wanglab/gogpt-training-data huggingface dataset:
Protein: Stress-activated protein kinase JNK (EC 2.7.11.24) (E9QE29)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
Interaction partners:
- Transcription factor Jun
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- Dual specificity mitogen-activated protein kinase kinase 7
- Cellular tumor antigen p53
- Transcription factor JunD
- C-Jun-amino-terminal kinase-interacting protein 2
- Nuclear factor of activated T-cells, cytoplasmic 3 isoform X1
- Mitogen-activated protein kinase kinase kinase 1, E3 ubiquitin protein ligase.
- Protein c-Fos
Sequence:
MTEGEGQFYSVQVGDSTFTVLRRYQQLRAIGSGAQGIVCSALDTVLGVPVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIIHLLNVFTPQKSLEEFQDLYLVMELMDASLCQVIHMDLDHERMSYLLYQILCGIRHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMKYKENVDIWSVGCIMGEMVKGSVIFQGTDHIDQWNKVIEILGTPSLEFMNRLMETVRNYVMNKPQFPGVSFNELFPDWAFPSETEHDKIKTSQARDLLSKMLVIDPECRISVQEALNHPYIHVWYDPAEADAPPPQISDKQLEEREHSIEQWKELIYKEVMDWEERNKNGVLKEECLDGTVNSSATPSQSSSINDISSMSTEQTLASDTDSSCIDTLTGPLEE
Protein: Nuclear envelope morphology protein 1 (EC 3.1.3.16) (O59718)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sporulation-specific protein spo7
- Nuclear elongation and deformation protein 1
Sequence:
MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHANIMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSYSYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSGHSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSRGSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALVDSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK
Protein: Candida glabrata strain CBS138 chromosome B complete sequence (Q6FX82)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MSAVAPYLKTIASRRTIYALKPELPSGVTINDVQSTIQAIVKETPTAFNSQVNRAVILTGETHKKVWDSVANAIADPAGKKRPESVRDEAYGSVIFFTDDKTTEKLQADFPAWSAAFPQFADHASGAAQINSWAALEALGLGGHLQHYNGYVKAALPSKIPASWSVHSQLVFGAPGAAPGEKTYIDNEVEIFN
Protein: Protein HYPER-SENSITIVITY-RELATED 4 (AtHSR4) (EC 3.6.1.-) (BCS1-like protein) (Q8VZG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 13
- Ubiquinol oxidase 1a, mitochondrial
- Pentatricopeptide repeat-containing protein At2g27800
- At5g54100
- Zinc finger AN1 domain-containing stress-associated protein 12
- Calcium-binding site protein
- Transcription factor MYB15
Sequence:
MEGSKLLPCVHKSPVPTSHQLYINYEILGLTKLKKHKYTQNKMSSSDSSSAESRLATAKTVLTTAASVAATAMLARSLVQDYLPDEVHHYISYGFRSIFGYFSSQMTIIIEEFEGFAHNEVFEAAEAYLATKISPSNKRIKVSKHEKENNYNVTVERDEEVVDTYNGVKFQWILHCRHVESKHFHNPRDLNSTLRSEVRSFELNFHKKFKDVALESYLPFMVKRATLMKQEKKTLKIFTLSPENMYGNYSDAWTSVTLDHPSTFKTLAMDSDVKTSVMEDLDKFVKRRDFYKRVGKAWKRGYLLYGPPGTGKSSLIAAMANHLNFDIYDLELTAVNNNSELRRLLIATANRSILIVEDIDCSLELKDRTSDEPPRESDDIEDPRYKKVTLSGLLNFIDGLWSSCGDERIIIFTTNYKEKLDAALLRPGRMDMHIHMSYCTPSTFKALALNYLEIKEHRLFSKIEEGIEATEVTPAEVAEQLMRNDSVDKVLEGLIEFLKVKKIENEQDKAKTEKQELENKKKTKEGTDSVVKKEVDEQLVRNDRVDKVLEGLVELLKAKKIEDDQDKAKHEEVEQH
Protein: Barttin (Q8R2H3)
Organism: Rattus norvegicus (Rat)
Function: Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q8WZ55}; Multi-pass membrane protein {ECO:0000255}. Note=Mostly sorted at the basolateral membrane. A significant amount also observed intracellularly. Staining in membranes of the renal tubule and of potassium-secreting epithelia of the inner ear is basolateral (By similarity). {ECO:0000250}.
