wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein 4-4 (Keratin-associated protein 4-13) (Keratin-associated protein 4.13) (Keratin-associated protein 4.4) (Ultrahigh sulfur keratin-associated protein 4.13) (Ultrahigh sulfur keratin-associated protein 4.4) (Q9BYR3)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MVNSCCGSVCSDQGCGLENCCRPSYCQTTCCRTTCCRPSCCVSSCCRPQCCQTTCCRTTCCHPSCCVSSCCRPQCCQSVCCQPTCCRPQCCQTTCCRTTCCRPSCCRPQCCQSVCCQPTCCCPSYCVSSCCRPQCCQTTCCRTTCCRPSCCVSRCYRPHCGQSLCC
Protein: Uncharacterized BCR (Q8NPY8)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- Predicted iron-dependent peroxidase
- Uncharacterized protein, homolog of Cu resistance protein CopC
- Two-component system, response regulators consisting of a CheY-like receiver domain and a HTH DNA-binding domain
- Thiol-disulfide isomerase and thioredoxins
Sequence:
MKKFFVAGAVLSSALVMAACSPANQSDSTSTSVETTSSSSTQVSDAVITTENAVVRASVEDSDMTAVFATLVNNSDDEINVSGFTADVDAASFEVHEVVDGVMQEKPGGFVIPAGESIELAPGGDHLMIMGLANPIEAGDEVTVTLELADGSEVKLDPIPARTIAAGDEDYGDLGTEGHEGH
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (E7F1U3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPLTMAKRESGSTSPVVRQIDKQFLVCSICLEHYHNPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMEVLQREQDCTRSEASSGLESAGAATYAPPLSCPNHEGKVMEFYCESCETAMCLECTEGEHREHVTVPLRDVLEQHKAALKNQLDAIRNRLPQLTAAIELVNEISKQLTDRKNEAVTEISNTFEELEKALHQRKTTLITDLENICSTKQKVLQGQLAALMQGKENIQSSCSFTEQALNHGSPTEVLLVQKQMGERMGALARHAFPEQPHENGHLDCQVETEGLRRSIQNLGVLLTTSSVGHTSVATGEGLRHAVVGQNTTVTVTTKDKDGELVKTGNAALRAQISGADGGVTETDVTDNKNGTYEIGYTLRSEGEFSFSVLLYGRHVRGSPFRLRAVKACDAPQSPDDVKRRVKSPGGGGGAGGHVRQKAVRRPSSMYSTTKKKENPIEDELIFRVGTRGRERGEFSNLQGISTTSSGRIVVADSNNQCIQVFSNDGQFKLKFGVRGRSPGQLQRPTGVAVDMNGDIIVADYDNRWLSIFSPDGKFKNKIGAGRLMGPKGVAVDKNGHIITADNKACCVFIFQSNGKLVTKFGAKGTSERQFADKSAPNTPTEPKQSKSGPAFSPHFVAINNKNEIVVTDFHNHSVKVYNADGEFLFKFGSHGEGNGQFNAPTGVAVDGNGNIIVADWGNSRIQVFDSSGSFLSYINTTADPLYGPQGLALTSDGHVAVADSGNHCFKVYRYLQ
Protein: Eye transformer, isoform B (MIP10547p) (Q9VWE1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGWRTRISRLLSLTLLATLMARALAENALHMPQANCEMQSLGGPSWRSGTIGKVSCKCDGGEGRKMSVRRQGTIESTDSYNGTVVHVDANPANEWERRYECLLDGVIQSHVCVRVYALLNLKDFVCRDVVYYLRCTFSRMENGNFENKTHYQLAMGRAKPIDCRKSEDERSRGKVECSVPIDPNSRAPEWRDFRLIMSDDLGNQSKVLRLTQAEMEVLEWPRGKHNMIQTPNQTCLEWNGPFIYPNRTFELNVQFRHSKLPNLSRNLTVSQMRAVSVFDQVCFGNPPEGNQLFYVSLSRRLHGSPWSERYPEFELTTNASLPARPPRFLANGFSHDRAKRELKVYWLPLDELEFNGAEQTYVASTRTKVATTQGSMLAIFTDWDDTQPATVSVWSSNVVGRSLESSQLEVPRLSDIRDRRIYLESYNKTSSRLSWQGPEELGNFTGYIVYWCKLSSKVHDACDDSSSIETTYARETAYNFSGIQGVIRMAVAANYSDGLTTGMRWWSGDSEVPEKPKILRYVEGTIALLVLGSLVLAIQKLRQMADIRVELPVMSEEPTANPLGDVRLFYPANVPPEKFYGTVRKTVTFAEEEPTRWPEIELQEVPRPQPVPQADAYVTNQYVSMSAIGAPCGDGYIKPPPVR
