wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc-finger nuclear protein hindsight (O46205)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAAQQQHNNSTVVLEMERQRRDSTTSESSLEHLDLGRTPKKLGGNSGSTQTTSTPHELATVTSSRKRKIRHLQLNHHQQQQHHQQSDLLSDEDVVEAEAEEDEDDEDGDQVAALGSRNLGRHKQRRSGGATTQASIVMDYSSGDASSLRKKFRLNRSAASLSESGFVDASSTTGHSGYLGNSSSATNTTATSGIGASAVAPSPVGGAAINAASSSSGSSSGGSGGSSPQGQCLSSGESGIGAGDEHMKYLCPICEVVSATPHEFTNHIRCHNYANGDTENFTCRICSKVLSSASSLDRHVLVHTGERPFNCRYCHLTFTTNGNMHRHMRTHKQHQVAQSQSQSQQQQSLQQQQQSQQQRRQQQQHQPSQQQQNPAQQQLMGNTLSAGAESYESDASCSTDVSSGHSHSRSSSSLNNNNNNSHKANNNLKDLEELEVSTEDQDTENKQRRLKTTINNNIIESEQQEDMDDEEADDADVAMLTSTPDVATLLAGASASGAASRSPTPSPSASPALLLSCPACGASDFETLPALCVHLDAMHSDIPAKCRDCEVIFATHRQLQSHCCRLPNALAGGLPPLLGASSSPLHNEEPEDEEHGDDEDLEQKERLASQSEDFFHQLYLKHKTANGCGAISHPPSPIKHEPADTKDLADIQSILNMTSSSSSFLRNFEQSVNTPNSSQYSLDGRDQEEEAQDAFTSEFRRMKLRGEFPCKLCTAVFPNLRALKGHNRVHLGAVGPAGPFRCNMCPYAVCDKAALVRHMRTHNGDRPYECAVCNYAFTTKANCERHLRNRHGKTSREEVKRAIVYHPAEDAGCEDSKSRLGEDLADTSFRSISPTPPPPPVNESKSQLKHMLLGENHLAPVNQQPPLKIQVKSLDQLVDKKPSAPAPQQQQQQQQQEKSGSALDFSMDVLDLSKKPTGGASLTPAVTRTPTPAAVAPVTPGGVGTPDLAAAIEQQQLLLAQQQLFGAGGEYMQQLFRSLMFQSQTSGFPFFPFMAPPPPQANPEKPPMVSPPNRINPMPVGVGVGVPVPPGGPVKMVIKNGVLMPKQKQRRYRTERPFACEHCSARFTLRSNMERHVKQQHPQFYAQRERSAHHVMRGRGASNVAAAAAAAAAAAAPTVMAGGPGSSGFGSNHHHGHGHGSHGHAPISEQVKCAILAQQLKAHKNTDLLQQALAHGSSSVAGNPLLHFGYPLTNPSPMHNGSSQGNGQATAMDDDEPKLIIDEDENEHDHEVEAEDVDDFEEDEDEEEMDEPEDEPELILDEQPAEKEAEEEQELPKPLEQLGTKEAAQKMAETILEQAIKAGKPLSPPPTKENASPANPTVATTMQEPAITAPSTNPSSLKTMIAQAEYVGKSLKEVASSPFKDESQDLVPVAKLVDNATSQNMGFNSYFRPSDVANHMEQSDEEGLVASGSASESNNSGTEDVTSSSSSSEPKKKSAYSLAPNRVSCPYCQRMFPWSSSLRRHILTHTGQKPFKCSHCPLLFTTKSNCDRHLLRKHGNVESAMSVYVPTEDVSEPIPVPKSVEEIELEEQRRRQEAEREKELELERERELERERELERERQLEKEKERERQQLIQKLAAQMNAAATAAAVVAAASAVNGGASGGPHGPIADALAGGDLPYKCHLCEGSFAERLQCLEHIKQAHAHEYALLLAKGAIETESLEANPHQQPSQQAVHSDDEAPNGGGNRGKYPDYSNRKVICAFCLRRFWSTEDLRRHMRTHSGERPFQCDICLRKFTLKHSMLRHMKKHSGRAHNGDTPGSDCSDDEQVSSPPSTPHPTQPTSANNNNSCHNNNNNANNNNNNNNNNNNNSSSKLGLKLHDLLDKASEWRASRLGEHKENMGEATPSGATVAGSDLIGNLLGISDQGILNKLLSSRTRRPNFWVWTTSERNSSDNRATPRAINTGVAAVLHRLTYTKA
Protein: Lysozyme g (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase) (C1BHE7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MGSHEMAGELPYMNKYKSIIKRVGSNHGVEPSIIAGIISRETRAGTGAGLVNGWGDNGNAFGLMQVDKNWHIPRGRWDSEEHLSQATGILVGIIGSVQRKFPSWTKEQQLRGGLAAYNVGLDKVHCYSRVDEMTTGGDYSMDVLARAQFYRRNGY
Protein: PHD finger protein 1 (Phf1 protein) (Q5XI49)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGSSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSKLLSALNSHKDRFISGREIKKRKCLFGLHARTPPPVELLTGDGSPTRAGPWGRGLTSPGETPEVGARTLEEEAEGESGGTGATHSSSQSAWVPGAEGPAGLRVSTTPQP
