wanglab/gogpt-training-data huggingface dataset:
Protein: Dual specificity protein kinase TTK (EC 2.7.12.1) (Phosphotyrosine picked threonine-protein kinase) (PYT) (P33981)
Organism: Homo sapiens (Human)
Function: Phosphorylates proteins on serine, threonine, and tyrosine. Probably associated with cell proliferation. Phosphorylates MAD1L1 to promote mitotic checkpoint signaling. Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint.
Interaction partners:
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Mitotic spindle assembly checkpoint protein MAD2A
- Kinetochore protein NDC80 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 20 homolog
- Kinetochore protein Nuf2
- Mitotic spindle assembly checkpoint protein MAD1
- Kinesin-like protein KIF11
- Disks large-associated protein 5
- Condensin complex subunit 3
Sequence:
MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK
Protein: Ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) (Alanine--glyoxylate aminotransferase 2-like 1) (Q8TBG4)
Organism: Homo sapiens (Human)
Function: Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Ethanolamine kinase 2
- Ethanolamine kinase 1
- Hydroxylysine kinase
- Ethanolamine-phosphate cytidylyltransferase
- Choline/ethanolamine kinase
- Choline kinase alpha
- Phosphoethanolamine/phosphocholine phosphatase
Sequence:
MCELYSKRDTLGLRKKHIGPSCKVFFASDPIKIVRAQRQYMFDENGEQYLDCINNVAHVGHCHPGVVKAALKQMELLNTNSRFLHDNIVEYAKRLSATLPEKLSVCYFTNSGSEANDLALRLARQFRGHQDVITLDHAYHGHLSSLIEISPYKFQKGKDVKKEFVHVAPTPDTYRGKYREDHADSASAYADEVKKIIEDAHNSGRKIAAFIAESMQSCGGQIIPPAGYFQKVAEYVHGAGGVFIADEVQVGFGRVGKHFWSFQMYGEDFVPDIVTMGKPMGNGHPVACVVTTKEIAEAFSSSGMEYFNTYGGNPVSCAVGLAVLDIIENEDLQGNAKRVGNYLTELLKKQKAKHTLIGDIRGIGLFIGIDLVKDHLKRTPATAEAQHIIYKMKEKRVLLSADGPHRNVLKIKPPMCFTEEDAKFMVDQLDRILTVLEEAMGTKTESVTSENTPCKTKMLKEAHIELLRDSTTDSKENPSRKRNGMCTDTHSLLSKRLKT
Protein: SAP30-binding protein (Transcriptional regulator protein HCNGP) (Q9UHR5)
Organism: Homo sapiens (Human)
Function: Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3. May be involved in the regulation of beta-2-microglobulin genes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15496587}.
Interaction partners:
- Histone deacetylase complex subunit SAP30
- Sin3 histone deacetylase corepressor complex component SDS3
- Poly
- Histone deacetylase complex subunit SAP130
- Cyclin-dependent kinase 11B
- Histone deacetylase complex subunit SAP30L
- Histone deacetylase complex subunit SAP18
- AT-rich interactive domain-containing protein 4B
- ATP-dependent RNA helicase DHX8
- THO complex subunit 1
Sequence:
MAGKKNVLSSLAVYAEDSEPESDGEAGIEAVGSAAEEKGGLVSDAYGEDDFSRLGGDEDGYEEEEDENSRQSEDDDSETEKPEADDPKDNTEAEKRDPQELVASFSERVRNMSPDEIKIPPEPPGRCSNHLQDKIQKLYERKIKEGMDMNYIIQRKKEFRNPSIYEKLIQFCAIDELGTNYPKDMFDPHGWSEDSYYEALAKAQKIEMDKLEKAKKERTKIEFVTGTKKGTTTNATSTTTTTASTAVADAQKRKSKWDSAIPVTTIAQPTILTTTATLPAVVTVTTSASGSKTTVISAVGTIVKKAKQ
Protein: Nutritionally-regulated adipose and cardiac enriched protein homolog (Q8N912)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MRTAAGAVSPDSRPETRRQTRKNEEAAWGPRVCRAEREDNRKCPPSILKRSRPEHHRPEAKPQRTSRRVWFREPPAVTVHYIADKNATATVRVPGRPRPHGGSLLLQLCVCVLLVLALGLYCGRAKPVATALEDLRARLLGLVLHLRHVALTCWRGLLRL
Protein: Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain] (P07314)
Organism: Rattus norvegicus (Rat)
Function: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (By similarity). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000305|PubMed:6136502}.
Interaction partners:
- Glutathione hydrolase 5 proenzyme
Sequence:
MKNRFLVLGLVAVVLVFVIIGLCIWLPTTSGKPDHVYSRAAVATDAKRCSEIGRDMLQEGGSVVDAAIASLLCMGLINAHSMGIGGGLFFTIYNSTTRKAEVINAREMAPRLANTSMFNNSKDSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARHGFPVGKGLARALDKKRDIIEKTPALCEVFCRQGKVLQEGETVTMPKLADTLQILAQEGARAFYNGSLTAQIVKDIQEAGGIMTVEDLNNYRAEVIEHPMSIGLGDSTLYVPSAPLSGPVLILILNILKGYNFSPKSVATPEQKALTYHRIVEAFRFAYAKRTMLGDPKFVDVSQVIRNMSSEFYATQLRARITDETTHPTAYYEPEFYLPDDGGTAHLSVVSEDGSAVAATSTINLYFGSKVLSRVSGILFNDEMDDFSSPNFTNQFGVAPSPANFIKPGKQPLSSMCPSIIVDKDGKVRMVVGASGGTQITTSVALAIINSLWFGYDVKRAVEEPRLHNQLLPNTTTVEKNIDQVVTAGLKTRHHHTEVTPDFIAVVQAVVRTSGGWAAASDSRKGGEPAGY
Protein: Receptor-type tyrosine-protein phosphatase V (R-PTP-V) (EC 3.1.3.48) (Embryonic stem cell protein-tyrosine phosphatase) (ES cell phosphatase) (Osteotesticular protein-tyrosine phosphatase) (OST-PTP) (Q64612)
Organism: Rattus norvegicus (Rat)
Function: May function in signaling pathways during bone remodeling, as well as serve a broader role in cell interactions associated with differentiation in bone and testis. Associated with differentiation in bone and testis.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MRPLILLAALLWLQGFLAEDDACSSLEGSPDRQGGGPLLSVNVSSHGKSTSLFLSWVAAELGGFDYALSLRSVNSSGSPEGQQLQAHTNESGFEFHGLVPGSRYQLKLTVLRPCWQNVTITLTARTAPTVVRGLQLHSAGSPARLEASWSDAPGDQDSYQLLLYHLESQTLACNVSVSPDTLSYSFGDLLPGTQYVLEVITWAGSLHAKTSILQWTEPVPPDHLALRALGTSSLQAFWNSSEGATSFHLMLTDLLGGTNTTAVIRQGVSTHTFLHLSPGTPHELKICASAGPHQIWGPSATEWTYPSYPSDLVLTPLRNELWASWKAGLGARDGYVLKLSGPMESTSTLGPEECNAVFPGPLPPGHYTLQLKVLAGPYDAWVEGSTWLAESAALPREVPGARLWLDGLEASKQPGRRALLYSDDAPGSLGNISVPSGATHVIFCGLVPGAHYRVDIASSTGDISQSISGYTSPLPPQSLEVISRSSPSDLTIAWGPAPGQLEGYKVTWHQDGSQRSPGDLVDLGPDTLSLTLKSLVPGSCYTVSAWAWAGNLDSDSQKIHSCTRPAPPTNLSLGFAHQPAALKASWYHPPGGRDAFHLRLYRLRPLTLESEKVLPREAQNFSWAQLTAGCEFQVQLSTLWGSERSSSANATGWTPPSAPTLVNVTSDAPTQLQVSWAHVPGGRSRYQVTLYQESTRTATSIMGPKEDGTSFLGLTPGTKYKVEVISWAGPLYTAAANVSAWTYPLIPNELLVSMQAGSAVVNLAWPSGPLGQGACHAQLSDAGHLSWEQPLKLGQELFMLRDLTPGHTISMSVRCRAGPLQASTHLVVLSVEPGPVEDVLCHPEATYLALNWTMPAGDVDVCLVVVERLVPGGGTHFVFQVNTSGDALLLPNLMPTTSYRLSLTVLGRNSRWSRAVSLVCSTSAEAWHPPELAEPPQVELGTGMGVTVMRGMFGKDDGQIQWYGIIATINMTLAQPSREAINYTWYDHYYRGCESFLALLFPNPFYPEPWAGPRSWTVPVGTEDCDNTQEICNGRLKSGFQYRFSVVAFSRLNTPETILAFSAFSEPRASISLAIIPLTVMLGAVVGSIVIVCAVLCLLRWRCLKGPRSEKDGFSKELMPYNLWRTHRPIPIHSFRQSYEAKSAHAHQTFFQEFEELKEVGKDQPRLEAEHPDNIIKNRYPHVLPYDHSRVRLTQLPGEPHSDYINANFIPGYSHTQEIIATQGPLKKTLEDFWRLVWEQQVHVIIMLTVGMENGRVLCEHYWPANSTPVTHGHITIHLLAEEPEDEWTRREFQLQHGTEQKQRRVKQLQFTTWPDHSVPEAPSSLLAFVELVQEQVQATQGKGPILVHCSAGVGRTGTFVALLRLLRQLEEEKVADVFNTVYILRLHRPLMIQTLSQYIFLHSCLLNKILEGPPDSSDSGPISVMDFAQACAKRAANANAGFLKEYKLLKQAIKDGTGSLLPPPDYNQNSIVSRRHSQEQFALVEECPEDSMLEASLFPGGPSGCDHVVLTGSAGPKELWEMVWEHDAHVLVSLGLPDTKEKPPDIWPVEMQPIVTDMVTVHRVSESNTTTGWPSTLFRVIHGESGKERQVQCLQFPCSESGCELPANTLLTFLDAVGQCCFRGKSKKPGTLLSHSSKNTNQLGTFLAMEQLLQQAGTERTVDVFNVALKQSQACGLMTPTLEQYIYLYNCLNSALLNGLPRAGKWPAPC
Protein: Chorion-specific transcription factor GCMb (mGCMb) (GCM motif protein 2) (Glial cells missing homolog 2) (O09102)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O75603}.
Interaction partners:
- Chorion-specific transcription factor GCMa
- Trophoblast-specific protein alpha
- Forkhead box protein N1
- Cathepsin Q
Sequence:
MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSYERTLDFTARYHSWKPTHGKPSLEEKVDCEQCQAVPTSPYYNLELPCRYLPVPAAGTQALQTVITTTVAYQAYQHPALKHSDSMQEVSSLASCTYASENLPMPIYPPALDPQEGVIQAASPSGRAPLKVPGDCQAPRPTLDFPQEADPSGTDGADVWDVCLSGVGSVMGYLDRTGQPFSFDNEDF
Protein: DNA mismatch repair protein msh2 (O74773)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in post-replicative DNA-mismatch repair. Binds to mismatch-containing DNA. Required for correct termination of copy synthesis during mating-type switching. Also required for proper chromosome organization during meiosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Putative MutL protein homolog 1
- DNA mismatch repair protein pms1
- DNA mismatch repair protein msh6
- DNA mismatch repair protein msh3
- Exodeoxyribonuclease 1
- Proliferating cell nuclear antigen
- DNA polymerase delta catalytic subunit
- Mating-type switching protein swi10
- DNA polymerase epsilon catalytic subunit A
- DNA repair protein rhp51
Sequence:
MSSRNASIANERTDEARMFNFYEKMPKDTNTVRVFDRGEFYVAIGEDASFVAQNAYHTTSVLKHHNVSNTSYCNLSPSLFIKFAEDVLSNLAKRVEIWGANSAKTGFELLKQASPGNMQMLEDLLVSENYQESTAISDSSVSSVLLAVTTRVKQDQRIIGVAFIDPILKKLGVSEFVDSDAYTNFEALIVQVGAKECIISQSGHESTNGNSAVSINTAEINRLRNIIEGCGALVTTIRSSEFSARDVELELSKVLDSPVTHALVPELGLQLAMASCNALLRYLGPALLNPDMEDDRENTSRKLHLYHHNLEQYMRLDIAAVRSLNLLPPPNGNAHKTMSLYGLLNHCRTAMGARNLRRWIVQPLLDAKSIERRHDLVSALVEDAEARQLLLDDDHLLRSIPDIPKLCRRLTRGSASLEDVVRIYQMAKALPKIVTVLDSLTSEHKDLVDKVYTNVLNNHCKNLEKLIELVETTIDLEALDSHQYIIRAEFDEELLDLRQRLDELQHSIFEEHKRVGSDLHQDTEKKLHLEQHHLYGWCLRLTRTEAGCLRGRSSHYTELSTQKNGVYFTTKRLHSLNNSYMDHQKSYRYHQNGLAREVIKIAATYGPPLEAIGQVIAHLDVILSFAHASTVAVIPYVRPNIVDSSIAQEKHGQSSNILDIVSLEDTPNFEEIRRTLENNHCARLYLKQARHPCLEAQDDVKFIPNDVNLEHGSSELLIITGPNMGGKSTYIRQVGVITVMAQIGCPVPCEVADLDIIDAILARVGASDSQLKGISTFMAEMLETATILRAATPRSLIIIDELGRGTSTTDGFGLAWAITEHIVTQIGCFCLFATHYHEMTKLSEEITTVKNLHVTAYVGDSESKDVALLYNVCEGASDRSFGIHVAKLAHFPPKIIEMASNKAAELEAEDSGAQGDTQEVKSKKEGMAIVRDIMRQWRSNVKPEMTQQQMMDQFQKVIGSFAQQINSNNWLQSRVSTNEVSS
Protein: Glycogen phosphorylase 2 (GP2) (EC 2.4.1.1) (P34114)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Interaction partners:
- Glycogen debranching enzyme
- Phosphoglucomutase-1
- 1,4-alpha-glucan-branching enzyme
- UTP--glucose-1-phosphate uridylyltransferase 1
- 4-alpha-glucanotransferase
- Probable phosphoglucomutase-2
- UTP--glucose-1-phosphate uridylyltransferase 2
- alpha-amylase
- Glycogen [starch] synthase
- Nudix hydrolase domain-containing protein
Sequence:
MEEKRSTNSPGFDKPKLNRSGSITSATSHPPRSNSNPKLVAKHQQQLYEESKNKRNQEQQNQQPQQQQQKQTSNQSEDPATQLSSLKFESDKEKEQALLWAFLASYLPEDKGSLQKEFVKHVEYTLAQTKSECTDFSSFQALSYCTRDRLIERWKDTKLFFKQKNVKQVNYMSLEFLLGRSLQNSLSALGLVGKYSDALMDLGFKLEDLYDEERDAGLGNGGLGRLAACFMDSLATCNFPGYGYGLRYKFGMFYQTLVDGEQVELPDYWLNYGSPWEIERLDVSYPINFYGKVSEVEDENGKKVMKWDQGEQMLAVAYDYPIPGFKTYNTVAIRLWSSKPSDEFNLDSFNRGDYLGAIEEKEKSENITNVLYPNDNTMQGKELRLKQQYLFVSATIQDIISQFKETGKPFSEFHNFHAIQLNDTHPTLGIPELMRILIDEEKKSWDEAWDITTKTFSYTNHTVLPEALEKWSVSMVENVLPRHIMIIYEINERFLKLVDQKWPGDMSKRRALSIIDESDGKFIRMAFLAIVGSHTINGVAYLHSELVKHDVFPLFYEIWPNKFQNKTNGVTPRRWIQQSNPQLAELITRSLNSDRWLVNLDIIKDLVHLADNSSFQKEWMEIKRNNKIRLAKYIEKRCDIQVNVDVLFDVQVKRFHEYKRQLLNVLSVINRYLDIKEGKKVAPRVVIFGGKAAPGYYMAKLIIKLINSVADVVNNDPKVGDLLKVVFIPNYCVSNAEIIIPASDISQHISTAGTEASGTSNMKFSMNGGLIIGTLDGANIEIRDAIGHENMYIFGARSEEVNKVKKIIHDGKFTPDTRWARVLTAIKEDTFGPHEQFQDIINSVSGGNDHYILSYDFGSYLDIQNSIDQDFKDRAKWAKKSIMASVCCGKFSSDRTIKEYAQQIWGIEEWKRPGPVPVSNEEARSLLVPPPSGSPNDINAISIERLSPLTFVKQTSASPLSVISGGDKTNNTLKPKQTTKGFNIGGQPGNPTN
Protein: Mitochondrial structure specific endonuclease I (SSE-1), putative (Q38CK4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVRERAVVLIDGPALIHRWYYRWLYTNRNNPVDVKRFAITNARHTIAIAHSFDPSHLMQHLLSPQVEYTHTPKHNKLIICFDQGDGGRREIYPKYKLNREGREVGEELGVIQKVATKVFLGEPKNTLLIVPHFDSKLKNVNAEADDMISTLAQHTQRIRIPTVIMSHDHDLYQLIDEASRCYYYDIRTKHLISEKGVIERLGVHPKLVRDYKCLAGDPSDNIPGVKGIGKTRALQLLKKYGDLEGVLTKGTKKQGGVVGDLLRAGVEGAELSRKLVELRDCPSVLRVCEFFLKL
Protein: Homeodomain-like superfamily protein (Q9ZPZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKKQEKGNEVVTFEENPSTYVHHHTKKASMVLSEQEIEVILQSNKETYNEKLEKNTKENAEKVGIEEGNGSSSKITPCIFYTSDEKARLRWSSDLHDCFVNAVEKLGGPNKATPKSVKEAMEVEGIALHHVKSHLQKFRLGKCNIRGGTNQYVRQSQSMPHKSQQQLQLNNDCVNHDSYCNATFLSVTVPPTIDSLHQDTLNNTILFPTTLQAIPTSVSHNTYMSSYPSYNTVEVVKAQLNALQDSSTSQTQETFSRETNLSSIVTRDEADPVDKYIDWNKVGETDIEHDSVEVLEALGLK
Protein: Mycocerosic acid synthase-like polyketide synthase (MAS-like PKS) (EC 2.3.1.-) (Polyketide synthase Pks5) (O53901)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Polyketide synthase likely involved in the biosynthesis of a polymethyl-branched fatty acid (PMB-FA) that might only be produced during host infection. Is required for the full virulence of M.tuberculosis during host infection.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Probable fatty acid synthase Fas
- Phenyloxazoline synthase MbtB
- Malonyl CoA-acyl carrier protein transacylase
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phthioceranic/hydroxyphthioceranic acid synthase
- Isonitrile lipopeptide synthase
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit C
Sequence:
MGKERTKTVDRTRVTPVAVIGMGCRLPGGIDSPDRLWEALLRGDDLVTEIPADRWDIDEYYDPEPGVPGRTDCKWGAYLDNVGDFDPEFFGIGEKEAIAIDPQHRLLLETSWEAMEHGGLTPNQMASRTGVFVGLVHTDYILVHADNQTFEGPYGNTGTNACFASGRVAYAMGLQGPAITVDTACSSGLTAIHLACRSLHDGESDIALAGGVYVMLEPRRFASGSALGMLSATGRCHAFDVSADGFVSGEGCVMLALKRLPDALADGDRILAVIRGTAANQDGHTVNIATPSRSAQVAAYREALDVAGVDPATVGMVEAHGPGTPVGDPIEYASLAEVYGNDGPCALASVKTNFGHTQSAAGALGLMKAVLALQHGVVPQNLHFTALPDKLAAIETNLFVPQEITPWPGADQETPRRAAVSSYGMTGTNVHAIVEQAPVPAPESGAPGDTPATPGIDGALLFALSASSQDALRQTAARLADWVDAQGPELAPADLAYTLARRRGHRPVRTAVLAATTAELTEALREVATGEPPYPPAVGQDDRGPVWVFSGQGSQWAGMGADLLATEPVFAATIAAIEPLIAAESGFSVTEAMTAPEVVTGIDRVQPTLFAMQVALAATMKSYGVAPGAVIGHSLGESAAAVVAGALCLEDGVRVICRRSALMTRIAGAGAMASVELPAQQVLSELMARGVNDAVVAVVASPQSTVIGGATQTVRDLVAAWEQRDVLAREVAVDVASHSPQVDPILDELAEALAEISPLQPEIPYYSATSFDPREEPYCDAYYWVDNLRHTVRFAAAVQAALEDGYRVFTELTPHPLLTHAVDQTARSLDMSAAALAGMRREQPLPHGLRALAGDLYAAGAAVDFAVLYPTGRLINAPLPTWNHRRLLLDDTTRRIAHANTVAVHPLLGSHVRLPEEPERHVWQGEVGTVTQPWLADHQIHGAAALPGAAYCEMALAAARAVLGEASEVRDIRFEQMLLLDDETPIGVTATVEAPGVVPLTVETSHDGRYTRQLAAVLHVVREADDAPDQPPQKNIAELLASHPHKVDGAEVRQWLDKRGHRLGPAFAGLVDAYIAEGAGDTVLAEVNLPGPLRSQVKAYGVHPVLLDACFQSVAAHPAVQGMADGGLLLPLGVRRLRSYGSARHARYCCTTVTACGVGVEADLDVLDEHGAVVLAVRGLQLGTGASQASERARVLGERLLSIEWHERELPENSHAEPGAWLLISTCDATDLVAAQLTDALKVHDAQCTTMSWPQRADHAAQAARLRDQLGTGGFTGVFVLTAPQTGDPDAESPVRGGELVKHVVRIAREIPEITAQEPRLYVLTHNAQAVLSGDRPNLEQGGMRGLLRVIGAEHPHLKASYVDVDEQTGAESVARQLLAASGEDETAWRNDQWYTARLCPAPLRPEERQTTVVDHAEAGMRLQIRTPGDLQTLEFAAFDRVPPGPGEIEVAVTASSINFADVLVTFGRYQTLDGRQPQLGTDFAGVVSAVGPGVSELKVGDRVGGMSPNGCWATFVTCDARLATRLPEGLTDAQAAAVTTASATAWYGLQDLARIKAGDKVLIHSATGGVGQAAIAIARAAGAQIYATAGNEKRRDLLRDMGIEHVYDSRSVEFAEQIRRDTAGYGVDIVLNSVTGAAQLAGLKLLALGGRFIEIGKRDIYSNTRLELLPFRRNLAFYGLDLGLMSVSHPAAVRELLSTVYRLTVEGVLPMPQSTHYPLAEAATAIRVMGAAEHTGKLILDVPHAGRSSVVLPPEQARVFRSDGSYIITGGLGGLGLFLAEKMANAGAGRIVLSSRSQPSQKALETIELVRAIGSDVVVECGDIAQPDTADRLVTAATATGLPLRGVLHAAAVVEDATLANITDELIERDWAPKAYGAWQLHRATADQPLDWFCSFSSAAALVGSPGQGAYAAANSWLDTFTHWRRAQDLPATSIAWGAWGQIGRAIAFAEQTGDAIAPEEGAYAFETLLRHNRAYSGYAPVIGSPWLTAFAQHSPFAEKFQSLGQNRSGTSKFLAELVDLPREEWPDRLRRLLSKQVGLILRRTIDTDRLLSEYGLDSLSSQELRARVEAETGIRISATEINTTVRGLADLMCDKLAADRDAPAPA
Protein: Protein TIFY 6A (Jasmonate ZIM domain-containing protein 4) (Q58G47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of jasmonate responses. Interacts with and suppresses RHD6 and RSL1 transcription factor activities to negatively regulate jasmonate-stimulated root hair development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Probable WRKY transcription factor 57
- Transcription factor MYC2
- Transcription factor ICE1
- Coronatine-insensitive protein 1
- AFP homolog 2
- Protein TIFY 5A
- Protein TIFY 3A
- Protein TIFY 9
- Transcription factor MYC4
- Transcription factor MYC3
Sequence:
MERDFLGLGSKLSPITVKEETNEDSAPSRGMMDWSFSSKVGSGPQFLSFGTSQQETRVNTVNDHLLSSAAMDQNQRTYFSSLQEDRVFPGSSQQDQTTITVSMSEPNYINSFINHQHLGGSPIMAPPVSVFPAPTTIRSSSKPLPPQLTIFYAGSVLVYQDIAPEKAQAIMLLAGNGPHAKPVSQPKPQKLVHHSLPTTDPPTMPPSFLPSISYIVSETRSSGSNGVTGLGPTKTKASLASTRNNQTAAFSMAPTVGLPQTRKASLARFLEKRKERVINVSPYYVDNKSSIDCRTLMSECVSCPPAHHLH
Protein: At2g30530/T6B20.12 (Expressed protein) (Zinc finger CCCH domain protein) (O04342)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNKVDEIEDFRFEDLEMETEKDKERMMTPTTRMSYSSSSSPSPSSASSSAASSLAAKAIRASSAHRDSSLSSAYSSPSSAPVPTPPKEVNKAYEYTSMKSLNEPKRGFWGSLASKAKAFLDEDDPNQLPQSPKRMEQSIPSATTSGTKEAGQTGRKSENPSLQRRLDAITSSLNYIGGTIGTVVEEGITAVENRTAGIIQETRKKIKKKPSLTRNQQNPEIQADLEIQLKASRDVAMAMAAKAKLLLRELKMVKSDLAFAKQRCAQLEEENKVLRENRSGDSQTDDDDLVRLQLETLLAEKARLAHENSIYTRENLYLRGVVEYHQLTMQDVVYFDEKTEEVTEVYPINVSSMSSSSDNSYNPNPSFLELK
Protein: tRNA pseudouridine synthase C (EC 5.4.99.26) (tRNA pseudouridine(65) synthase) (tRNA pseudouridylate synthase C) (tRNA-uridine isomerase C) (P0AA41)
Organism: Escherichia coli (strain K12)
Function: Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs.
Interaction partners:
- Uncharacterized protein YqcC
- tRNA pseudouridine synthase D
- Flavodoxin YqcA
- tRNA pseudouridine synthase B
- tRNA pseudouridine synthase A
- Ribosomal large subunit pseudouridine synthase E
- Dual-specificity RNA pseudouridine synthase RluF
- Ribosomal small subunit pseudouridine synthase A
Sequence:
MLEILYQDEWLVAVNKPSGWLVHRSWLDRDEKVVVMQTVRDQIGQHVFTAHRLDRPTSGVLLMGLSSEAGRLLAQQFEQHQIQKRYHAIVRGWLMEEAVLDYPLVEELDKIADKFAREDKGPQPAVTHYRGLATVEMPVATGRYPTTRYGLVELEPKTGRKHQLRRHLAHLRHPIIGDSKHGDLRQNRSGAEHFGLQRLMLHASQLSLTHPFTGEPLTIHAGLDDTWMQALSQFGWRGLLPENERVEFSAPSGQDGEISS
Protein: Inhibitor of nuclear factor kappa B kinase regulatory subunit gamma (A0A087X0G7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
Protein: Serine/threonine-protein phosphatase PP1 isozyme 6 (EC 3.1.3.16) (Type one protein phosphatase 6) (P48486)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm {ECO:0000269|PubMed:19329567}.
Interaction partners:
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Flowering time control protein FY
- Transducin/WD40 repeat-like superfamily protein
- Protein ANTHESIS POMOTING FACTOR 1
- Serine/threonine-protein phosphatase 4 regulatory subunit-like protein
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3-I
- Protein phosphatase 1 regulatory subunit INH3
- Putative 26S proteasome non-ATPase regulatory subunit 8 homolog B
- 30-kDa cleavage and polyadenylation specificity factor 30
Sequence:
MDETLLDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKASEKKGRFGFNNNVPRPGTPPHKGGKGR
Protein: Isocitrate/homoisocitrate dehydrogenase (EC 1.1.1.286) (Homoisocitrate dehydrogenase) (HICDH) (Q72IW9)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Function: Catalyzes the NAD(+)-dependent oxidative decarboxylation of homoisocitrate to 2-oxoadipate (alpha-ketoadipate), a reaction involved in lysine biosynthesis through the alpha-aminoadipate pathway. In addition, has high activity with isocitrate, but is inactive with 3-isopropylmalate.
Interaction partners:
Sequence:
MAYRICLIEGDGIGHEVIPAARRVLEATGLPLEFVEAEAGWETFERRGTSVPEETVEKILSCHATLFGAATSPTRKVPGFFGAIRYLRRRLDLYANVRPAKSRPVPGSRPGVDLVIVRENTEGLYVEQERRYLDVAIADAVISKKASERIGRAALRIAEGRPRKTLHIAHKANVLPLTQGLFLDTVKEVAKDFPLVNVQDIIVDNCAMQLVMRPERFDVIVTTNLLGDILSDLAAGLVGGLGLAPSGNIGDTTAVFEPVHGSAPDIAGKGIANPTAAILSAAMMLDYLGEKEAAKRVEKAVDLVLERGPRTPDLGGDATTEAFTEAVVEALKSL
Protein: Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3) (P52757)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Ras-related C3 botulinum toxin substrate 1
- Probable serine carboxypeptidase CPVL
Sequence:
MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPREVENRPKYYGREFHGIISREQADELLGGVEGAYILRESQRQPGCYTLALRFGNQTLNYRLFHDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYISKMTTNPIYEHIGYATLLREKVSRRLSRSKNEPRKTNVTHEEHTAVEKISSLVRRAALTHNDNHFNYEKTHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKRIKKVYCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFGPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF
Protein: Snaclec mamushigin subunit alpha (Q9YGG9)
Organism: Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Function: Binds to platelet GPIbalpha (GP1BA) and enhances platelet aggregation at low-shear stress. At high-shear stress, blocks platelet aggregation in a dose-dependent manner.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MGRFIFVSFGLLVVFLSLSGAEDDSDCPSDWSSNGRFCYKLFQQKMKWADAERFCTEQRTGAHLVSIESNTEAAFVNQMISENIKKTDYVWIGLTVQNEEQQCKSRWSDRSSVSYENLVKPNSKKCFVLKEYEGSRKWFNVYCGQKYAFMCKFLRPR