Protein: U3 small nucleolar RNA-associated protein 13 (U3 snoRNA-associated protein 13) (U three protein 13) (Q05946)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
Interaction partners:
- rRNA-processing protein FCF1
- U3 small nucleolar RNA-associated protein 16
- Ribosome biogenesis protein ENP2
- NET1-associated nuclear protein 1
- 13 kDa ribonucleoprotein-associated protein
- Periodic tryptophan protein 2
- Protein SOF1
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein MPP10
- rRNA processing protein RCL1
Sequence:
MDLKTSYKGISLNPIYAGSSAVATVSENGKILATPVLDEINIIDLTPGSRKILHKISNEDEQEITALKLTPDGQYLTYVSQAQLLKIFHLKTGKVVRSMKISSPSYILDADSTSTLLAVGGTDGSIIVVDIENGYITHSFKGHGGTISSLKFYGQLNSKIWLLASGDTNGMVKVWDLVKRKCLHTLQEHTSAVRGLDIIEVPDNDEPSLNLLSGGRDDIINLWDFNMKKKCKLLKTLPVNQQVESCGFLKDGDGKRIIYTAGGDAIFQLIDSESGSVLKRTNKPIEELFIIGVLPILSNSQMFLVLSDQTLQLINVEEDLKNDEDTIQVTSSIAGNHGIIADMRYVGPELNKLALATNSPSLRIIPVPDLSGPEASLPLDVEIYEGHEDLLNSLDATEDGLWIATASKDNTAIVWRYNENSCKFDIYAKYIGHSAAVTAVGLPNIVSKGYPEFLLTASNDLTIKKWIIPKPTASMDVQIIKVSEYTRHAHEKDINALSVSPNDSIFATASYDKTCKIWNLENGELEATLANHKRGLWDVSFCQYDKLLATSSGDKTVKIWSLDTFSVMKTLEGHTNAVQRCSFINKQKQLISCGADGLIKIWDCSSGECLKTLDGHNNRLWALSTMNDGDMIVSADADGVFQFWKDCTEQEIEEEQEKAKLQVEQEQSLQNYMSKGDWTNAFLLAMTLDHPMRLFNVLKRALGESRSRQDTEEGKIEVIFNEELDQAISILNDEQLILLMKRCRDWNTNAKTHTIAQRTIRCILMHHNIAKLSEIPGMVKIVDAIIPYTQRHFTRVDNLVEQSYILDYALVEMDKLF
Protein: S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase) (P9WGV1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Methionine synthase
- Large-conductance mechanosensitive channel
- S-methylmethionine:homocysteine methyltransferase
- Adenosylhomocysteinase
- Guanylate kinase
- Ribulose-phosphate 3-epimerase
- GMP synthase
- Phosphoglycerate kinase
Sequence:
MSEKGRLFTSESVTEGHPDKICDAISDSVLDALLAADPRSRVAVETLVTTGQVHVVGEVTTSAKEAFADITNTVRARILEIGYDSSDKGFDGATCGVNIGIGAQSPDIAQGVDTAHEARVEGAADPLDSQGAGDQGLMFGYAINATPELMPLPIALAHRLSRRLTEVRKNGVLPYLRPDGKTQVTIAYEDNVPVRLDTVVISTQHAADIDLEKTLDPDIREKVLNTVLDDLAHETLDASTVRVLVNPTGKFVLGGPMGDAGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLAERVEVQVAYAIGKAAPVGLFVETFGTETEDPVKIEKAIGEVFDLRPGAIIRDLNLLRPIYAPTAAYGHFGRTDVELPWEQLDKVDDLKRAI
Protein: PSP1 C-terminal domain-containing protein (Q38A41)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEHEIHKGMEAIVEQSGDNRASGEVNAESNVHSPASVTAKDGCEFARRRISTRGIRGSVRSPYYSPTRSSAMSPVGNGEKGDQEKEEGEGAAEPDVVPDIDVIPRYRSHPNRSQGSFSHLTYNVHSPAHSRMSSYERISWDSQAWKDVFPENAFLGDQSKDLLRLPHSSMDFYHGSPTQQCRKHVRSLATWGKVEGDGSPELLATRNSSPMRPAGCQSLVSTLDALPEPIYETAPLGHQHCFSLSSRKDAAYLKTEAGGEATAVTNEAGEQPSKGPAMTHVLVAFKSLYGVYYVPEAQWGTIGIGDLVSVESHSGENTGKVICDLTHIMSEASHMPAEMAQCPRHVLWPEDASAPLETINPKTNEEVLQRLPRVLRRGMNKGKKRLYYARRRENEALDVGNRLVRDRNFNLALTSVEYQVDFKRITVFCKGDRSHVDPSEVLIFSQQLASSLRGSIVSVVFANEIPERLDVTGSITKAAFQDIYTDALAKIKEAESAQPQRQASSSPVRQSTTAAGGPHNNMRASHIYPDPQLAAMNHTPLMPFYGVPPPFSPPVAPGAPPLMNAVGMNGLYGMTGVPPMNWGMPTPPPYIPPHLPQNVPGRM
