wanglab/gogpt-training-data huggingface dataset:
Protein: NAD-dependent malic enzyme 1, mitochondrial (AtNAD-ME1) (NAD-malic enzyme 1) (EC 1.1.1.39) (Q9SIU0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of sugars and amino acids metabolisms during the night period.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:21841088}.
Interaction partners:
- Malate dehydrogenase 1, cytoplasmic
- Pyruvate, phosphate dikinase 1, chloroplastic
- Malate dehydrogenase 1, mitochondrial
- Malate dehydrogenase 2, cytoplasmic
- Fumarate hydratase 2
- Fumarate hydratase 1, mitochondrial
- Malate dehydrogenase 3, cytoplasmic
- Malate synthase
- Malate dehydrogenase, chloroplastic
- Malate dehydrogenase 1, peroxisomal
Sequence:
MGIANKLRLSSSSLSRILHRRILYSSAVRSFTTSEGHRPTIVHKQGLDILHDPWFNKGTAFTMTERNRLDLRGLLPPNVMDSEQQIFRFMTDLKRLEEQARDGPSDPNALAKWRILNRLHDRNETMYYKVLINNIEEYAPIVYTPTVGLVCQNYSGLFRRPRGMYFSAEDRGEMMSMVYNWPAEQVDMIVVTDGSRILGLGDLGVHGIGIAVGKLDLYVAAAGINPQRVLPVMIDVGTNNEKLRNDPMYLGLQQRRLEDDDYIDVIDEFMEAVYTRWPHVIVQFEDFQSKWAFKLLQRYRCTYRMFNDDVQGTAGVAIAGLLGAVRAQGRPMIDFPKMKIVVAGAGSAGIGVLNAARKTMARMLGNTETAFDSAQSQFWVVDAQGLITEGRENIDPEAQPFARKTKEMERQGLKEGATLVEVVREVKPDVLLGLSAVGGLFSKEVLEAMKGSTSTRPAIFAMSNPTKNAECTPQDAFSILGENMIFASGSPFKNVEFGNGHVGHCNQGNNMYLFPGIGLGTLLSGAPIVSDGMLQAASECLAAYMSEEEVLEGIIYPPISRIRDITKRIAAAVIKEAIEEDLVEGYREMDAREIQKLDEEGLMEYVENNMWNPEYPTLVYKDD
Protein: Separase (Q57ZZ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAYVSNAVKQQLRASRSSYTAEAVHAAYKMLQEFEESSEGDPSLERNVSSELYILCTEAAIEKKEWALAGACLKKYTGRRAQTKALEARALYCDALVALSGVPHSLRGRAKLAAHIRCATKIVSGIKIVLEEWPKEPETLIAGIDYLWLSIQDVCGRIISNSMLDILVLVVTLHEKLSLGGIHTQLQWIVRYAVCLRATGRVQDALNQIVSGAELVAKTGSERLQLQFYRIQVAFTASTSSNRTKQDNTRPVFQALAAVYSFFCGATDDSSAKQELIQATEKLLGDPEKKEVKQKGRKAAEAEAAFRDPAIISDVLSEVALALAMCGADDTCNTILPKLLNGDNARARLFTEYAKAIMRARDCGSLAASKALDAGYLTKNMAEKLFACIGHVEDVIDAARTSVDVSESMYAIEVGCVVLWNLCLPLLQPQTRGRLRLTLSRIVMLLRLCNSRLNRLFVRAAYESALAEFEEENMNATIEQIDKALAVEQLSGSADNTSAYPMEFALLWLRRRAVVRKAHEGTSFISDGDHIVHLIEQARLASANRVPLLQAAADRLPPITRTESVAETRTKNVSVNGEKNKGGKSRKQDVVRETVDERVPFTFEDFSTPNVYYLLLKEASTTNDPAVDEIIIKAAEGLARIAVPDNGFARDLLAMKAEAHLVMSELLEKRGQTSPRALGDATHEDGMSHISKAAQLGARLSAAGYGGGWIVLNACTALINQNTEMFKKGLFLPAAATLRDLSLALGQVNADPMGEYKLFDSIGFGYVMSLVQTYISAKGEVNGELHCESLAETMRKTYLYPICEAHNSVLKQAAEACHQIMSKWSLPSRRKNFSLILPCINRLLDRTHETSTHPQEQLLFLLGRLNGPIELDERRHLVNTECLDMLRADPSVELCARLASHSVQIPQNERVTLEICRTADRLYHEGKLGWGTKSLITVNSGRDKSLASTVVSTQQPSPSVMYLGNLKGSVVANSNGGMQPKPSDMDWYWYADILLHEATLFLHLGVGADRTHRLEFEKRVLVAITNSAVAASRSIPEAQITQITKAYRALCRVATSISRASYRVLQSGLRILLSPPILRIVNKFLRSRTNGRCDAEFDDLCTLTSTLGGYLFTSLLEDENYDEGIKQMHELLRVLPSRYHGSLCAYEAQLRTKLRLSTSELHEKARTVDAEVEAAVCVAVAKNAHDISEGMRAWNQALKILEGKPVQRADLVLSMAEWLAGRNAVTKSELISLLMNGLSDLERVDSMLLSAWLNKSAGRRNTDVSPALRHALTGTMVGRTFAIAQSLTCTNVVPVDKQKDLPSLLETLTALRLLYFLFVVAPITPCASRPFVYKRCCASTLLYYVLSCWKVVAVLLQIHRGEDIRGVKVDPLHLPETLYEWRGFHANPQHAIIIRDLCKDGLALNTHRLWGMLLDVCDYLLEDGMELYVFLILSWVEFCIYWRYDESDPRGRAAVRAVRLKGFISAARCGWAEVCDAYNVEPPDAECWSSVNEVLLSTETPALSVPWPSSGPLDFSNFVGSTHRFILSEAEDLFTLGRVQEALLWKAKVKQCASRTGDRGALARCHLLEARASILRGRWDPPTSEEASAEDSTEEETKTEDMGDGEGTGLPTSLTVAAWTELQLVHIDGFLSCDKVAEAVAFVRQLLTRLLWRLEEVGEGDIEKDTTEMCHKVLLQRCAPRFVAFLRRPFDTLFPGGPREGDVKGLLDEVCSQLDQYADWKSRLVSLRVRQILRPCVDDVLATGKGGVDKALPERLFNEYSEILKVADMLQSEVNAVVPVLALGGDVTTCPSAAAAYDEVLVMCARNCLERKLLKNFISQRFSALSVADLGIPTGGPVELEGYVASYMRDPALYEQSRMLNDSANAALPSQEGICGHDNEVASSLSHFGIPLNYMVNTSTPHIEALLYRAMGGVGTVSSVQMEASIIAALSEFSRRLTAATRAMESPEASVNTTFSGDVNERENAFLTAQWSKITISVPHPSVPRRMSVAERRAAKLASIHVEDPNRLAANAWIEINSNLQMLLLAAVRQARHMFEYKQMAKCYIYLAHNFMLSGNFNAAGTAIEYAETAAMYGFVSDLVTSLTHTTPEAELIRLVNKTKMDAPYLVNTKAFDSLRNNLMEISSMWRRFDLVGAWPAEPNKADPLLSDICTLSAVREGTTSYFLVAFRRQDGEVCSRRAELDMGALRECTSQIEELKRLKKVEVAAGPSAGERSPDAKWGSVFHSYLEKVRTVVFPLLGDFSDLFSSQRAASCSLYLCLDPILQPLPFEQLPELSSFMAVHRELSVLNLRQKTALRTGKPQSNGVAYIIDPFGENEEALQYIFGGGRTKTSNAEIVTFVKDGQGSSSRPSLAYVHRIFANKAYANVLVSACGSFSDIIKPSVIAELSLDHLQTVLIAMATNDASYCREQGCDTCRAYMDFFYEKNYVVSILLLARGVHHVLSNIFTLTASECNVFSKRCLSFVGGGGGKALAEAVKGSNGDAAGPSTQLHISYGVIHHNVKAK
Protein: Uridine kinase (EC 2.7.1.48) (Uridine monophosphokinase) (P27515)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of uridine into UMP and cytidine into CMP in the pyrimidine salvage pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uridine nucleosidase
- Putative uridine kinase DAS2
- Cytidine deaminase
- Orotidine 5'-phosphate decarboxylase
- Uracil phosphoribosyltransferase
- Uridylate kinase
- Golgi apyrase
- Pre-rRNA-processing protein ESF1
Sequence:
MSHRIAPSKERSSSFISILDDETRDTLKANAVMDGEVDVKKTKGKSSRYIPPWTTPYIIGIGGASGSGKTSVAAKIVSSINVPWTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVKPTMKNADAIIPSMSDNATAVNLIINHIKSKLELKSNEHLRELIKLGSSPSQDVLNRNIIHELPPTNQVLSLHTMLLNKNLNCADFVFYFDRLATILLSWALDDIPVAHTNIITPGEHTMENVIACQFDQVTAVNIIRSGDCFMKSLRKTIPNITIGKLLIQSDSQTGEPQLHCEFLPPNIEKFGKVFLMEGQIISGAAMIMAIQVLLDHGIDLEKISVVVYLATEVGIRRILNAFDNKVNIFAGMIISREKLQNHQYKWALTRFFDSKYFGCD
Protein: Small ribosomal subunit protein eS10 (40S ribosomal protein S10) (A0A2R8Y7H1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MLMPKKNRIAIYELLFKEGVMVAKKDVHMPKHPELADKNVPNLHVMKAMQSLKSRGYVKEQFAWRHFYWYLTNEGIQYLRDYLHLPPEIVPATLRRSRPETGRPRPKGLEGERPARLTRGEADRDTYRRSAVPPGADKKAEAGAGSATEFQFQNLQRSNQSAAHADVMCFLLQRGGFGRGRGQPPQ
Protein: E3 SUMO-protein ligase SIZ2 (EC 2.3.2.-) (E3 SUMO-protein transferase SIZ2) (SAP and Miz-finger domain-containing protein 2) (Q12216)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May act as an E3 ligase mediating SUMO/Smt3 attachment to septins. May be involved in chromosome maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:11587849}.