Protein: Ubiquitin-conjugating enzyme E2 C (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme C) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme C) (UbcH10) (Ubiquitin carrier protein C) (Ubiquitin-protein ligase C) (O00762)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
Interaction partners:
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 2
- Cyclin-A2
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 15
- Cell division cycle protein 16 homolog
- Baculoviral IAP repeat-containing protein 5
Sequence:
MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP
Protein: CCAAT/enhancer-binding protein (A5X2V9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005879}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-4
- C-myb C-terminal domain-containing protein
- DNA damage-inducible transcript 3 protein
- BZIP domain-containing protein.
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Uncharacterized protein
- Runt-related transcription factor 2
Sequence:
MEVAGFYDGDCFAFQSRNSIISPISDNSTCKQRVDGSMTELGIAEHEKAIDFSDYLDPAAAHCQLVTHNETQQRGGGVFASFLAEESRIKRLSSLEQNYRNYISLNERETSAHANPREPYVLGYPELQETRVDTVFSPEFLGNHFKTGERDDLQEDQRMDNNGSSGYDMRYLHYQSTPSGSLGNISTASSSSSSPPGTPATPGKGRSPLQGGKMSSGGKGKKRLEKDSEEYKQRRERNNLAVRKSRDKAKIRNMETQHKVLELAAENDRLQKRVEQLSRELATLRNLLSATGQC
Protein: DUF1935 domain-containing protein (Q38BY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTELVPEAEVTFNCGSPSFPYVRVYRCFKTTNSGMLYRLEDDKGRWAFYNDTPLTVFNVYVKFNADSVVTSDTDVALEMTQGEWDYWATTVVLPGHTQRFVEGTISSFLLNFASEGELAKDVTFVNGTPTVGYDRVYRCFKQNANGMLFRLVKVERPGNECVWNFYNDSRELSVEVELTLIEKDSAKPLGDTQVIPPPDGVGVALYKIVVPPLKTVPFLRGHPRFSKQSYVAKSMYDENMLDASEITFENGQPDRAVIDYPRTKVFRGFNNNGNGLAFLLVDPEEKKWAFYNDTTNYNVTATVRFAAGSVYKAAANTRVEVDPAVEGGTVCTITVMPLATELFITEGNPEQYQISLSAECSTGPKPEENPDYQNGQPDTKVMLRWEKVYRCFKNRGNGLLFRLVGDNDRRWGFYNDTTDFIFTVTVSFENGETVKTLGNTSVSEDPELGKVFTLEVAPLSTEVFVFGDLSGYKTRFAARSVRCA
Protein: Saposin B-type domain-containing protein (Q9XVI5)
Organism: Caenorhabditis elegans
Interaction partners:
- Saposin B-type domain-containing protein
- Saposin B-type domain-containing protein
- Saposin B-type domain-containing protein
- Saposin B-type domain-containing protein
Sequence:
MFSKTVVVLLMVVPAISLAQPASPLVLKKSHGAFCHLCEDLIKDGKEAGDVALDVWLDEEIGSRCKDFGVLASECFKELKVAEHDIWEAIDQEIPEDKTCKEAKLC
Protein: Malate synthase G (MSG) (EC 2.3.3.9) (P37330)
Organism: Escherichia coli (strain K12)
Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein GlcG
- Isocitrate lyase
- Glycolate oxidase subunit GlcD
- Glycolate oxidase iron-sulfur subunit
- Glycolate oxidase subunit GlcE