Protein: Protein Wnt (B1WBR9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
- Frizzled-6
- Frizzled-4
- Frizzled-2
- Frizzled-3
- Receptor-like tyrosine kinase.
- Frizzled-5
- Frizzled-9
- Frizzled-1
- Frizzled-8
- Frizzled class receptor 7
Sequence:
MLVPGHWDGLRPAMPSLLLLFVAALLSSWAQLLTDANSWWSLALNPVQRPEMFIIGAQPVCSQLPGLSPGQRKLCQLYQEHMSYIGEGAKTGIRECQHQFRQRRWNCSTVDNLSVFGRVMQIGSRETAFTYAVSAAGVVNAISRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNVEYGYRFAKEFVDAREREKNFAKGSEEQGRALMNLQNNEAGRRAVYKMADVSCKCHGVSGSCSLKTCWLQLAEFRKVGDRLKEKYDSAAAMRITRQGKLELTNSRFNQPSPEDLVYVDPSPDYCLRNETTGSLGTQGRLCNKTSEGTDGCELMCCGRGYDRFKSVQVERCHCRFHWCCFVRCKKCTEIVDQYVCK
Protein: HTH-type transcriptional regulator CueR (Copper efflux regulator) (Copper export regulator) (A0A0F6AXY2)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNISDVAKKTGLTSKAIRFYEEKGLVTPPLRSENGYRTYTQKHLNELTLLRQARQVGFNLEECGELVNLFNDPRRHSADVKKRTLEKVAEIERHISELQSMRDQLLALAESCPGDDSADCPIIDNLSGCCHHKAQKPR
Protein: NADPH oxidase 4 (EC 1.6.3.1) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase) (Superoxide-generating NADPH oxidase 4) (Q9JHI8)
Organism: Mus musculus (Mouse)
Function: Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NPH5}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9NPH5}; Multi-pass membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q924V1}. Nucleus {ECO:0000250|UniProtKB:Q9NPH5}.
Interaction partners:
- Cytochrome b-245 light chain
- Neutrophil cytosol factor 1
- NADPH oxidase 1
- Neutrophil cytosol factor 2
- NADPH oxidase 2
- NADPH oxidase 3
- Toll-like receptor 4
- Neutrophil cytosol factor 4
- NAD
- Polymerase delta-interacting protein 2
Sequence:
MAVSWRSWLANEGVKHLCLLIWLSLNVLLFWKTFLLYNQGPEYYYIHQMLGLGLCLSRASASVLNLNCSLILLPMCRTVLAYLRGSQKVPSRRTRRLLDKSKTLHITCGVTICIFSGVHVAAHLVNALNFSVNYSEDFLELNAARYQNEDPRKLLFTTIPGLTGVCMVVVLFLMVTASTYAIRVSNYDIFWYTHNLFFVFYMLLLLHVSGGLLKYQTNVDTHPPGCISLNQTSSQNMSIPDYVSEHFHGSLPRGFSKLEDRYQKTLVKICLEEPKFQAHFPQTWIWISGPLCLYCAERLYRCIRSNKPVTIISVINHPSDVMELRMIKENFKARPGQYIILHCPSVSALENHPFTLTMCPTETKATFGVHFKVVGDWTERFRDLLLPPSSQDSEILPFIHSRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFQWFADLLCVLHNKFWQENRPDFVNIQLYLSQTDGIQKIIGEKYHTLNSRLFIGRPRWKLLFDEIAKCNRGKTVGVFCCGPSSISKTLHSLSNRNNSYGTKFEYNKESFS
Protein: Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)] (P47989)
Organism: Homo sapiens (Human)
Function: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).