Interaction partners:
- Ubiquitin-like protein SMT3
- SUMO-conjugating enzyme UBC9
- E3 SUMO-protein ligase MMS21
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8
- Ubiquitin-like-specific protease 1
- E3 SUMO-protein ligase SIZ1
- DNA damage tolerance protein RHC31
- E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5
- Ubiquitin-activating enzyme E1-like
- Ubiquitin-like-specific protease 2
Sequence:
MASVMSNNNNNNNNNNASYMFTNPLSNTGGGLINEIKDAINEMEQLKVLELKQICKSLDLSITGKKAVLQDRIKQFLRKSCDIGHIDPWRPKAIKILIAKVRINSSLPKYSTLWETLKTGAFKHPVASGQLPVTALQSTALPPYSQQQALAYSFTSPFYKPIVQIPDANKKLKQSAGRGCTKMKFKVSKSNHDLLKSNKSYKLYLFSGFSIPFIYETVGHEAIDFPYPCELVFNGTKLEDNVKGLKKQNGTGNPANLTPYLKVPTEMNHLDLHYLNIDKEYSISCFIVEVFSPEALLGKILKRPKIIKQATTAYIKRTLNEQDDDDIITTSTVLSLQCPISCTRMKYPAKTDQCKHIQCFDALWFLHSQSQVPTWQCPICQHPIKFDQLKISEFVDNIIQNCNEDVEQVEISVDGSWKPIHNSSAVITDTVNQNHSVKNENQGTVKQEQDYDSRNAFDTNLRNGSNHNEPEIISLDSSDDEAFIPASKSFPTHVNPRNDQLRADIFPSESEGSSDYNPNHTSTPKGSPTMDQDNYQDAFQMRSFLNQGATTNINDTPTNNSSINSFVTATNGDSRIFYNRGPSTPLLPAVLQNLTNQTEAQRNPYGPNYNTTAQDRNLLGIEGDLPPIPPVDPNSEAETELPTRTTSAAHLPPYIHVSTSGHGDDGKIRKRRHSNVSIYIPKNPYATLMKRRPQANHAIMNKTLAQTNDFNTSAQDNSEVVDLTSD
Protein: TRPM8 channel associated factor 2C (A0A1B0GVM2)
Organism: Homo sapiens (Human)
Interaction partners:
- cTAGE family member 6
Sequence:
XYGEDVRQDQQQLLEGISELDIRTGGVPSQLLVHGALAFPLGLDASLNCFLAAAHYGRGRVVLAAHECLLCAPKMGPFLLNAVRWLARGQTGKVGVNTNLKDLCPLLSEHGLQCSLEPHLNSDLCVYCCKAYSDKEAKQLQEFVAEGGGLLIGGQAWWWASQNPGHCPLAGFPGNIILNCFGLSILPQTLKAGCFPVPTPEMRSYHFRKALSQFQAILNHENGNLEKSCLAKLRVDGAAFLQIPAEGVPAYISLHRLLRKMLRGSGLPAVSRENPVASDSYEAAVLSLATGLAHSGTDCSQLAQGLGTWTCSSSLYPSKHPITVEINGINPGNNDCWVSTGLYLLEGQNAEVSLSEAAASAGLRVQIGCHTDDLTKARKLSRAPVVTHQCWMDRTERSVSCLWGGLLYVIVPKGSQLGPVPVTIRGAVPAPYYKLGKTSLEEWKRQMQENLAPWGELATDNIILTVPTTNLQALKDPEPVLRLWDEMMQAVARLAAEPFPFRRPERIVADVQISAGWMHSGYPIMCHLESVKEIINEMDMRSRGVWGPIHELGHNQQWHGWEFPPHTTEATCNLWSVYVHETVLGIPRAQAHEALSPPERERRIKAHLGKGAPLCDWNVWTALETYLQLQQAFGWEPFTQLFAEYQTLSHLPKDNTGRMNLWVKKFSEKVKKNLVPFFEAWGWPIQKEVADSLASLPEWQENPMQVYLRARK
Protein: Opacity protein opA57 (Q04880)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
ASEDGGRGPYVQADLAYAYEHITHDYPEPTAPNKNKISTVSDYFRNIRTRSVHPRVSVGYDFGGWRIAADYARYRKWNNNKYSVSIKELLRNKGNGNRTDLKAENQENGTFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKTTEVTTILHGPGTTPTVYPGKNTQDAHRESDSIRRVGLGAVAGVGIDITPNLTLDAGYRYHYWGRLENTRFKTHEASLGVRYRF