Interaction partners:
- Chloride channel protein ClC-Ka
- Chloride channel protein ClC-Kb
- Solute carrier family 12 member 1-chloride cotransporter 1)
- ATP-sensitive inward rectifier potassium channel 1
- Solute carrier family 12 member 3
- Chloride channel protein 1
- Ubiquitin carboxyl-terminal hydrolase 24
- H
Sequence:
MADEKTFRIGFIVLGLFLLSLGTFLMSHDRPQVYGTFYAMGSIMVIGGVLWSMCQCYPKITFVPADSDFQGMLSPKALSLLETGLSEVKSPQPPYVRLWEEAAYDQSLPDFTHIQMKVMGYSEDPRPLLAPELKTGTSSAKEGEPHSAQTWMEAAVVVHRELDEKEGEKSRSQSSPPACSQGSAPLASFHDDLDVGSSEGRSPQPSPPDRDEAHLQVPWASRGPLDRFGDFALIDDTPISEDMGLEGQAQEEALPSKQPWSLRMKEETVQAGAEEPEQEEEDLYYGLPDSPGDPLPDKELGFEPDVQG
Protein: Zinc finger protein 438 (Q7Z4V0)
Organism: Homo sapiens (Human)
Function: Isoform 1 acts as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:17669267}.
Interaction partners:
Sequence:
MQNSVSVPPKDEGESNIPSGTIQSRKGLQNKSQFRTIAPKIVPKVLTSRMLPCHSPSRSDQVNLGPSINSKLLGMSTQNYALMQVAGQEGTFSLVALPHVASAQPIQKPRMSLPENLKLPIPRYQPPRNSKASRKKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPELLYKPSPFEEVPSLEQAPASISTAALTNGSDHGDLRPPVTNTHGSLNPPATPASSTPEEPAKQDLTALSGKAHFVSKITSSKPSAVASEKFKEQVDLAKTMTNLSPTILGNAVQLISSVPKGKLPIPPYSRMKTMEVYKIKSDANIAGFSLPGPKADCDKIPSTTEGFNAATKVASRLPVPQVSQQSACESAFCPPTKLDLNHKTKLNSGAAKRKGRKRKVPDEILAFQGKRRKYIINKCRDGKERVKNDPQEFRDQKLGTLKKYRSIMPKPIMVIPTLASLASPTTLQSQMLGGLGQDVLLNNSLTPKYLGCKQDNSSSPKPSSVFRNGFSGIKKPWHRCHVCNHHFQFKQHLRDHMNTHTNRRPYSCRICRKSYVRPGSLSTHMKLHHGENRLKKLMCCEFCAKVFGHIRVYFGHLKEVHRVVISTEPAPSELQPGDIPKNRDMSVRGMEGSLERENKSNLEEDFLLNQADEVKLQIKCGRCQITAQSFAEIKFHLLDVHGEEIEGRLQEGTFPGSKGTQEELVQHASPDWKRHPERGKPEKVHSSSEESHACPRLKRQLHLHQNGVEMLMENEGPQSGTNKPRETCQGPECPGLHTFLLWSHSGFNCLLCAEMLGRKEDLLHHWKHQHNCEDPSKLWAILNTVSNQGVIELSSEAEK
Protein: ATP-dependent translocase ABCB1 (ATP-binding cassette sub-family B member 1) (Multidrug resistance protein 1) (EC 7.6.2.2) (P-glycoprotein 1) (Phospholipid transporter ABCB1) (EC 7.6.2.1) (CD antigen CD243) (P43245)
Organism: Rattus norvegicus (Rat)
Function: Translocates phospholipids and drugs across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08183}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000250|UniProtKB:P08183}. Cytoplasm {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane versus cytoplasm). {ECO:0000250|UniProtKB:P08183}.
