISQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAGSPLGEQPPEGQFLQHRAEVQIARKLQCIADQFHRLHTQQHQQNRDRAWWQVFLFLQNLALNRQENREGVGPW
Protein: Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) (P24529)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30936473}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well as at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals (PubMed:17296554). {ECO:0000250|UniProtKB:P04177, ECO:0000269|PubMed:17296554}.
Interaction partners:
- Alpha-synuclein
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- Pterin-4-alpha-carbinolamine dehydratase 2
- Sepiapterin reductase
- Synaptic vesicular amine transporter
- Dihydropteridine reductase
- Aspartate aminotransferase, mitochondrial
- Tyrosinase
- Dopamine beta-hydroxylase
Sequence:
MPTPSASSPQPKGFRRAVSEQDTKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASAEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRALKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGEPIPHVEYTKEEIATWKEVYATLKGLYATHACREHLEAFQLLERYCGYREDSIPQLEDVSHFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFSDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIRRSLEGVQDELHTLTQALSAIS
Protein: Centrin-3 (O15182)
Organism: Homo sapiens (Human)
Function: Plays a fundamental role in microtubule-organizing center structure and function.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9256449}. Nucleus, nucleolus {ECO:0000303|PubMed:22307388}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic cells (PubMed:9256449). Localizes to centriole distal lumen (PubMed:26337392). Localization at the nuclear pore complex requires NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}.
Interaction partners:
- Transcription and mRNA export factor ENY2
- Germinal-center associated nuclear protein
- PCI domain-containing protein 2
- Protein SFI1 homolog
- Centrin-2
- Nuclear pore complex protein Nup153
- Nucleoprotein TPR
- Centrosomal protein POC5
- Mitotic spindle assembly checkpoint protein MAD2A
- E3 SUMO-protein ligase RanBP2
Sequence:
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
Protein: Myocardin related transcription factor A (A0A087X287)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEAIIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLEARVSEPLLSATSASPTQVVSQLPMGRDSREMLFLAEQPPLPPPPLLPPSLTNGTTIPTAKSTPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDRGAPPMDSSYAKILQQQQLFLQLQILNQQQQQHHNYQAILPAPPKSAGEALGSSGTPPVRSLSTTNSSSSSGAPGPCGLARQNSTSLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAATSILHKAGEVVVAFPAARLSTGPALVAAGLAPAEVVVATVASSGVVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDTFGEMVTSPLTQLTLQASPLQILVKEEGPRAGSCCLSPGGRAELEGRDKDQMLQEKDKQIEALTRMLRQKQQLVERLKLQLEQEKRAQQPAPAPAPLGTPVKQENSFSSCQLSQQPLGPAHPFNPSLAAPATNHIDPCAVAPGPPSVVVKQEALQPEPEPVPAPQLLLGPQGPSLIKGVAPPTLITDSTGTHLVLTVTNKNADSPGLSSGSPQQPSSQPGSPAPAPSAQMDLEHPLQPLFGTPTSLLKKEPPGYEEAMSQQPKQQENGSSSQQMDDLFDILIQSGGNPRNFSRFQGAAIPAREGEAIPEDSLWVPPGSTAITFC
Protein: Mannosylglycerate hydrolase (EC 3.2.1.-) (2-O-(6-phospho-mannosyl)-D-glycerate hydrolase) (Alpha-mannosidase mngB) (P54746)
Organism: Escherichia coli (strain K12)
Function: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-phosphate and glycerate.
