wanglab/gogpt-training-data huggingface dataset:
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase 1 (EC 1.3.1.22) (SR type 1) (Steroid 5-alpha-reductase 1) (S5AR 1) (P24008)
Organism: Rattus norvegicus (Rat)
Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Subcellular location: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Aldo-keto reductase family 1 member C18
- 17-beta-hydroxysteroid dehydrogenase type 6
- Aldo-keto reductase family 1 member D1
- Polyprenal reductase
- Estradiol 17-beta-dehydrogenase 2
- Aldo-keto reductase family 1, member C1
- Aromatase
Sequence:
MVPLMELDELCLLDMLVYLEGFMAFVSIVGLRSVGSPYGRYSPQWPGIRVPARPAWFIQELPSMAWPLYEYIRPAAARLGNLPNRVLLAMFLIHYVQRTLVFPVLIRGGKPTLLVTFVLAFLFCTFNGYVQSRYLSQFAVYAEDWVTHPCFLTGFALWLVGMVINIHSDHILRNLRKPGETGYKIPRGGLFEYVSAANYFGELVEWCGFALASWSLQGVVFALFTLSTLLTRAKQHHQWYHEKFEDYPKSRKILIPFVL
Protein: Putative transcription factor sre2 (Sterol regulatory element-binding protein 2) (O43019)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Putative transcription factor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000305|PubMed:16823372}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=May be released from membranes by a process known as regulated intramembrane proteolysis (RIP).
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- Silenced mating-type M-specific polypeptide Mi
- Rhomboid-type serine protease 2
- E3 ubiquitin-protein ligase brl2
- DSC E3 ubiquitin ligase complex subunit 2
- UBX domain-containing protein 10
- Negative regulator of ofd1
- DSC E3 ubiquitin ligase complex subunit 3
Sequence:
MCPSQHSSLKDIHRQLENTAISNPTENADPSSYVDGSNIMDFKHPSIVSSSASSSYPISHVPSVGTRGIPRSYSMASAYPYQVNSNSMDASTAFNLNQDVADKPMLARNSIDSSINTELGPLESNHWFTQAQDHSRQYSSSWDPSIDPFEVKNSLHDSTDLSITHHPHLPINHQGNTWKHANESLQSNQGPVPNTKFVGLETTQTDSYQQSSVNSVVKIEEADATYALREESGQFNTFTGAENPSISPHSLNPNFPQYTEKPALTLLQSPKQNSNYDTSNFQNSVSDSSMQFTNEGMPSPVKGIMSSDDAVAFNFSQYSTVYPQNAPENGNEFETPNKLKRTVSSPCASISSKRSYGDIAQDCSYISSKTNGGGPSDSPSSSSTSVRGSVNDSNSPISSSATFAIQSNGVEPVGLSTQEQNLSPLSKRSAHNMIEKRYRSNLNDKIAELRDAVPTLRSGYNSTTADELKGTYVPLSRKLNKATILSKATEYIKSLQSKNKKLIEENKILQKRLSEYTSVIQASLTAPSQPASLSLLGPPGNTPGHRNVPPILKRSSIGTPSQQAYFPDAPHNCHSVPQNSSYPRPPMQVNRSPIDSMQTIPHANFNEMHNAYSSRYPLKYSKSCNAVSHTSMMHPQEYGGSLPSSTVPSDYNQPQLVSPRAQADQQGLSYKNVGRAVLNGLVGLETVHMLTNPDDAGSSNRFSMSVLPISPSLHSILRFLLLLLAFLCFAMHILLTPEATLRKWASSIYLSFRLECVFISFLIFSVPIYDWGNYLNLRGKLLSELNLESGVAT
Protein: Transferrin receptor protein 2 (TfR2) (Q9UP52)
Organism: Homo sapiens (Human)
Function: Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation.
Subcellular location: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000305}. Note=Lacks the transmembrane domain. Probably intracellular.