- Citrate synthase
- Malate synthase A
- Glyoxylate carboligase
- Acetyl-coenzyme A synthetase
- NADP-dependent malic enzyme
Sequence:
MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREKESH
Protein: Ferrochelatase, mitochondrial (EC 4.98.1.1) (Heme synthase) (Protoheme ferro-lyase) (O42479)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22315}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22315}; Matrix side {ECO:0000250|UniProtKB:P22315}.
Interaction partners:
- Protoporphyrinogen oxidase.
- Uroporphyrinogen decarboxylase.
- Uroporphyrinogen-III synthase
- Frataxin.
- Heme oxygenase 1
- Uncharacterized protein.
- Uncharacterized protein.
- Hephaestin
- Protoheme IX farnesyltransferase
- Heme oxygenase
Sequence:
MAAAGRAARPLVAGGRQLRVPLRWRGQVAAAAPSTKPQAEPETRKPKTGILMLNMGGPERLDDVHDFLLRLFLDRDLMTLPAQNKLAPFIAKRRTPRIQEQYSRIGGGSPIKKWTAVQGEGMVKLLDSMSPQTAPHKYYIGFRYVHPLTEEAIEEMEDDGIERAIAFTQYPQYSCSTTGSSLNAIYRYYNKKGKKPKMKWSIIDRWPTHPLLIQCFADHIQKELDLFPPDKRKDVVILFSAHSLPMSVVNRGDPYPQEVGATVQRVMEKLNHSNPYRLVWQSKVGPMPWLVPQTDETIKGLCQRGKKNMLLVPIAFTSDHIETLYELDIEYAQVLANECGVENIRRAESLNGNPLFSKALADLVCSHIQSNEICSKQLTLCCPLCVNPVCRETKAFFTNQQL
Protein: Uncharacterized protein C1834.10c (Q9P7Q5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MNMPSEILLGARRWFASTSFSLAAVYDAPLKKAIGNIKKFSIGSLGLTYMISPVMLLLDAGGLSLGTRMSMVFLACTTTSLSTAIIHWAAKSYVSEATLKGNVLSLNTFNILGKKRLSQYTLDKLKIPDTNNSRPFANLESTTVPKRYFYLHPELATPIFNAIRQAQQPKQINKNDSK
Protein: Chitinase-3-like protein 1 (39 kDa synovial protein) (Cartilage glycoprotein 39) (CGP-39) (GP-39) (hCGP-39) (YKL-40) (P36222)
Organism: Homo sapiens (Human)
Function: Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:9492324}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Interleukin-13 receptor subunit alpha-2
- Immunoglobulin heavy variable 3-43D
- Tumor necrosis factor receptor superfamily member 10A
- Neutrophil gelatinase-associated lipocalin
- Insulin-like growth factor-binding protein 3 receptor
- Neurofilament light polypeptide
- Galectin-3
- Interleukin-1 beta
- Interleukin-13
Sequence:
MGVKASQTGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT
Protein: Tenascin C (B2LYI9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGAVXWLLPGIFLALFALTPEGGVLKKVIRHKRESGLNLTLPEENQPVVFNHVYNIKLPMGSQCSVDLESTSGEKDLSPTPESSGSFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELEMLVSSLREQCTMGTGCCLQPAEGRLDSRPFCSGRGNFSAEGCGCVCEPGWKGPNCSEPECPGNCNLRGQCLDGQCICDQGFTGEDCSQLACPNDCNDQGKCVNGVCVCFEGYAGLDCGLEVCPVPCSEEHGMCVDGRCVCKDGFAGEDCNEPLCFNNCNNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGELTCPNNCQGHGQCEEGQCVCNEGFAGADCSEKRCPADCHHHGRCLNGQCECDDGFTGADCGELQCPNGCSGHGRCVNGQCVCDEGYTGEDCSQRRCPNDCHNRGHCVQGKCICEQGFKGFDCSEMSCPNDCHQHGRCVNGMCICDDDYTGEDCRDRRCPRDCSQRGRCVDGQCICEDGFTGSDCAELSCPGDCHGHGRCVNGQCICHEGFTGXDCKEQRCPSDCHGQGRCEDGQCICHEGFTGLDCGQRSCPNDCSNQGQCVAGRCICNEGYTGVDCSEVSPPKDLIVTEVTEETVBLAWDNEMRVTEYLIMYTPTHADGLEMQFRVPGDQTSTTIRELEPGVEYFIRVFAILENKRSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKKVTTTRLDAPSQIEVRDITDTTALITWSKPLAEIDSIELSYGIKDVPGDRTTIDLTHEDNQYSIGNLKPDTEYEVSLISRRVDMASNPAKETFITGLDAPRNLRRVSQTDNSITLEWRNVKADIDSYRIKYAPISGGDHAEIDVPKSQQATTKTTLTGLRPGTEYGVGVSAVKGDKEGDPATINAATEIDAPRDLQVSETTQDSLTLFWKTPLAKFDRYRLNYSLPTGQSIEIQLPKDATSHVLTDLEPGQEYTVLLTAEKGRHKSKPARVKASTEEVPSLENLTVTEAGWDGLRLNWTADDLAYEYFVIQVQEANKVETAHNFTVLGNLRTADIPGLKAATPYRVSIYGVARGYKTPVLSAETFTGKTPSLGEVTVAEVGWDALKLNWTAPEGAYTNFFIQVLEADMTQTVQNLTVPGGLRSVDLPGLKAATRYYITVRGVTQDFSTAPLSVEVLTEEIPQLGGLSVTEVSWDSLTLNWTTDDLAYKHFIIQVQEANNVEAAQNLTVSGSLRVVDIPGLKADTPYRVSIYGVIQGYRTPMLSADVSTAKEPEIGNLNISDVTPESFNLSWTATDGIFDMFTIEIIDSNRLLQTAEHNISGAERTAHISGLPPSTDFIVYLSGIAPSIRTKTISTTATTEAEPEVDNLLVSDATPDGFCLSWTADEGIFDSFVIRIRDTKKQSEPQEITLPSPDRTRDITGLREATEYEIELYGISRGRRSQPVSAIATTAMGSPKEIMFSDITENAATVSWRAPTAQVESFRITYVPVTGGPPSMVTVDGTDTETRLVRLTPGVEYHVSVIAMKGFEESDPVSGSLITALDGPSGLLTANITDSEALAMWQPAIATVDSYVISYTGERVPEITRTVSGNTVEFELHDLEPATEYTLSVFAEKGHQKSSTIATKFTTDLDSPRELTATEVQSETAFLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYTARIQALSGSLRSKLIQTIFTTIGLLYPFPRDCSQAMLNGDTTSGLYTIYINGDKTQALEVYCDMTSDGGGWIVFLRRKNGREDFYRNWKAYATGFGDRREEFWLGLDNLSKITAQGQYELRVDLQDHGESAYAVYDRFSVGDAKSRYKLKVEGYSGTAGDSMNYHNGRSFSTYDKDTDSAITNCALSYKGAFWYKNCHRVNLMGRYGDNNHSQGVNWFHWKGHEYSIQFAEMKLRPSNFRNLEGRRKRA
Protein: Triosephosphate isomerase (PfTIM) (EC 5.3.1.1) (Triose-phosphate isomerase) (Q7KQM0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic and gluconeogenic pathways.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Enolase
- Phosphoglycerate mutase
- transketolase
- Suppressor of forked domain-containing protein
- Triosephosphate isomerase
- Deoxyribose-phosphate aldolase, putative
Sequence:
MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
Protein: Aquaporin-6 (AQP-6) (Q9WTY0)
Organism: Rattus norvegicus (Rat)
Function: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10318966, ECO:0000269|PubMed:10647010}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aquaporin-11
- Aquaporin
Sequence:
MEPGLCNRAYLLVGGLWTAISKALFAEFLATGLYVFFGVGSVLPWPVALPSVLQVAITFNLATATAVQISWKTSGAHANPAVTLAYLVGSHISLPRAVAYIAAQLAGATVGAALLYGVTPGGVRETLGVNVVHNSTSTGQAVAVELVLTLQLVLCVFASMDSRQTLGSPAAMIGTSVALGHLIGIYFTGCSMNPARSFGPAVIVGKFAVHWIFWVGPLTGAVLASLIYNFILFPDTKTVAQRLAILVGTTKVEKVVDLEPQKKESQTNSEDTEVSV