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (E9QEY0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dual specificity protein phosphatase
- Krev interaction trapped protein 1
- Dual specificity protein phosphatase
Sequence:
MASNKMDETNNSHTAGEASEGDSRRESNIEKVQQRGVTEGPAQPSNDTSTVTDDTTVADKNLALLKAHSLDVKFEVGDEYDIIETIGTGAYGVVSSARRRDNGQQVAIKKIPNAFEVVTNAKRTLRELKILKHFKHDNIIAIKDILQPVVPHSAFKSVYVVLDLMESDLHQIIHSRQPLTPEHTRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLSAVYSEESRSFMTEYVATRWYRAPELMLSLHHYSLAIDLWSVGCIFGEMLGRRQMFPGKNYVHQLQLILSVLGTPPESIVGSIGSDRVRSYVRSLPSKAPEPLAALYPQAEPSALNLLAAMLRFDPRERISACQALEHPYLSKYHDPDDEPVCVPAFNFEFDRQPMGKEQIKEAILTEIQDFHKKKQGVRKKIQFKPLHSSGSALVGVSSNSHCTAQQSQHLKEMSQTHQQHSLNFKPADTTQMNVNSFQTPHLIGQILPHLEQSVSCQDVDMPSANSDGQPETIDLTTPTDKDTSFTEPAIDCRKDKSVLSNYTAPSRSVSQTPPTSLPQSVPSLSLSQSQVQSLSQNLSRSLGKGGKPTAAEGTKKEGAISEDTKAALKAALQKSALRQKARDEGTAALGIDLVRGASVGLSSSISSSNSCPEQRRPITAQERQREREEKRKKRQERAMERKRKLKEKEKKEGKHGESLGGVLLSDNDKMLLQRWVRMMDKPADKSQGIETSNAKTSDSNMAQIQPATGNNIIKTNSNGGESVLPKQPNKAQVFKPPQLVSQMGQCVTAGLFYPTSTHDASVPLGQAQNGDVGIVAGVGSVGGLGMVTAPCAFAKNNILKSQFVGTVFTGLENWTGTSSHKTHQPPPELNNPGFAHMPTHSKPNTHVQLLPLEPFMNKQSALNTGIRVSDTSTNAESRDGPQALEKLCFLGERQNGSHSQGSSRQPPGAAVQPCLSLTDTGQSSNSIPDIHTVTQQLSKSQVEDILPPVFSVTPKGSGAGYGVGFDLDDLLTQSLTELQHSDLRESHNDLAPLSASLLSDWLEVHRMTPADMESLQQELQLGSPMILSDNSTLPDT
Protein: Probable peroxygenase 3 (AtPXG3) (EC 1.11.2.3) (Caleosin-3) (Protein RESPONSIVE TO DESICCATION 20) (O22788)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable calcium-binding peroxygenase. May be involved in the degradation of storage lipid in oil bodies, in abiotic stress-related signaling pathway and in drought tolerance through stomatal control under water deficit conditions.
Subcellular location: Microsome membrane. Plastid, chloroplast membrane. Lipid droplet.
Interaction partners:
- Low-temperature-induced 65 kDa protein
- Cytochrome P450 86A1
- Low-temperature-induced 78 kDa protein
- Cytochrome P450 704B1
- Protein HOTHEAD
- NAC domain-containing protein 72
- BURP domain protein RD22
- Galactinol synthase 2
- Very-long-chain enoyl-CoA reductase
- Acyl-CoA thioesterase family protein.