Interaction partners:
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
- Alpha-galactosidase
- Mannosyl-D-glycerate transport/metabolism system repressor MngR
Sequence:
MKAVSRVHITPHMHWDREWYFTTEESRILLVNNMEEILCRLEQDNEYKYYVLDGQTAILEDYFAVKPENKDRVKKQVEAGKLIIGPWYTQTDTTIVSAESIVRNLMYGMRDCLAFGEPMKIGYLPDSFGMSGQLPHIYNGFGITRTMFWRGCSERHGTDKTEFLWQSSDGSEVTAQVLPLGYAIGKYLPADENGLRKRLDSYFDVLEKASVTKEILLPNGHDQMPLQQNIFEVMDKLREIYPQRKFVMSRFEEVFEKIEAQRDNLATLKGEFIDGKYMRVHRTIGSTRMDIKIAHARIENKIVNLLEPLATLAWTLGFEYHHGLLEKMWKEILKNHAHDSIGCCCSDKVHREIVARFELAEDMADNLIRFYMRKIADNMPQSDADKLVLFNLMPWPREEVINTTVRLRASQFNLRDDRGQPVPYFIRHAREIDPGLIDRQIVHYGNYDPFMEFDIQINQIVPSMGYRTLYIEANQPGNVIAAKSDAEGILENAFWQIALNEDGSLQLVDKDSGVRYDRVLQIEESSDDGDEYDYSPAKEEWVITAANAKPQCDIIHEAWQSRAVIRYDMAVPLNLSERSARQSTGRVGVVLVVTLSHNSRRIDVDINLDNQADDHRLRVLVPTPFNTDSVLADTQFGSLTRPVNDSAMNNWQQEGWKEAPVPVWNMLNYVALQEGRNGMAVFSEGLREFEVIGEEKKTFAITLLRGVGLLGKEDLLLRPGRPSGIKMPVPDSQLRGLLSCRLSLLSYTGTPTAAGVAQQARAWLTPVQCYNKIPWDVMKLNKAGFNVPESYSLLKMPPVGCLISALKKAEDRQEVILRLFNPAESATCDATVAFSREVISCSETMMDEHITTEENQGSNLSGPFLPGQSRTFSYRLA
Protein: Ribose-5-phosphate isomerase A (EC 5.3.1.6) (Phosphoriboisomerase A) (PRI) (O50083)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Interaction partners:
- Ribose-phosphate pyrophosphokinase
- 3-hexulose-6-phosphate synthase
- 455aa long hypothetical phospho-sugar mutase
- AMP phosphorylase
- Uncharacterized protein
- Pyridoxal 5'-phosphate synthase subunit PdxT
- Pyridoxal 5'-phosphate synthase subunit PdxS
- 315aa long hypothetical proliferating-cell nucleolar protein p120
Sequence:
MNVEEMKKIAAKEALKFIEDDMVIGLGTGSTTAYFIKLLGEKLKRGEISDIVGVPTSYQAKLLAIEHDIPIASLDQVDAIDVAVDGADEVDPNLNLIKGRGAALTMEKIIEYRAGTFIVLVDERKLVDYLCQKMPVPIEVIPQAWKAIIEELSIFNAKAELRMGVNKDGPVITDNGNFIIDAKFPRIDDPLDMEIELNTIPGVIENGIFADIADIVIVGTREGVKKLER
Protein: RNA transcription, translation and transport factor protein (Q6QI16)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- ATP-dependent RNA helicase DDX1
- RNA-splicing ligase RtcB homolog
- Protein FAM98A
- Ashwin
- Family with sequence similarity 98, member C
- Protein archease
- LSM12 homolog
- Family with sequence similarity 98, member B
Sequence:
MFRRKLTALDYHNPTGFNCKARLNQDPNTAAAARRRSARFPAPRRLSGHLLGQQDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAIDVLLLSEAFEFGARGKAEKYKDSVPDNRKNADNAAKNSEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILVQERLTQDAVAKANQMKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR
Protein: Catechol 1,2-dioxygenase (EC 1.13.11.1) (P86029)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Can cleave 4-methylcatechol at lower rates than catechol, but has no activity with 3-methylcatechol, 4-chlorocatechol, 4-carboxycatechol or hydroxyquinol.