Interaction partners:
Sequence:
MEFEEGLNGRADKNFSKMGKKSKKEKEKKPAVGIFGMFRYADWLDKLCMALGTLAAIIHGTLLPLLMLVFGYMTDSFTPSRDPHSDRAITNQSEINSTHTVSDTSLEEDMAMYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVNDAGELNTRLTDDVSKINDGIGDKLGMFFQSITTFSAGFIIGFISGWKLTLVILAVSPLIGLSSAMWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRVGIKKAITANISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGQVLTVFFSILLGTFSIGHLAPNIEAFANARGAAYEIFKIIDNEPSIDSFSTKGHKPDSIMGNLEFKNVYFNYPSRSEVKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHEELMKEKGIYFKLVMTQTRGNEIEPGNNAYESQSDTGASELTSEESKSPLIRRSIRRSIHRRQDQERRLSSKEDVDEDVPMVSFWQILKLNISEWPYLVVGVLCAVINGCIQPVFAIVFSKIVGVFSRDDDHETKQRNCNLFSLLFLVMGMISFVTYFFQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDHKNTTGSLTTRLASDASNVKGAMGSRLAVVTQNVANLGTGIILSLVLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKELEISGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFAFTQAMIYFSYAACFRFGAYLVARELMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIGIIEKIPEIDSYSTEGLKPNWLEGNVKFNGVKFNYPTRPNIPVLQGLSFEVKKGQTLRLVGSSGCGKSTVVQLLERFYNPMAGTVFLDGKEIKQLNVQCVRALGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIVRAAREANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCVVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVQAGAKRS
Protein: Outer envelope protein 39, chloroplastic (Q5PP51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-barrel pore-forming protein which possesses voltage-dependent channel activity. Required for proper plastid development. Involved in the maintenance of metabolic homeostasis of full-grown plants.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:25401771}.
Interaction partners:
- Mitochondrial outer membrane import complex protein METAXIN
- Mitochondrial import receptor subunit TOM40-1
- Probable mitochondrial import receptor subunit TOM40-2
- Mitochondrial import receptor subunit TOM9-2
- Mitochondrial import receptor subunit TOM9-1
- Histidine-containing phosphotransfer protein 2
- Histidine-containing phosphotransfer protein 3
- Protein TOC75-4, chloroplastic
- Protein TOC75-3, chloroplastic
Sequence:
MGAQKSIHAGRAKIDVNVDFTHKLCTSLMFPAFRDTSSPLSLVIGSLCIKHPNLFGGSEKLDVSWDKGLYDSNVLVAFRRPRPEWRPQQCFFIQHSLSPEIGVHGTPVDNFSRSGSGGVNLSKLALGLDLSEPASSKWSSTTSIKFEHVRPINDDGRAITRDLDGFPITCSGNTHDSMVVLKQESRFAKATDQGLSHFSMQIEQGIPVVSKWLIFNRFKFVASKGVRFGPAFLLASLTGGSIVGDMAPYQAFAIGGLGSVRGYGEGAVGSGRSCLVANTELALPLNKMTEGTIFLDCGTDLGSSRLVPGNPSMRQGKPGFGYGFGYGLRFKSPLGHLQVDYAINAFNQKTLYFGVTNLASST
Protein: Protein OXIDATIVE STRESS 3 (AtOXS3) (Q9LVB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes the tolerance to a range of metals, including cadmium (Cd), arsenic (As) and copper (Cu) and to oxidizing chemicals (e.g. diamide and tert-butyl hydroperoxide (t-BOOH)). May act as a chromatin remodeling factor for stress responses. Negative regulator of flowering, especially during drought stress, probably to prevent precocious flower development and subsequent low seed set. Repress the AP1 promoter in a SOC1-dependent manner.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:18980652, ECO:0000269|PubMed:31540691}. Nucleus speckle {ECO:0000269|PubMed:18980652}. Note=Observed in a subnuclear speckling pattern, discrete parts of the chromatin of the nucleosome. {ECO:0000269|PubMed:18980652}.
