wanglab/gogpt-training-data huggingface dataset:
Protein: Hepatocyte nuclear factor 1-beta (HNF-1-beta) (HNF-1B) (Homeoprotein LFB3) (Transcription factor 2) (TCF-2) (Variant hepatic nuclear factor 1) (vHNF1) (P35680)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3'. Binds to the FPC element in the cAMP regulatory unit of the PLAU gene (By similarity). Transcriptional activity is increased by coactivator PCBD1.
Subcellular location: Nucleus.
Interaction partners:
- Hepatocyte nuclear factor 1-alpha
- Hepatocyte nuclear factor 6
- Pterin-4-alpha-carbinolamine dehydratase
- Pancreas transcription factor 1 subunit alpha
- Fibrocystin
- Hepatocyte nuclear factor 4-alpha
- Uromodulin
- Pancreas/duodenum homeobox protein 1
- Neurogenic differentiation factor 1
- Hexokinase-4
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQTVQSSGNMTDKSSQDQLLFLFPEFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHSLNPLLSHGSPHHQPSSSPPNKLSGVRYSQQGNNEITSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHNLLSPDGKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQSLNTSQAQSVPVINSVAGSLAALQPVQFSQQLHSPHQQPLMQQSPGSHMAQQPFMAAVTQLQNSHMYAHKQEPPQYSHTSRFPSAMVVTDTSSISTLTNMSSSKQCPLQAW
Protein: Axin-related protein (xARP) (Q9PTP2)
Organism: Xenopus laevis (African clawed frog)
Function: Regulates the wnt signaling pathway by interacting with dvl2/dsh, which displaces gsk3b from the axnr-gsk3b complex and thus prevents degradation of ctnnb1/beta-catenin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10688669}. Cytoplasmic vesicle {ECO:0000269|PubMed:10688669}.
Interaction partners:
Sequence:
MSSAGVLTCIPDSGPIFRETSLRPPVPGQETNNFKPEKFTMDSQHLKHKEDFNREAEGCVAHDSRFSRWGRSLNLLLDDQDGATLFRMYLEGEGLGDLLTFWFACNGFRAMDPLEPKTSKTAKAIYRWYVQNSSAVSGRLKPTTRTQVKECVKNHQLNKTVFDQAQQEIQRAMEQEAFTSFLQSDICKEYARGVEDSPTPESPGPGLPTLTEDEEFGGLHHFSSGMGKINRAFSRIPPRNQRSHFRKLEQTYQYFAPAASINDSEISSDALTEDSMSMTDGSVDGIPPYRSKKQREIHRSVSANGKVSLPFVPRTMRPPAEMMPTSPAEFAAKLTIALEKVKKQRDAEEKLEEKLQRLKEEEEIADYDIPSSSHETVPGAALEDDPQSILDDHVSRVLKTPANLSPRSQSPFVQRKGKFQPAFSKGQTSTSCHLRPKVPQGMEATSTLASELRSSVSSQLPRSSRKPEGCTQPHRPEEGTSAAVLTTPLSPEQEAERNHSVLQWVLDSAKLMKKHHRETASVTPCPELKKATHRAASQPAHLFLQDTSMPPLTAPNTLDQLEEARRRLVEDKRVPKLHKSRCVQSTTLKEKGKTAESVPSSGFSTLKLSEEQKTAKKPSSECPGQGLAIVYYFCGERIPYMIRTKEPSLTLQEFKELLSKKGSNKYYFKKESHEFECNAVFQEVSEEDAVLPLFEEKIICKVERAC
Protein: Centrosomal protein of 55 kDa (Centrosomal protein 55-like) (Q502I3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in mitotic exit and cytokinesis. Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis. Not required for microtubule nucleation (By similarity). Plays a role in the development of the brain and kidney.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q53EZ4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q53EZ4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53EZ4}. Cleavage furrow {ECO:0000250|UniProtKB:Q53EZ4}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q53EZ4}.