Interaction partners:
- Hereditary hemochromatosis protein
- Hemojuvelin
- Ferroportin
- Erythropoietin receptor
- Hepcidin
- Transmembrane protease serine 6
- Transferrin receptor protein 1
- Bone morphogenetic protein 6
- Beta-2-microglobulin
- Natural resistance-associated macrophage protein 2
Sequence:
MERLWGLFQRAQQLSPRSSQTVYQRVEGPRKGHLEEEEEDGEEGAETLAHFCPMELRGPEPLGSRPRQPNLIPWAAAGRRAAPYLVLTALLIFTGAFLLGYVAFRGSCQACGDSVLVVSEDVNYEPDLDFHQGRLYWSDLQAMFLQFLGEGRLEDTIRQTSLRERVAGSAGMAALTQDIRAALSRQKLDHVWTDTHYVGLQFPDPAHPNTLHWVDEAGKVGEQLPLEDPDVYCPYSAIGNVTGELVYAHYGRPEDLQDLRARGVDPVGRLLLVRVGVISFAQKVTNAQDFGAQGVLIYPEPADFSQDPPKPSLSSQQAVYGHVHLGTGDPYTPGFPSFNQTQFPPVASSGLPSIPAQPISADIASRLLRKLKGPVAPQEWQGSLLGSPYHLGPGPRLRLVVNNHRTSTPINNIFGCIEGRSEPDHYVVIGAQRDAWGPGAAKSAVGTAILLELVRTFSSMVSNGFRPRRSLLFISWDGGDFGSVGSTEWLEGYLSVLHLKAVVYVSLDNAVLGDDKFHAKTSPLLTSLIESVLKQVDSPNHSGQTLYEQVVFTNPSWDAEVIRPLPMDSSAYSFTAFVGVPAVEFSFMEDDQAYPFLHTKEDTYENLHKVLQGRLPAVAQAVAQLAGQLLIRLSHDRLLPLDFGRYGDVVLRHIGNLNEFSGDLKARGLTLQWVYSARGDYIRAAEKLRQEIYSSEERDERLTRMYNVRIMRVEFYFLSQYVSPADSPFRHIFMGRGDHTLGALLDHLRLLRSNSSGTPGATSSTGFQESRFRRQLALLTWTLQGAANALSGDVWNIDNNF
Protein: Solute carrier family 26 member 6 (A9C3T3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Anion exchange protein.
- Sodium/hydrogen exchanger
- Solute carrier family 13
- Carbonic anhydrase
- Solute carrier family 12 member 1.
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MEEDMKELRKRVPYHIQREVLDELSVDQVAEKSDFNISVKEKLKDAVRCTGPKAKSCFLSFIPLLAWLPKYPFRENAIGDLISGISVGIMHLPQGMAYALLAAVPPVFGLYSSFYPILIYFIFGTSKHISVGTYAVMSVMIGSVTERLAPDSDFTFPGNETNSTYIDFSSRDAERVKIAATVTFLSGIFQLLLGVVRFGFVVTYLSEPLVRSYTTAAAIHVIVSQLKYSFGINPHRYSGPLSLIYTVIEICALLGKTNIGTLVVSIVTIVGLIIAKELSALAAKKIPIPIPVELITIIIATVVSWYMDLKTIYKVEVVGEIPSGLQAPVAPKVSQLGSMVGDAFALAVVGYGIAISLGRIFALKYAYKVDSNQELIALGLSNSIGGLFSCFAISCSMSRSMVQVSTGGKSQVAGAISALVILVILLKIGELFEELPKAVLAAIIYVNLQGMMKQFGDICSLWRTNKVDMVVWVMTMILTILFNPDMGLAASIAFSILTVVFRTQLPKYSILGQIPGTDIYKPVEDYNQVKEIPGITIFRSSATLYFANAEMYIDALYEKTGVDVAKLLSHKKKLQAKRLRKEKKAAKKAKKEAKKRAKEAARQAKEEPVFSDTEESEEEPELVSHSQTNGNVHELSVKEPKDMVVVEAGPYTDPDTPLPKAIILDLNPVNFLDTVGVKTLRNIYKDYGEAGVQIYLCGCQRGVVESMEKGDFFNEKVTKSILFSTVHDAVLYCQQGNNEKVMQGTHL
Protein: Deoxycytidine kinase (dCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) (P27707)
Organism: Homo sapiens (Human)
Function: Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine. Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.
Subcellular location: Nucleus {ECO:0000269|PubMed:9342341}.
