wanglab/gogpt-training-data huggingface dataset:
Protein: Dehydrogenase xptC (EC 1.1.-.-) (Prenyl xanthone synthesis protein C) (Q5AUN2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC.
Interaction partners:
Sequence:
MAKLSVILLFRSLLLCGALTVSRHATLVTEREVQSSKYDFIVVGGGVSGLTVADRLTEIPDVSVLVIEAGPVDRGEDFVYVPGSYERDPYIWPGLTNEPSAELNNRVFDSVVARVAGGGSIVNAMIFLRGTALDFDGWESLGNHGWGWEGMLPYFIKSENFTRPTPELAHEGNITWDDSVRGHDGPVRYSYPNYIYPGLGRLYEAALHIGIQPRLDPNGGQNTGVFNQPFAIDAATWTRSSARRNHYDPAVSRPNYHFLSDTTVARVIFDGTRAVGVEYLPSRGGGISTAFAAKEVLVAAGALHTPQVLQLSGVGPRDLLEALNIPIISDLPGVGSNLQDQTTFPFVYTWDSAVTPNVTTFLTNTTWATEQRVLYDQHLPSVWTLTRPLAPKFAFLSYEDATANTAYASILDDAQARDPADSLPGDIHPTVLAGYAVQRQIMFNEFRDAGLAVGGMSWDTDANVQVFNVKPFSRGYVYINQTDPLANPVIDFRTASDPTDFQLHIALLHKQRELFNAPSLAALGPTEVVPGPAVQTDEDIIKLMREILQPSNGHQCCSAPMMPRELGGVLSPEMKVYGTTGLRVIDISHWPKELSGPPMASIYAAGEKAADIIKGEHGWLGN
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial (Glu-AdT subunit F) (EC 6.3.5.-) (P53260)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for proper protein synthesis within the mitochondrion.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03151, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106, ECO:0000269|PubMed:21799017}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03151, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106, ECO:0000269|PubMed:21799017}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03151, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106, ECO:0000269|PubMed:21799017}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Glutamine--tRNA ligase
- Uncharacterized protein YDR114C
Sequence:
MYKTWRLCRTHTVGGLCHDGSHRFVSTGGAKIGKKFENMNQIRDYLSRPVWSVHEYLGINTKEEKLEPPSAEAVKKLLRLSGLPLEGADIKEIQMRLAKQLSFINKLHNIPVEGEKHTKEYDARLVQRNTKQLNYTKLLEGISHQKQDAELGEVSGSWKATGLAAESKNAYFVVKEGLLKNRK
Protein: Spastin (EC 5.6.1.1) (E5KRP6)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021}. Midbody {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. {ECO:0000256|HAMAP-Rule:MF_03021}.
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease) (Pr); Assembly protein (AP) (Capsid assembly protein)] (Q6SW62)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular location: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.
Interaction partners:
Sequence:
MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACVIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTSELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase-like protein) (Q0WL44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein
- Transmembrane protein
- At1g70770
- Methylesterase 2
- Type II inositol polyphosphate 5-phosphatase 15
- Peroxidase 66
- Defensin-like protein 4
Sequence:
MIECGTVYRNNSACFTFKICPSPTSINKTTKRCNGKSENERKNGDEERISKYSFVSPLCMRGGDGYNSYSSNSLLQRRVLSKAKPVLVKNTKDLMINLNFPTYIKVADLGCSSGQNTFLAMSEIINTINVFCQQRNQNPPEIDCCLNDLPSNDFNTTFKFIQFFNGMNITSKESYFVYGVPGSFYSRLFPRRSLHFVHSSYGLHWLSKVPEGLEKNKMSVYITNSSPLSTYKAYLNQFQRDFATFLKLRSEEMVSNGRMVLTFIGRNTIDNPLHRDCCHFWTLLSKSLRDLVAEGLVSASKVDSFYLPFYDPNEKEIKEMVQKEGSFEIRDLETHGYDLGHCNQDESKRSKSGQNEANYIRAVSEPLLAAHFGDAIINILFNKFACHVSQHVSCRNKTTVSIVVSLTKKKTFLMS
Protein: Centrosomal protein of 162 kDa (Cep162) (E7F5E1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Note=Localizes to the distal end of centrioles throughout the cell cycle. {ECO:0000250}.