Interaction partners:
- Discs, large
- Kinesin family member 11
- Kinesin-like protein
- Kinetochore protein Nuf2
- Tumor susceptibility 101a.
- Dual specificity protein kinase Ttk
- Borealin
- Programmed cell death 6-interacting protein
- Maternal embryonic leucine zipper kinase
- Lymphokine-activated killer T-cell-originated protein kinase homolog
Sequence:
MAAKGAKETLVNKLGFKSSSSSSKSAELEVEKLKRENQQMKKSLEDMKRAGRHQHTHPDTDKARLLERILALETLREKNNQQLLGREQEITTLRQQLRSAHGEVVSSLQSQLENKQHEAEQRERQYQALVKETEDLKNKYCAVSERCDTLEKQKGSSGELAVVQEQLRDALEKNQHWLVYDQQREAYVQGVLARIKDLEAQLNEANQALQQQHKEAKSDDQSAQKVQQELEAERNKVSRMQMEVEDLQVRYEEKSREAAQAREQLLEERRREREDRKSSVERDALLQDQHRKREAELIMQVNLLQKSLMNQKEEQKRMAILEQQIQLSAKESENEKLDRQTLQHQLHKVLKELRKARDQITRLESSKQQRESRFSEPSSYNRMDLERLTIQDHMTSPSKVHNILDESVLECPNCGASYPTSQHRELLAHLDYCFT
Protein: Uncharacterized protein C13G7.09c (Q10273)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MESSLDRLNFDEFVAKLLIHESKKKNKSFVDHGYIEKEKTKLRPNKVFLNNMVRNVQSHNRGINNRRRDQKRKQLISIKQDNDLNVSSERLSRRIDVPRPTSKKKRLYKETPDLDEPGSREKRVSQKGQLKIEKV
Protein: Uncharacterized protein (Q38ET1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- 30S Ribosomal protein S17, putative
- Mitochondrial ribosomal protein S18
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
Sequence:
MSVSGVFSKGRGIGHEAATSILRYIPRARVPWQPSRFGRENLTAADMARLWSRGRYRDGPGNYNSGYCTERTHVLEENTVSIIPRRELEKYMPDITIGPKALVTPVSLMNARNGHRVTHDLLHSYDPHIGRLGKPAVVDHDNITVEDPNRVGLNAATLDCRGRIYRWLRRGPFFQVDNYFRRSVKLNRDGTLPTDFVHEAPLMRKIIRLAHRGHLKAACEEYRRVTTVPPVEVYRALTACCVPGAKLADAVSIFEDGNSKLFYVSRDGEVLHNLMRCAIAARHRARIMWVYNVMRGRFYENVVVRAEVDLIWRYRIAMIALEYLLDHECAEEAAAIYSYLVEEELLRCDVHVRVGLHMREAIAAGKPITLNDDVMNATSLVRDATAVAPEVARELQRRHAQTLQNSAVEAVGAENVREGSAPWSILGPLTAIGPTAEDTMVWLQQHYGDVDVMSIMRWARFRKGKDLMAKDRPQYLARAAAWIELLSKRNREMEEVPLTYMRKSKPLVLGTNSNVRVAWQTPLMRSGGPPRLLAREEGYVFHHSNSSRFVEETYRHPGESLQSRYLALQPLHTEVSVKEDFQRLYYQAQKHHKQQERLLPVSTAAIPSRIVHHSVMSALHGVSGKGEPANRSLFTGNRSNDSHSNTGVASGTSACTDGAGSATPEF
Protein: X11Lbeta, isoform E (X2JB44)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVSTTLTTLAAGQTTSSSNHHHHHHHSHQQQQQQQQQDQSQQQPHQQLPYQQRGYYALNGSLELDCDTSNTNSSSSSNNIGYQQHQQQQQQQQQPPLILSQALLSPSPPLNDQISLLFPKCRPKQQQQQQQQQQQQQQQQQQQLQPAQQHQQHVHPTDVNSSCNSNRSSSPTTAGAVGEPLASVSVSPPPPKATPTSSTPSYYKSVNIITQSPPPHSASSHSSESLSSVTPRISTNPFLCAPLTPPTPPHHHHHHHHQQQHQQKQQQPKQQHQTQQQEQQEEDTTGESVVEHSRSGAAGEVLEYPASFYYHTVGDSRRGPGSYTEMPRKRSSALPASNRQQQLHNGNGSQNPFIKENYWEAPPTRASLLLHSPTEYSEEPQQQQQIQQQQQQQQQQQQQQQQQQQQHLHASARRAYHQQREQVYGINQRPQQQQQQNILRVGRSPVNRSFPQQHQQQQQQQQQQQQQQQQQQQPHQQIPTARSNPCADGLTPLASHYLYGSKSSLDQHPGDWEPREQRKLRLREEREREREREREREREREREHLLLEQQQQLQLQEVQVARDNHLSHLAGQQQQQQQRKRHVYGEERERERDRERDMDRDHRLVNGNADPNESWQHLRVTTETLAEEGGKHGKPADKAQHQMHNTNQSQNSDVNVYREHQLDAWKLERSYTLAVESRHGIIEYEGSPRRIGVTTTSNLGATGAAAASAAADESEPPAAAEGAAAATATSQPQQQVPMATVPPLSSTATSLQKTAARAALAALAQSHPHSSHNILSTLLPHSPNPVNPGQMHAAQQSIQNYPVRPGFPQRIISPPSRDPRSSSPPLQQQQYQQQQQQQLQHQQQHFASLMSSHSNNNSNTNKQPLSSDNNAEDTSNDVSEIGTISDLTTPEAVGLSIGIAAGEMASRASTPPQTAQAPPTAVAGSTANGTGSGNGTATGNATAAGSGLGPLSLHTKSSTFDYLYEFSETRKVLEEFFKCPSTDEQPIMENGSDVDSIYEFHSNFERDEEDLAEEEEAEDDEEVDDDADEENDEAEDEDEPLEQDRDQNYRAQAPPQSGHIDSERLVYSGYGQQPQLQAQLTAQPMSGARRHYSGSPLMRDFDFFLDSTSRSSGERDADQDGLNHNQLLSTSSGHGGGVGVSGGLGVGPGGGHNYRYSPETTDYDSNCGDLDSLSGEMNGGVSTSCSNYAKFYASAMPVLEDGLSSGHTSDTENNNNNQKNLQQSTVNQGGQCPTSLSGSTSIGGSGGISMLMDMKRISTNHSLNSMNNQTTTASTTTDSNGGVGGVGHHLVATLVASPNNEQAKSQCQTQLQSHPPKTLSLDQSPSNHSKVFKNIDPELDSLYSIGVFHRPDTVQMTPPPPAPAPHRKPNNNGCSSGVVNTNGSLAGGSNDVDLLQPSSKHTPLAAAISSTLQRSSPTSTITGNGIGNGSGKTRSAGSNCSSSANGGMPPPIPERTNLVSAVQRSPSPGPNSPVWLSRHLDGGAGKDLLESGSDNHSKNHSADEEDVDTDLETDRLLGHQRLDDQGYYDENKSWDRKPRSLLSKISPKQQIPSTKTRNGYNALLSSTPELPPPIPPKGQSGLGLGLTLGAGNGGKLLDLVGGMVQRSLSRSSSEHSEKSLSKMPISGGDLCAGGVDVVASTVAATSATVVASTPALGSPGNGGGSERSAAEMANPGGAVKLSEQEIGTINGGSVMPLGSGSGTGSGAGSGAGSGTGTNAAVVANSNANNNVGGGGGGGNNSSGSGAGSNSNSGEKKVKKSGAVLIEGVLFRAKYLGSTQLVCEGQPTKSTRMMQAEEAVSRIKAPDGDVQPSTEVDLFISTEKIMVLNTDLKEIMMDHALRTISYIADIGDLVVLMARRRFVPQDIDDAPKPNRTPKMICHVFESDEAQFIAQSIGQAFQVAYMEFLKANGIEDHRFVKEMDYQEVLNSQEIFGDELEIFAKKELQKEVVVPKAKGEILGVVIVESGWGSMLPTVVIANLMSSGAAARCGQLNIGDQLIAINGLSLVGLPLSTCQTYIKNTKNQTVVKFTVVPCAPVVEVKIKRPETKYQLGFSVQNGVICSLLRGGIAERGGVRVGHRIIEINNQSVVAVPHEKIVNLLATSVGEILMKTMPTSMFRLLTGQENPIYI
Protein: Thiamine biosynthetic bifunctional enzyme [Includes: Thiamine-phosphate synthase (TP synthase) (TPS) (EC 2.5.1.3) (Thiamine-phosphate pyrophosphorylase) (TMP pyrophosphorylase) (TMP-PPase); Hydroxyethylthiazole kinase (EC 2.7.1.50) (4-methyl-5-beta-hydroxyethylthiazole kinase) (TH kinase) (THZ kinase)] (P41835)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for thiamine biosynthesis. The kinase activity is involved in the salvage synthesis of TH-P from the thiazole.
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Constitutive acid phosphatase
- Thiamine thiazole synthase
- Thiamine biosynthesis protein THI22
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5
- Repressible alkaline phosphatase
- Probable acid phosphatase DIA3
- Repressible acid phosphatase
- Acid phosphatase PHO11
Sequence:
MVFTKEEVDYSLYLVTDSTMLPPGTTLCSQVEAGLKNGVTLVQIREKDIETKNFVAEALEVQKICKKYNVPLIINDRIDVAMAIDADGVHVGQDDMPIPMVRKLLGPSKILGWSVGKPSEVETLAKWGPDMVDYIGVGTLFPTSTKKNPKKSPMGPQGAIAILDALEEFKATWCRTVGIGGLHPDNIQRVLCQCVASNGKRSLDGISLVSDIMAAPDACAATKRLRGLLDATRYQFVECELNNTFPTTTSIQNVISQVSNNRPLVQHITNKVHQNFGANVTLALGSSPIMSEIESEVSELARIPNASLLLNTGSVAPIEMLKAAINAYNEVNRPITFDPVGYSATETRLCLNNTLLTYGQFACIKGNCSEILSLAKLNNHKMKGVDSSSGKTNIDTLVRATQIVAFQYRTVAVCTGEFDCVADGTFGGEYKLSSGTEGITAEDLPCVIIEDGPIPIMGDITASGCSLGSTIASFIGGLDSTGKLFDAVVGAVLLYKSAGKLASTRCQGSGSFHVELIDALYQLFHENKPEKWSASLKKFK
Protein: Phenazine biosynthesis protein PhzA1 (Q9HWH1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzA1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
- Trans-2,3-dihydro-3-hydroxyanthranilate isomerase
- 5-methylphenazine-1-carboxylate 1-monooxygenase
- Phenazine-1-carboxylate N-methyltransferase
- Phenazine biosynthesis protein PhzB1
- anthranilate synthase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Phenazine biosynthesis protein PhzD1
- 3-
- Elastase
Sequence:
MNGQRYRETPLDIERLRRLNRATVERYMAMKGAERLQRHSLFVEDGCAGNWTTESGEPLVFRGHESLRRLAEWLERCFPDWEWHNVRIFETEDPNHFWVECDGRGKALVPGYPQGYCENHYIHSFELENGRIKRNREFMNPIQKLRALGIAVPQIKRDGIPT
Protein: MAD2L1-binding protein (Q9DCX1)
Organism: Mus musculus (Mouse)
Function: May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle (By similarity). {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Mitotic spindle assembly checkpoint protein MAD2A
- Pachytene checkpoint protein 2 homolog
- Mitotic spindle assembly checkpoint protein MAD1
Sequence:
MAASGEEDMSELSPAAAPNLDWYEKPEETHAPEVDLETVIPPAQEPSNPAEPFCPRDLVPVVFPGPVSQEDCCQFTCELLKHILYQRHQLPLPYEQLKHFYRKVPQAEDTARKKAWLATEARNRKCQQALAELESVLSHLRDFFARTLVPQVLILLGGNALSPKEFYELDLSRLAPFGVDQGLNTAACLRRLFRAIFLADPFSELQTPPLMGTIVMVQGHRDCGEDWFQPKLNYRVPSRGHKLTVTLSCGRPSVPAMASEDYIWFQAPVTLKGFHE
Protein: Ceramide synthase 4 (CerS4) (EC 2.3.1.-) (LAG1 longevity assurance homolog 4) (Sphingosine N-acyltransferase CERS4) (EC 2.3.1.24) (Translocating chain-associating membrane protein homolog 1) (TRAM homolog 1) (Q9D6J1)
Organism: Mus musculus (Mouse)
Function: Ceramide synthase that catalyzes formation of ceramide from sphinganine and acyl-CoA substrates, with high selectivity toward long and very-long chains (C18:0-C22:0) as acyl donor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12912983}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alkaline ceramidase 1
- Neutral ceramidase
- Alkaline ceramidase 2
- Sphingolipid delta
- Ceramide kinase
- Sphingomyelin phosphodiesterase 2
- Acid ceramidase
- Ceramide glucosyltransferase
- Sphingolipid delta
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
Sequence:
MSFSLSEWLWQETYWLPPNVTWAELEDRDGLVFAHPHHVLAAFPVALVLVAVRIVFERFVALPLSRWMGVQDPIRRKIKPNPVLEKYFLRMKQCPEETQMVLLASQCGLTLRQTQRWFRRRRNQDRPSLSKKFCEACWRFVFYLCSFVGGTSILYHESWLWSPSLCWENYPHQTLNLSLYWWYLLELGFYLSLLITLPFDVKRKDFKEQVVHHFVAVGLIGFSYSVNLLRIGAVVLLLHDCSDYLLEGCKILNYAHFRRGCDALFIMFALVFFYTRLIFFPTQVIYTSVYDSIKNSGPFFGYYFFIVLLVMLQILHVYWFCLILRMLYSFLHKGQMTEDIRSDVEEPDSSDDEPVSEGPQLKNGMARGSRVAVTNGPRSRAAACLTNGHTRAT
Protein: TLE family member 5 (Amino-terminal enhancer of split) (Amino enhancer of split) (Grg-5) (Groucho-related protein 5) (Protein ESP1) (Protein GRG) (P63002)
Organism: Mus musculus (Mouse)
Function: Transcriptional corepressor. Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state. Essential for the transcriptional repressor activity of SIX3 during retina and lens development.
Subcellular location: Nucleus {ECO:0000269|PubMed:12050133}.
Interaction partners:
- TLE family member 7
- Transducin-like enhancer protein 6
- Nucleolar RNA helicase 2
Sequence:
MMFPQSRHSGSSHLPQQLKFTTSDSCDRIKDEFQLLQAQYHSLKLECDKLASEKSEMQRHYVMYYEMSYGLNIEMHKQAEIVKRLNGICAQVLPYLSQEHQQQVLGAIERAKQVTAPELNSIIRQQLQAHQLSQLQALALPLTPLPVGLQPPSLPAVSAGTGLLSLSALGSQTHLSKEDKNGHDGDTHQEDDGEKSD
Protein: Putative prephenate dehydratase (PDT) (EC 4.2.1.51) (O14361)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Putative prephenate dehydratase required for the syntheis of L-phenylalanine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chorismate mutase
- Probable prephenate dehydrogenase [NADP
- Aromatic amino acid aminotransferase C56E4.03
- Aromatic amino acid aminotransferase C569.07
- Histidinol-phosphate aminotransferase
- Aromatic amino acid aminotransferase C1773.13
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Pentafunctional AROM polypeptide
- Chorismate synthase
Sequence:
MSASKIAFLGPRGTFSHQAALLARPDSLLCSLPSFAAVLEALSSRQVDYAVLPIENSTNGAVIPAYDLLKGRDDIQAVGEVLVPAHHCIIGKSLENVQKILSHPQAFGQCSKWISANVPNAEFVSVSSTSQAAALASKDITGTIVAISSELCAVENQFNLLVKNIEDDSNNRTRFLLLRSGGFQDDLSPLKEKSLLQFYLSHPKKLSAVFEVFAAHKVVITNLVVRPSCKFPWTYIYFVECLGMEKHLIDRVGKYCDTFTFMGSYTNQISYF
Protein: Stork-head box protein ham-1 (HSN abnormal migration 1) (G5EEC5)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Required for asymmetric cell division in neuroblasts, perhaps acting by regulating spindle positioning and myosin polarization, and thus the position of the cleavage plane. Required to produce daughter cell size asymmetry in neuroblasts undergoing asymmetric cell division, usually giving rise to one precursor cell and one apoptotic cell. Positively modulates expression of the serine/threonine kinase pig-1/MELK during asymmetric division of the Q.a neuroblast. Plays a role in neural fate specification in several dopaminergic lineages, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB), acting in concert with the kinase, ham-1, and the T-box protein tbx-2 and the homeobox protein egl-5.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:15979607, ECO:0000269|PubMed:26703426}. Nucleus {ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}. Cytoplasm {ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}. Note=Distributed asymmetrically in the cell cortex in some embryonic cells, including the hermaphrodite-specific neuron (HSN)/phasmid neuron (PHB) neuroblast (PubMed:15979607, PubMed:26703426). Localized to nucleus during interphase and evenly distributed in the cytoplasm of dividing Q.a and Q.p neuroblasts (PubMed:23946438). {ECO:0000269|PubMed:15979607, ECO:0000269|PubMed:23946438, ECO:0000269|PubMed:26703426}.
Interaction partners:
- Maternal embryonic leucine zipper kinase
- Protein lin-32
- Numb-related protein 1
- Arf-GAP with ANK repeat and PH domain-containing protein cnt-2
- Nuclear hormone receptor family member nhr-127
Sequence:
MTYLAVVLNGPKAKNGRKVFDSFLEQNRQMFWNRELTSACESITYMGFMRPGTLFVSGPASQLTVLKDAWARRILKPAMGYTITSLGDLGAIQQVEQMHFVPLGDVICDAVAQLNRQGLAATEQAIRQYVARHCPHVAPPGIEMVRQTITSLLSTGFVYKMADHYFVSVPTNSPMRPPAKAATKTTKTTVECQTGASMMCPQQTSTSSDEHVIEPAKKDHKKCQNSNRRSIFARLFSRGMKPQTIMPSASPIHVGGPPTPPPAAMLPTKNKYPTYHHDLNEECQRKARRRNHPRRGETQKLLSSSSECLKYYPVDMPETRPTRRRARMASPLRSSTPNNSDSAYSISPPHTDSNEEAGSISDSEINHTYININKFRRQNFDSTQFEDLTGATATTSEEPEILGRHIRGVLISNL
Protein: Electron transfer flavoprotein regulatory factor 1 (LYR motif-containing protein 5) (Q6IPR1)
Organism: Homo sapiens (Human)
Function: Acts as a regulator of the electron transfer flavoprotein by promoting the removal of flavin from the ETF holoenzyme (composed of ETFA and ETFB).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:27499296}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
- LYR motif-containing protein 1
- LYR motif-containing protein 2
- Complex III assembly factor LYRM7
- Large ribosomal subunit protein mL46
- LYR motif-containing protein 9
- LYR motif-containing protein 4
Sequence:
MKMANSLRGEVLKLYKNLLYLGRDYPKGADYFKKRLKNIFLKNKDVKNPEKIKELIAQGEFVMKELEALYFLRKYRAMKQRYYSDTNKTN
Protein: Amino acid tansporter, putative (Q38B26)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTSREGIHPPYEVPVDAIFQPEGEGADISRSGTLISGAASARTVASPSQTQPADSRLSLSPQLKSPKITATPREVSQGERFSGESLDQPLTPGCAKERVGPSSSRGSDLASVGDGFTRFTYGSVQDCDELDRHSLGPQLTDALECSFRSGTFVPSSGQSYTSLGRAAFHIFKGNVGTGVFLLPAYYRDAGYALGGVVVVLMGWLIIDCVLALIRAKQIIGHTGARTYPAVVKYVLGKLWMHFAKFSLLFTQFGFCVVYIQYASSLFAEFFTGHDLYKLFVFISIVVVTFMTFVSHRLGFLAYMSMIAAVFVMVVLAGATAEEVCSLSTTGVAPEVWAIVPTMRIFLFISGHVFSLEGIGVVLPVENSISPEDYPKFEKVVKYVNASIVALYVFFGVLGYLAYGEALESSVVLAMPASTMKVLMQVLLGLSLIFGYPIQFVPAIQLLDRALGIELHREKSMFVMVRVTFNIFVGAIAASIGAETVSLFAGFLGAFTGIHLMVTLPALLAIFTERVENARSSTDVDGVSAELSFCDYMKIFCTFPDNPFDCRWYAYIIFSLFVWVAGIYFTFAPMLSK
Protein: Inhibin beta B chain (Activin beta-B chain) (P17491)
Organism: Rattus norvegicus (Rat)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Inhibin beta A chain
- Activin receptor type-2A
- Activin receptor type-2B
- Follistatin
- Activin receptor type-1B
- Activin receptor type-1C
- Bone morphogenetic protein receptor type-1A
- Serine/threonine-protein kinase receptor
- Activin receptor type-1
- Inhibin alpha chain
Sequence:
MDGLPGRALGAACLLLLAAGWLGPEAWGSPTPPPSPAAPPPPPPPGAPGGSQDTCTSCGGGGGGFRRPEELGRVDGDFLEAVKRHILSRLQLRGRPNITHAVPKAAMVTALRKLHAGKVREDGRVEIPHLDGHASPGADGQERVSEIISFAETDGLASSRVRLYFFVSNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVKVYFQEQGHGDRWNVVEKKVDLKRSGWHTFPITEAIQALFERGERRLNLDVQCDSCQELAVVPVFVDPGEESHRPFVVVQARLGDSRHRIRKRGLECDGRTSLCCRQQFFIDFRLIGWNDWIIAPTGYYGNYCEGSCPAYLAGVPGSASSFHTAVVNQYRMRGLNPGPVNSCCIPTKLSSMSMLYFDDEYNIVKRDVPNMIVEECGCA
Protein: glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Q383W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tyrosyl/methionyl-tRNA synthetase, putative
- serine--tRNA ligase
- Alanine--tRNA ligase
- leucine--tRNA ligase
- isoleucine--tRNA ligase
- arginine--tRNA ligase
- Valine--tRNA ligase, mitochondrial
- tyrosine--tRNA ligase
- glutamate--tRNA ligase
- cysteine--tRNA ligase
Sequence:
MSTGLPSKLESLVRSEFEDTCRRRFFFGLAFDPYGGSAGLYDMGPPLCAMKANLLAHWRQHFVLAESMCEVDTTCLTPQEVFVTSGHVTRFNDVMVRDTVTGECIRADKFLEEYCETQLRDSQLSSEQRDQLERLRIGAGAMSTEEIRASIKELQLKSPKGNALSDPFPFNLMFSTSIGPEGDRVGYMRPELAQGIILNFKRLLDTGNAQRMPFACASIGTAFRNEIAPRANLIRVREFTLAEIEHFVNPNDKTHEKFALVKDVEIWMWARKQQELNQEPVQTTVGDAVAQKIIDNETLAYFIARTAQFLEAVGARYVRFRQHLRNEMAHYAQDCWDAELLTSYGWVECVGVADRSAYDLTQHSGATKKDLCAREEFAEPRTERQLQRKLQKGAIGKAFGKNAGDVMEYLNTAPDDVCVELSKKLSGGGSVDITTDRGFTASITSNMVQFEYKDVKVTGRSFIPSVIEPSFGVGRILYALLEQSYWVRRDESAKNEKRAVFGLRPLIAPQKVAVFPLLMKPELIRTVEEIKERMLLHGISTRTDDSGASIGKKYARVDELGVPFCVTCDMENDGCVTLRERDSAQQVRIPKEKVADIVAEMCRPLRPREWASVLAEFPAQAAAT
Protein: Ectonucleoside triphosphate diphosphohydrolase 2 (NTPDase 2) (EC 3.6.1.-) (CD39 antigen-like 1) (Ecto-ATP diphosphohydrolase 2) (Ecto-ATPDase 2) (Ecto-ATPase 2) (P79784)
Organism: Gallus gallus (Chicken)
Function: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nucleoside-triphosphatase
- Adenylate kinase isoenzyme 1
- Ribonucleoside-diphosphate reductase
- Uncharacterized protein.
- Ribonucleoside-diphosphate reductase subunit M2
- Ribonucleotide reductase regulatory TP53 inducible subunit M2B.
- Ectonucleoside triphosphate diphosphohydrolase 8
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ectonucleoside triphosphate diphosphohydrolase 3
- Adenylate kinase 5
Sequence:
MARRAAAVLLLLALGCLLGILLLCLGSGDARGPPSFKYGIVLDAGSSHTAVFIYKWPADKENDTGVVSEHSMCDVEGPGISSYSSKPPAAGKSLEHCLSQAMRDVPKEKHADTPLYLGATAGMRLLTIADPPSQTCLSAVMATLKSYPFDFGGAKILSGEEEGVFGWITANYLLENFIKRGWLGEWIQSKKKTLGAMDFGGASTQITFETSDAIEDPKNEVMLKLYGQPYKVYTHSFLCYGRDQVLKRLLSKVLQAENYQETVANPCWPTGYRKSLSLSSIYDSPCTEKERPGLPLNTTVVVSGTGNGNLCAVHVNKLFDFTSCSFSHCSFDGVFQPEVSGNFIAFSAFFYTVDFIRTVMERPVHSPSDLKDAAETICATSWNELYQKAPRLEKRLPDYCATSTFVYLLITKGYNFNNRSFPSIAFQKKAGETSIGWALGYMLNLTNMIPAQEPASHRSMLYNYWVILILLFVITTLTALLTAVYLLRRSKSSTI
Protein: Gram-positive cocci surface proteins LPxTG domain-containing protein (Q51912)
Organism: Finegoldia magna (Peptostreptococcus magnus)
Interaction partners:
Sequence:
MAALAGAIVVTGGVGSYAADEPIDLEKLEEKRDKENVGNLPKFDNEVKDGSENPMAKYPDFDDEASTRFETENNEFEEKKVVSDNFFDQSEHPFVENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADALKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADLLAKENGKYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFAEATAEAYRYADLLAKENGKYTADLEDGGYTINIRFAGKKVDEKPEEKEQVTIKENIYFEDGTVQTATFKGTFAEATAEAYRYADLLSKEHGKYTADLEDGGYTINIRFAGKEEPEETPEKPEVQDGYASYEEAEAAAKEALKNDDVNKSYTIRQGADGRYYYVLSPVEAEEEKPEAQNGYATYEEAEAAAKKALENDPINKSYSIRQGADGRYYYVLSPVEAETPEKPVEPSEPSTPDVPSNPSNPSTPDVPSTPDVPSNPSTPEVPSNPSTPGNEEKPGNEQKPGNEQKPGNEQKPGNEQKPGNEQKPDQPSKPEKEENGKGGVDSPKKKEKAALPKAGSEAEILTLAAASLSSVAGAFISLKKRK