wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma tubulin complex adapter SPC72 (P39723)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Spindle pole body component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque. Anchors cytoplasmic microtubules at the at the half bridge of the spindle pole body (SPB) and accordingly functions in nuclear position and spindle orientation, including anaphase spindle migration into the bud. Recruits KIN4 kinase to both SPBs when cytoplasmic microtubules are defective. Links cytoplasmic microtubules with spindle orientation checkpoint (SPOC) components and, therefore, could function as part of the sensors of spindle orientation defects. Is strictly required for mating and karyogamy.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10428957, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9585415, ECO:0000269|PubMed:9606209, ECO:0000269|PubMed:9670012, ECO:0000269|PubMed:9718373}. Note=localized at the outer plaque and the bridge of the spindle pole body.
Interaction partners:
- Spindle pole body component SPC97
- Spindle pole body component SPC98
- Tubulin gamma chain
- Spindle pole body component 110
- Spindle pole body component SPC42
- Chaotic nuclear migration protein 67
- Cell division control protein KAR1
- Protein STU2
- Mitotic check point protein BFA1
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
Sequence:
MVRRWIPSGRHLRNNDNTGDDDDSEFTNSMDSGMSIPSLRDSMTTRSSHNDPIKPALMNDSNKVKNLEKELTNAKIKIQVLYEYIRRIPNKDGNAPSLGNDTDFRNSIIEGLNLEINKLKQDLKAKEVEYQDTLQFVQENLENSESIVNTINHLLSFILTHFNEQDENAHLLDKEERETLEETLELSSDYVLEKMDTLSKFIIQFLQDFLHSKSRAESKQDKEEFLSLAQSSPAGSQLESRDSPSSKEENTDGGYQNDEIHDSNNHIDTENVMANSTSLPISAVESRFEKTLDTQLEIVIENLHKEYDQFINSIRLKFEKSQKLEKIIASKLNEQSHLLDSLELEENSSSVIEKQDHLISQLKEKIESQSVLINNLEKLKEDIIKMKQNEKVLTKELETQTKINKLKENNWDSYINDLEKQINDLQIDKSEEFHVIQNQLDKLDLENYQLKNQLNTLDNQKLILSQYESNFIKFNQNLLLHLDSIFNILQKILQESSIAQFDRKMKSIKSVPNALKNLNLIQPKLESLYTFIETALESIINSYISSLISMETPEQPHQQGNELTATPNKELTLRIEELQRRWISERERRKLDANASEARIKALEQENESLRSKLFNLSINNP
Protein: Probable WRKY transcription factor 51 (WRKY DNA-binding protein 51) (Q93WU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Involved in defense responses. May act as positive regulator of salicylic acid (SA)-mediated signaling and negative regulator of jasmonic acid (JA)-mediated signaling.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein TIFY 5A
- Probable WRKY transcription factor 70
- Probable WRKY transcription factor 46
- Probable WRKY transcription factor 41
- Probable WRKY transcription factor 54
Sequence:
MNISQNPSPNFTYFSDENFINPFMDNNDFSNLMFFDIDEGGNNGLIEEEISSPTSIVSSETFTGESGGSGSATTLSKKESTNRGSKESDQTKETGHRVAFRTRSKIDVMDDGFKWRKYGKKSVKNNINKRNYYKCSSEGCSVKKRVERDGDDAAYVITTYEGVHNHESLSNVYYNEMVLSYDHDNWNQHSLLRS
Protein: KH-type splicing regulatory protein (M0QYH3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGD
Protein: Zeta-sarcoglycan (Zeta-SG) (ZSG1) (Q96LD1)
Organism: Homo sapiens (Human)
Function: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix. May play a role in the maintenance of striated muscle membrane stability (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Epsilon-sarcoglycan
- Sarcospan
- Beta-sarcoglycan
- Alpha-sarcoglycan
- Desmoglein-1
- Delta-sarcoglycan
- Dystroglycan 1
- Dystrophin
Sequence:
MTREQYILATQQNNLPRTENAQLYPVGIYGWRKRCLYFFVLLLLVTMIVNLAMTIWILKVMNFTVDGMGNLRVTKKGIRLEGISEFLLPLYVKEIHSRKDSPLVLQSDRNVTVNARNHMGQLTGQLTIGADAVEAQCKRFEVRASEDGRVLFSADEDEITIGAEKLKVTGTEGAVFGHSVETPHIRAEPSQDLRLESPTRSLIMEAPRGVQVSAAAGDFKATCRKELHLQSTEGEIFLNAETIKLGNLPTGSFSSSSPSSSSSRQTVYELCVCPNGKLYLSPAGVGSTCQSSSNICLWS
Protein: Ecdysone-induced gene 71Ec (Q9VUS6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ecdysone-induced gene 71Ef
- Ecdysone-induced gene 71Ed
- Ecdysone-induced gene 71Ea
- Ecdysone-induced gene 71Eb, isoform A
- Ecdysone-induced gene 71Eg
- LP05252p
- LP08087p
- Peptidoglycan recognition protein SB2, isoform B
- Eig71Eh
- Uncharacterized protein, isoform B
Sequence:
MSKITLIFAILCLCVAVQAQTREQEICRQENETCRRNERRLGVQNDVSTTFNNHCRRQSGIRNWRNVSRCELSLATCRLTLERCAVINCKNVRNSIDGGVTARPPTSRRTTRRIPDTRRPRTTRRTPTTRRAPTTRSSRRTTRRRAPTTRTTRRTTRRRAPTTRTTTRRPTEE
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC 3.1.3.16) (Calcineurin A1) (Calmodulin-binding protein 1) (P23287)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Interaction partners:
- Calcineurin subunit B
- Calmodulin
- Calcipressin-like protein
- Serine/threonine-protein phosphatase 2B catalytic subunit A2
- Transcriptional regulator CRZ1
- Protein phosphatase PP2A regulatory subunit A
- FK506-binding protein 1
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
Sequence:
MSKDLNSSRIKIIKPNDSYIKVDRKKDLTKYELENGKVISTKDRPIASVPAITGKIPSDEEVFDSKTGLPNHSFLREHFFHEGRLSKEQAIKILNMSTVALSKEPNLLKLKAPITICGDIHGQYYDLLKLFEVGGDPAEIDYLFLGDYVDRGAFSFECLIYLYSLKLNNLGRFWMLRGNHECKHLTSYFTFKNEMLHKYDMEVYDACCRSFNVLPLAALMNGQYFCVHGGISPELKSVEDVNKINRFREIPSRGLMCDLLWADPVENYDDARDGSEFDQSEDEFVPNSLRGCSFAFTFKASCKFLKANGLLSIIRAHEAQDAGYRMYKNNKVTGFPSLITMFSAPNYLDTYHNKAAVLKYEENVMNIRQFHMSPHPYWLPDFMDVFTWSLPFVGEKVTSMLVSILNICSEQELDPESEPKAAEETVKARANATKETGTPSDEKASSAILEDETRRKALRNKILAIAKVSRMFSVLREESEKVEYLKTMNAGVLPRGALARGTEGLNETLSTFEKARKEDLINEKLPPSLSEVEQEKIKYYEKILKGAEKKPQL
Protein: Pyruvate kinase (EC 2.7.1.40) (A8B498)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Interaction partners:
- phosphopyruvate hydratase
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Glucose-6-phosphate isomerase
- Ribosomal protein L8
- Ribosomal protein L11
- Ribosomal protein L5
- Small ribosomal subunit protein uS2
- Ribosomal protein L3
- Ribosomal protein L23A
- Ribosomal protein L6
Sequence:
MLNNKFTANQITEYNLTNLKKLVEQGLKGVDKNHPHFNRVKICCTLGPSSFNVEVIAGMIRAGADIIRINFSHGNTDDHTQIFHKVQQAMQLTGKTVAIMGDIQGPKLRIAGFSNPDNCIELKEGQEFTLDHNNVNGDESRVYLPHKEFFAVCEPNDDIILNDGYIRLVATSVDRQAMRIVTRVKTGGKLGARKGITIPTRILPLSGLSPKDLGDIRNACRLGMDWIALSFVQTKADVIEARDYIAKLHAENPASFCPRVCSKIEKPTAVLDIDDIALLSDMLMVARGDLAIETCLSKVCSIQKYICERARYHGCQAMVATQMVESLIENTVPTRAEVTDVASVCFDGANSVLVTAETAAGHDPVNVVKVLRSILTTTEQSEAFIKQVLTDNYINQRTSKEHKRPDSIALGACLLARELGAKLIIVFSKSGNSTGRVLRQLPHCPVLCITSEQRSYQWLHMCWGCRPVLHPGNIDSMKTLISVADTHALESGQAERGDAVVLVFGTPFSDVNRKGCNNIMAHVVGGGSFNNSTDVEYGVTPQLAELTPVVGDS
Protein: Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta (E9QAN8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Inositol polyphosphate 5-phosphatase OCRL
- Inositol polyphosphate-4-phosphatase type I A
- Synaptojanin-2
Sequence:
MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHHKEESRAKQNTEPSLISWDEPALDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSISPPEGLPNSTSQDPQPGPDPWPKGSLSGDYLYIFDGSEGRCSLSPGSGDTDGSCKKLSPPPLPPRVSIWDAPPLPPRKGSPSPSKISQPNDINSFSSAEQPPDKLLVAQDPEEGELPDGRGQGHTLGSVDYDGINDAITRLNLKSTYDSEISSDATRGWKEGRGPLDFNKDTSGKPVARSKTMPPQVPPRTYTSRYANRKNATPGNNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRTGSDIQDYSLTGCVWSTVTPSPEHLGDEVNLKVTVLCDSLREPLTFTCNCSSTVDLLIHQTLCYTHDELREVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDISIRLQLMEQKAIRSDLARTVNDDQSPSTLNYLIHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAICNALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLSVRENREKVVEALTAAILDLVELYCSTFNADFQTAVPGSRKHDLVQEACHFPGALAFTVYGTHRIPIIWATSYEDFYLSCSLSHGGKELCSPLQTRRAHFSKYLFHLIIWDQQICFPVQVNRLPRETLLCATLYALPVPPPGGSSEANKQKRVPEALGWVTTPLFNFRQVLTCGRKLLGLWPATQENSGARWSAPNFHQPDSVILQIDFPSSAFDIKFTSPPGDKFSPRYEFGSLREEDQRKLKDITQKESLYWLTDADKKQLWEKRYYCHTEVSSLPLVLASAPSWEWACLPDIYALLQQWTHMNHQDALGLLHATFPDQEVRRMAVQWIGSLSDAELLDYLPQLVQALKYECYLDSPLVRFLLKRAISDLRVTHYFFWLLKDSLKDSQFSIRYQYLLAALLCCCGKGLREEFNRQCWLVNTLAKLAQQVREATPSARQGILRVGLEEVKQFFALNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKLAFQNVDPLGENIRVIFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGKGMVEMIPNAETLRKIQVEHGVTGSFKDRPLADWLQKHNPGEDEYEKAVENFIYSCAGCCVATYILGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEANATTYFTRLIESSLGSVATKLNFFIHNLAQMKFTGSDDRLTLSFAPRTHTLKSSGRIRDVFLCRHEKIFHPSKGYVYVVKVMRENAHEATYIQRTFEEFQELHNKLRLLFPSSFLPSFPSRFVIGRSRGEAVAERRKEELNGYIWHLIHAAPEVAECDLVYTFFHPLPRDEKASGPSPAPKSSDGTWARPVGKVGGEVKLSISYKNNKLFIMVMHIRGLQPLQDGNDPDPYVKIYLLPDPQKTTKRKTKVARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENLLLGEVHIRLRELDLAQEKTGWFGLGSRGHGT
Protein: MAP kinase-activated protein kinase mak-2 (MAPK-activated protein kinase mak-2) (EC 2.7.11.1) (Q965G5)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which is involved in maintaining synapse and axon morphology as well as touch neuron axon regeneration after injury by regulating cebp-1 mRNA stability downstream of the dlk-1, mkk-4 and pmk-3 signaling cascade. May play a role in body wall muscle contraction. Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord.
Subcellular location: Perikaryon {ECO:0000269|PubMed:19737525}. Nucleus {ECO:0000269|PubMed:19737525}. Synapse {ECO:0000269|PubMed:19737525}. Note=Colocalizes with snb-1 and partially with cebp-1 at synapses. {ECO:0000269|PubMed:19737525}.
Interaction partners:
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase pmk-1
- Mitogen-activated protein kinase pmk-2
- CCAAT/enhancer-binding protein homolog 1
- Transcription factor atf-4 homolog
- Transcription factor ets-4
- SHSP domain-containing protein
- MAP kinase-activated protein kinase mak-1
- C3H1-type domain-containing protein
- Heat shock transcription factor hsf-1
Sequence:
MAFHEYPVTQDYRISRKVLGVGINGKVVECEHRQSGDKFALKVLRDTQKARREVELHVMASGHGHVVSVHDVYKNSYNGVDCLLVVMENMKGGELFNRIQERGQKAFTEREAAGIVNEICSAVAHLHRMSIAHRDLKPENLLYVTTASNAALKLTDFGFAKKTDESEPQGLKTACFTPYYCAPEVLGTEKYDKSCDLWSIGVIMYILLCGYPPFYSQHGQPMSPGMKAKIKSGQYTFPSPEWDCVSEAAKDLIRKLLRTEPTERITIEQTMEHKWISHYRRVPDTPLFTSSNLNDQREQWTDMQDEMEATLASMRVGPENIQIKSLGDSNNKLLAKRRKGGASPKDDPMDDIKEEEKDDEEEKMIS
Protein: Protein kintoun (Dynein assembly factor 2, axonemal) (Q499A3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}. Dynein axonemal particle {ECO:0000250|UniProtKB:B1H1W9}. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia. {ECO:0000255|HAMAP-Rule:MF_03069}.