Interaction partners:
- Centrosomal protein of 290 kDa
- Sine oculis-binding protein homolog B
- Transmembrane protein 17B
- Tectonic family member 1
Sequence:
MAHRLTKEELDQQFEQFLKESVSDDSVDLGTSSKRPSVLDSLGKAPVRPVKKASASVPWWQDDDDNDDDSEEKGMSSTGRSFLKSLRKTPSIKEVDEEQPKELFLEDEGNRDHVILSRDSLEPEDSLVIPSAGARGLDTLDEDDDDARFLSNLKKVSSSSIDFSRINREQELSAPTSPLRREEMDSTIEEEQRMNKDTAASPAYSEDFEEEASDKSDVEPQEKKPERLGMLAKVSLHDSLNSTDGALAPAVPSLAVARENRPESKQTDMPALEPAVQSYGQSGGSEMEALQEAYRQISGSAGVCEDGQVEAGRTPLSLSTLQPASTVESDLPTAEELMQPIGPDSGFTRGFSLQPITEAVPRSRDNQSPLRISSDESPFSSANEGYGGGNTANLTGGEHPDSYKFTQKSISEEIRRLMQEQDTSSQEPPPLKPKKRQVPARSNASTSASSRKAPVPSVRVKKPESKPLHRVPAPSRAAQAAKPPSPPTLRKAQNQTFKKTQNLNQTHTIKGLDTSLKLSSELVESVQSFAAFLQHQVEASSLQDKGPFQANKIASEAMTAHKGMQEKMDGGPELASLERLRLQLAKKERELSLREDQLQEQHKQELTALRQENYILQSKLHRAEEASNKRKWSFGEASDPVTEEKLKLIEKEMKEQETLIQGYHQENEKLYLQMKALQAQSKQNEEALFMENQRLLTELSFARDRMNTNNIQRTIRERSIVDQSFNIAELTSQVQAAQKKEERLQEEVRRLKQEKQALHVDLEMMRKERDLAKVQAVCKSGDKGFELKLLHDKHREEVTELKKRLQWYAKNQELLDKDAARLHAATAEIQKLTEQVEKLKAEVSRRANEQQRKAKEKAGEAKRIQDLERQLKQKEELLKRRHPNSLPALILAAASTGAEEDRLDVRSLAQSSQTAALLERRVHRLEAELEGRDEAAKRSLRAMEQQYHRIKLQYEQQISDLEQRLSEKSHSYPAISSELIKSHTQTLKAELEEVKEVHQKQVSVLQAEVDSLQEQLRQAQASTQTEKPARSPSRHQLHAEAAQAARIERLTQELNSKSRSIQELTRTIERLQRERRTMLSGPSHERPNNEPKRHLGTAKDTKKPSVETFPPTQDEKDYHPGAFSGTHISEVQLENDSLRTKLEELEVLREKEKVSLQAAVTHAQNQLLRIEEQNAEQLTSVKAEHRKEIEHLLARHALEHSSSRVAELTSQLNTQEIIVQHLQGQVKELQGTKEALAVTKLREETLQNQLSKLLEELKEAKEAHSPELKHFTSLEQKIQSMEFRYSQREKQLQQVIADTRRVVEQEQQSEVERWRKLAQGRAKELEAFRMELDSILDVLRELQRQGVVIPMPEHTSTNTHTYLPLRS
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FP28)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MASNPPGKCCFEGFYHEGQAKGTHKDVCGVDTYVTGAENSSDRVIVILTDIYGNRLNNVLLTADQMATDCYQVYIPDILFNDPVVALDGSTDFNAWLAAHPAEKVQELVTKYLTDLRAQLKPKFLAVVGYCYGAKFAIQQIGANPLADCCAIAHPSFVSIEEVDAISKPVLISAAEEDPIFPEELRHQTEAKLKENKARYQLDLFSGVSHGFAARGDTSNPVVKYAKEKVLVDQLYWFNYFSGCCQK
Protein: Beta-mannosyltransferase 1 (EC 2.4.1.-) (WRY family protein 4) (Q5ADQ9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the first beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan. Plays a key role in reducing host inflammatory response.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDKFIQSFSHQYLDSSSSLKLTARRKRKLTILGLFLFSLISLMIIISYSNNNILPGLSGISISSTFSDYYSNPKQQNKFEQQIQDHQTTKKGKRTIIFPNNFNHVHDHKGSYMMKDSELVKYYVETMEQALDPEDLIYRNRFTYKLPNIPYTEQKIEMFSDGGGGGGDTSDSNTDMCPKLSTTIKVEASPAMNKNGDLKKILKTFLQEDSFYYRELSPFFPDLKKHFDEDTIDKHWYQFIGSTVWLEQYGVHLMVSRIIYTEKDQGSPKFSLAYLQVFDRNWKELDNVELIVPDPENISTTNNKNKNKKPYGYKSVLYPTIAPIPVYHNSKQTGGRFYGIEDPRIVLIKTRHGYEEPVLIYNSHHRKISEKHFDNDQEGKINFNNYRSLFIGWIWQTQLGKIHLEELPNNEFKKNEYIKIKEFVKPNNNRGRTEKNWALFINYNQRLNQGFDSHVYFANQLKNLKILKCSILNDNDDDCEWEFQMDDYEDAGVLHGGTELININQLLHQYDYPELNSIKDLIPNGREYWVGFARASLKNCGCGSRMYRPNLIVLMKDGKNYKFAYVSSFVGLGIEILPWYLDKGLCEHYNLIIPNGISSWTIEKDLHQKEKDKQVMDYMAFTISRRDATVDVVYVKGLLKALFTDSSSSKHLLAVEQTGFKSVTNVDCALKNSEKFCKIYGETF