Interaction partners:
- At3g14430
- At4g10262
- Emb|CAB82975.1
- Rhodanese-like domain-containing protein 15, chloroplastic
Sequence:
MFKEMNLNLKQMGNMIYEDPTRIQEEEDIVQEVSTTFSDEEDNSSSCSLSSSMCSDFTEDDDDDDVSSSSSNGPLEDLSDLMSHLPIKRGLSKFYEGKSQSFTSLGNVKSLEDLMKRGFKSRNYGAKRKSSRSTGGILDQSYKRVFSPKATISKKPNRTPSSVLSCLARRRH
Protein: SD07232p (Q7YU82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLANDSATTDSEVSTPPSSRKDLADGVAEGDNDNDIDTGDTDANADEDVDAAAAIALEAEEREELQQFISELREKIESKRQLRLQNSTIELPGEEYFAKLDSNLKKNTAFVKKLKLFTATQLDGLLREISALNLSKYISEICAALVEAKLKMTDVPAVVTLASRLHCTYADFDVHFLEAWQKALNIKATEKIGNPSKLRVDLRLFAELVSSGVIQMKPGLAQLGVVLVHLIALDKDDHSNFSIILSFCRHCGEEYAGLVPQKMQQLATKYGVEVPKSDFLTADKQLNLRTMLKGYFKALCKHVLAEQAELMNMTKNIRRTMECKGEISTEKREKCELMQAGFDKLLASAQSLSELLGEPLPELAKESEGCNPGTVIDNMLDSASFGVLDPWGDEETRAFYTDLPDLRQFLPNFSAPKVDLETLEEPSELTEEAIDANLDAEMDLDDPPSTTSDTTPENPIEEQPTTPVAAAEDLKPQKMGNALMELGRQQQQQSQLNQNPIQIQNQMRQQFDGFLVNLFNCVNKELIDSAAIEFLLNFNTKHQRKKLTRTIFSVQRTRLDILPYLSRFVAIVHMCNTDVATDLAELLRKEFKWHIHKKNQLNIETKLKIVRFIGELVKFGLFKKFDALGCLKMLLRDFQHHQIEMACAFVEVTGVYLYNCRDARLLMNVFLDQMLRLKTATAMDSHRLAGSGDKLLCH
Protein: NCAM (Neural cell adhesion molecule 1a) (B3DH85)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLQIRDLIWTLLFLGYAAALQVEITPTQGEISVGESKFFLCEVVGDAKEIDWFAPNGEKLLPGRPDISISKTDESSSTLTIYNANVDHAGMYKCVAKSGEKESQGTIIVKIFQKLTFQYAPSPQEFNEGDDADIICDVISSPPPTIIWRYKKMRIQPETDVRLKVLSNNHLQIRGIKKTDEGDYTCEGRIMARGEIDLRVIKVIVNVLPSIRTRYTELNATADINQAVTLACHADGYPEPTVKWARGNTELESDEKYSLNEDGSELTIKDVNKLDEGDYKCIARNKAGERSEEVTLNVFVQPKITFLENQTASELEEQITLTCEATGDPTPNIIWSFGRRVFTENEQSLDGNVVVRSDARVSSLTLKYVQFTDAGQYLCTARNSIGQDIQSMYLEVRYAPKIQGPQAVFTWEGNPANITCEALAHPGASVLWFRDGQQLPSANTTNVKIYNTPTVSFLEVTPDSQNDFGSYNCTATNVIGTESKEFILVQADVPSAPSIERVEPYSSTAMIEFEEPASSGGVPVLKYKAEWRIAGQDWTDREYELEDGLNLITIVGLKPETTYEVKISAINGKGEGESSAPESFKTQPVREPNPPKLEAKPQSTGNEMKVHFIKQDDGGSPIKHYLVRYRAKNRQDWKPEIRMPDASDYIVLRGLDWNTEYEVYVIAENQRGRSEPGTLSFRTLPEPTAIPETSSGLGTGAIVGILIVVFILLLFGVDVTCYFLNKCGLLMCIAVNFCGKSGPSAKSKDIEEGKAAFTKDESKEPIVEVRTEEERTPNHEGGGPTEPNETTPLTDPDGKIIVDDKSKAPETEVKKPPAEVKTVPNEAPQANGNESKA
Protein: Complement factor B (EC 3.4.21.47) (C3/C5 convertase) [Cleaved into: Complement factor B Ba fragment; Complement factor B Bb fragment] (P04186)
Organism: Mus musculus (Mouse)
Function: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase.