Sequence:
MAGEAEALATTAPLAPVTSQRKVRNDLEETLPKPYMARALAAPDTEHPNGTEGHDSKGMSVMQQHVAFFDQNDDGIVYPWETYKGFRDLGFNPISSIFWTLLINLAFSYVTLPSWVPSPLLPVYIDNIHKAKHGSDSSTYDTEGRYVPVNLENIFSKYALTVKDKLSFKEVWNVTEGNRMAIDPFGWLSNKVEWILLYILAKDEDGFLSKEAVRGCFDGSLFEQIAKERANSRKQD
Protein: Unconventional myosin-VIIb (Q99MZ6)
Organism: Mus musculus (Mouse)
Function: Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:11401444}. Cell projection, microvillus {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:32209652}. Note=Enriched in the microvilli of the intestinal brush border. {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:32209652}.
Interaction partners:
- Ankyrin repeat and SAM domain-containing protein 4B
- Harmonin
Sequence:
MSVFRLGDHVWLDPPSSSKTGVAIGGIVKETKLGKTLIEDDEGKEHWVHAEDLSTLRPMHPNSAQGVDDMIRLGDLNEAGVVHNLLIRYQQHKIYTYTGSILVAVNPFQMLPLYTLEQVQIYYSRHMGELPPHIFAIANSCYFNMKKNKRDQCCIISGESGAGKTETTKLILQFLATVSGQHSWIEQQVLEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNSSGVIEGASIEHFLLEKSRVCRQAPEERNYHIFYCMLMGMSPEEKQMLSLGMPSEYHYLTMGSCTSSEGLSDAKDYAHVRSAMKILQFSDSENWDISKLLAAILHLGNVGFMAAVFENLDSSDVMETPAFPLAMKLLEVQHQALRDCLIKHTIPVLGEFVSRPVNIAQATDRRDAFVKGIYGRLFQWIVKKINAAIFTPQAQDPQNVRRAIGLLDIFGFENFQNNSFEQLCINFANEHLQQFFVKHVFTMEQEEYLSENITWNYIHYTDNQPILDMLALKPMSIISLLDEESRFPQGTDVTMLQKLNSIHANNKSFLSPRSIHDTRFGIAHFAGDVYYQAEGFLEKNRDVLSTDILILIHSSKNKFLKEIFNVDSSQTKLGHGTICQVKAGSQLFKSSDSIKRPVTLASQFKQSLDQLMRILTNCQPYFVRCIKPNEYKKPLLFDRELCIQQLRYSGMMETVHIRKSGFPIRYTFDEFSQRFRVLLPSPERMQFQNKPRQMTLHIADLCLGTDKDWKVGKTKIFLKDHQDTVLEIRRSQALDGAAIRIQRVLRGHKYRKEFLRQRRAAVTLQAGWRGYSQRKNFKLILVGFERLQAIARSHLLMRQFQAMRQRIVQLQARCRGYLVRQQVQAKRRAVVIIQAHARGMVVRKSYWQQKSTGPQVILAKEPKAQVAVHERKRKSIYDTVTDTAMVEKVFGFLPAMIGGQEGPAPTRFEDLEVKTQKLHEVDLDTVPMMAMPEEEVDSLAEYTFPKFAVTYFQKSASHTHIQKPLRYPLLYHENDTDHSAALDVWIIILRFMGDLPEPVVYGRNSLTGSSVMRQIHDKLGKDSVTQHNRSSQVASQLNFGEEAFKFDGPISDRPMSNLEKVHFIVGYAIMRPGLRDEIYCQICKQLSENYKTSSRARGWILLSLCLGCFPPSERFMKYLLNFISQGPPSYGPFCAERLQRTFANGVRAEPPTWLELQAVKSKKHIPIQVILATGRSLTISVDSASTSREICQHVAQKQGLRDNLGFSLQVAVYDKFWSLGSGCDHLMDAVAQCEQLARERGESQRQAPWRIYFRKEFFTPWHDSQEDPVSTELIYHQVLRGVWSGEYNFEKEEELVELLARHCYVQLGATVKSNAVQELLPSCVPSKLYRTKSPEKWASLVTAAHAKAQYTQSKATPLAVREQTVEAARLLWPLLFSRLFEVTTLSGPRLPKTQLVLAINWKGMYFLDQKERTLLGLSFAEVMGLVANRDAPGGKKLLLATLQEEYEFVSPSSVAIAEMVALFLGGLKERSVFAMALQDRRATDDITLLPFKKGDLLILTKKQGLLASENWALGQNDRTGKTGLVPTACLYTIPSVTKPSTQLLSLLAMSPEKRKLAAQEVRALEPPLEDQLTESPYTLEEFSYQFFRAPEKETISRAAMPMARSRGHLWAYSPEPLRQPLLKSVHDKAKLRDAACQIFLAILKYTGDYPSRQSWHSLELTDQMFSLALQDPALQDELYCQILKQLTHNSIRFSEERAWQLLWLCTGLFPPGKTLLPHAQKFIDSRKKKPLALDCSRRLHRVLRVGPRKQPPHDVEVKAAEQNVSKLHHEVYLPNDTSKSMEVGSSSRVRDLCEGIGTRLQLASWDGCSLFIKITDKVISLKEGDFFFDSLRQVSDWVKKNRPQKEGASVTLPYQVFFMRKLWLNVTPGKDVNADTILHYHQELPKYLRGFHKCSREDAIHLGGLICKIQFGSDSSQLASVSKVLKELVPQNLTRLMSSEEWKKSLLLECDKNKRKTVAEAKVEFLKYMYRWPTFGSAFFEVKQTSEPSYPDILLIAINRHGLLLIHPKTKELLNTYPFTKISSWSSGNTYFHMALGSLGQGSRLLCETSLGYKMDDLLTSYVQQLLNTVNKQRGFRAPAPANP