Interaction partners:
- Pentafunctional AROM polypeptide
- Probable electron transfer flavoprotein subunit alpha
- Probable electron transfer flavoprotein subunit beta
- Oleate-induced peroxisomal protein POX18
- Oleate-induced peroxisomal protein POX18
- Cysteine dioxygenase CDG1
Sequence:
MSQAFTESVKTSLGPNATPRAKKLIASLVQHVHDFARENHLTTEDWLWGVDFINRIGQMSDSRRNEGILVCDIIGLETLVDALTNESEQSNHTSSAILGPFYLPDSPVYPNGGSIVQKAIPTDVKCFVRGKVTDTEGKPLGGAQLEVWQCNSAGFYSQQADHDGPEFNLRGTFITDDEGNYSFECLRPTSYPIPYDGPAGDLLKIMDRHPNRPSHIHWRVSHPGYHTLITQIYDAECPYTNNDSVYAVKDDIIVHFEKVDNKDKDLVGKVEYKLDYDISLATESSIQEARAAAKARQDAEIKL
Protein: At1g10580 (Transducin/WD40 repeat-like superfamily protein) (A4FVN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8A
- DExH-box ATP-dependent RNA helicase DExH12
- At1g31870
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SPF27 homolog
- CwfJ-like family protein
- At3g05070
- Peptidyl-prolyl cis-trans isomerase CYP18-2
Sequence:
MDLIQSYEEEDEAVASSPESSPPRMLKAKSSAPEVDDTALALTVANVNQSKSKPIDPTQHVVFYNPTHDQLWAPMFGPAHPYAKDGIAQGMRNHKLGSVEDASIGSFGFEEQYHTFHKCGYAADPSGMNYVGDVEAFKKNDGLSVFNIPQSEQKRRKIERSKEEREGEEKKEEIEPEAENPETEAWLRKNRKSPWSRKKEVVQGELTEEQKKYAEDHAKKKEEKGQQGETKGEHYADKSTFHGKEEKDYQGRSWIEAPKDAKANNDHCYIPKRLVHTWSGHTKGVSAIRFFPKQGHLLLSAGMDCKVKIWDVYNSGKCMRTYMGHAKAVRDICFSNDGSKFLTAGYDKNIKYWDTETGQVISTFSTGKIPYVVKLNPDDDKQNILLAGMSDKKIVQWDINTGEVTQEYDQHLGAVNTITFVDNNRRFVTSSDDKSLRVWEFGIPVVIKYISEPHMHSMPSISVHPNGNWLAAQSLDNQILIYSTRERFQLNKKKRFAGHIVAGYACQVNFSPDGRFVMSGDGEGKCWFWDWKSCKVFRTLKCHNGVCIGAEWHPLEQSKVATCGWDGLIKYWD
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase protein, putative (EC 2.3.1.51) (Q381S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Diacylglycerol kinase
- Phosphatidic acid phosphatase, putative
- Phospholipid/glycerol acyltransferase domain-containing protein
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MGANYAVRCLATVYLFLLMLIGWIGAWLLQLVVITFTYPFWTSEQRADCCALIFRIANFLSLDALNPFWKSTILRPFPNVQEKKVLVVMNHLSGADPFLMVRVLLPRDAAWVAKNDLFRVPFGGWAMANGDDLCVQFKNKKAGLETVKGTVAPMMEAARAKIHRGRMLAVFPEGARNDTPENGLKPFRPGFFTLAKEEGATIVPIAISGTDDCWPKHSFLMDVGHAYFSCGDPIATNNFNTVEELVDYVWNAVTDLRSTHPSTKENSHKDR
Protein: Interleukin (O42288)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMCKVLIFGCISVAMLMTTAYGASLSSEKWKTLQTLIKDLEILENIKNKIHLELYTPTETQECTQQTLQCYLGEVVTLKKETEDDTEIKEEFVTAIQNIEKNLKSLTGLNHTGSECKICEANNKKKFPDFLHELTNFVRYLQK
Protein: Extracellular metalloprotease 1 (EC 3.4.24.-) (C5P3X6)
Organism: Coccidioides posadasii (strain C735) (Valley fever fungus)
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Pays a pivotal role as a pathogenicity determinant during infections and contributes to the ability of the pathogen to persist within the mammalian host. Digests an immunodominant cell surface antigen (SOWgp) and prevents host recognition of endospores during the phase of development when these fungal cells are most vulnerable to phagocytic cell defenses.
Subcellular location: Secreted {ECO:0000269|PubMed:16177346}.