Subcellular location: Secreted.
Interaction partners:
- Complement factor D
- Properdin
- Complement C3
- Complement factor H
- Plasma protease C1 inhibitor
- Complement C4-B
- Complement factor I
- Complement decay-accelerating factor, GPI-anchored
- Complement C5
- Mannose-binding protein A
Sequence:
MESPQLCLVLLVLGFSSGGVSATPVLEARPQVSCSLEGVEIKGGSFQLLQGGQALEYLCPSGFYPYPVQTRTCRSTGSWSDLQTRDQKIVQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAICDDGAGYCPNPGIPIGTRKVGSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQDSFMYDSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDADWVTEKLNQISYEDHKLKSGTNTKRALQAVYSMMSWAGDAPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALLDIGRDPKNPREDYLDVYVFGVGPLVDSVNINALASKKDNEHHVFKVKDMEDLENVFYQMIDETKSLSLCGMVWEHKKGNDYHKQPWQAKISVTRPLKGHETCMGAVVSEYFVLTAAHCFMVDDQKHSIKVSVGGQRRDLEIEEVLFHPKYNINGKKAEGIPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTTRALRLPQTATCKQHKEQLLPVKDVKALFVSEQGKSLTRKEVYIKNGDKKASCERDATKAQGYEKVKDASEVVTPRFLCTGGVDPYADPNTCKGDSGGPLIVHKRSRFIQVGVISWGVVDVCRDQRRQQLVPSYARDFHINLFQVLPWLKDKLKDEDLGFL
Protein: F-box/kelch-repeat protein At1g15670 (Q9LMR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box/kelch-repeat protein At4g39580
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 1
- BTB/POZ domain-containing protein At2g30600
- Probable aspartyl protease At4g16563
- U-box domain-containing protein 45
- Probable CCR4-associated factor 1 homolog 5
- U-box domain-containing protein 29
- F-box protein PP2-A14
- Kelch repeat-containing protein At3g27220
Sequence:
MELIPDLPETVAYECLLRSSYKQFPLMASVCKLWQREISLSDFFRHRKASGHSQELVVLSQARVDPVKELVSGNKTIPTPVYRISVLELGTGLRSELPPVPGHSNGLPLFCRLVSVGSDLVVLCGLDPVTWRTSDSVFVFSFLTSTWRVGKSMPGGPRSFFACASDSQRNVFVAGGHDEDKNAMMSALVYDVAEDRWAFLPDMGRERDECTAIFHAGKFHVIGGYSTEEQGQFSKTAESFDVTTWRWSPQGEEFLSSEMTMWPPICAAGENGDLYACCRRDLMMMKDDTWYKVGNLPADVCNVSYVAIRRSGNLVVIGSARYGEPSVGYNWDMSNSRWLKLETHDKYEGHVQAGCFLEI
Protein: Nuclear transcription factor Y subunit gamma (CAAT box DNA-binding protein subunit C) (Nuclear transcription factor Y subunit C) (Q6P0F1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSADSFGAGGSDAQQSLQSFWPRVMEEIRNLTVDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDDLKPPKRQEEVRQSVAPTEPVQYYFTLAQQPSAVQVQGQQQGQQVSAPTATTLQPGQIIIAQPQQGQVLQGTTMQQLQQVQVAQSQATPITSAPVTMQVGEGQQVQIVQAAAQGQAQAQTAQPAGQTMQVMQQIITNTGEIQQIPVQLNTGQLQYIRLAQPVSGTQVVQGQIQTLAANTQQLSQTEVQQGQQQFNQFTDGQQLYQIQQVTMPAGQELTQPMFIQSTNQTADGQVTTQVSAD
Protein: Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase II) (Cephalosporinase) (Metallo-beta-lactamase type II) (Metallothioprotein beta-lactamase II) (Penicillinase) (Zinc-requiring beta-lactamase II) (P04190)
Organism: Bacillus cereus
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHTLDLLK
Protein: Decapping and exoribonuclease protein Rai1 (DXO) (EC 3.1.13.-) (EC 3.6.1.-) (Dom-3 homolog Z) (Dom3Z) (NAD-capped RNA hydrolase) (DeNADding enzyme) (Q9VXA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control.