Protein: Serine hydroxymethyltransferase, cytosolic (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Serine methylase) (P37291)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Interconversion of serine and glycine.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8132653}.
Interaction partners:
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Low specificity L-threonine aldolase
- Alanine--glyoxylate aminotransferase 1
- Methylenetetrahydrofolate dehydrogenase [NAD
- Bifunctional purine biosynthesis protein ADE17
- Glycine cleavage system H protein, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
- Phosphoribosylglycinamide formyltransferase
Sequence:
MPYTLSDAHHKLITSHLVDTDPEVDSIIKDEIERQKHSIDLIASENFTSTSVFDALGTPLSNKYSEGYPGARYYGGNEHIDRMEILCQQRALKAFHVTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLYLPDGGHLSHGYATENRKISAVSTYFESFPYRVNPETGIIDYDTLEKNAILYRPKVLVAGTSAYCRLIDYKRMREIADKCGAYLMVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSINPKTGKEVLYDLENPINFSVFPGHQGGPHNHTIAALATALKQAATPEFKEYQTQVLKNAKALESEFKNLGYRLVSNGTDSHMVLVSLREKGVDGARVEYICEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGMGEEDFHRIVQYINKAVEFAQQVQQSLPKDACRLKDFKAKVDEGSDVLNTWKKEIYDWAGEYPLAV
Protein: Trafficking protein particle complex subunit (F4K1U5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, cis-Golgi network {ECO:0000256|ARBA:ARBA00004222, ECO:0000256|PIRNR:PIRNR018293}.
Interaction partners:
- Trafficking protein particle complex II-specific subunit 120 homolog
- Trafficking protein particle complex II-specific subunit 130 homolog
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Tetratricopeptide repeat
- SNARE-like superfamily protein
- Trafficking protein particle complex subunit 2-like protein
- Transport protein particle
- Trafficking protein particle complex subunit-like protein
Sequence:
MAPVGPRSGDAIFSSIDRVNAELFTLTYGAIVRQLLTDLEEVEEVNKQLDQMYSSSTIYVDSLPWGYNIGIRLIDEFLAKSGVSRCVDFKETAEMIAKVGFKMFLGVTASVTSWDSDGTCCSIILEDNPLVDFVELPDTCQGLYYCNVLSGVIRGALEMVSMKTEVTWTRDVLRGDDAYELQVKLLKQVAEEYPYKDDE
Protein: Casein kinase I homolog HRR25 (EC 2.7.11.1) (P29295)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase which phosphorylates serine and threonine residues. Can use casein as a substrate. Phosphorylates elongator complex member ELP1/IKI3 on 'Ser-1198' and 'Ser-1202' which promotes the tRNA modification function of the complex. Associated with repair of damaged DNA and meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12628929}. Nucleus, nucleolus {ECO:0000269|PubMed:12628929}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12628929}.
Interaction partners:
- Monopolin complex subunit MAM1
- Protein LTV1
- Monopolin complex subunit LRS4
- Essential nuclear protein 1
- Serine/threonine-protein kinase RIO2
- Prospore formation at selected spindle poles protein 1
- Monopolin complex subunit CSM1
- Ribosome biogenesis protein TSR1
- Small ribosomal subunit protein uS3
- 20S-pre-rRNA D-site endonuclease NOB1
Sequence:
MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL
Protein: Zinc finger protein-like 1 (Q9DB43)
Organism: Mus musculus (Mouse)
Function: Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130 (By similarity).
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNTPLASRETTRLVCYDLFHWACINERAAQLPRNTAPAGYQCPSCNGPIFPPANLAGPVASALREKLATVNWARAGLGLPLIDEVISPEPEPLNSSDFSDWSSFNATTTSVQEERASTPSAPAFYSQAPRPPPSPSRPEQHTVIHMGSTEALAHAPRKVYDTRDDDRTAGIHGDCDDDKYRRRPALGWLAQLLRSRAGSRKRPLTLLQRAGLLLLLGLLGFLALLALMSRLGRAAADSDPNLDPLMNPHIRVGPS
Protein: Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase) (Q29626)
Organism: Bos taurus (Bovine)
Function: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8051072, ECO:0000305|PubMed:8280118}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase
- Prostaglandin-H2 D-isomerase
- Prostaglandin E synthase 2
- Prostaglandin E synthase 3
- Hematopoietic prostaglandin D synthase
- Prostamide/prostaglandin F synthase
- Methylsterol monooxygenase 1
- Lanosterol synthase
Sequence:
MSWAVVFGLLAALLLLLLLTRRRTRRPGEPPLDLGSIPWLGHALEFGKDAAGFLTRMKEKHGDIFTVLVGGRHVTVLLDPHSYDAVVWEPRSRLDFHAYAVFLMERIFDVQLPHYNPGDEKSKMKPTLLHKELQALTDAMYTNLRTVLLGDTVEAGSGWHEMGLLEFSYGFLLRAGYLTQYGVEAPPHTQESQAQDRVHSADVFHTFRQLDLLLPKLARGSLSAGDKDRVGKVKGRLWKLLSPTRLASRAHRSRWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELETVLLGAEQPISQMTTLPQKVLDSMPVLDSVLSESLRLTAAPFITREVVADLALPMADGREFSLRRGDRLLLFPFLSPQKDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYSLPWGAGHNQCLGKGYAVNSIKQFVFLVLTQFDLELITPDVDIPEFDLSRYGFGLMQPEHDVPVRYRIRP
Protein: D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (BDH) (Q80XN0)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q02337}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q02337}.
Interaction partners:
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial
- Dehydrogenase/reductase SDR family member 6
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Acetoacetyl-CoA synthetase
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
Sequence:
MLAARLSRPLSQLPGKALSVRDRENGTRHTLLFYPASFSPDTRRTYASQADAASGKAILITGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGDAGVKELDSLKSDRLRTIQLNVCNSEEVEKAVETIRSGLKDPEKGMWGLVNNAGISTFGEVEFTSMETYKEVAEVNLWGTVRTTKSFLPLLRRAKGRVVNISSMLGRMANPARSPYCITKFGIEAFSDCLRYEMHPLGVKVSVVEPGNFIAATSLYSPERIQAIAKKMWDDLPEVVRKDYGRKYFDEKIAKMETYCNSGSTDTSSVINAVTHALTAATPYTRYHPMDYYWWLRMQIMTHFPGAISDKIYIH
Protein: Uncharacterized protein (Q550K3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4
Sequence:
MMDPSTISPPLSPSPCFLLGSPAPPFSTTMPQPPTLFLSNPNNSSSNSTSSSSSSCPTNNNHLNRGQNNQSNHHYHHTTESNNQLSLSLSSSTIQTQELPNQNLVIPLNSSLSTVPVPPHNNNNNNNNNISNNINNNNNNNNNNNNNNNNNNNNNNSSINNNINNNNDNNNNNNSLNNDDTDTNKSNNENIKVHHDTINSSGLVLDTNIINSEKMDIEIKINSNDINGNNDNDNDNDNDNNNDDNNNNNNNNKNNNNSNSNNNNNNNNDSNNKNDTSNDDINTIESDINSGSNNSSENNNSKNSNSLNFPQSFLSDPNSPLFENEKQSSSISQPLEKSNINNNNNNDNNNNDNSDDRNNINCNNNILENENKNENENENKNNNSTTTNSNTTIFDQTNINSIIPNTTTTTTTTTTTSTNSSTTTPTATTTTTTTTTNLQSNYNFNFNPLKRSLDIEAQLDREHMELKRRQKAQLKTHTLEYQLRQREMSRPKPGTASLQSRKFYLNIAPDKTVYNIDVPNCIIKKFTSDGEKLLCFSRDFKEIQLYRFIGSNFNIPKGATKESKEKIEKNFNTYFRLLYQSHVPNFNEYLCRDFSLTTLCGNYFILASSGQSSTLGNQAQNNQINNILEHQDINRNRNVVQSLNLPNCEDITFYLVSINDGVVRDKITFKRDVIHLAHHSGVYLYKDLFIVLSLQYQAIHIFQIKDTNFVNLKTIGPHCNEDDQAEIDDLAKKEIPHLKAAHEKKLLHDSYSTITPMNPLFAQFYINKTLNAQSNNGKDLNPKISNSLNKTIINNNININNNNNNNNNNINNSNNNNIHHNHHHHHHHHHHHNNNNNNNNNNNNNNNNNNNNNNNNNNNTPQHGLNNILTASLNLSSSNVLNSSTATARNIPLSTTTTNIPPTDHPIQQQQQQQQQQQQQQQQQQQQPQPQQLQLPQHQHQQQQQQPHQQPHQHQQQQHQQPHQQPHHQQQHHQNNHQQHQQHQQHQHHQQQQLQQQQQQQQQQQHHQHQQHHHHQQQQQQQQQQQQQQQQQQQQQQQQQQHQQQQQQQQQQHQHQQQHQHQQHQHQQHQHQHQQHQHQHQHQHQHQHQHQHQHQHQHQHQHQHQHQHQHQQHQQHQQHQQQHHHQQNQHHHQQNQHQQNTMNYQQMFGQTFSEINNSNENRYISGIKQRFLSYLFKKALTSENKKKALSMYYSLYPQYCSLVMWKMQSLDASHLLIKLGSIDGLLGRVTDYCNQICFFVVYNVYTTEVIGVYENSNKEFAKTFEQFCEHFRACSCPSGLIKFRSTCSNNSFVREHLIKQKLAVVNARYGGETQAVKRILSALPFSPQSWNESPYFDKYLFSYDEKIISSTERPKPLVDYPIKFYSRVSGEVKFKLNTGGAQEKIERQNKKYATYIFHPYYPFIISLLHSPSTGSAAVNFHFINDDDENNDGYNTDQDDEHDIIILDNNNNNNNNNNNNTVS