Interaction partners:
- Cytidine deaminase
- Deoxycytidylate deaminase
- Cytosolic purine 5'-nucleotidase
- UMP-CMP kinase 2, mitochondrial
- Purine nucleoside phosphorylase
- Adenosine deaminase
- AMP deaminase 2
- Adenine phosphoribosyltransferase
- AMP deaminase 1
- 5'
Sequence:
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL
Protein: Probable xyloglucan 6-xylosyltransferase 3 (EC 2.4.2.39) (Putative glycosyltransferase 3) (AtGT3) (EC 2.4.-.-) (Q9LF80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable xyloglucan xylosyltransferase involved in the biosynthesis of xyloglucan.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Trihelix transcription factor GT-1
- Trihelix transcription factor GTL1
- Subtilisin-like protease SBT1.2
- Trihelix transcription factor GT-4
- Two-component response regulator ARR22-like protein
- Probable glycosyltransferase At5g11130
- Probable glycosyltransferase At3g42180
Sequence:
MGKEDGFRTQKRVSTASSAAAGVLPTTMASGGVRRPPPRGRQIQKTFNNVKMTILCGFVTILVLRGTIGINFGTSDADVVNQNIIEETNRLLAEIRSDSDPTDSNEPPDSDLDLNMTYTLGPKITNWDQKRKLWLTQNPDFPSFINGKAKVLLLTGSPPKPCDNPIGDHYLLKSVKNKIDYCRIHGIEIVYNMAHLDKELAGYWAKLPMIRRLMLSHPEIEWIWWMDSDALFTDMVFEIPLSRYENHNLVIHGYPDLLFDQKSWIALNTGSFLFRNCQWSLDLLDAWAPMGPKGPIREEAGKILTANLKGRPAFEADDQSALIYLLLSQKETWMEKVFVENQYYLHGFWEGLVDKYEEMMEKYHPGLGDERWPFITHFVGCKPCGSYADYAVERCLKSMERAFNFADNQVLKLYGFGHRGLLSPKIKRIRNETTFPLKFVDRFDIRRTTPLKIEARS
Protein: Perilipin-4 (Adipocyte protein S3-12) (O88492)
Organism: Mus musculus (Mouse)
Function: May play a role in triacylglycerol packaging into adipocytes. May function as a coat protein involved in the biogenesis of lipid droplets.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9624692}. Cytoplasm {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. Lipid droplet {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}. Note=Nascent lipid droplet surface-associated; association with lipid droplets is triacylglycerol synthesis-dependent. {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}.
Interaction partners:
- Perilipin-1
- Perilipin-2
- Lipid transferase CIDEC
- Patatin-like phospholipase domain-containing protein 2
Sequence:
MSASGDGTRVPPKSKGKTLSSFFGSLPGFSSARNLVSHTHSSTSTKDLQTATDPSGTPAPSSKVSTNSQMAGDAAGLLQPSEQTAGDKDMGSFSVTSSEDAFSGVFGIMDAAKGMVQGGLGATQSALVGTKEAVSGGVMGAVGVAKGLVKGGLDTSKNVLTNTKDTVTTGVMGAANMAKGTVQTGLDTTKSVVMGTKDTVATGLAGAVNVAKGTIQGGLDTTKSVVMGTKDTVTTGLTGAVNVAKGVVQGGLDTTKSVVMGTKDTVTTGLTGAMNVAKGTAQMGIDTSKTVLTGTKDTVCAGATGAINVAKGAAQGGLDTTKSVLIGTKDTVTTGLTGAVNVAKGAVQGGLDTTKSVVMGTKDTVTTGLTGAMNVAKGTAQMGLGTSKTVLTGTKDTVCAGLTGAINVAKGAAQGGLDTTKSVLMGTKDTVTTGLTGAVNVAKGTIQGGLDTTKSVVMGTKDTVTTGLTGAVNVAKGTIQGGLDTTKSVVMGTKDTVTTGLTGAVNVAKGAAQGGLDTTKSVVMGTKDTVTTGLTGAMNVAKGTAQMGLGTSKTVLTGTKDTVCAGLTGAINVAKGAAQGGLDTTKSVLMGTKDTVTTGLTGAVNVAKGTIQGGLDTTKSVVMGTKDTVTTGLTGAVNVAKGAVQGGLDTTKSVVMGTKDTVTTGLTGALNVAKGTAQMGIDTSKTVLIGTKDTVCAGATGAINMAKGAAQGGLDTTKSVLMGTKDTVTTGLTGAINVAKGSAQGGLDTTKSVLIGTKDTVTTGLTGALNVAKGTVQTGLDTSQRVLTGTKDNVYAGVTGAVNVAKGTIQGGLDTTKSVVMGTKDTVTTGLTGAVNVAKGAVQGGLDTTKSVVMGTKDTVTTGLTGAMNVAKGTAQMGIDTSKTVLTGTKDTVCAGLTGAINVAKGATQGGLDTTKSVLMGTKDTVTTGLTGAINVAKGAAQGGLDTTKSVLLGTKDTVTTGLTGAANVAKETVQMGLDTSKNILMDTKDSICAGATGAITVVKGAAQGGLDTSNAALTGTMDTAKGTVQTSLDTSKHMLIGMKDTVCAGVTSAMNMAKGIHKNTDTTRDTQSSVLAHSGNVATNAIHTGVHTVPSSLSGSHSIICHEPSIYRATNHGVGQAILTSTESLCCETSSFSDKYGLGHVTEPRADTKTLVSGMASSACAATRSVEECGQLAATGFAALPDELKGLGDIFQPMTTEEQAQLAVSESGPRVLSADRGSYYIRLGDLAPSFRQRAFEHALSHIQHNQFQARAALAQLQEAFQMTDMTMEAACGKLCSDQSLNTMVEAVGSHEMRASVAQDRLCTLAHQLHAAYSSLVTSLQGLPEVQQQAGQARHSLCKLYGLVSSEAGSELQTEQLAQSSAGVVEAWQGLEVLLEKLQQNPPLSWLVGPFTSMPCGQL
Protein: Chromosome transmission fidelity factor 18 (A0A0D9SF58)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHVNASARRWGRGGAAALPGPAASPRRPAPRTGPVGRPTLAPSPSRAHAHAKTNLLPGRAVQAPDAVPGAGSSRAPARWRPRDPGSSAPDAWQRFRPAPLRAQPRPPPRPAPGPPPPRKGGCGGQWRAPQDRTRGLRSRNSPRPPLAQPRLRHANQWRAPPGTPAADWRRPARSGRAVRDGGGGAGGSERELGLADGMEDYEQELCGVEDDFHNQFAAELEVLAELEGASTPSPSGVPLFTAGRPPRTFEEALARGDAASSPAPAASVGSSQGGARKRQVDADLQPAGSLPHAPRIKRPRLQVVKRLNFRSEEMEEPPPPDSSPTDITPPPSPEDLAELWGHGFSEAAADVGLTRASPAARNPVLRRPPILEDYVHVTSTEGVRAYLVLRADPMAPGVQGSLLHVPWRGGGQLDLLGVSLASLKKQVDGERRERLLQEAQKLSDTLHRSGEEEAAQPLGAPEEEPTDGQDASSHCLWVDEFAPRHYTELLSDDFTNRCLLKWLKLWDLVVFGHERPSRKPRPSVEPARVSKEATAPGKWKSHEQVLEEMLEAGLDPSQRPKQKVALLCGPPGLGKTTLAHVIARHAGYSVVEMNASDDRSPEVFRTRIEAATQMESVLGAGGKPNCLVIDEIDGAPVAAINVLLSILNRKGPQEVGPQGPAVPSGGGRRRRAEGGLLMRPIICICNDQFAPSLRQLKQQAFLLHFPPTLPSRLVQRLQEGMRADPGVLAALCEKTDNDIRACINTLQFLYSRGQRELSVRDVQATRVGLKDQRRGLFSVWQEVFQLPRAQRSSQHVSVLTCHGTPGDAGLVVLQDMGDAGLGLWDVLLLAWTRRGTFPGRFYRVLHAAASAGEHEKVVQGLFDNFLRLRLRDSSLGAVCVALDWLAFDDLLAGAAHHSQSFQLLRYPPFLPVAFHVLFASSHTPRITFPSSQQEAQNRMSQMRNLIQTLVSGIAPATRSRATPQALLLDALCLLLDILAPKLRPVSTQLYSTREKQQLASLVGTMLAYSLTYRQERTPDGQYIYRLEPNVEELCRFPELPARKPLTYQTKQLIAREIEVEKMRRAEASARVENSPQVDGSPPGLEGLLGGIGEKGVHRPAPRNHEQRLEHIMRRAAREEQPEKDFFGRVVVRSTAVPSAGDTAPEQDSVERRMGTAVGRSEVWFRFNEGVSNAVRRSLYIRDLL
Protein: Early estrogen-induced gene 1 protein (EEIG1) (Q5T9C2)
Organism: Homo sapiens (Human)
Function: May play a role in estrogen action.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q78T81}. Cytoplasm {ECO:0000250|UniProtKB:Q78T81}. Membrane raft {ECO:0000250|UniProtKB:Q78T81}.