Interaction partners:
- 5'-3' exoribonuclease 2 homolog
- Ribosomal RNA-processing protein 42
- Chromo domain-containing protein rhino
- Uncharacterized protein, isoform A
- Twitchy
Sequence:
MAENAGFISVPWGQHKLGAMYNTPFPSISRPKCIGVCSINASREFVDDASCASYLAGQPWPPLPFDLNGGIEDVIRKPVENGKRDLEIMLTYIKQHQKELLRQSSSDARNLRLDSDFVTLRGILRQIMCLQYDNRSFRVKATLLNGNVYMCKEETPEQQLENANMSRAQRVMCSWGFKFEQYLTSAQAQGKPVTNVPVNEAEEFMGVYRTNLAGILMLYGAELDCVDSKEPVDFKDCRVLDSLKFVELKTSVFNMNPHQIRTFKSFKSANWWSQSFLVGITTLYVGLRDTKGMLQRIDEIDVATLARNKPWSASAMAWYLEQFLRNLKKLLVNINDPFAVVQVTFLNKHASYEVLRGPEHQILPNWYRDLLKTRS
Protein: Possible conserved protein CpsA (O06347)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible transcriptional regulatory protein
- Acyl-CoA:diacylglycerol acyltransferase
- Possible exported protein
Sequence:
MARSEGNRPRHRAVPQPSRIRKRLSRGVMTLVSVVALLMTGAGYWVAHGALGGITISQALTPEDPRSSGNNMNILLIGLDSRKDQEGNDLPWSVLKQLHAGDSDDGGYNTNTLILVHVGADGKVVAFSIPRDDWVPFTGVPGYNHIKIKEAYGLTKQYVAEQLANQGVSDRKELETRGREAARAATLRAVRSLTGVPIDYFAEINLAGFYDLAQTLGGVDVCLNHAVYDSYSGADFPAGRQRLNAAQALAFVRQRHGLDNGDLDRTHRQQAFLSSVMRELQDSGTFTNLDRLDNLMAVARKDVVLSAGWDEDLFRRMGDLAGGNVEFRTLPVVRYDNIDGQDVNIIDPTAIRAEVAAAFGSAPPTSQTAAAAKPNPSTVVDVVNAGSISGLASQVSGALLKRGYTAGQVRDRESGDPFTTAIEYGAGAETDAQNVADLLGIDAPNHPDPAVAPGHIRVTVDTNFSLPAPDEATAAATSTETSTYPLYGGGTTTDPTPDQGAPIDGGGVPCVN
Protein: Cystatin-B (Stefin-B) (Q62426)
Organism: Mus musculus (Mouse)
Function: This is an intracellular thiol proteinase inhibitor.
Subcellular location: Cytoplasm.
Interaction partners:
- Cathepsin B
Sequence:
MMCGAPSATMPATAETQEVADQVKSQLESKENQKFDVFKAISFKRQIVAGTNLFIKVDVGGDKCVHLRVFQPLPHENKPLTLSSYQTNKERHDELSYF
Protein: Putative auxin response factor 23 (Q9LP07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that binds specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Mitotic spindle checkpoint protein MAD2
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 2
- Anaphase-promoting complex subunit 6
Sequence:
MESGNVVNVQSELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGEKVYYFPQGHIELVEASTREELNELQPNCDLPSKLQCRVIAIHLKVENNSDETYVEITLMPDTTQVVIPTENENQFRPIVNSFTKVLTASDTSAQGEFSVPCKHAIECLPPLDMSQPIPAQELIAIDLHGNQWRFKHSYRVPRGDTTGWNAFTTSKKLVVGDVIVFARGETGELRVGIR
Protein: Nucleoporin nup107 (Nuclear pore protein nup107) (Q10331)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:15226438}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11309419, ECO:0000269|PubMed:15226438}.