Subcellular location: Cytoplasm {ECO:0000250}. Peroxisome {ECO:0000250}. Secreted.
Interaction partners:
- Butyrophilin subfamily 1 member A1
- Purine nucleoside phosphorylase
- Butyrophilin subfamily 2 member A2
- Guanine deaminase
- Butyrophilin subfamily 2 member A1
- Butyrophilin-like protein 9
- Thiopurine S-methyltransferase
- Erythroid membrane-associated protein
- Butyrophilin-like protein 8
- Butyrophilin-like protein 3
Sequence:
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV
Protein: Putative two-component response regulator ARR19 (Q9M9B9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Histidine-containing phosphotransfer protein
- Histidine-containing phosphotransfer protein 4
- Two-component response regulator ARR16
- Histidine-containing phosphotransfer protein 2
- Histidine-containing phosphotransfer protein 1
- Histidine-containing phosphotransfer protein 5
- Histidine containing phosphotransfer protein
- Histidine-containing phosphotransfer protein 3
- Pseudo histidine-containing phosphotransfer protein 6
Sequence:
MLVGKISGYEDNTRSLERETSEITSLLSQFPGNTNVLVVDTNFTTLLNMKQIMKQYAYQVSIETDAEKALAFLTSCKHEINIVIWDFHMPGIDGLQALKSITSKLDLPVVIMSDDNQTESVMKATFYGACDYVVKPVKEEVMANIWQHIVRKRLIFKPDVAPPKPRMTWSEVFQPVQSHLVPTDGLDRDHFDSITINGGNGIQNMEKKQGKKPRKPRMTWTEELHQKFLEAIEIIGGIEKANPKVLVECLQEMRIEGITRSNVASHLQKHRINLEENQIPQQTQGNGWATAYGTLAPSLQGSDNVNTTIPSYLMNGPATLNQIQQNQYQNGFLTMNNNQIITNPPPPLPYLDHHHQQQHQSSPQFNYLMNNEELLQASGLSATDLELTYPSLPYDPQEYLINGYNYN
Protein: TNF superfamily member 9 (Tumor necrosis factor ligand 5a) (Tumor necrosis factor ligand superfamily member 9) (Q80WE6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- TNF receptor superfamily member 9
- Tumor necrosis factor receptor superfamily member 4
- Tumor necrosis factor ligand superfamily member 4
- CD27 antigen
- Inducible T-cell costimulator
- CD40 ligand
- CD70 antigen
- T-lymphocyte activation antigen CD80
- Tumor necrosis factor receptor superfamily, member 14
- Tumor necrosis factor receptor superfamily member 8
Sequence:
MDQHALDVGGTVDAGHPPGTAQPPDAAFLRDTGLPSDAAFLVDTVRLTEAALPTDAACPAVNVRDPEAAWPPALNFCSRHPRLYCLGGLVLLLLVACVPIFIRILPQPALTITTSPDLDTGENTADQVTPVSHIGCANTTQQGFPVFAKLLAKNQASLSNTTLNWHSQEGAGSSYLSRGLRYEEDKKELVVDSPGLYYVFLELKLSPTSINTGRKVQGWVSLVLQAKPQVDHLDSLALTVELFPCSMEDKLVDRSWNRLLRLKAGHRLSVDLRAYLHGAQDAYRDWELSHANTTSFGLFLVKPDPPQG
Protein: Hydroxypyruvate isomerase (EC 5.3.1.22) (Glyoxylate-induced protein) (P30147)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). Does not catalyze the isomerization of D-fructose to D-glucose or that of D-xylulose to D-xylose. Also does not catalyze racemization of serine, alanine, glycerate or lactate.
