wanglab/gogpt-training-data huggingface dataset:
Protein: L-lysine N6-monooxygenase MbtG (EC 1.14.13.59) (Lysine 6-N-hydroxylase) (Lysine N6-hydroxylase) (Lysine-N-oxygenase) (Mycobactin synthase protein G) (P9WKF7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Flavoprotein monooxygenase required for N-hydroxylation of the two acylated lysine residues during mycobactin assembly, thus producing the hydroxamate groups necessary for iron sequestration. Is also able, but less efficiently, to hydroxylate L-lysine (non acylated) in vitro. Shows 5-fold preference for using acetylated lysine over lysine.
Interaction partners:
- Peptide synthetase MbtE
- Peptide synthetase MbtF
- Phenyloxazoline synthase MbtB
- Protein MbtH
- Polyketide synthetase MbtC
- Polyketide synthetase MbtD
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Salicylate synthase
- Lysine N-acyltransferase MbtK
- Mycobactin import ATP-binding/permease protein IrtB
Sequence:
MNPTLAVLGAGAKAVAVAAKASVLRDMGVDVPDVIAVERIGVGANWQASGGWTDGAHRLGTSPEKDVGFPYRSALVPRRNAELDERMTRYSWQSYLIATASFAEWIDRGRPAPTHRRWSQYLAWVADHIGLKVIHGEVERLAVTGDRWALCTHETTVQADALMITGPGQAEKSLLPGNPRVLSIAQFWDRAAGHDRINAERVAVIGGGETAASMLNELFRHRVSTITVISPQVTLFTRGEGFFENSLFSDPTDWAALTFDERRDALARTDRGVFSATVQEALLADDRIHHLRGRVAHAVGRQGQIRLTLSTNRGSENFETVHGFDLVIDGSGADPLWFTSLFSQHTLDLLELGLGGPLTADRLQEAIGYDLAVTDVTPKLFLPTLSGLTQGPGFPNLSCLGLLSDRVLGAGIFTPTKHNDTRRSGEHQSFR
Protein: STE20-like serine/threonine-protein kinase (STE20-like kinase) (EC 2.7.11.1) (STE20-related serine/threonine-protein kinase) (STE20-related kinase) (O08815)
Organism: Rattus norvegicus (Rat)
Function: Mediates apoptosis and actin stress fiber dissolution.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase PLK1
- Cyclin-dependent kinase 1
Sequence:
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKEEDDDDETESALPIPANKRASSDLSIASSEEDKLSQNACILESVSERTEHNTSGDKFSNKVLSEKPTPEGPEKTVDVDGPANDVNLETVAEPNDQAVGFHENGREKKRPQLESQPDTEDQQTVDVNLVGEGNDSNIVILETNTDCLKPEEDRNEENQEIIENKLTQSEEIKDIHIQTMDLVSQETGEKEADFQAIDNEVGFTKEETQEKLGKDDKTHKVVISDITSEVGTDEPPGDTQKSAEQSQDAEGGAGEEAPEPAQTLTEKATEGPEAHGAEEEPRSGERVEDKQLEQQSAVCEGEGQVTSTSESTRATTEEPETDEVDQVSESNSIEELERLGVTGAEEQALGSKGEAATELDLEREENAQELPVKAEPQAPAASQASEPPPVLIPSINIHSENTENKGEMGALPKPETILPPEPENGKGNDTDSGTGSTVENSSSDLNLSISSFLSKTKDSGSVSLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRLLQKEEQKAQQQLNGKLQQQREQIFRRFEQEMLSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNMLRNRKKEEQEFVQKQQQELDGALKKIIQQQKAELANIERECLNNKQQLLRAREAAIWELEERHLQEKHQLLKQQLKDQYFIQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDREKIKQFAAQEEKRQKNERMAQHQKHESQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSAQSRGCLQTSHPSSTRAPAWAG
Protein: Uncharacterized HTH-type transcriptional regulator YdcI (P77171)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YhjC
- Uncharacterized HTH-type transcriptional regulator YneJ
- HTH-type transcriptional activator AaeR
- HTH-type transcriptional regulator DmlR
- Uncharacterized protein YdcA
- HTH-type transcriptional activator TtdR
- Uncharacterized HTH-type transcriptional regulator YcaN
Sequence:
MEKNSLFSQRIRLRHLHTFVAVAQQGTLGRAAETLNLSQPALSKTLNELEQLTGARLFERGRQGAQLTLPGEQFLTHAVRVLDAINTAGRSLHRKEGLNNDVVRVGALPTAALGILPSVIGQFHQQQKETTLQVATMSNPMILAGLKTGEIDIGIGRMSDPELMTGLNYELLFLESLKLVVRPNHPLLQENVTLSRVLEWPVVVSPEGTAPRQHSDALVQSQGCKIPSGCIETLSASLSRQLTVEYDYVWFVPSGAVKDDLRHATLVALPVPGHGAGEPIGILTRVDATFSSGCQLMINAIRKSMPF
Protein: Clc-like protein 2 (Q11085)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Chloride channel protein clh-3
- Chloride channel protein
- CBS domain-containing protein
- Clc-like protein
- Chloride channel protein
- Chloride channel protein
- Clc-like protein 5
- Chloride channel protein
- Neurexin like receptor 1
Sequence:
MSQAVSYAILVLTIIAFLLTAAALCTPAWQVVYAREIRQWVQSGLWLSCQTRPNGMYSCTYTFSHDDFNTYFSDEVSGFRTPSFYPWQRTLFHIYLISQAFAMLSLISFCVSVSHKESKMPNILRSVFLVLAAVIAFGCLIAFAVYSYMVEYRFFHVSVSGIYEKHRGYSWYIALTGAFVYLVAIILSVVHVLLQARNSNTTMSRQNINSSLQSDFFEYQYHPNRSMESFEDRFAMRTLPPVPRQEKKTTVF
Protein: Ionotropic receptor 75c (Q9VVL2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ionotropic receptor 8a
- Adenylate cyclase type 3
- Odorant receptor 35a
- Odorant receptor 22a
- Ionotropic receptor 41a
- IP13856p
Sequence:
MTSWPLYRLIVFNLLEINLSNLMVFHCWSIKEAFPLVEMLNQNGIFSQYIDVQNPDNLANVHKEYLDSDLVRLGVFLDLGCDKAELVTNQSSRARLYNQNLHWLLYDEAGNFTKLTQLFEGANLSLNADVTYVSREDEERFILHDVYNKGSHLGGKLNITVDQTLQCNRSHCQVKEYLSELHLRPRLQHRMDLSSVTFRLAALVSVLPINSSEEELLEFLNSDRDSHMDSISRIGNRLIMHTQEILGFKLHYIWCGTWSVQDAFGGAIGMLTNESAELCTTPFVPSWNRLHYLHPMTEQAQFRAVCMFRTPHNAGIKAAVFLEPFMPSVWFAFAGLLIFAGVLLWMIFHLERHWMQRCLDFIPSLLSSCLISFGAACIQGSYLMPKSAGGRLAFIAVMLTSFLMYNYYTSIVVSTLLGSPVRSNIRTIQQLADSSLDVGFDTVPFTKTYLVSSPRPDIRSLYKQKVESKRDPNSVWLSPEEGVIRVRDQPGFVYTSEASFMYHFVEKHYLPREISDLNEIILRPESAVYGMVHLNSTYRQLLTQLQVRMLETGITSKQSRFFSKTKLHTFSNSFVIQVGMEYAAPLFISLLVAYFLALLILILEICWARYAKKKFSTIIPQNQ
Protein: Sodium channel regulatory subunit beta-4 (Q7M729)
Organism: Mus musculus (Mouse)
Function: Modulates channel gating kinetics. Causes negative shifts in the voltage dependence of activation of certain alpha sodium channels, but does not affect the voltage dependence of inactivation. Modulates the susceptibility of the sodium channel to inhibition by toxic peptides from spider, scorpion, wasp and sea anemone venom (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8IWT1}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8IWT1}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 1 subunit alpha
- Sodium channel protein type 7 subunit alpha
- Sodium channel regulatory subunit beta-3
- Sodium channel protein type 8 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 11 subunit alpha
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
Sequence:
MSRAGNRGNTQARWLGTGLLGLFLLPMYLSLEVSVGKATTIYAINGSSILLPCTFSSCYGFENLYFKWSYNNSETSRILIDGIVKNDKSDPKVRVKDDDRITLEGSTKEKTNNISILLSDLEFSDTGRYTCFVRNPKEKDLNNSATIFLQVVDKLEKVDNTVTLIILAVVGGVIGLLVCILLLKKLITFILKKTREKKKECLVSSSGNDNTENGLPGSKAEEKPPTKV
Protein: Translationally-controlled tumor protein (TCTP) (Fortilin) (Histamine-releasing factor) (HRF) (p23) (P13693)
Organism: Homo sapiens (Human)
Function: Involved in calcium binding and microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9059837}.
Interaction partners:
- Large ribosomal subunit protein uL13
- Elongation factor 1-beta
- Elongation factor 1-gamma
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL10
Sequence:
MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC
Protein: DNA polymerase III subunit alpha (EC 2.7.7.7) (Q9A700)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Beta sliding clamp
- DNA-directed DNA polymerase
- DNA polymerase III, delta prime subunit
- DNA polymerase III subunit gamma/tau
- DNA polymerase III subunit epsilon
- DNA polymerase III, chi subunit, putative
- Exonuclease
- DNA polymerase IV
- Protein ImuB
- Protein ImuA
Sequence:
MSDAEGQGFVHLRVRSAYSLLEGAIKADQIGKLAAEAKMPAAGLADRANLFGALEYSSYAKDAGVQPIIGCAIPVVGIGGGPTERWARAPTLMLLAQNERGYLNLSELSSIAYLDSAELPEPVVPWAKVAEHSEGLILLSGGTDGPVDALFAAGKTAEASAALAEMHRVFGDRFYVELQRHGLPRQAAAEPGLVNWAYDHDVPLVATNDVYFAKPGFYDAHDALLCISDGAFVGQDERRRVTPEHWFKPAEEMRKLFADLPEACDNTLDIARRCAFMVHKRDPILPSFPTGDGRNEAEELEHQAREGLKMRLEGLTLSAPEEEYWKRLDFELGIIKKMGFPGYFLIVSDFIKWGKAHGIPVGPGRGSGAGSLVAWVLTITDLDPLRFGLLFERFLNPERVSMPDFDVDFCQERREEVISYVQEKYGRDRVAQIITFGSLQARAVLRDVGRVMQLPLGLVDRLCKMVPNNPAAPVTLAQAIDLEPRLKQAKKEDANVSACLDVALQLEGLFRNASTHAAGLVIGDRPLTQLTPLYKDPRSDLPATQFNMKWVESAGLVKFDFLGLKTLTVLDRAVKHLKKRGFEIDLGKLPFDDAKTYELLASGQTVGVFQLESQGMRDTLRKMRCGSIEEITALISLYRPGPMDNIDTFVDCKFGRKPVDTLHPSLEAVLKETYGVIVYQEQVMQIAQILAGYSLGEADLLRRAMGKKKKEEMDLQKIRFVSGAKEKNVPEEQSGSIFELVAKFAGYGFNKSHAAAYAFISYQTAWLKANTPVEFFAASMSLDLSNTDKLAVFHQDARRFGITVRAPDVNRSGADFEVENGEVLYALGAIRNVGLEAMKHLVAVRAEGGPFRDVFDFVERIDPRQVNKRAIENLARAGAFDSIHKNRAQIVASADVLIAHAQSCHADRQGGQGGLFGSDPGAGRPRLSKTENWNQVDLLDEELSAVGFYLTGHPLEDMVGMLRRRRTVMLAEAMAQAEAGAEAFRMCGVVRRRQERASQSGEKFAFVSLSDPTGEYEVLYPPESLRKCRDVLEPGKAVAIKVRAKARDGEVRFFGDDAEPIEKAVENVVAGLRVHLSPSAAEIDALKRRLEPAQAQKGGEVTFVAAIGGGREIELRLPGRYTLDAALRGALKTAPGVALLEDV
Protein: Translocon-associated protein subunit alpha (TRAP-alpha) (Signal sequence receptor subunit alpha) (E9PAL7)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU368074}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU368074}.
Interaction partners:
Sequence:
MRLLPRLLLLLLLVFPATVLFRGGPRGLLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQIMQSRRDKASPRRLPRKRAQKRSVGSDE
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (G5EE54)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQSSSILIYLLTVVGCSIAFLDNTLPLYLFKNLDTKETSTVQTGLVTDKVRRVPPYFSYKLERQYVVGVGGNINLTCVAVGYPMPRVFWKKTDLMVLDDPSTAPIGKNVLTLTHVESTENFTCVAVSALGNIEATTTVIAKELPPPPVNIVVSSVTSESVVITWKPPKYNEAINKYVVNYRLKYSEGRSSRGKTMETLENSLVIDGLVAFQTYEFTVRSAGPVGVGLESLPVEAQTKPSKPATAPVSPQARSLNRDSILVKWGPCEQPNGLITGYKVYYTNDLVTTPIREWKQHDAKSDEFMTTINGLEPDSRYFVRVIAQNSEGDSPLSTLVTVATRQGIPGQPPMLTVKALDSRRMQLTWDKPLYSSPVVGYTVRYNTSDGEKELTLTSPHEKHVVTGLHPDKYYYFRVAAYSDRGQGEFTEPMISKTIASIPLSSPTIVSAAATSSKSVEIRWKGPEQKKLNGVLTAYRINYFRLEDSKTANLESVEYDEDMDDSSSFLDRMSVVVPSDATSYVLSDLLPYSSYEITVAASTMDGYGPESSIRVVKTLEDVPSAPRNFNAELTSATSVKLTWDAPAAANGALLGYYVYLDRMVNGEPVVEKGSKKRIVMIRDSSKRYFELDSLDPNTEYSFRLNAFNRNGDGEFSERKSIITQGIPPEAPEIVSVSLDRDEPPVVARIEWKMPKMKPNETPIEKYNLWLRAQGYPDSYVKAKTVDGTDLSTTISGLWMGVVYDVLLAAENREGRSQNATETIATPVGSPDGEPIDVQYEVMKGKIVVSWRPPSEEKRNGNITSYKAILSAMDATADRYEQPVPAPSTSSTFEVNVRRAYLFKVAAATMKGIGPYSPVLTINPDPAALVGPPTNVRVEATSNSTAVVQWDFESQKADSFVVKYMHEPGNRMDTEKWKQLPVVSIDKENPKRFAVVSDLNAHKPYAFCVLAVKNNRQGPCSDPPTVLESVTPTYMVQNLRVLWKTSNSVQLTWEYNGPRNVGFYVNHTGRKDYVNHELQEKTMSTPGFGQDVDEKHREYLWTNLRPHMMYTIHVGVRTLPPGARKYWPQEVVTITDPTGPPFVDVPKLVDSSGTQPGQQMIRLTPATEEYGPISHYWIILVPANYSTEDVVNLDPIELEKATAEKRAQLARSLSVSPSKKLKRKASEVGDDSQSASYHPKEKRARRATVPGAYVTARLSADRVKQQYRNNQPFIVGDSQLYDGFTNYPLEHNLHYRLMMRAFAKNDVRTKDSFEQRAPMSEKLSRMYSDSVLTEPFTIKSALRGASQKSSPWVGACIAFLVLFSIVGMLICWWLRCNKKSAGRHPRHGSITKVALTGNIMNGGGGIPGETSKLLSTSNEYGRQIMNPYEQMNGNHHMESSMDLYPLPTSHSRSNGYAPVPVAIPSLPNNGNNMTTVSHPAVPIAELANHIERLRMNNNAGFQSEFESIETGQHFTWEHSSADMNKHKNRYANVAAYDHSRVVLSNVEGYPGMDYINANYVDGYDKPRSYIATQGPLPETFSDFWRMVWEEQSVTIVMLTNLEERSRVKCDQYWPSRGTATYGDIEVTLLESVHLAHYTMRTMRLKMVGEPEVREIKHLQYTAWPDHGVPDHPTPFLIFLKRVKTLNPNDAGPIISHCSAGIGRTGAFIVIDCMLERLRYDNTVDIYGCVTALRAQRSYMVQTEEQYIFIHDAVLDAVNSGSTEVPASRLHQHLHILSQPSADQLSGIDMEFRHLTTLKWTSNRCTVANLPVNRPKNRMLSAVPYDSNRVIMRLLPGADGSDYINASWIDGYKERGAYIATQAPTNETAADFWRAIWEHNSPIIAMLVRTNERGQEQCSDYWPLETGVQVGMLVVEPMAEYDMKHYHLREFRISDINTREVRTVRQFHFMEWPDVGKPHTADHFLDFVTQVHNTYAQFGCTGPITVHCCSGAGRTAVFIALSIILDRMRAEHVVDVFTTVKLLRTERQNMIQEPEQYHFLYLAAYEYLAAYDNFS
Protein: Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 pre-mRNA-processing factor 4 homolog) (X2JG22)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADDKSYDSSNNSETEERRAKHKKAKKHKKHKKSSTGKTEKDRHVHKKQKKAKKRPHRTSESTNESDAPENAKLKLSQNCGLSSKFTEIMQKASRNGADFRVGKPLLPTDPSSLVEEITKTIQNKMLPVLEVASSSSESDVPADAASPIILSIIEDELNLEELMRQKALLQARLGAYMSDPEAEDKGDLLPHTHSQQLVVHTKSVLKAVTSVPQPQPSKSAAPLATATSKHANIKKSTTHNSNESDVILLDDSSGGQRTPSPTPEKRRRHASPLPAAPRSRCRRDRRSRDRDRSPPRRRASDQQTQVRPRSRNRNMEDLRQEINRDKQRERRDHSRDRDRRGLDRPPPPTDMRPGRARERDVRPSRMQRSHSRSKFESDRRRERERQKDRDRGGGRVGARSGTDNGDRDRYKGSLSEGQNKLDKESSDEEVNVNIDILEEDDEERIIELRRKKREELLKLGTGQESPAPHNSVSYESRSTSQGSSQRERPLRTPSPTMPCPNPLISEIPKDREDMDNSTSQKTCSAKEKRNEWDMFADQDVDSNFDSPNTIVQNKHQHENPALTDNWDDAEGYYRVRIGEVLDNRYLVNGYTGQGVFSNVVRGRDQARGQANVAIKIIRNNEIMHKTGLRELEILKKLNDADPEDRFHCLRLYRHFFHKQHLCMVFEPLAMNLREVLKKYGKNVGLHIKAVRSYTQQLFLALKLLKKTGILHADIKPDNILVNENNLILKLCDFGSASAISDNEITPYLVSRFYRSPEIILGIPYDYGIDTWSAGCTIYELYTGKILFSGKSNNQMLKFFMDVKGKIPNRIIRKGQFREQHFDQSCNFLYHEIDKLTEREKIVVMPVVKPSRSLQQELIADQNLPDDQHRKVTQLKDLLENMFALDPAKRISLNQALVHPFIQEKM
Protein: Chlorophyll a-b binding protein 3, chloroplastic (Light-harvesting chlorophyll B-binding protein 3) (LHCB3*1) (Lhcb3) (Q9S7M0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Modulates the rate of photosystem II (PSII) state transitions and influences PSII macrostructure. Involved in PSII excitation energy transfer and charge separation during photosynthesis in thylakoids.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16551629}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- DNA repair protein RAD50
- Chlorophyll a-b binding protein CP26, chloroplastic
- Chlorophyll a-b binding protein
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Chlorophyll a-b binding protein CP29.1, chloroplastic
- Photosystem II 22 kDa protein, chloroplastic
- Nibrin homolog
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem II protein D1
- Oxygen-evolving enhancer protein 2-1, chloroplastic
Sequence:
MASTFTSSSSVLTPTTFLGQTKASSFNPLRDVVSLGSPKYTMGNDLWYGPDRVKYLGPFSVQTPSYLTGEFPGDYGWDTAGLSADPEAFAKNRALEVIHGRWAMLGAFGCITPEVLQKWVRVDFKEPVWFKAGSQIFSEGGLDYLGNPNLVHAQSILAVLGFQVILMGLVEGFRINGLDGVGEGNDLYPGGQYFDPLGLADDPVTFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLLDHLDNPVANNAWAFATKFAPGA
Protein: G2/mitotic-specific cyclin-B3 (Q8WWL7)
Organism: Homo sapiens (Human)
Function: Cyclins are positive regulatory subunits of the cyclin-dependent kinases (CDKs), and thereby play an essential role in the control of the cell cycle, notably via their destruction during cell division. Its tissue specificity suggest that it may be required during early meiotic prophase I.
Subcellular location: Nucleus {ECO:0000269|PubMed:12185076}.
Interaction partners:
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Cyclin-dependent kinase 2
- M-phase inducer phosphatase 1
- G2/mitotic-specific cyclin-B1
- G2/mitotic-specific cyclin-B2
- Growth arrest and DNA damage-inducible protein GADD45 gamma
- Growth arrest and DNA damage-inducible protein GADD45 beta
- Growth arrest and DNA damage-inducible protein GADD45 alpha
- 14-3-3 protein sigma
Sequence:
MLLPLPPQSSKPVPKKSQSSKIVPSHHDPSEKTGENCQTKISPSSLQESPSSLQGALKKRSAFEDLTNASQCQPVQPKKEANKEFVKVVSKKINRNTHALGLAKKNKRNLKWHKLEVTPVVASTTVVPNIMEKPLILDISTTSKTPNTEEASLFRKPLVLKEEPTIEDETLINKSLSLKKCSNHEEVSLLEKLQPLQEESDSDDAFVIEPMTFKKTHKTEEAAITKKTLSLKKKMCASQRKQSCQEESLAVQDVNMEEDSFFMESMSFKKKPKTEESIPTHKLSSLKKKCTIYGKICHFRKPPVLQTTICGAMSSIKKPTTEKETLFQELSVLQEKHTTEHEMSILKKSLALQKTNFKEDSLVKESLAFKKKPSTEEAIMMPVILKEQCMTEGKRSRLKPLVLQEITSGEKSLIMKPLSIKEKPSTEKESFSQEPSALQKKHTTQEEVSILKEPSSLLKSPTEESPFDEALAFTKKCTIEEAPPTKKPLILKRKHATQGTMSHLKKPLILQTTSGEKSLIKEPLPFKEEKVSLKKKCTTQEMMSICPELLDFQDMIGEDKNSFFMEPMSFRKNPTTEETVLTKTSLSLQEKKITQGKMSHLKKPLVLQKITSEEESFYKKLLPFKMKSTTEEKFLSQEPSALKEKHTTLQEVSLSKESLAIQEKATTEEEFSQELFSLHVKHTNKSGSLFQEALVLQEKTDAEEDSLKNLLALQEKSTMEEESLINKLLALKEELSAEAATNIQTQLSLKKKSTSHGKVFFLKKQLALNETINEEEFLNKQPLALEGYPSIAEGETLFKKLLAMQEEPSIEKEAVLKEPTIDTEAHFKEPLALQEEPSTEKEAVLKEPSVDTEAHFKETLALQEKPSIEQEALFKRHSALWEKPSTEKETIFKESLDLQEKPSIKKETLLKKPLALKMSTINEAVLFEDMIALNEKPTTGKELSFKEPLALQESPTYKEDTFLKTLLVPQVGTSPNVSSTAPESITSKSSIATMTSVGKSGTINEAFLFEDMITLNEKPTTGKELSFKEPLALQESPTCKEDTFLETFLIPQIGTSPYVFSTTPESITEKSSIATMTSVGKSRTTTESSACESASDKPVSPQAKGTPKEITPREDIDEDSSDPSFNPMYAKEIFSYMKEREEQFILTDYMNRQIEITSDMRAILVDWLVEVQVSFEMTHETLYLAVKLVDLYLMKAVCKKDKLQLLGATAFMIAAKFEEHNSPRVDDFVYICDDNYQRSEVLSMEINILNVLKCDINIPIAYHFLRRYARCIHTNMKTLTLSRYICEMTLQEYHYVQEKASKLAAASLLLALYMKKLGYWVPFLEHYSGYSISELHPLVRQLNKLLTFSSYDSLKAVYYKYSHPVFFEVAKIPALDMLKLEEILNCDCEAQGLVL
Protein: FAST kinase domain-containing protein 2, mitochondrial (Q9NYY8)
Organism: Homo sapiens (Human)
Function: Plays an important role in assembly of the mitochondrial large ribosomal subunit. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation. May play a role in mitochondrial apoptosis.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:25683715}. Mitochondrion matrix {ECO:0000305|PubMed:18771761}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids. {ECO:0000269|PubMed:25683715}.
Interaction partners:
- Neugrin
- Fas-activated serine/threonine kinase
- Transcription termination factor 3, mitochondrial
- Pseudouridylate synthase RPUSD4, mitochondrial
- Pentatricopeptide repeat-containing protein 1
- Pseudouridylate synthase TRUB2, mitochondrial
- Probable ATP-dependent RNA helicase DDX28
- Mitochondrial mRNA pseudouridine synthase RPUSD3
- G-rich sequence factor 1
- Leucine-rich PPR motif-containing protein, mitochondrial
Sequence:
MLTTLKPFGSVSVESKMNNKAGSFFWNLRQFSTLVSTSRTMRLCCLGLCKPKIVHSNWNILNNFHNRMQSTDIIRYLFQDAFIFKSDVGFQTKGISTLTALRIERLLYAKRLFFDSKQSLVPVDKSDDELKKVNLNHEVSNEDVLTKETKPNRISSRKLSEECNSLSDVLDAFSKAPTFPSSNYFTAMWTIAKRLSDDQKRFEKRLMFSHPAFNQLCEHMMREAKIMQYKYLLFSLHAIVKLGIPQNTILVQTLLRVTQERINECDEICLSVLSTVLEAMEPCKNVHVLRTGFRILVDQQVWKIEDVFTLQVVMKCIGKDAPIALKRKLEMKALRELDRFSVLNSQHMFEVLAAMNHRSLILLDECSKVVLDNIHGCPLRIMINILQSCKDLQYHNLDLFKGLADYVAATFDIWKFRKVLFILILFENLGFRPVGLMDLFMKRIVEDPESLNMKNILSILHTYSSLNHVYKCQNKEQFVEVMASALTGYLHTISSENLLDAVYSFCLMNYFPLAPFNQLLQKDIISELLTSDDMKNAYKLHTLDTCLKLDDTVYLRDIALSLPQLPRELPSSHTNAKVAEVLSSLLGGEGHFSKDVHLPHNYHIDFEIRMDTNRNQVLPLSDVDTTSATDIQRVAVLCVSRSAYCLGSSHPRGFLAMKMRHLNAMGFHVILVNNWEMDKLEMEDAVTFLKTKIYSVEALPVAAVNVQSTQ
Protein: BTB/POZ domain-containing protein 1 (O74881)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- BTB/POZ domain-containing protein 2
- Cullin-3
- BTB/POZ domain-containing protein 3
- Cullin-1
- Elongin-C
- GTP-binding protein ypt1
- Inositol diphosphatase siw14
Sequence:
MSHLLFAYYLCNDIRSFQNLLKQDDSKVKEPRKGFSEKSGQKLRINQKDRYGRTVLHIAVSENKNSFVRSLLQHKGIDVFVQDEESGYTALHRAIYVGNLEAASLLLSKDPSFRSLRIKDKEGLSPFQFLSRVLSSTIHPVLDLPIIGNELYGFGTNVNNTLGIANGKEPSSPERVFLLKNQTESPTSGQLFSRDKILDVQASKFHSVVLTDEPSQNVYVCGIGAGGRIGFNTDVQYNFIPIPGIIHKVIQISVSHTHSLALTKFGSIYSWGKNGSGELGLSNDELKKDDPIQITPRRISAFKDYQIIGMAAGKSYSVAWTDTDIYSWGLNNGQLGISDHISVVSTPRRVAGLLSPVIHAVCTTRATICLLQNNSIIAFCNYNQVKLPFNVDFGSSLKVTKHPLSLTRFNVRKLLASENKLAVLTELGEVYEFDMKLLLDRDSTSSKNSTRTSFKFTPLWIFESSDLAALDIAWTADNSLILCTRNGTCWKRELRSKKREKSSSSPYSRGPYKYNRIENLQMVVGVRASASGSFFAIRNDYLPPPIYKPSNMLIDLLRSLLPYDHLLHVRQPRLIPPEDEDGVPIFDEDRAASSNEMQLLFEGSIPILTSYENYKQSFSDVTIYCGTSMFHSHKFILCARSSFLRKLLLQKKKSSVSNIIYIEEITQSHSTIRVEDIPPLAVAILLHYLYTDTLLSPWHLDSRFSPLKENLSKLANLLELPHLAEVLPFSVSRQPLLSLTNDILQLYNNFYVLCEETMDTVIKLKDGELKAHGLFLSLRSEYFSSYFQFVSMESNSFDIPITVNLSHLTVEHMSIVLRHVYSDLKVELFDDLKESDFHNWLETMFEILSIADELLFLELKSIAQQSLLRFLNLKTLPTLMDLSLSYHAEELYSRCIDYACHNIEFFLEANRISEWDGFHLKKVAQRLTELLSDQRVHLPSSKIANRLLIRDPVLMEKRNYELKVLREYLFSQESSQLWDDSPYRSIFEDRRCSTSAVILESGIVPSSNQSDSLNKEDAEEKSPKPNVVNVTSITKTAGASVEIQNNIESASSGGDKTQLNGPGADQPVTATITFDKTSPWRNRENLSHNNNTTRASLRELLEQEKADASTTTVLSDSRFMKAPTKKSQREKKKELSKQVPISKTNVGHIDIELGKSNHSNPWSVATHQRGSFSSSTGVKKSFNGILREAAREEGSSQVIYQESKKRISNGSPTSWNLLTKPSPRSASLPKNSQPLSISEIMTEQKEEIESQKRRSSFRKTIEEIQQEEEFQKWWEEESLRVQKELGILKTERDTSTNRKQGQASKQPQRRHRKEKDSKVSESTAEFKSLPIDIPRTTHKKGKARAVK
Protein: Pertactin autotransporter (P.94) [Cleaved into: Outer membrane protein P.68; Pertactin translocator] (Q03035)
Organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Function: Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough.
Subcellular location: [Pertactin autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Outer membrane protein P.68]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Pertactin translocator]: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane.
Interaction partners:
Sequence:
MNMSLSRIVKAAPLRRTTLAMALGALGALGAAPAAHADWNNQSIIKAGERQHGIHIKQSDGAGVRTATGTTIKVSGRQAQGVLLENPAAELRFQNGSVTSSGQLFDEGVRRFLGTVTVKAGKLVADHATLANVSDTRDDDGIALYVAGEQAQASIADSTLQGAGGVRVERGANVTVQRSTIVDGGLHIGTLQPLQPEDLPPSRVVLGDTSVTAVPASGAPAAVSVFGANELTVDGGHITGGRAAGVAAMDGAIVHLQRATIRRGDAPAGGAVPGGAVPGGAVPGGFGPLLDGWYGVDVSDSTVDLAQSIVEAPQLGAAIRAGRGARVTVSGGSLSAPHGNVIETGGGARRFPPPASPLSITLQAGARAQGRALLYRVLPEPVKLTLAGGAQGQGDIVATELPPIPGASSGPLDVALASQARWTGATRAVDSLSIDNATWVMTDNSNVGALRLASDGSVDFQQPAEAGRFKVLMVDTLAGSGLFRMNVFADLGLSDKLVVMRDASGQHRLWVRNSGSEPASANTMLLVQTPRGSAATFTLANKDGKVDIGTYRYRLAANGNGQWSLVGAKAPPAPKPAPQPGPQPGPQPPQPPQPPQRQPEAPAPQPPAGRELSAAANAAVNTGGVGLASTLWYAESNALSKRLGELRLNPDAGGAWGRGFAQRQQLDNRAGRRFDQKVAGFELGADHAVAVAGGRWHLGGLAGYTRGDRGFTGDGGGHTDSVHVGGYATYIANSGFYLDATLRASRLENDFKVAGSDGYAVKGKYRTHGVGASLEAGRRFAHADGWFLEPQAELAVFRVGGGAYRAANGLRVRDEGGSSVLGRLGLEVGKRIELAGGRQVQPYIKASVLQEFDGAGTVRTNGIAHRTELRGTRAELGLGMAAALGRGHSLYASYEYSKGPKLAMPWTFHAGYRYSW
Protein: Cystathionine beta-lyase (CBL) (EC 4.4.1.13) (Beta-cystathionase) (Cysteine lyase) (Cysteine-S-conjugate beta-lyase) (Sulfur transfer protein 3) (P53101)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cystathionine gamma-synthase
- Homocysteine/cysteine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-synthase
- Putative cystathionine gamma-synthase YML082W
- Homocysteine S-methyltransferase 1
- Putative mitochondrial cysteine synthase
- Adenosylhomocysteinase
- Homocysteine S-methyltransferase 2
- Thiosulfate sulfurtransferase TUM1
Sequence:
MPIKRLDTVVVNTGSQNDQHSASVPPVYLSTTFKVDLNNEDAQNYDYSRSGNPTRSVLQHQIGKLYRVPQENVLAVSSGMTALDVILRGLVLLNGTDNHTPTIIAGDDLYGGTQRLLNFFKQQSHAVSVHVDTSDFEKFKTVFQSLDKVDCVLLESPTNPLCKVVDIPRILRFVKCISPDTTVVVDNTMMSGLNCNPLQLNPGCDVVYESATKYLNGHHDLMGGVIISKTPEIASKLYFVINSTGAGLSPMDSWLLVRGLKTLGVRLYQQQRNAMILAHWLENSCGFKPTRTNKATKTRFVGLRSNPDFKLHKSFNNGPGAVLSFETGSFEHSKRLVSSKKLSIWAVTVSFGCVNSLLSMPCKMSHASIDPELRKERDFPEDLVRLCCGIENIVDLKKDLLAAMVDADIIEVRENGKYLFNKLNKNLAVNTTIDDLHKPLSIYEEFYNQDLIRKDSELNIKSSKL