Interaction partners:
- Nucleoporin nup132
- Protein transport protein sec13
- Nucleoporin seh1
- Nucleoporin nup189
- Nucleoporin nup131
- Nucleoporin nup85
- Probable nucleoporin C890.06
- Nucleoporin nup120
- Nucleoporin nup186
- Uncharacterized WD repeat-containing protein C4F10.18
Sequence:
MACCCYSTILTHTRLDFKTMHQNALNNATLNVLGHKKNGSSSIQELIEMDEEEAEMNQNVVCIGPNETAVSVELGDEYEKFNIITSLKKDNLFSKDGLLYAYYELCQEKFEKCLKEDDEEWIELWDLESRTWDLIQRLYSFRLSEQQGHIQSHAFSSRAVLEEEYYSQNPEAFENNIVFNWARDNSSDPPSIEIRGNRWFYTREDIKMKNRGGSRFSSNISGTIVSNLDPDADIRDDKRLDERDDNFERQFFHTAFCLFRSGSFEELLELCRRTGNHWRSASLQGILEYRDNLIDDVLQSETSGNKRKELLRRSCLALTKNKRIDSYERALYGALCGDLNSVLDVCTTWEDAMWAYYNSMTQYNLDVYLSSKAPQTETQLPPVDSGLGLTPELIFNSLSNSSIASIQEEASHPLIKLQTHIICNKISEILSSAHIQLEAIRTGNAPESGDLVTPPLLRILTHIILFLKISGLAVDEYTSDSIIQAYIELLASAKKVNLVPLYIQYLSNQVQYEAYSRFLILVDEESARSEQLQLAKKYSLDINHAALLAVEYVYDEVVSVSPEEVHTVYLKSIEEPVEPSYKKLICTLEWLLITSQTDELLRFANLVYRFFLSIGELNSAYDLYTHIPSDALNTLSSSDGEPENDSKFRDAYELMNYRALCRALKFYQEWEELSKQEVFEDSAVTKASTSYKVWKKKLNFASRKCVKSFTDLLQANWLHPSTLELKPDDDPLLYKTLMTIRNLYVPELILGLHNVYFSLEDYDSCFALANEVASEDLKLYHCLIKSGRLVEYVSYLGKAGECSLSTPNGLFSL
Protein: Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c (EC 2.7.1.49) (EC 2.7.4.7) (Hydroxymethylpyrimidine kinase) (HMP kinase) (Hydroxymethylpyrimidine phosphate kinase) (HMP-P kinase) (HMP-phosphate kinase) (HMPP kinase) (Q9USL6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable thiamine biosynthetic bifunctional enzyme
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2
- Probable acid phosphatase SPBC4.06
- Alkaline phosphatase
- Thiamine-repressible acid phosphatase pho4
- Low molecular weight phosphotyrosine protein phosphatase
- Acid phosphatase
- Thiamine-repressible acid phosphatase SPBC21H7.03c
Sequence:
MEANQSHNAKTNHPTCLTIAGSDCSGAAGIQADLKVMTAHQVYGMSVLTALTCQNSHGITGIYPLHPSLIQRQIDACLSDIQCRVVKIGMLPDPKSIPVISQALTKYKITDVVMDSVIISSMGNVMCETPTIPATIQHLFPHLLVYASNVMEAFILVEKTLKKSPPPLKSFPDIQNLMSIIHRLGPKFVVLRGHHVAFDKNMMITEKPDSKSWTADLIYDGKEFYIFEKPYNTTKSIHGESCSLTAAIASNLACNIPPLQAIHEALYSIEWAIQRVHKKSSDPYKSAQLFTALGHSSKFSGSLISLKSENYIPQADLTSVLLSHIPS