Protein: Foxm1 protein (Q922T7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MQPEEDIAHLERPIKVESPPLEEWPSPCASLKEELSNSWEDSSCSPTPKPKKSYCGLKSPTRCVSEMLVTKRREKREVSRSRRKQHLQPPCLDEPDLFFSEDSSTFRPAMELLAESSEPAPHLSCPQEEGGPFKTPIKETLPVSSTPSKSVLSRDPESWRLTPPAKVGGLDFSPVRTPQGAFGLLPDSLGLMELNTTPLKSGPLFDSPRELLNSEPFDLASDPFGSPPPPHVEGPKPGSPELQIPSLSANRSLTEGLVLDTMNDSLSKILLDISFPGLEEDPLGPDNINWSQFIP
Protein: Uncharacterized protein (Q385F8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNSLMLQKALRVCSVRRLLFMIAIAHSSRRFCSSGSHGGHNSLKGAEGTPIASNAPLQDLLDMDESMTINVCRLSKEQDSALHVATRTYLHTLITTTDEQEWKDMLVAAIRLDTWREHHLRSVLRSVHQSQYDVDTVEGRHGKIKSNCTPSTRLQRALGVVQTAVEEGYRVTPESVHALLVILLRAAGADITASSGAAGEPTPQSQLTNSAAVWQFLSWMERNDYHVMSDAVLQSLEKIIEENVGDRSAGEHHMSVSQNRLDYLRREHRLLRQDCPSSLSERRGARGVPVRRETDTGCE
Protein: 2,4-dinitrotoluene dioxygenase system ferredoxin--NAD(+), reductase component (EC 1.18.1.3) (Ferredoxin--NAD(+) reductase (2,4-dinitrotoluene dioxygenase ferredoxin-specific)) (Q45692)
Organism: Burkholderia sp. (strain RASC)
Function: Component of the 2,4-dinitrotoluene dioxygenase (DNTDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into 2,4-dinitrotoluene (DNT) to form 4-methyl-5-nitrocatechol (MNC) and nitrite. Ferredoxin reductase catalyzes the transfer of electrons from NADH to ferredoxin (DntAb). Also able to convert naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene.
Interaction partners:
Sequence:
MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGAYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSYPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGHRSGLVTDLIGRDLPNLAGWRLHPVWRSGHGRGPEPARCSPRHSTRAHPCRCVLSQRRLSEGTMRTQFNPRIPSHE
Protein: DNA helicase/primase complex-associated protein (HEPA) (Primase-associated factor) (Q2HR92)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04010}.
Interaction partners:
Sequence:
MATSEETAAGYVIGVYFHSVHVHCRIIVWQVNFLPLDPNDGETECYFVVDTLTKEAMERMPEIQECVPSITEHARDLAIWELALRLQNQTIVKAVRTASLPVVLIMTVGRIVNDVIPCPNVRTPRPLACAYLHCEATVTFEVPLTGPAASTGTWHSSIYRECAISAIEICLKTSRGIYSCQSNEAPEAKREKRGLDISDVFVCLTYDIPIAGRVLSLLVPHAPAFHVLWINEDSKWNGAAVEFFRALHHKLFSERNGIPPLWLYVFPGAVEEGTAFAPLLPAFPCIPLRYGSPTSLDRASVQWDLFEPHILTHFDGIKRTSLADTVFGYDSLAISRECEDQYVWPTPVTDININLCTDSDTMAIVREPSGLVAVNLEALLRTDSVLSRVSSIVSLDTLLDLSTPECRRSVELRYNSLLSTVLSWSTSRGHKWAAIVKWKLFFLVQALEPEQWSPEFKDLKRACQMAGFTLKGGTSGDLVFSSHANLLFSTSMGYFLHAGSPRSTAGTGGEPNPRHITGPDTEGNGEHRNSPNLCGFVTWLQSLTTCIERALNMPPDTSWLQLIEEVIPLYFHRRRQTSFWLIPLSHCEGIPVCPPLPFDCLAPRLFIVTKSGPMCYRAGFSLPVDVNYLFYLEQTLKAVRQVSPQEHNPQDAKEMTLQLEAWTRLLSLF
Protein: Core histone macro-H2A.2 (Histone macroH2A2) (mH2A2) (Q9P0M6)
Organism: Homo sapiens (Human)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in stable X chromosome inactivation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11262398, ECO:0000269|PubMed:11331621, ECO:0000269|PubMed:15621527}. Chromosome {ECO:0000269|PubMed:11262398, ECO:0000269|PubMed:11331621, ECO:0000269|PubMed:15621527}. Note=Enriched in inactive X chromosome chromatin (PubMed:11331621, PubMed:11262398) and in senescence-associated heterochromatin (PubMed:15621527). {ECO:0000269|PubMed:11262398, ECO:0000269|PubMed:11331621, ECO:0000269|PubMed:15621527}.