Interaction partners:
Sequence:
MAFLMKKKKFKFQTTFTLEELTAVPFVNGVLFCKVRLLDGGDFVSLSSREEVQENCVRWRKRFTFVCKMSANPATGLLDPCVFRVSVRKELKGGKAYSKLGFADLNLAEFAGSGSTVRCCLLEGYDTKNTRQDNSILKVTIGMFLLSGDPCFKTPPSTAKSISIPGQDSSLQLTCKGGGTSSGGSSTNSLTGSRPPKARPTILSSGLPEEPDQNLSSPEEVFHSGHSRNSSYASQQSKISGYSTEHSRSSSLSDLTHRRNTSTSSSASGGLGMTVEGPEGSEREHRPPEKPPRPPRPLHLSDRSFRRKKDSVESHPTWVDDTRIDADAIVEKIVQSQDFTDGSNTEDSNLRLFVSRDGSATLSGIQLATRVSSGVYEPVVIESH
Protein: TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II) (P38438)
Organism: Rattus norvegicus (Rat)
Function: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P37173}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P37173}. Membrane raft {ECO:0000250|UniProtKB:P37173}.
Interaction partners:
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-2 proprotein
- TGF-beta receptor type-1
- Receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 7
- Activin receptor type-1-like
- E3 ubiquitin-protein ligase
Sequence:
MGRGLLRGLWPLHIVLWTRIASTIPPHVPKSVNSDLMAGDNSGAVKLPQLCKFCDVTLSTCDNQKSCMSNCSVTSICEKPQEVCVAVWRKNDKNITLETVCHDPKFTYHGFTLEDATSPTCVMKEKKRAGETFFMCSCNTEECNDYIIFNEEYTTSSPDLLLVIIQVTGVSLLPPLGIAIAVIAIFYCYRVHRQQKLSPSWESSKPRKLMDFSDNCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYSSWKTEKDIFSDINLKHENILQFLTAEERKTEMGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENMESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQIVCETLTECWDHDPEARLTAQCVAERFSELEHPDRLSGRSCSQEKIPEDGSLNTTK
Protein: GM08392p (Q9VGL2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPEYMLCRICLTEDINSEAMAPLFDDNDAQCRELVRKIEEVGSIKLVPLQNIPSMLCYSCVERLTSAHKFRELCQESERTFATNVVKAEMKSEPTDEVPHVVADNIEYIYESANDFIDGVEDDIGMENIMEEPLEDGVGETSQAYETSTVVDDLDEDDLLVPNSTDSDYQPIERCRKAKVRKTRMTKRGRGRPRGASSGHPRSFSEERPPVQASFKSSPEVSSTNIMCEICGNIYSKRAALNIHMRRHMAEKPFKCEICSKSFAGPSELNRHIRVHTGEKPFLCKYCNRSFADRSSNIRHERTHTNERPFTCSTCGKAFSYSNVLKNHMLTHTGEKPFLCRVCNKTFSRKHQLDQHLGTMTHQQTVIHHKNERTGRY
Protein: Cyclin-dependent kinase 11.2 (EC 2.7.11.22) (Q23357)
Organism: Caenorhabditis elegans
Function: Probable cyclin-dependent kinase whose activity is most likely regulated by the cyclin cyl-1/Cylin-L. Acts partially redundantly with cdk-11.1 to ensure embryonic viability. In contrast to cdk-11.1, not essential for male and female fertility.