Interaction partners:
- 2-hydroxy-3-oxopropionate reductase
- Glyoxylate carboligase
- 2-hydroxy-3-oxopropionate reductase
- Glyoxylate/hydroxypyruvate reductase A
- Glyoxylate/hydroxypyruvate reductase B
- Putative purine permease YbbY
- Glycerate 3-kinase
- 5-keto-4-deoxy-D-glucarate aldolase
- Oxamate carbamoyltransferase subunit AllF
- Allantoinase
Sequence:
MLRFSANLSMLFGEYDFLARFEKAAQCGFRGVEFMFPYDYDIEELKHVLASNKLEHTLHNLPAGDWAAGERGIACIPGREEEFRDGVAAAIRYARALGNKKINCLVGKTPAGFSSEQIHATLVENLRYAANMLMKEDILLLIEPINHFDIPGFHLTGTRQALKLIDDVGCCNLKIQYDIYHMQRMEGELTNTMTQWADKIGHLQIADNPHRGEPGTGEINYDYLFKVIENSDYNGWVGCEYKPQTTTEAGLRWMDPYR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (E7EDM2)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MTTMDLRVGNKYRIGRKIGSGSFGDIYLGTNIISGEEIAIKLESVKAKHPQLEYEARVYKSLAGGVGIPFVRWFGTECDYNAMVIDLLGPSLEDLFNFCNRKFSLKTVLLLADQLISRIEYIHAKSFIHRDIKPDNFLMGIGKRGNQVNVIDFGLAKKYRDPKTHFHIPYRENKNLTGTARYASINTHLGVEQSRRDDMESLGYVMLYFCRGTLPWQGLKAATKKQKYDRIMEKKMTTPTEVLCRGFPNEFSIYLNYTRSLRFDDKPDYSYLRKIFRDLFVRESFQYDYVFDWTVYKYQKNAAMMSDAKKDKEAEEQARRQGATMPLTTSGAAKPGAISSQRRKIMERGALDNTPDTNRAVGGSDR
Protein: Leukemia inhibitory factor (LIF) (Cholinergic neuronal differentiation factor) (P17777)
Organism: Rattus norvegicus (Rat)
Function: LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.
Subcellular location: Secreted.
Interaction partners:
- Leukemia inhibitory factor receptor
- Interleukin-6 receptor subunit beta
- Ciliary neurotrophic factor receptor subunit alpha
- Cardiotrophin-1
- Oncostatin-M
- Ciliary neurotrophic factor
- Interleukin-12 receptor subunit beta-2
- Oncostatin-M-specific receptor subunit beta
- Interleukin-11
- Fibroblast growth factor 2
Sequence:
MKVLAAGIVPLLLILHWKHGAGSPLPITPVNATCAIRHPCHGNLMNQIKSQLAQLNGSANALFISYYTAQGEPFPNNVDKLCAPNMTDFPPFHANGTEKTKLVELYRMVTYLGASLTNITWDQKNLNPTAVSLQIKLNATTDVMRGLLSSVLCRLCNKYHVGHVDVPCVPDNSSKEAFQRKKLGCQLLGTYKQVISVLAQAF
Protein: Shaven, isoform H (Q59DN9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLIMDIQTSTHHIHGLGTHELQHRILHPHILHSTQEETLNTSTGQLEHDSQHLQQHHLTHHQQQDVSPTLHNLQNTRTGDSLSTTINTNQNQHGHQHLSGSNMYTSSQMEDKSKANKYDEYSSRTLSNISDANTTPSANNFITQSQGIEWITAMNDIQNGAEDSHSSQGSISGDGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHNGVRPCDISRQLRVSHGCVSKILSRYYETGSFKAGVIGGSKPKVATPPVVDAIANYKRENPTMFAWEIRDRLLAEAICSQDNVPSVSSINRIVRNKAAEKAKHVHHHQQHHVSQSLGGGHIATESVDSSTGTIGEPQPPTSNSSANSVNTNVSASASVHASIPTSGTDSVQVSVGHINANSNETTHINSTAEQRTTGYSINGILGIQHGHHSHNNNNNSSVNNNNNTESSCKRKRIEAHDENHDTNIHSDNDDGKRQRMSTYSGDQLYTNIWSGKWCIKDDHKLLAELGNLTASTGNCPATYYEASNGFSTTPISGSGATASGNDTSMLYDSITTISQTQSSIYTPAIGPSIGSLTPLVPISMHEMKLSANSIQEQTVPPFYTALAFDGNYTSMTSLENCSSLVGQEHIVMPESSDSNTLCPISTRIVPDITETNSTRVKEPLTNSDGCSEDNNKEPEKSNSSQSSDHIASPHLHHIGEEQLRGNRRSNLNASTHPSSLIPLQPSGGSSLLNINPSENRSDVELNLSNNVGLYSTPTVLPSFNHYSAGCSSVVPGSDYAYNPAYTQYGGAYGSYGYGTGSGLINSSYYYESGQTQSPLTHDLRSPLVATRANSLASAASPGSGSACTKSESSDIFLA