Protein: Long-chain fatty acid transport protein 4 (FATP-4) (Fatty acid transport protein 4) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 4) (Very long-chain acyl-CoA synthetase 4) (ACSVL4) (EC 6.2.1.-) (Q6P1M0)
Organism: Homo sapiens (Human)
Function: Mediates the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across cell membranes. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis (By similarity). Probably involved in fatty acid transport across the blood barrier. Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22022213, ECO:0000305|PubMed:24269233}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Long-chain fatty acid transport protein 1
- Beta-alanine-activating enzyme
- Long-chain-fatty-acid--CoA ligase 1
- Platelet glycoprotein 4
- Scavenger receptor class B member 1
- Magnesium transporter NIPA4
- Lysosome membrane protein 2
- Peroxisome proliferator-activated receptor alpha
- Bifunctional coenzyme A synthase
Sequence:
MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
Protein: Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 (EC 7.2.1.3) (Cytochrome b ascorbate-dependent protein 3) (Cytochrome b561 family member A3) (Lysosomal cytochrome b) (LCytb) (Q8NBI2)
Organism: Homo sapiens (Human)
Function: Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late endosome and lysosome. Reduced iron can then be extruded from the late endosome and lysosome to the cytoplasm by divalent metal-specific transporters. It is therefore most probably involved in endosomal and lysosomal cellular iron homeostasis.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q6P1H1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}.
Interaction partners:
Sequence:
MVSGRFYLSCLLLGSLGSMCILFTIYWMQYWRGGFAWNGSIYMFNWHPVLMVAGMVVFYGGASLVYRLPQSWVGPKLPWKLLHAALHLMAFVLTVVGLVAVFTFHNHGRTANLYSLHSWLGITTVFLFACQWFLGFAVFLLPWASMWLRSLLKPIHVFFGAAILSLSIASVISGINEKLFFSLKNTTRPYHSLPSEAVFANSTGMLVVAFGLLVLYILLASSWKRPEPGILTDRQPLLHDGE
Protein: Probable V-type proton ATPase subunit d 2 (V-ATPase subunit d 2) (Vacuolar H+ ATPase subunit AC39-2) (Vacuolar proton pump subunit d 2) (Q9VCQ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in coupling of proton transport and ATP hydrolysis (By similarity).