Subcellular location: Nucleus {ECO:0000269|PubMed:29886128}. Cytoplasm {ECO:0000269|PubMed:29886128}. Note=Evenly distributed between the cytoplasm and nucleus in embryos, but becomes more enriched in the nucleus from the 4- and 6-cell stage as embryos develop (PubMed:29886128). In the germline, localizes to the nucleus and cytoplasm in the mitotic region, but is enriched in the cytoplasm (PubMed:29886128). Nuclear localization increases as cells enter late pachytene, and then the distribution between the cytoplasm and nucleus becomes more even as oocytes mature (PubMed:29886128). {ECO:0000269|PubMed:29886128}.
Interaction partners:
- Cyclin L homolog cyl-1
Sequence:
MSNYSTNGSRKIRISNSDDDSRETRFSIQPRNSHKTKEERYRDKEKERDHERHHDRERRDDRYRKVDSRDHRDRNRRSPAGSRTYCRDEPDRRRNNHSDRNRRDRSSERDRDNRSSKSKTKSPDSLRSKSSRKSQTPNHLPDDGKLFDRILDPNYKKKEKTVMEVEDVEMSPVEMLDEEEVSTFTFDDACGPVRPSNEPEEKDYKSEGDPESRPATPKTPLTPDYLENTIVSLNETLSDDEDKGPDDKYGKTPDKEQWESMTENEQKLHRDAMKKRREQRHREAVSKLPVYYPGLRGCQHISEYVILNVIAEGTYGEVFRGKNTRTDEVVALKRFKMEKEKEGFPITALREINMLLKAGAHENIVNVKEILVGSTKTEVYMAMEYVEHDVKSLIDKMRSRNQRFKTGQQKTLMSQLLSGIEHMHKLWILHRDLKTSNLLISHSGILKIADFGLAREYGEARDIEKRMKLTPIVVTLWYRSPELLLEPKTYSTPVDMWSIGCIMAEFIMMKPMFQGDSEPNQVHQIFQMMGTPTEQIWPDIKELKVWNMVEFPPVKPGQLRRIFKGEKLVNETGFDLLNGMLCLNPANRLTASEALQHDWFSEHPKAVPPEDLPVYPAKSELNAAPPENRRKNRLEALLADEEPERAALLRQFNVKAEQLKPSGFQLRG
Protein: Large ribosomal subunit protein mL37 (39S ribosomal protein L37, mitochondrial) (S4R369)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MALASGPARRALAGSGQLGLGGFGAPRRGAYEWGVRSTRKSEPPPLDRVYEIPGLEPITFAGKMHFVPWLARPIFPPWDRGYKDPRFYRSPPLHEHPLYKDQACYIFHHRCRLLEGVKQALWLTKTKLIEGLPEKVLSLVDDPRNHIENQDECVLNVISHARLWQTTEEIPKRETYCPVIVDNLIQLCKSQILKHPSLARRICVQNSTFSATWNRESLLLQVRGSGGARLSTKDPLPTIASREEIEATKNHVLETFYPISPIIDLHECNIYDVKNDTGFQEGYPYPYPHTLYLLDKANLRPHRLQPDQLRAKMILFAFGSALAQARLLYGNDAKVLEQPVVVQSVGTDGRVFHFLVFQLNTTDLDCNEGVKNLAWVDSDQLLYQHFWCLPVIKKRVVVKNKRHSSGPKCVCKTRNGKWLLDGPQIFKVRWIPSLPTHLPPRPSRLHKNTEFAGPGKEGRRLKHKTSCYAPGTKTVPKKSPCIL
Protein: Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I) (Q57179)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Interaction partners:
- Acetolactate synthase large subunit
- Acetolactate synthase small subunit
- Dihydroxy-acid dehydratase
- branched-chain-amino-acid transaminase
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase
- 3-isopropylmalate dehydratase small subunit
- L-threonine dehydratase biosynthetic IlvA
- Diaminopimelate decarboxylase
Sequence:
MAIELLYDADADLSLIQGRKVAIVGYGSQGHAHSQNLRDSGVEVVIGLREGSKSAEKAKEAGFEVKTTAEAAAWADVIMLLAPDTSQAEIFTNDIEPNLNAGDALLFGHGLNIHFDLIKPADDIIVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPTGTAQALTLSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLTEAGYEPEMAYFEVLHELKLIVDLMFEGGISNMNYSVSDTAEFGGYLSGPRVIDADTKSRMKDILTDIQDGTFTKRLIANVENGNTELEGLRASYNNHPIEETGAKLRDLMSWVKVDARAETA
Protein: Leucine-rich repeat-containing protein 56 (Q8IYG6)
Organism: Homo sapiens (Human)
Function: Required for the assembly of dynein arms.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q387Y5}.
Interaction partners:
Sequence:
MDLGWDRSRGPRRSTSSVRVRELSWQGLHNPCPQSKGPGSQRDRLGEQLVEEYLSPARLQALARVDDLRLVRTLEMCVDTREGSLGNFGVHLPNLDQLKLNGSHLGSLRDLGTSLGHLQVLWLARCGLADLDGIASLPALKELYASYNNISDLSPLCLLEQLEVLDLEGNSVEDLGQVRYLQLCPRLAMLTLEGNLVCLQPAPGPTNKVPRGYNYRAEVRKLIPQLQVLDEVPAAHTGPPAPPRLSQDWLAVKEAIKKGNGLPPLDCPRGAPIRRLDPELSLPETQSRASRPWPFSLLVRGGPLPEGLLSEDLAPEDNTSSLTHGAGQVLCGNPTKGLRERRHQCQAREPPEQLPQHRPGDPAASTSTPEPDPADSSDFLALAGLRAWREHGVRPLPYRHPESQQEGAVAPWGPRRVPEEQVHQAEPKTPSSPPSLASEPSGTSSQHLVPSPPKHPRPRDSGSSSPRWSTDLQSRGRRLRVLGSWGPGLGDGVAAVPVLRALEVASRLSPRAQGCPGPKPAPDAAARPPRAAELSHPSPVPT
Protein: DNA replication complex GINS protein SLD5 (Q582Q4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- Uncharacterized protein
- DNA replication licensing factor MCM3
- Cell division cycle 45
- GINS subunit domain-containing protein
- DNA helicase
- Uncharacterized protein
- GINS subunit domain-containing protein
- DNA polymerase epsilon catalytic subunit
Sequence:
MSFSHFVPPISRRRMFFEDQLDEALSREGSPRLSTSNTVGGADLVAAGAANDETFPFPSHAAPGHLLKSLIQATENERCAPDILPYPEAIVDSVVAQIVAQNEQIRLLGTDERQKAAGSDSGVSLLPFKPSDIMALEVQRAQFFLCELLRCRLRKIEALALTINYESQSGAEAHTQLREHLSHNEIVVADRLAELISKCVRQAGLQSAPSELQQLVPNAPYAEGNEVLPIPDIDHYVFCVVLDDLGVVRLGDDAEQTVHAGEVFIVPYRTFRPYILEGRVRLV
Protein: Ectoine dioxygenase (EC 1.14.11.55) (Ectoine hydroxylase) (Q2TDY4)
Organism: Virgibacillus salexigens (Salibacillus salexigens)
Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
Interaction partners:
Sequence:
MEDLYPSRQNNQPKILKRKDPVIYTDRSKDNQAPITKEQLDSYEKNGFLQIKNFFSEDEVIDMQKAIFELQDSIKDVASDKVIREPESNDIRSIFHVHQDDNYFQDVANDKRILDIVRHLLGSDVYVHQSRINYKPGFKGKEFDWHSDFETWHVEDGMPRMRAISVSIALSDNYSFNGPLMLIPGSHNYFVSCVGETPDNNYKESLKKQKLGVPDEESLRELTRIGGGISVPTGKAGSVTLFESNTMHGSTSNITPYPRNNLFMVYNSVKNRLVEPFSGGEKRPEYIAVREKQPVYSAVN
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 (Complex I-MWFE) (CI-MWFE) (NADH-ubiquinone oxidoreductase MWFE subunit) (O15239)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
Sequence:
MWFEILPGLSVMGVCLLIPGLATAYIHRFTNGGKEKRVAHFGYHWSLMERDRRISGVDRYYVSKGLENID
Protein: PLAC8 protein (Q96EJ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQAQAPVVVVTQPGVGPGPAPQNSNWQTGMCDCFSDCGVCLCGTFCFPCLGCQVAADMNECCLCGTGVAMRTLYRTRYGIPGSICDDYMATLCCPHCTLCQIKPSDYRRRAMRTF