Interaction partners:
Sequence:
MRVSVPVLALAFGSLAAAAPNAGRRTCGSVPPPEFFEASEKVAALEESGAFADLQAPIEVETYFHVVASSRSERDGYISDQMLSDQIRVMNEDYAPHGVHFNLRETTRTINPSWASDGNEIAMKRSLRKGGYAALNVYFLKDLGGALGYCYFPTNAAPGSTTFIRDGCSVLSSSVPGGSGAPYDLGKTATHEVGHWMGLFHTFQGGCSGQGDYVSDTPPQRSPSSGCPVGRDSCPGGGVDPIHNYMDYSVDSCMNQFTRGQGTRMSSMWRQFRAGK
Protein: RNA helicase (EC 3.6.4.13) (C9J8G5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHVVVKNDPELDQQLANLDLNSEKQSGGASTASKGRYIPPHLRNREASKGFHDKDSSGWSCSKDKDAYSSFGSRDSRGKPGYFSERGSGSRGRFDDRGRSDYDGIGNRERPGFGRFERSGHSRWCDKSVEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQT
Protein: Pcf11 cleavage and polyadenylation factor subunit, isoform G (A0A0B4LFE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQLFQNYRDDERRIGEEYLSSLQDLNCNSKPLINMLTMLAEENINYAHIIVKVVEYYISQVAPEFKLPILYLIDSIVKNVKSSYVQLFGQCIVNIFLHAFESVQHSQSQVLEKVRERMYALRQTWNEVFPPSKMYALDVKVKRLDNNWPITAKQPTNKIHVNPAIHVNPDFLKPGLVPGMPGNPTITSDMEEILQAKTRELLELKKRKLELELEQTKKHLEEQERQLTQTTDAMVGAPIIMPAPTPAAICPPITDPGIAVHNQRAPGVMGNVGPVMHNMPVAPQLFANKPKVHPVNPALLNSVRQRDPRLARQMHAASSHPAAPARNDPRLEAKSSSSQKSSRSRSKSPVRNSSSRSGKSGSSSHSSSSSRKRSESKSSTTSSSSSSSDVRHKGVTASSSNQPTVKRSGKITSKDSDRYVRNGSPLGSAKRKSSSPSSSPSKSKRSTSHKSSSSRGKTSSLRSRSRSPVFMDVDLRTGVRSKSPESRAVAPSSLPLAGASLPASAKAPKDLEKRHPPAPPSPPIIDVSSMDIDLRRPKTPPPPTFDSVDSLDQKDTTSGHISSTIIQASGASNASPSGASTSKLPAKVSFKIQKQFNKLEKSTANLSTVSMLNSNPTTSGTPAASLVRQSSPSPSSSSISSQGNVSDALQLSINKLLQVQGGAGEKRPADALPPHIDGEEQPPQQKRSKSAKLDALFGSEDVDLRREILVVKPGVIVVEDDSMDECDVDKPTKKSGSPPKKATLEELRAKLANSARIQNKQGKSDKSRDQAVSQRLKQLAELKVNDDSQEAHDEKVRTILSQAQEMYENNGMNQEQYKDLVQKVVAINENSKIKESRRRDNDLERNAARDAVLRKRIPKLKGNENHSAGSPHTDGSPRYDDQPAAAPEKPSNKRDKTKREMKRRKPTKWGEQVDAGAAQRTAWQLANVNNNNNNNNNKRGGIQLPVQPQAGFRGMPWQQPPAMVLGQSAVPPPPQPPSMISMPPVPPVTMTKAINSLDNPMADVVRSITIDGGSKEIRFYNQVAIIFMDGDQPHEIGFQPGQRVIFIDHNEPLPLCFNDDYKPFHLDGQLHRIRFGFPSRELYIDEHWYEIYFGGPAVSVPIGNKLHIIKAEGPPPNVDIGRVRRDLVVGKINMIADAHTIVPLFLDARQQTFQLGAEQHSLQFVDSFQYALLDGQLQKMEYGGLPKGMMLNGGRSCFIRFGTLPKGVIAGKTHVADMVYIKTDAPAEPPKPPPIIVKPPPVVEQPKPAPVAVAPISLPAAAAALESLNINDLFQKLVSSGIIGGATAAPTLPAADSSAAKEPTASATEPSTASATVAPATLPAGPPAEPIKRIDLRKPESIKTRQAAVVAVLYLGMQCSSCGVRFPPEQTIKYSQHLDWHFRQNRRERDSTRKATSRKWYYDLNDWRQYEEIEDVEEREKNFLEAQGQPGGVEALDELSQQRSLDSPVPTCAAGRDDVDHCCDMCHEKFEQFYNEELEEWHLRSAIRVEDKIYHPLCYEDYKASLNPPTEVKSDQDVDMNNTDDNAMDTLIKVEDDEDEGTPNSSQPIFEDDDDDVIVLPNEEPSVTEIVDDDDEDEYVPGNVTRADMGNESQDKTESNSETKEPKKDQVELGEQQQNESANESDVEIQEPNIPFTDLDTYVEKEMDEATRAALLNVKIKEEPKDEYEEDEDDGFEDVGTVVSLLPLPEDEISIHSSETQTHTIGSSASPATIERPASVTSLSLPANEADELEQGDANTDTDAELNGEKQEATHNLSAVGPALPLASIVNKIKINITKNTSSNSHNSASNTTTTDSQVSAISVIGGSGAAGGASGAGDPVQQVNAIQTISTIPVLCGGNTFVPKIATSTPSNVISSISVIGSTYGASSSSNGSRSTTSTASSAPAASLLAETGSLKSPTPPLATVDPDPEPVVEQKPALRNATLKRTKKVQNGIETSGLCSIM