Interaction partners:
- Ganglioside-induced differentiation-associated protein 2
- Histone deacetylase 2
- Histone H2B type 1-N
- Histone deacetylase 1
- ADP-ribose glycohydrolase MACROD1
- Histone deacetylase 11
- Aprataxin and PNK-like factor
- Histone H2B type 1-A
- Histone deacetylase 3
- Histone deacetylase 5
Sequence:
MSGRSGKKKMSKLSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSETILSPPPEKRGRKATSGKKGGKKSKAAKPRTSKKSKPKDSDKEGTSNSTSEDGPGDGFTILSSKSLVLGQKLSLTQSDISHIGSMRVEGIVHPTTAEIDLKEDIGKALEKAGGKEFLETVKELRKSQGPLEVAEAAVSQSSGLAAKFVIHCHIPQWGSDKCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGRNCFPKQTAAQVTLKAISAHFDDSSASSLKNVYFLLFDSESIGIYVQEMAKLDAK
Protein: Probable dual specificity protein phosphatase DDB_G0269404 (EC 3.1.3.16) (EC 3.1.3.48) (Q55E39)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Interaction partners:
Sequence:
MAKNKDDEESYCGGGGYWDMVEDLEEEICFDAQEVIPNLYIGSISAATCTTSLKEHKITHILSISTNPPKIKEFTTLCINIEDESQKDISSYFQQCHGFIENGRKLGGILVHCSAGVSRSASVVISYLMSVFFKPFWYCMQYLRNIRPCIQPNTGFINQLINYEATILKNQNVISTTTTTTTTTTITKKKLISNDCNNDDNSSGGSGGGMES
Protein: Zinc finger protein 620 (Q6ZNG0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MFQTAWRQEPVTFEDVAVYFTQNEWASLDSVQRALYREVMLENYANVASLAFPFTTPVLVSQLEQGELPWGLDPWEPMGREALRGICPGDEARTEKEGLTPKDHVSKETESFRLMVGGLPGNVSQHLDFGSSLEQPQGHWIIKTKSKRRHFTDTSARHHEAYEVKNGEKFEKLGKNISVSTQLTTNQTNPSGQISYECGQCGRYFIQMADFHRHEKCHTGEKSFECKECGKYFRYNSLLIRHQIIHTGKKPFKCKECGKGLSSDTALIQHQRIHTGEKPYECKECGKAFSSSSVFLQHQRFHTGEKLYECNECWKTFSCSSSFTVHQRMHTGEKPYECKECGKRLSSNTALTQHQRIHTGEKPFECKECGKAFNQKITLIQHQRVHTGEKPYECKVCGKTFSWCGRFILHQKLHTQKTPVQA
Protein: Uncharacterized protein (Q5AWD9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MLAKARWLLPLLGASAVQCAHLNLHAQSLLDESMTLQDAIYDPAASYLRYIYFPFAAGPHETRSSVWYSVGLLQRNQGSDAEEAFKILRNVIGDQEKNEIVQWYGDYTKYPEQPTVGTAAYPPVIYNSWDPNWRGFIGTALIIIYEEFQHLLPPDLSDLILESVYNSTKGDSYRVGGVNEDNLYPAYSNAWLMRTVTSSWTGRHLNDANMTAAGDADASDFLDLFDRNHTLSEFNGPTYAGVSLYALTIAAKYMGSTNATIGRNAARLIQQIWEYESIFWNPYMRNFAGPWDRSYGYDMNNYVAIMSLWVWALVGKESAWNTTFPIWTLAHADDFEVAPVIAVLSEFHKALIPDTAISRLTAFSGERTYHGHVYAPPADHEPRNVTTWVSANLSIGTQSFNQSVVGGFSKDSSSFSPSVVQWLRPDESIGYFNLYPTETALKAEVRPYSLNLTYPLGNASSTFTFVLAANPLGKKRDIRSLADVDGLSIKVGGTVDPIPQISFCGLLGGACDVIHGFEFWNATFSMPANTSDVPRIEFQFELTM