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B
- VhaAC45-related protein, isoform B
- ATPase H
- V-type proton ATPase subunit a
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit H
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase catalytic subunit A isoform 1
- H
Sequence:
MSMIFNTEYGYLEALTRGFKNGMLKHSDYLNLTQCESLEDVMISIQGTDYGLIFGGEQSAPSVEVIERCLRDRLLQQYYYIRSHSTEPLTTFMEFIRYPFMIDNVALLVAGLNNHRSMKRLLRMCHPLGEFDQLGAIEVASNSAELFDAVLIDTPIARFVPRDLPMESLRYLDVEIVRAHLYRAYLEKFYAYCSQLGGNTANVMTNLLSFEADRRTITIAVNAIGSDIIPKERLKMFPTCGYLPKIALASMSTLNDTDKIRDVCNVFDGYGKMFDNLERDSDGMITLEDRFLMMEAKKNVQTFLQQYHFGIFYSFIKLKQLEVRNIVWISECIAQRQTDRINAFIPIPLD
Protein: Peroxide stress-activated histidine kinase mak3 (EC 2.7.13.3) (His-Asp phosphorelay kinase phk2) (Mcs4-associated kinase 3) (O74539)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the control of the SAPK-dependent transcriptional response to peroxide stress. Regulates sty1 activity.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11179424}.
Interaction partners:
- Peroxide stress-activated histidine kinase mak2
- Multistep phosphorelay regulator 1
- Response regulator mcs4
- Uncharacterized oxidoreductase C22A12.17c
Sequence:
MYSQHELRNKVSLALSSLLRYTFELTPFFELYEADFAYALYAGFELATNRKVVGKFSFQNVHLENEYNILTEIAKDERASKFSPTPIEFTSFPHIDLSACIAYDFGHGAELSTSYAYFRENPAEFVRFCIAICKCIEYLHSKGMVHGEIRLDSFIPISSYDNVYMLTVGSGASYFHNCLQAHNWRKYSEDSESMSRILFISPEQTGRTSYSVGYRTDIYSLGVLFFHYLSDCSPYTGSFVQRIRSILTEPLPDISKSCPKLPHLIFKIIEKMTRKNPDERYTSCSGIVNDLEACLDDIDKGLILNDHVLEKTGRTSLFYLPCSIYGREHEIKLIRKILRNSPRAINHQDKKDLETFNPYYLNAIESESSSQSLSLSQRASEVMPLVILITGCEGIGESSLIQTICDRREGYMAITKFEVSQSIVYSAIVSAVAEFIRQILAEDQLLLNNFFEELKNKLESDLYLLDSVFDLVPEIRSLLQQFSTSSGNTRKTSLLGSNHSSYSDKLGSPTILSTSFSLARPYPEPALVSPSTERPPRSSFSAALMTLLNIIASFKKVTMVIENIHLADESSLIILQKIVYSDLPLTLMITCDKENDHVINRFRLANDRIHEIELKPLSFNAVNSYVQATLHRTDDGLARFSSYVYHISKGVPLLVRNVLLSIYENKIIYFDWKKNRWEVNYDEMYTLDNDYSEPDAFMTAKKKISKLNDSSRAILGWASLLGPSFSFATVKKLCKDTDNIELNVEALQSALREGIIYATSSDDTYTFSRSIYVKAMRDLLNEAKIQIMHACLIDVCLKNRDRYNIFDIAFHINAAFDFVKGDKRSVEYCHYLHLAAEEALKIGANQEALDLYNRCIKMIPHEIPEESDDSYIRCQLIGMYVGCAEAYWVNDNFDTASEMLKLAEEKACNNSEVFPARFLYSRILFEGVHIEECTQYVLSCLKPLGYELKRHSLEDSKSIISALIPRIIDKITKSSEESQSSTDDDDRRIFEILSFLYVGSVATSYFSETAEMAIDFGIAQVEFFLSTVVNSFSAFALVYFAILANSLLEPSEDILFIGNYGEKLNREAENPIIFSRTEYLYVQSLGFIDSTTKERRLTIDYLDRNCVTCSDKHVIISLLLVSSWEKFLTSNNYSNYLADFETTHAQIMEMKPWVGDTSLITQLKRFLMCLQDNIKLDLIKSKSFLSDHNIQLSSPAAQESAKLAFSLHGWINSWYLLALVMHGEWDMAISYGENFKREFKNALLTSSRVFGIFMFTWSLVNKMLICPEFTKQKKYYEQYKENLGFFDSLCIGDNECITRVYFLLLKACGLIMNGLNFEASVMLEEVISLTEKLELFLLQAFAFETVGSIFVSMELYTSATQYLEEAIRNYAALGVKQKARHLRDKFGDLLVSNNLQVSIDEATQTDFPLVFSPERSSIDINASSMRSEKASFEIPFPEEQIDDDVSPVAQDSSLEELLISLDIIDLTSVMRSCQTIASEIELTGLLSTMTQRMLEDSSANAAVIAIRDDVGFKIAAYRTGELNEVFAPPMPITEDQTYVPSRVINYVVHTQKALFSNNINHEFDLQQERWNIENHMGRSVIAIPLYQKKEVFAILYLQGPPSAFHSRHMSVLSILGAQASFAIVNISLFHKVKEATNVNTIIIKAQREALNLVQKSEAKYRSFVDTMPCLLSKLEFDEELRIELFGSFWKEYCGELNINDPNTWKEYVHLDDHLKLQDFLLSHLHNPLPFELEIRIKRKDGVYRWNLTRCTPTTNEKNRTSFLCATIDIDDQKKARATALELARLRSNFLANISHELRTPFSGFYGMLSLLDDTNLDSEQRDIVSAARISCEMLLRVINDLLNFSKLEAGKVTLESDLEFSLESVVCDCMQSVYSACAEKGINLSYNVSPDIPFFTAGDGMKIGQMLKSILDNSVKTVNNGFIRVRAFLAGSSKKNDRDQLQIAFIVEDTREESNAIFLANMINSLNRGCNDYLPMDLSGTALGMSTCLQLCKIMGGSVSVEVSQNNPTFKICYDLKIHELGKERYDIIATPLFQNLTEFNDLIKSKVAIRVSKTSTEYDNITTYLQAARKVLHVFKGLQDLASIFDLSPDSALLRCSVVVVDVYSMDDVKAVEKILKSYPDVHVIYLCCDPSRLNIEQELQKPSGRSFACKKRWGFLQMPCTRENFLKVTLQVFKSNEDTCNFYSYVNEYGESPKPDDDMDRLNKCVGSKILIAEDNPIVRMTLKKQLEHLGMDVDAAEDGKETLQIFESHPDNYYQVCFVDYHMPVYDGLEVTRRMRKIERKHGCAPLPIFALTADMQPTMETQFQEVGITHYLSKPFKKETLIKMLLQYLVNGTDGNANTS
Protein: Forkhead box K, isoform N (M9PF47)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Checkpoint suppressor 1-like, isoform A
- Ubiquitin carboxyl-terminal hydrolase calypso
- Polycomb group protein Asx
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Sequence:
MAATTTTTTTTLATTTGNSSSTNNSSSNNNNSIASSHNNNNNIVTVHTVLNNPPTNTAGGGVADAATVAIAKDMLQLHHGAAAAATAALNNYNNSSNNNNNSADQLTGNSNNSANHPPATSSTTNSSSSSTTSANTNNPSANAASTLTSSSPPYGELRFNQEVLPITDAVTVIGRNSSTSLVHFNVAENNLVSRKHFQVLYDVELRAFFVQCLSKNGIFVDDFLQRRNVDPLRLPQRCYFRFPSTEIRIEFESYVPATSSDAIDGHSPSLVVGGGGGVAGGGAHVIITPLPRDELHQQQLHHHQQQPHLQQQQHPHHPPAHHLPLQQQQQQQQPAHHPLPHTPHHPLHHTALHQQQQRSGSIVVAPPAGAAAHLIAGDGPGIYSPLKISIPKKEQKSPYLSPTGTISAANSCPASPRQGFIQNQPNNYNNYGNNNTQDLFQTPSTASYNHNEKPPYSYAQLIVQAISAAPDKQLTLSGIYSFIVKHYPYYRKETNKGWQNSIRHNLSLNRYFIKVARSQDEPGKGSFWRIDPDSGAKLIDHSYKKRRQRSSQGFRPPYGMPRSAPVSPSHMDNSRESSPLQDIVLQSAPGSPGMSLEQRAADPEIIYNSQNAHQQQQQQQQQQQQQTLSNNSNQYSSGSPYYVTNQSSGVATPQTHVEGSAASGGGGGGGVGALLALKRNHVMGGGASQHTLHQQQAVAQQQHSEIIYEELPTDYSGHIEASEEECVTTATDATVAKRPKYVSEVLXCVRIQKHRQNKGK
Protein: PHD finger family protein (F4I8J3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNVDQCQWRKKMMGRGVDGGCGAEEKPYRPFRRVALDKENGYEDMGSLEIDFLAQASKNLSERSPFDVPEDGSTSVLSVPTLPIALANLLKNHSDNKKRHKKSHSGADKKKKKSSRQGDKLRSGSIWLEHEDYFRRLDFPDLETLSDLASLRSLSSRNCFSIPSVEYDSIDIQQRETDASAKNEDVVCGDGVVLEQIKNLLTKDISEGTVRKEEDVVKPMGVDNVGNGISSGSDYSGSLEWVLGNRNRILLTSERPSKKRKLLGSDAGLGKLMVAAPCEGNALLCDFCCTGHHQLIVCTSCKATVHKKCYGLLEDSGKPWLCSWCELENGRADSERPCLLCPKKGGILKPVLSKTENGGPAEFAHLFCSLWMPEVYIEDLKKMEPILNFPGIKETRRKLLCNLCKVKSGACIRCCNVVVLTLSMPDNPIVWIIFTGKCFVGIYYHNAVEAGNRLEVWGKHGCDTVELRAFCSKHSDIQESGKSVEGGESNAAESRSPICHLPSESVGEGHLSNDEMGVDVGTPGTGSDISRNSDLQELESPHSKFNLSATDNVESGMTGRSNEDERTLSKSLSFGLILKKLIDLGKVDVKDVAAEIGINPDALRAKLTDGDLLPDLLGKVVKWLSQHAHMGSSDKGKNLKPKANGSVLKKEGSVSLAPDHSPEEKNSIVLDQKVHHGKSSVIPSDDHGEQSNSSSSGVMMENAFSLRPNSSQNRGNLNCPNPIILDLFNQEAYPGFNPHRYIHKELSELGKEQTLKSSTDSDVARMTTNFDGSEEGNKHLQGAETFLQLSKARKLGILDLSPEDELEGELLYYQLQLLGTAVSRKQLSDNLVYEVAKKLPLEIDEQHGRRWDDVLVNKYFHDVREARKQGRKEQRNKQAQAVLAAATAAAATSSRNTSLRKDMSEEPAQQEMSTSRRKVVGSSHLVPQTKESLLKMAVSGPPSEKRSDHHTPDFLVENPRTCDICRRSETIWNLIVVCSSCKVAVHIDCYKCAKESTGPWYCELCAESSSEPSFNFGEKPNSSTECTLCGGTTGAFRKTTNGQWVHAFCAEWSLESTFRRGQINPVQGMESLAKKTDNCCVCQRIYGACTKCSYGNCQTTFHPSCARSAGFHMTGGGKHPHKAYCEKHSMEQKAKAESQKHGAEELKSLKHYRVELERLRLLCERIVKREKLKRELAISSHEILAAKRDHAARPLHVRNPFSPPEVSSDSATTSIKGHPDSNISGSEAIQRSDDITIDSTVTDKRRGKGPLLMDTDQKTDDSATSKSRFSRKLTERQILSGKTVPRKHCIVSPSVSEDGDNGSKPKKQHVETFAKELVMTSDEASFKNRRLPKGYFYVPVDCLQEDKPGNQKLASSDKPANQKTSSGDQSGKDDG
Protein: Collagen, type IV, alpha 5 (F7CK55)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
XGVPGFPGVKGEMGMMGPPGPPGPLGIPGRSGAPGLKGDDGMQGQPGLPGPAGEKGGKGEPGLPGPPGPMHPDFLGSKGEKGEPGLPGIPGLSGPKGYQGLPGDPGQPGLSGQPGSPGLPGPKGNPGLPGPPGLTGPPGPKGNIGDMGFPGPQGVDGPPGPPGFPGQPGSPGLPGQKGSKGEPGVSGIGLPGLPGPKGEPGLPGYPGNPGIKGSVGETGLPGLPGNPGAKGQPGLPGFPGTPGLPGPKGMNGPPGNPGFPGEPGPVGAGGRPGPPGPPGEKGKPGQDGIPGPAGQKGEPGQPGFGIPGPPGLPGLSGQKGDGGSPGLPGNPGLPGSKGEPGFQGFPGMPGPPGPPGSPGQALEGPKGNPGPQGPPGRPGPPGTEGPRGPPGNGGIKGERGNPGPPGQPGLPGLKGDQGPPGLPGNPGRPGLNGMKGDPGLPGVPGFPGMKGPIGVPGSTGPDGEPGLTGPPGPPGLPGPSGQSIVIKGDPGPPGIPGQPGLKGLPGLPGPQGLPGPIGPPGDPGRNGLPGFDGAGGRKGDPGLPGQPGARGLDGPPGPDGLQGPPGPPGTTSVAHGFLITRHSQTTEAPQCPRGTVHIYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLSTPEPMPMNMEPLKGQSIQPFISRCAVCEAPAVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATVDMSDMFNKPQSETLKAGDLRTRISRCQVCMKRT
Protein: Incenp-like protein ICP-1 (Inner centromere protein ARK-binding domain-containing protein) (G5EE37)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Aurora/IPL1-related protein kinase 2
- Kinesin-like protein
- Aurora kinase
- ATP synthase subunit beta, mitochondrial
- Chromosomal passenger complex protein bir-1
- Baculoviral IAP repeat-containing protein bir-2
- Serine/threonine-protein kinase plk-1
- Mitotic checkpoint serine/threonine-protein kinase bub-1
- Protein regulator of cytokinesis 1
- Kinesin-like protein
Sequence:
MPPKKRAVSRKPAEPTIKLFSSIPKISSIFDEVSEAHDDAAAKVFADLYKRMSSITEELATPQFSAEQLLNAVLKPGRIDAEFVELISRQKAKPAQPSSSSHRGDDDMETDEVETDQAGPITPRAGSVATDGDFEEDILPVTLKRMQQMSISKKKTEGSISRNAAYSGTPRRNPPREAHNQATPRNIFSSTPGRMAGTPGRAAVVPRTPHRVIPFNDAEKDPNARMKHADELRMKELEKKREKARKDEEKRNAVMERRKEQERVRQEKLDQLKQKEERNANLAKLHNSAKSPTRARLMQDHAPNKAASRKIFPTAESTSTPGRGPAKKGKVEILIGSDGQKTAPVAQPTVELSPSRELQRNGSRQVKMEPMSCDDSTPPARQHKPKAKATKRSAHAASSSTSNVEAAAALAALQEQQRIQLEQEQYLLQLAEDERRKREQKEMKEKAEKERQLRAREEQEHFLAVQREEQAQLEKQREREEAELQATLARCAEKQARQEALRKTPPPAAYEMTPPRTYQNNSKNDYGLNDLNSDDETDQEDDPRKDVPAWAEFAVVRENVRRHAINPPFDVAQFFGSIGKPNLKEIFSDAVKVKKRGSSAVWKKSPSTLNTSSRTILQDISE