Protein: Chromosome 1 open reading frame 43 (A0A1W2PQP6)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MASGSNWLSGVNVVLVMAYGSLVFVLLFIFVKRQIMRFAMKSRRGPHVPVGHNAPKDLKEEIDIRLSRVQDIKYEPQLLADDDARLLQLETQGNQSCYNYLYRMKALDAIRTSEIPFHSEGRHPRSLMGKNFRSYLLDLRNTSTPFKGVRKALIDTLLDGYETARYGTGG
Protein: Activating transcription factor 7 interacting protein (A8MV73)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSLEEPQKKVFKARKTMRVSDRQQLEAVYKVKEELLKTDVKLLNGNHENGDLDPTSPLENMDYIKDKEEVNGIEEICFDPEGSKAEWKETPCILSVNVKNKQDDDLNCEPLSPHNITPEPVSKLPAEPVSGDPAPGDLDAGDPASGVLASGDSTSGDPTSSEPSSSDAASGDATSGDAPSGDVSPGDATSGDATADDLSSGDPTSSDPIPGEPVPVEPISGDCAADDIASSEITSVDLASGAPASTDPASDDLASGDLSSSELASDDLATGELASDELTSESTFDRTFEPKSVPVCEPVPEIDNIEPSSNKDDDFLEKNGADEKLEQIQSKDSLDEKNKADNNIDANEETLETDDTTICSDRPPENEKKVEEDIITELALGEDAISSSMEIDQGEKNEDETSADLVETINENVIEDNKSENILENTDSMETDEIIPILEKLAPSEDELTCFSKTSLLPIDETNPDLEEKMESSFGSPSKQESSESLPKEAFLVLSDEEDISGEKDESEVISQNE
Protein: Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) (A0A1D8PMP1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- glycerol kinase
- Dihydroxyacetone kinase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Aqy1p
- Something about silencing protein 4 domain-containing protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Lysophosphatidic acid acyltransferase
Sequence:
MSRFLKSTLAKSVLAASAAVGGTVVYLDFIRPKNEPHLATSYKPFNKDIPPPPSRESLIGNLKKVPQFDVLVIGGGAVGTGTAVDAATRGLNVCLLEKTDFGAGTSSKSTKMAHGGVRYLEKAIFQLSRAQLDLVIEALNERGNMLRTAPHLCTVLPIMIPVYNWWQVPYFFAGCKMYDWFAGKQNLRSSTIFSTEQAAAIAPMMDTSNLKATCVYHDGSFNDTRYNVTLALTAIENGATVLNYFEVEQLLKDSNGKLYGVKAKDLETNESYEIKAKSVVNATGPFADKILEMDEDPQGLPPKVEQSPRMVVPSSGVHVVLPEYYCPTTYGLLDPSTSDGRVMFFLPWQGKVLAGTTDTPLKKVPENPVPTEEEIQDILNEMQKYLVFPIDRNDVLSAWSGIRPLVRDPSTIPKGQEASGKTEGLVRSHLLVQSPTGLVTISGGKWTTYREMAQETIDYVVKHFDFGDKKILPCQTNKLILVGGTDYSKNYSARLIHEYHIPLKLAKHLSHNYGSRAPLILDLYAESDYNKLPVTLAATEEFEPSEKKANEDNQLSYQRFDEPFSIAELKYSLKYEYPRTPLDFLARRTRLAFLNAREALSAVDGVVEIMSKEYGWDKETEEKLRKEARQYIGNMGISPKKFDVEKIVIQ
Protein: Ran GTPase-activating protein 1 (RanGAP1) (P46061)
Organism: Mus musculus (Mouse)
Function: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export. Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:26506250, PubMed:9442102, PubMed:9456312). Shuttles between nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- E3 SUMO-protein ligase RanBP2
- Ran-specific GTPase-activating protein
- Small ubiquitin-related modifier 1
- GTP-binding nuclear protein Ran
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 3
- Regulator of chromosome condensation
- Sentrin-specific protease 1
- Exportin-1
Sequence:
MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI