wanglab/gogpt-training-data huggingface dataset:
Protein: Metallothionein B (MT-B) (P68501)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Interaction partners:
Sequence:
MDPCECSKTGSCNCGGSCKCSNCACTSCKKSCCPCCPSDCSKCASGCVCKGKTCDTSCCQ
Protein: Rab3 interacting molecule, isoform R (A0A0B4K7E7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDEMPDLSHLTPHERMQIENVLMRQKQEEEKQNEIMRRKQDEVVTLEMQIRQRSEQQKKAGVELDATCHICLKTKFADGVGHICHYCNIRCCARCGGKVTLRSNKVIWVCILCRKKQELLSKTGQWINKTAAQQDGFIRRIEPDGSSDISQHPIVDPHDTTDKRPKLERTRSAAEKENLPMQRAGSMLRRQYSQQEQPTNRRLSASDSGMDPVMSPGQQMQHHQQQQRARMQPMNPQQAQQGYGMQQQQQPRSGGAYPDDDPRYYQGELDGLMRQHPHLAHPSQVQPQHTPQSHSQQQQSQHQQQHLMPQQHRPSPQQHSQQQQQQQQHSQQFAARQQQHQQQQHQQQVQQSYHAQIHQQPQQHPHPHSQQQQHHQQMQHQHGQSVPQMGGYQKPPPLTRNLTISGGHAMDSSAYSQQQQQQQRRALAGSQYASQQQRSFSSSEEEFQHQLLAAQGAVTVTAGSDYDGGRLQVRTSLDPWRQQRSLNERDLLSSGGGGGGGVGGADFRHLSHATQRLYASADQRDRYELQLQHRERLEQYPLTRTARLDVQQRNSLNRSNHERQFSGGGAGVGPGGAGGGGAAGAYRRAPPLAAAGGGGSSSSSTTSSSYYPQSKPQIVIGPGSGYDRGSGSMASMASAAAATAADAQGQAARNSQRGGLLGATRGGGGSSSVSSTEAAYWDEPATSSSSSAAQDSRRFTERRIKKTVRFDAHDEEASILASSSLPPVTAILPSTAVDVGAATILSSGKSLDAVGVGGADWSRWEAERQGSQDSATKDSGIDTSSTFTSSEDSNRGDGPKNPVNWQTSADNTRLIGHMILRKYYDGEDILGLKVNGGQPLATGGSVSGAGTGAAIGAGGPCGAIVEKVKRGSVADLEGRIRPGDEILEWNGRGLHNKSADEVYDIIDESRLDAQVELIVSRPIGSGGGSGGSSANVSPISGASGGSANSVPARRSSANFPHSGLASSMAGSAVVSSGGRYLQRKAPAVEAIEIHRDKPSVLITSPGSPDIHTSVSGPGSVSGSGLRQRGGVGQTQRLGPSHSTHSHSSSGSGSGSGSSTSSVHAPASAHGPVHASASASGSAPGGLHGTTTAGHHHHPHPHHYHPHQHPLPHPHQHQGPPAAHLQGHGVGGGIGMGSGSGTTTQPIPIEGRLQLKLGYDQNTLQLIVTLVCATGLSLRQSGAGRNPYAKVFLLPDRSHKSKRRTKTVGTTCEPRWGQTFVYSGLRRCDLNGRLLEVTLWDYVRYGANDFIGEVVIDLAHHILDDEAEWYQLQPHQDTSYLLRDEGSDVDGLILTPTDHLSPPSTMSRLSDSDTTSDCDIDGMTPGASISSMGSSASPPPLLELDLNERRSRRDMSPQGRKRVAGMVARDYRTVSGIGQSYHNQASATGYYRRGGGNGVGSAIGPGGMSLSQRSHSAAPSDGYHSSGVGGAASGGPAYGYRSTSPRRGSLSPPDDRYIDYPVLPVHGSSPNAPSVYQGPGGVSSAAASASQQQRFQSRSATATPTGSPKKRQLPQVPQTSRSAMLRDRLGQDFDERLASGGRFGRHRTRQPHHQATYRSTGMGGWERHYTGLSDSDLHSMDARMRPRHSLSPDKDFMGEFGDSDMESVVSVTSSAFSTQSERPRTSRGLSEYDKDKNGAEEAGGSKSAEGAGAEDKVDGSLSDTANDRKKGGGVDQERSPKGGSGMGKKSNSTSQLSATGRKRRMGFGKKGKNSFTVHRSEEVLPGDITRELRTGGGLGVSLGGAGGAAGGSGGAGGGGLSRGSSSEVDAIEQFFGDGAGGERFSPSLRNDGALNEFVDGLGPGQLVGRQVLGAPSLGDIQLSLCHQKGCLEVEVIRARGLQQKAQSKMLPAPYVKVYLVSGKRCVDKMKTSSARRTLDPLYQQQLVFKQSYTGCILQITVWGDYGRIEKKVFMGVAQIMLDDLNLSNIVIGWYKLFGTTSL
Protein: Nucleophosmin (A0A140VJQ2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKAH
Protein: phenylalanine--tRNA ligase (EC 6.1.1.20) (Q86B36)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTAETDVRSTENLPQQILDFLQESNEFNSIQLAQQWNLDHQKVIGAIKSLLANEGVLTTKDVTEKRLELTNEGVQFANEGSPEYLVFEFVGTDGAAQADIQKKPFGKIGMAKAMQFKWVSVDKGRVVRQATEVTDSTRKQLESLRIGSSDVSENEKKELKKRKLISEVNIKALVVSKGTSFTTSLAKQEADLTPEMIASGSWKDMQFKKYNFDSLGVVPSSGHLHPLMKVRSEFRQIFFSMGFSEMATNRYVESSFWNFDALFQPQQHPARDAHDTFFVSDPAISTKFPEDYLERVKTVHSKGGYGSAGYNYDWKIEEAQKNVLRTHTTAVSARQLYQLAQEGFRPSKLFSIDRVFRNETLDATHLAEFHQVEGVIAEKNLSLAHLIGIFTEFFKKLGITNLRFKPTYNPYTEPSMEIFAYHQGLTKWVEIGNSGMFRPEMLLPMGLPADVNVAGYGLSLERPTMIKYGINNIRDLFGSKIDLNVVYNNPICRLDK
Protein: Fgr22p (Q5ALJ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Plc2p
- 1-phosphatidylinositol 4-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase PIK1a
- Phosphatidylinositol 4-kinase
- Phosphatidylinositol 3-kinase VPS34
- Phosphatidylinositol-3-phosphatase
- Phosphatidylinositol-3-phosphatase
Sequence:
MVDYKTWLKDIDNNTRISKLSIPGTHNSAACHTALPSVQCQGASVTEQLEHGVRFLDIRVGKLFVGNDVKDLQVIHGKFPVKIPFPLKLNDSLEEVYKFLAHNSSETVIVSIKQEGSDDWDNSQDEFGKLIWDRYVNPNKDRWYLNTDIPKLGDARGKAILFRRFGVQDEQLKKQFGFSASSWAYNTTNDDRGQFVVQDFCEVNTADDLPKKIDYVKDLAKRAQDYTSKGDDKVFLNFTSASNFFDQSCWPQPIAEAMIKGNIQETFHKGVGIIVLDYAETDNWKLPEALIDTNF
Protein: Pineapple eye protein (Q9VKW2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for survival of imaginal disk cells possibly by regulation of cell apoptosis. Required for germline stem cell self-renewal through mediation of BMP signaling.
Interaction partners:
- Plexus, isoform A
Sequence:
MEDNKELQCLICKYSDTDDLVFGEWMIVRNLQVHYFCLLLSTHLPQRGGDSSGILGFLLRDIREEAAAAEKRKCWYCNKIGASLQCDRCRSLFHLKCGLENRAVFEFCGQYKSYCYKCRPMDDYKRQLQSNPPRNATCPICFSSIYKVELHCVVYGDCCRLGFAHKKCMRQYALTSGYYLRCIWCRSERFRDSIRLQSVFVPDRDATWEKQRNAYRELHERNLKCDQPNCLCPSGRTYNRLSWVILCCSSCAATSAHLKCLVGALRLPKKRERTDFKCSMCLDVERRIAEGPARTTEETNADGDNQVDGSFYVQKLGPDAATRSLTQTPVFSEEDESERSSNITVIFSQPKSNATSERLSLSPPQEEMIVEIPDSPEASPKTSIDENHSPQPIARRDTSDSPQPIAASEIPDSPQPTAASEIPDLPQTTAINVNPELTQQTALNTIPHSPQPEASFSTQLVSQTFDCPQPQEQAVAKAPNSPSLPKEDPNTLLVLKSGFQCPGEPFFYLVIYEFEHGTCMGECIGTCVLRFKEDDPRIQDTSQAALERVNITPDDVWCRSEDRGIFEHIEKFHEWYRSEGFS
Protein: RNA 3'-terminal phosphate cyclase-like protein (Q9JJT0)
Organism: Mus musculus (Mouse)
Function: Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9Y2P8}.
Interaction partners:
- BMS1 homolog, ribosome assembly protein
- U3 small nucleolar RNA-associated protein 4 homolog
- Periodic tryptophan protein 2 homolog
- Bystin
- WD repeat-containing protein 43
- U3 small nucleolar RNA-interacting protein 2
- HEAT repeat-containing protein 1
- WD repeat domain 36
- Nucleolar complex protein 4 homolog
- U3 small nucleolar RNA-associated protein 18 homolog
Sequence:
MATQAHSLSYAGCNFLRQRLVLSTLSGRPVKIRRIRARDDNPGLRDFEASFIRLLDKITNGSRIEINQTGTTLYYQPGLLYGGSVEHDCSVLRGIGYYLEALLCLAPFMKHPLKIVLRGVTNDQVDPSVDVLKATALPLLKQFGIDGESFELKILRRGMPPGGGGEVLFSCPVRKVLKPVQLTDPGKIKRIRGMAYSVRVSPQMANRIVDSARSILNKFIPDIYIYTDHMKGVSSGKSPGFGLSLVAETTNGTFLSAELASNPQGQGAAVLPEDLGRNCAKLLLEEIYRGGCVDSTNQSLVLLLMTLGQQDVSKVLLGPLSPYTIEFLRHLKSFFQVMFKVETKPCGEELKGGDKVLMTCVGIGFSNLSKTLK
Protein: Uncharacterized membrane protein YML131W (Q03102)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- NADPH-dependent methylglyoxal reductase GRE2
Sequence:
MVLAKQWVLKNLPTPGEPFNFHFHDPACTFELIEKELSSEQLKDGELLLETTYLSNDPAQKFWISSMDKNYAKGVQPGEIIPARGIGKVLASRNKAFSPGDYVSAVTGWTTHAIISQENVQGLRKLDKNKVGKLWWYLSVLGGTSLTAYFIFFTYAQLQEREEDYGKVYLISGAAGAVGTVCIQLALNVFKASKVIAIAGGPEKVAFVESFGDNVVGVDYKDPSFKQKLIEAAGGENTVDYFIDNVGSNVLEAGVLLLKQRAMLIACGAISAYNDPSKFVFKGYSFILTKRLVVKGVLVTDNIDDFPKALDKLGSLVKHGKIDLLKSATLEDGTGDKFKNVPLIWKGLFSGVNKGKLITKVNNEE
Protein: Transmembrane protein 65 (Q4VAE3)
Organism: Mus musculus (Mouse)
Function: May play an important role in cardiac development and function. May regulate cardiac conduction and the function of the gap junction protein GJA1. May contribute to the stability and proper localization of GJA1 to cardiac intercalated disk thereby regulating gap junction communication. Regulates mitochondrial respiration and mitochondrial DNA copy number maintenance (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26403541}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6PI78}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the intercalated disk in ventricular tissue and cardiomyocytes. {ECO:0000269|PubMed:26403541}.
Interaction partners:
Sequence:
MSRLLPLLGSRTARSLRPGPAAAPRLPSWCCCGRGLLALGVPGGPRLLGTHPKKEPMEALNTAQGARDFIYSLHSTERSCLLKELHRFESIAIAQEKLEALPPTPGQLRYVFFHNAIPFVGFGFLDNAIMIVAGTQIELSIGIILGISTMAAAALGNLVSDLAGLGLAGYVEALASRLGLSIPDLTPKQVDMWQTRVSTHLGKAVGVTIGCILGMFPLIFFGGSEEDEKLETTN
Protein: Pescadillo homolog (B2RDF2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03028}. Chromosome {ECO:0000256|HAMAP-Rule:MF_03028}. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. {ECO:0000256|HAMAP-Rule:MF_03028}.
Interaction partners:
Sequence:
MGGLEKKKYERGSATNYITRNKARKKLQLSLADFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIRFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNTVERLKDNKPNYKLDHIIKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFMHYIIAARALRKVFLSIKGIYYQAEVLGQPIVWITPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQLLNLHYPPKLEGQAQAEAKAGEGTYALDSESCMEKLAALSASLARVVVPATEEEAEVDEFPTDGEMSAQEEDRRKELEAQEKHKKLFEGLKFFLNREVPREALAFIIRSFGGEVSWDKSLCIGATYDVTDSRITHQIVDRPGQQTSVIGRCYVQPQWVFDSVNARLLLPVAEYFSGVQLPPHLSPFVTEKEGDYVPPEKLKLLALQRGEDPGNLNESEEEEEEDDNNEGDGDEEGENEEEEEDAEAGSEKEEEARLAALEEQRMEGKKPRVMAGTLKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDEAVRSEKKAKKARPE
Protein: Seminal plasma protein PDC-109 (BSP-A1 and BSP-A2) (Seminal vesicle secretory protein 109) (SVSP109) (P02784)
Organism: Bos taurus (Bovine)
Function: Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins.
Subcellular location: Secreted.
Interaction partners:
- Spermadhesin-1
- Metalloproteinase inhibitor 2
- Spermadhesin Z13
- Seminal ribonuclease
Sequence:
MALQLGLFLIWAGVSVFLQLDPVNGDQDEGVSTEPTQDGPAELPEDEECVFPFVYRNRKHFDCTVHGSLFPWCSLDADYVGRWKYCAQRDYAKCVFPFIYGGKKYETCTKIGSMWMSWCSLSPNYDKDRAWKYC
Protein: Atypical kinase COQ8B, mitochondrial (M0QZZ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWLKVGGLLRGTGGQLGQTVGWPCGALGPGPHRWGPCGGSWAQKFYQDGPGRGLGEEDIRRAREARPRKTPRPQLSDRSRERKVPASRISRLANFGGLAVGLGLGVLAEMAKKSMPGGRLQSEGGSGLDSSPFLSEANAERIVQTLCTV
Protein: Carbohydrate-binding domain-containing protein (Q54SH6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- HECT-type E3 ubiquitin transferase
Sequence:
MKKRVTIRFYVKKKLEYGQRLKVCGSVRGLGSWNSKSAIQMNWTENDWWTGEFQFEATSNLPKNNFKLETSSYYFRNKNQYHNNNNNNNNNEGFIDQQQINNLFSNSKKQNHLPKSSSSSSSSFSSSSISSYTVEEDDYFGNNNNNNNNYNNQSVDNNSFMNNQMSSYDENNNNNNNNNNNNNNNNNNNGYNNGYNSDTLNYGCGDGSSNSVNYQLSNSQSLSPSLKGTSPQLIEFDYKYMYESYDCQYWEKGANHRVSFMMWSNDFSNEEEEIYIEIRDEYEGGNEVFPTLDYRSLSKVSSPPLYSLDELSLIDSNSNINNNNTTSTPSSSITTTTLTSNNSNDDLVGLQFKYSFLQPLESQIIPRFPAQICTFVVMDEGDSEFHSVNLVSQFFGTDSQKSLRMYPVTRAGSSNTIWIGQIYSPQPMKFEYHYVVTSSNNRGIYWEKEKRTFSTSNCNDNLVINNDGMIKYSDVSDSWVKTGFVGLLEQDYNCSISCVVQLLYHIVPLRNIIKNLGGKIGFPFTQCLAKIFTSMEMGFGTTDISPLPNSIGSQDSAEILDIIVNALIEEISRISKNNNDYSLSIECCKLFEGEQQHTYVCIDKDGRINSMKTSNEKFVNIILPVKGFSSLEDSLEFYKHSEEKSVVGDGSIYESMNEFVTIPDILIFQLDRTDYENRKTIKVSNNFSFPKSLDITSHNGDRVKFKIVGILCHSGSDFYGGGHFFLFIHQNNKFYKFDGSNVSISNNQEAIINNFGGDSNQTAYVLIYQKINQLDSFN
Protein: Right handed beta helix domain-containing protein (Q388V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEATNEGCLTPSWNVSSVRIAFANFMESAPSLLTTHASPATLPAELKKIAGSQSFRVCLQNGDYGQSYIKNGAPCLIMGAAPPAASTDGESADSRKESRGDSGRSLWSVFKQPVKIDAHSLIVFKCVWFANRVEVTGDGPVFFNECMFGAAAQRVHRGISSTESFASVHVSATNLCAFSECEFVHNCGSAADVGGSEIPVLLGSGRATLNVHNSSFLGSGVASTAMMLTDNASLEVENVSVSRCSGHSLIVSDTSSAVVFRSVFSQNSGSIWVRNQGSLEIRDSSLEAVYGGRSNLVLTEKGRCTSHGCTISATATSGFSSGRSLVVARDKAHLSLDTCELFWVNEKGLPEGRCKLPLKVPISGHDRDQLDELGLFLVMLMECSEGTFTRCLLRLPLVEEEGGWCAAVGVLLRSVPRVNTFPLYAVQNSVVYDREWGKRTPTKGKSSATADSQCMWGLVLPYTSDYRHAPDLQQLKSMWTETNHFFEGTGERLKDIAQAVTTYEVYCRATGRSPSMFHADNHENLPSFSTNSYTKEGDFSIVNHPSLENTSPPPASMAEKKPDQEEGTGNKQAQSEDHLRSSVRRTNEDGINSSSTSLTSYGDDEEENNDPSNPPTRRGSPVSVRAKPKNPSNGAASLQTEGKKHSNIVDDADVRQDTVLKEKHRQGNEMSPTANGLVSMPPIFVRAPEEPAAKGHSVSVANGQQNSDRQSGTRGSLQITNLRSLEKRESGRKGERSPNFLDGGSAPSVPRTRNNPVSKKRYKQFNGEKDISMHSDGLLLTCFTPCSASPPRRASSSVGIGELCTHKYYNNVSSASDMKPWDVRTAREMAGRGFELGKNGTYSKVSKGQAESVWDEEENFNYANGLSYASTDKDSSSVSRSRRYNATGSYNGKTYKSFTSARGGLGFHVRRVQSGHADDATARLYDEFLRKWKTTQHFSELLDELRNDQRRRERLSREAMERQAERLHSMGLQTRCERHSPQVAGSGRNYALQRRNEQRLRTNDDTTNDSTAGLCTPESVRRPAHANTTVNSEVVKRRAENGGESSCGGKSPSETVTASDKTPETKQARKGKKRGHTKRKRRKQKH
Protein: SKP1-like protein 21 (AtSK21) (Q8LF97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RING-box protein 1a
- F-box protein 7
- U4/U6 small nuclear ribonucleoprotein PRP4-like protein
- CDT1-like protein b
- RING-box protein 1b
- Cullin-1
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- Cullin-like protein 3
- SKP1-like protein 16
Sequence:
MSEGEMAIIKPEMMKSYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVGSSKNYAISLPQRVNPAMLSLIFDYCRFHQVPGRSNKERKVYDEKFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEEKLEPLKNTMDDPRIRLLNRLYAKKRKELKEREKLKSVEVEEHVDERSVDDLLSFINGRDPKVVKTSKSKKKNKKRKEQKNGSSNGTCEALEKDLHNLDSKSQSAEIVDNTASCLGDVSNLPSMEDDIFTPKTEFEDGYIDDEIDPALKELLDREVEDFARRLNSSWVLSIGQERQPVNFSINGNGTSRRLTGPAAGHK
Protein: Circadian clock oscillator protein KaiB (Q79PF5)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB switches to a thioredoxin-like fold (KaiB(fs)) in complex with KaiC. KaiB(6):KaiC(6) formation exposes a site for KaiA binding that sequesters KaiA from the CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex that results in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12727879}. Cell membrane {ECO:0000269|PubMed:12727879}; Peripheral membrane protein {ECO:0000269|PubMed:12727879}. Note=From circadian time (CT) 12-16 to CT 20 the major fraction is membrane-associated, is then translocated to the cytosol, where it probably interacts with KaiC and KaiA.
Interaction partners:
- Circadian clock oscillator protein KaiA
- Circadian clock oscillator protein KaiC
- Circadian input-output histidine kinase CikA
- Thiamine-phosphate synthase
- Protein RecA
- Light dependent period A
- Amidophosphoribosyltransferase
- Large ribosomal subunit protein bL21
- Circadian phase modifier
Sequence:
MSPRKTYILKLYVAGNTPNSVRALKTLKNILEVEFQGVYALKVIDVLKNPQLAEEDKILATPTLAKVLPLPVRRIIGDLSDREKVLIGLDLLYGELQDSDDF
Protein: Lanosterol synthase (Q57ZG6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Lanosterol 14-alpha-demethylase
- NAD
- Squalene monooxygenase
- C-5 sterol desaturase, putative
- Lathosterol oxidase, putative
- squalene synthase
- Methyltransferase
- Cytochrome P450, putative
- Delta
- Hydroxymethylglutaryl-CoA synthase
Sequence:
MMLYQRRGRGEMHRPGIRTIVGSGNSAPSSLCAPFPFDSVIPPPPRGLLERFLRRLTSTISWVVSFLLVVCSIPFLLLIHALLVYCDGYNREVVARHRRKWLHQTVPHVRPVRVAPSPNFPLEGWHMRCEDGRQRWHYGRLLNVEEGNELGKAQAEGCPYTPYGEAGNANDDFEDTGATRTGPRGGPDMRAVKEERCRFVERYQLGLTGTAHVKPRGSVEEAMRAGAEFLLRLQHPYSGHWPNDYSGPLFLTPGVIFVRYIVARGNIRNMFPPHADHQHEGDEPCLCGEAERLELIRYIRNYMNEDGGFGQHTEGHSTMLGTVLNYVALRLMGVSDDDSDAARARQWIRGEGGAVSIPTWGKVWLCVLGLYDWDGVNPIPPELSLLPNWIPFSPSRLWCHSRVVSIAFSYLYGLRWRQPDNLLLQCLRYEIYLEPYGNIKWAKHRSNICAKDCYTPLSSVYKVFAAVMSLYEKRPIKFLRRRALEVAWTHIAYDDESTHFICLGPVNKAFDMLITWIREGETSGRYLNHLNRLDDYFFMGPEGLRMSGYNGSQLWDTSFAVQALCACNMELLYPEEMALAHHYVDVAQVQENPVAATQFYRHRTKGAWNFSTRPQAWQVSDCTAEGLRVLLLLRHKPFPHQRIYDAVDQILSLRNRGGGWASYEPTCAPHYVELLNCSDVFKDVMTDYVYTECTSSCVHTLSLFREHFPDYRREDVDRAIRDGVKCMLANQRTDGSYYGSWAVCFTYAAWLCASALRISGEIYGMEGDPTCVRLVNFLLSHQNTDGGWGEDVSACARGVWVDNPSGSQVVNTAWAVMAIMAASGEASSTELRRQLRILKAVSAGIHFIVSRQLSTGDWAQERISGVFNGNNPIHYPGYKNTMPVWALGVYRRWSKTYGQHFPRSMD
Protein: Ab2-427 (Tripartite motif-containing 24) (Q7TP39)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAQRQQVQRRPAPVGSPNPRMQGPIQQPSISLQHPPPRLINFQNHSPKPNGPVLPPYPQQLRYPPSQNIPRQAIKPNPLQMAFLAQQAIKQWQISSGQATPTTASSSSSTPSSPTITSAAGYDGKAFSSPMIDLSAPVGGSYNLPSLPDIDCSSTILLDNIARKDTSVDPGQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNTNYPRSILTSLLLNSSQSSASEETVLRSDAPDSTGDQPALHHENSPNGKSEWPDASQKSPVHVGETRKEDDPNEDCGEWICTFCRDLSKPEVEYDCDAPSHNSDKRKSEGLTKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTPDSEVANAGIKLESYFEELLKNLYPEKRFPKLEFRHDVEDCKFSDDSDDDFVQPRKKRLKSMEDRQLLKTSTNIDLKSLGICETIPISSYLKEKERLRQPTAAHSQPRRHEVWRRKQSGVRTIKRGGPADERLVIAIAEDNIHFGQGLGGTEMESTWKPPPRGLILTSNDSQQAAKREEQSLVLPSGKAQTHNHQQQGNIPSGATVALTSADADACVVIKDGVLNGYRFEFYKHVTFIYFSCVRGCECIHGACGGQRITRRLRTVLLSRRSGELNSDYPVWQQASSPSICHSDKFEEHPDFIRKGRDLVFERLDFSRLNKRGEIHIKLSGIISTGRFKKLVKWLSAVRDAQAESSPGTSHASAPLPNAHLSSVNVDGVEVRRHQGPQHEEEANEAGTEEEAEEVIGTDTEDLPGWPHKALSLGRLLFLNRPNCGILSQFPHNPFTK
Protein: ANK_REP_REGION domain-containing protein (Q1NZ17)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSEEREVSPKDLVVEKNYGQEDIDIPKNDDHEEQEEPRAPTPAEDLSHYVKEPSPPVSLAATDLDSNNGADEGNGEGHDEPKLIPLTTRQSLDSDPGDFEKVDKEEAAKLADTSPAVAGIAAAIPIISAQVEEEQNDPTVLESEHEPSFVPPASAHQAPSTKATVVEESKQVPEGREPSDLATWIHNNPDVVRNVAAAAAVAGVAGLGYYVYVKKFK
Protein: Sulfate transporter 1.1 (AST101) (High-affinity sulfate transporter 1) (Hst1At) (Q9SAY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity H(+)/sulfate cotransporter that mediates the uptake of the environmental sulfate by plant roots under low-sulfur conditions. Plays a central role in the regulation of sulfate assimilation.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Assimilatory sulfite reductase
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Cysteine synthase 1
- ATP-sulfurylase 3, chloroplastic
- ATP sulfurylase 4, chloroplastic
- Protein SULFUR DEFICIENCY-INDUCED 1
- Adenylyl-sulfate kinase 1, chloroplastic
Sequence:
MSGTINPPDGGGSGARNPPVVRQRVLAPPKAGLLKDIKSVVEETFFHDAPLRDFKGQTPAKKALLGIQAVFPIIGWAREYTLRKFRGDLIAGLTIASLCIPQDIGYAKLANVDPKYGLYSSFVPPLIYAGMGSSRDIAIGPVAVVSLLVGTLCQAVIDPKKNPEDYLRLVFTATFFAGIFQAGLGFLRLGFLIDFLSHAAVVGFMGGAAITIALQQLKGFLGIKTFTKKTDIVSVMHSVFKNAEHGWNWQTIVIGASFLTFLLVTKFIGKRNRKLFWVPAIAPLISVIISTFFVFIFRADKQGVQIVKHIDQGINPISVHKIFFSGKYFTEGIRIGGIAGMVALTEAVAIARTFAAMKDYQIDGNKEMIALGTMNVVGSMTSCYIATGSFSRSAVNFMAGVETAVSNIVMAIVVALTLEFITPLFKYTPNAILAAIIISAVLGLIDIDAAILIWRIDKLDFLACMGAFLGVIFISVEIGLLIAVVISFAKILLQVTRPRTTVLGKLPNSNVYRNTLQYPDAAQIPGILIIRVDSAIYFSNSNYVRERASRWVREEQENAKEYGMPAIRFVIIEMSPVTDIDTSGIHSIEELLKSLEKQEIQLILANPGPVVIEKLYASKFVEEIGEKNIFLTVGDAVAVCSTEVAEQQT
Protein: Cell division protein FtsZ (P17865)
Organism: Bacillus subtilis (strain 168)
Function: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
Interaction partners:
- Cell division protein SepF
- Cell division protein ZapA
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsA
- Septation ring formation regulator EzrA
- Septum site-determining protein MinC
- Cell division inhibitor MciZ
- Processive diacylglycerol beta-glucosyltransferase
- Cell shape-determining protein MreB
- Septum site-determining protein DivIVA
Sequence:
MLEFETNIDGLASIKVIGVGGGGNNAVNRMIENEVQGVEYIAVNTDAQALNLSKAEVKMQIGAKLTRGLGAGANPEVGKKAAEESKEQIEEALKGADMVFVTAGMGGGTGTGAAPVIAQIAKDLGALTVGVVTRPFTFEGRKRQLQAAGGISAMKEAVDTLIVIPNDRILEIVDKNTPMLEAFREADNVLRQGVQGISDLIATPGLINLDFADVKTIMSNKGSALMGIGIATGENRAAEAAKKAISSPLLEAAIDGAQGVLMNITGGTNLSLYEVQEAADIVASASDQDVNMIFGSVINENLKDEIVVTVIATGFIEQEKDVTKPQRPSLNQSIKTHNQSVPKREPKREEPQQQNTVSRHTSQPADDTLDIPTFLRNRNKRG
Protein: Tyrosine-protein kinase receptor ver-3 (EC 2.7.10.1) (Vascular endothelial growth factor receptor related 3) (Q21038)
Organism: Caenorhabditis elegans
Function: Receptor tyrosine kinase which may be involved, downstream of pvf-1, in the positioning of ray 1, the most anterior ray sensillum in the male tail.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein let-756
- Sex muscle abnormal protein 5
- Protein ver-2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma plc-3
- G-protein coupled receptors family 1 profile domain-containing protein
Sequence:
MKLKLTVLLILVHASASYKPPAIEVEDYQVQEHDSIGKFVELEEHTRLILKCSAHHNGDLKYNFPSMEGNVGYDENNFKKRMEEYYDDAFGDKVLTLNDVRESDTGTYSCSSMEHSSLNDTIYVFVHRKKVFLPLKSVMIIYKQGEVMVPCKTTKFVDKSDIELYASNVLVKEASKYNYDQRYGFKITKKLYSEKQIVDVNFECRYKKEENQTATYIITEKEASSDDGYHFSWEKGFQWPHVGYNFSLTCNLNYNGSKIFHGYTNKLSIECPQCSHDPGSHVHVDRHRIIGNKISTTVRIQHLELEDSGKYTCIWEHENKETKYTDYHLYVAPKKAQIKVIETSPTIMRIKENRATSLTAKFAIYPFEKESYTAKWSRIYNSSIHEGPQSETIINDDFRKIAATSFGDGAFSENLDIKAFAVSTNMSGTYVLSISHMDTVQVVQWEVAIENDEPDVQITVREPSSFFISNQEYYKPDTNLHIECISISIPPADVVFEYKTKNSEQFQEIEPNKLVSVGGTFDRGLIYNVTFTEGMDLKCSSIRKGNRAITVNKLIKIGEGFEVRPHHEKSSKATESEPSKIIYEGDNVKLTCVFPLDSDDWSVSWRFENSKSSDISSIPTTTETEIKQYSKHLILNLRDVTTSFTGTYTCVVKNEDSEKLLETSIDVKAISKPSITGGNSNAVVIVDYDQYFEINCNMTGTPPPVYQWFKDGNPYTHGDVDGSILRVSRARGEDDGEFHCLATNRAGDKLNSIEVQVNNAPKGSLFFYWFLALLLLISIIAVFLLTCKLRASNRLTKQKDIALNTLYETMIKHQAGPLPEEMKDLPVEERTYYLPYNNDYEIDPVNLEILNPIGSGHFGVVKKGLLGMAYPKSKIESKTRLPVAVKSSTNPFNVELQKMMAEELKVMCAIPKNPNVLALIGAVTKNMRQGQLYIVTEFIDGGNLREFLQAHRNTFINELVEDEHVPVDDSYLVPNSVKKKIYKFDEKLGEGTRLLVEDPDALCTSDLLSIGLQIAKGMAWLADVPCVHRDLACRNVLITKTKIVRIADFGLSKKHTNKTYYRTKKSKDTPLPVRWMPLECIEEFKFTQKSDVWSFGICLYEIFTLGGTPYPNCDTFNVIEFIRNGNRNKQPEYCHDEIYELMKVCWQFNPKDRPTFNDCITFFENHMRDSSSQFLERVENMLHTEMQEQSKLDDWIQDSRPDVPNVSFQKSPKKQKEERYLIVESHA
Protein: Delta(14)-sterol reductase (EC 1.3.1.70) (C-14 sterol reductase) (Protein FACKEL) (Sterol C14-reductase) (Q9LDR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Required for cell division and expansion and is involved in proper organization of the embryo.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sterol 14-demethylase
- Probable 3-beta-hydroxysteroid-Delta
- Delta
- Delta
- Methylsterol monooxygenase 2-2
- Putative Delta
- Methylsterol monooxygenase 2-1
- Cycloeucalenol cycloisomerase
- Cycloartenol-C-24-methyltransferase
- Ergosterol biosynthetic protein 28
Sequence:
MLLDMDLGVLLPSLQSVYVLVFYFVYLAVAGEILPGKVIRGVLLSDGSQLRYRCNGLLALILLVAILGICAKLGIVSPLVVADRGLELLSATFIFCVLVTLALYVTGRSSSNKGSSLKPHVSGNLVHDWWFGIQLNPQFMSIDLKFFFVRAGMMGWLLINLSILAKSVQDGSLSQSMILYQIFCALYILDYFVHEEYMTSTWDIIAERLGFMLVFGDLLWIPFTFSIQGWWLLHNKVELTVPAIVVNCLVFLIGYMVFRGANKQKHIFKKNPKTPIWGKPPVVVGGKLLVSGYWGIARHCNYLGDLMLALSFSLPCGISSPVPYFYPIYLLILLIWRERRDEVRCAEKYKEIWAEYLRLVPWRILPYVY