Protein: MARVEL domain containing 2 (Tricellulin isoform c) (A1BQX2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNDGRSRNRDRRYDEVPSDLPYQDTTIRTHPTLHDSERAVSADPLPPPPLPLQPPFGPDFYSSDTEEPAIAPDLKPVRRFVPDSWKNFFRGKKKDPEWDKPVSDIRYISDGVECSPPASPARPNHRSPLNSCKDPYGGSEGTFSSRKEADAVFPRDPYGSLDRHTQTVRTYSEKVEEYNLRYSYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDSEWYNLFGYSQPYGMGGVGGLGSIALVCLKLWRHEAARRHREYMEQQEINEPSLSSKRKMCEMATSGDRQRDSEVNFKELRTAKMKPELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDERERYKAVFQDQFSEYKELSAEVQAVLRKFDELDAVMSRLPHHSESRQEHERISRIHEEFKKKKNDPTFLEKKERCDYLKNKLSHIKQRIQEYDKVMNWDVQGYS
Protein: Glutaredoxin-8 (Glutathione-dependent oxidoreductase 8) (Q05926)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Monothiol glutaredoxin-7
- Glutaredoxin-2
- Monothiol glutaredoxin-3
- Alpha-ketoglutarate-dependent sulfonate dioxygenase
- Putative uncharacterized transporter YOL162W
- High affinity cysteine transporter
- Uncharacterized transporter YIL166C
- Putative uncharacterized transporter YOL163W
Sequence:
MSAFVTKAEEMIKSHPYFQLSASWCPDCVYANSIWNKLNVQDKVFVFDIGSLPRNEQEKWRIAFQKVVGSRNLPTIVVNGKFWGTESQLHRFEAKGTLEEELTKIGLLP
Protein: UbiA prenyltransferase domain-containing protein 1 (EC 2.5.1.-) (EC 2.5.1.39) (Transitional epithelial response protein 1) (Q9Y5Z9)
Organism: Homo sapiens (Human)
Function: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform present at high concentrations in the brain, kidney and pancreas, and is required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20953171}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:23374346}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:20505825}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:11314041}. Nucleus {ECO:0000269|PubMed:11314041, ECO:0000269|PubMed:12497587}.
Interaction partners:
- Protein dispatched homolog 3
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Acyl-coenzyme A thioesterase 13
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- F-box only protein 2
- Isopentenyl-diphosphate Delta-isomerase 1
- 2-Hydroxyacid oxidase 2
Sequence:
MAASQVLGEKINILSGETVKAGDRDPLGNDCPEQDRLPQRSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSHGVLDPRLLVGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVRFGVFLYTLGCVCAACLYYLSPLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLIILITFGPLAVMFAYAIQVGSLAIFPLVYAIPLALSTEAILHSNNTRDMESDREAGIVTLAILIGPTFSYILYNTLLFLPYLVFSILATHCTISLALPLLTIPMAFSLERQFRSQAFNKLPQRTAKLNLLLGLFYVFGIILAPAGSLPKI
Protein: Melanization protease 1 (EC 3.4.21.-) (A0A126GUP6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea. Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway.
Interaction partners:
Sequence:
MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYATQRRTVTTKQMCAGGVEGVDSCRGDSGGPLLLEDYSNGNSNYYIAGVVSYGPTPCGLKGWPGVYTRVEAYLNWIENNVRA