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A1ZA05)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDYEPSDKIIDRYHVIRKLGWGHFSTVWLCWDLQAMGYVAIKIVKSAPHFAETARDEIKILKTVRETDPSNPRRHKTVQMLDDFKITGVNGTHICMVFEVLGDNLLKLIRKSNYRGIPLANVKTITRQVLEGLDYLHTCCKIIHTDIKPENVLLCVDEPHVRSLATEATQLYCMNSKMYPSLVSRAPKEYREPPITGKMSKNRKKKLKKKAKKRMELFKQQRDYLEQADGQGAINPNEVQNGDAGISDADEYFDANSVEDNVHVAAGQPSRKQREERKAPPEQSEEAQEQDPLTEGTDKAKKKKKKKNKNKSNQSKGQQPPQLENSTSSAESSSALKSQQANGSNSTTNNKSNTNSSGTLKGQSNGKKMPLRPKQEKQGSNHQLNNNNSKPNSNSDSKISSGSVENTSSATNGPHSNSTLPTPPPPPQAKHKAKKDPALDECNVHVKIADLGNACWVDRHFTEDIQTRQYRSLEVIIGAGYNTSADIWSTACMVFELATGDYLFEPHSGESYTRDEDHLAHIIELLGPIPREILLNGTYAAKSFTRSCELRNISGLKPWGLMDVLLEKYEWSQKDAASFASFLTPMLEFDPNKRATAAECLQHPWLR
Protein: ADP-ribosylation factor, putative (Q38EI8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ADP-ribosylation factor
- ADP-ribosylation factor
- Coatomer subunit gamma
Sequence:
MGNVLSWFEGLFSKKDATILMVGLDAAGKTTILWKLKLNEVQQTVPTLGFNVQTVEYRNVKFHLWDVGGQKLLRSLWKHYYEGANAIIFVVDSNDRDRVMEVRSELTKLLGEPLLSSATLLVFCNKQDLPNRLTPGELVDKLGFREQGAAGLGPLLRERQWYVQGCCAQTGEGLFEGLDWLCSHLPDTH
Protein: Nuclear mitotic apparatus protein 1 (H0YFY6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XRAERDSALETLQGQLEEKAQELGHSQSALASAQRELAAFRTKVQDHSKAEDEWKAQVARGRQEAERKNSLISSLEEEVSILNRQVLEKEGESKELKRLVMAESEKSQKLEERLRLLQAETASNSARAAERSSALREEVQSLREEAEKQRVASENLRQELTSQAERAEELGQELKAWQEKFFQKEQALSTLQLEHTSTQALVSELLPAKHLCQQLQAEQAAAEKRHREELEQSKQAAGGLRAELLRAQRELGELIPLRQKVAEQERTAQQLRAEKASYAEQLSMLKKAHGLLAEENRGLGERANLGRQFLEVELDQAREKYVQELAAVRADAETRLAEVQREAQSTARELEVMTAKYEGAKVKVLEERQRFQEERQKLTAQVEELSKKLADSDQASKVQQQKLKAVQAQGGESQQEAQRLQAQLNELQAQLSQKEQAAEHYKLQMEKAKTHYDAKKQQNQELQEQLRSLEQLQKENKELRAEAERLGHELQQAGLKTKEAEQTCRHLTAQVRSLEAQVAHADQQLRDLGKFQVATDALKSREPQAKPQLDLSIDSLDLSCEEGTPLSITRHKALMTIIPDLSPNNPLSKLPRTQPDGTSVPGEPASPISQRLPPKVESLESLYFTPIPARSQAPLESSLDSLGDVFLDSGRKTRSARRRTTQIINITMTKKLDVEEPDSANSSFYSTRSAPASQASLRATSSTQSLARLGSPDYGNSALLSLPGYRPTTRSSARRSQAGVSSGAPPGRNSFYMGTCQDEPEQLDDWNRIAELQQRNRVCPPHLKTCYPLESRPSLSLGTITDEEMKTGDPQETLRRASMQPIQIAEGTGITTRQQRKRVSLEPHQGPGTPESKKATSCFPRPMTPRDRHEGRKQSTTEAQKKAAPASTKQADRRQSMAFSILNTPKKLGNSLLRRGASKKALSKASPNTRSGTRRSPRIATTTASAATAAAIGATPRAKGKAKH