Interaction partners:
- Coiled-coil domain-containing protein 39
- Coiled-coil domain-containing protein 40
- Thioredoxin-related transmembrane protein 1
Sequence:
MDADRLAELQLTRAEMRRIGEALQDRRFRELLTEYVEEISSPENRRRYEEEIRRLEEERGAAVQFIHPTPHHVLKGRGPSGKCFINICSDQLIEKPRSEAATDDRGRSGHSWRIPYSLTPGRAGRDAAGAPCVLFDAVFHPDALLMAENNARFMTLIHRTATGGIQDNFRIRLEHVTRLKMMKYKGEPQPTMIRRPNPGQTEAADRGPQQTTGPQQPTGPQQPTDPQQPTDTQQPTDPQQTTGPQQTTGPQQTTGPHQPTDPQQTTGPQQPTDPQQPTGPHQPTDPQQTTDPPPTAPQYRLKYRSVLDLQDYRCCRDSGSAGRPTAIIIEVEVPRLRSAQEAELRVEERRLLLEAPTAEYRLELPLAYPVEEERAEAQFNHTHRLLTVTLPVLKRRRVEEEERRAEEEESRKGGDEDGELHPDCGPDPPMMELQTEDTHTPAADTHTPAADTHTPAADTHTPAAETGAGLGSGVALLSSSNVISVCGADVHQQLEEPGDPSAHTDPADTHPADTDPADTDPAHTDPADTDPADTDPAHTDPAHTDPEMESRIAGLHLQNTLCFQLD
Protein: small monomeric GTPase (EC 3.6.5.2) (Q9NFN8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00037843}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037843}.
Interaction partners:
Sequence:
MFIWDWFTGVLGYLGKQRRHCRPCALGLWKKSGKLLFLGLDNAGKTTLLHMLKDDKLAQHVPTLHPSSEELSIGNMRFTTFDLGGHTQGKCLARRVWKDYFPAVDAIVFLIDAWDRGRFQESKNELDSLLTDEALSNCPVLILGNKIDKPGAASEDELRNVFGLYQLTTGPLELFMCSVLKRQGYGEGFRWLAQYID
Protein: Variegin (P85800)
Organism: Amblyomma variegatum (Tropical bont tick)
Function: Thrombin inhibitor. Does not inhibit other serine proteases.
Subcellular location: Secreted {ECO:0000269|PubMed:17684009}.
Interaction partners:
Sequence:
SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES
Protein: Protein PatA (PAT-1) (P39048)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Controls heterocyst pattern formation. Required for the differentiation of intercalary heterocysts but not for terminal heterocysts.
Subcellular location: Cell septum {ECO:0000269|PubMed:20622060}. Note=Localizes at sites of cell division.
Interaction partners:
- Circadian input-output histidine kinase CikA
- Heterocyst differentiation protein
- Transcriptional regulator peptide PatS
- histidine kinase
- Circadian input-output histidine kinase CikA
- Heterocyst differentiation protein
- histidine kinase
- Circadian input-output histidine kinase CikA
- histidine kinase
- DNA-binding transcriptional activator HetR
Sequence:
MKTLPITRYRFFQKIQPLSLLKKITGKTITGCLQVFSTSGTWSIYVEEGKLIYACYSERMFEPLYRHLGNLSPQIATLPKEINEQLRAIFETGIENQAIPNPDYLAICWLVNQKYISSSQAAVLIEQLALEVVESFLMLEEGSYEFIPESFLDDLPKFCYLNVRLLVEQCQQHGRVPEAFRREASSQEISSSTEHNQIPVNNRRSTKFTSPPHTQPKPEPRLPQINTNKSTEYSKRYASQPNTVNHGYSQTSATSTDKKIYTIFCIDENPIVLNNIKNFLDDQIFAVIGVTDSLKALMEILCTKPDIILINVDMPDLDGYELCSLLRKHSYFKNTPVIMVTEKAGLVDRARAKIVRASGHLTKPFNQGDLLKVIFKHIT
Protein: Keratin, type I cytoskeletal 18 (Cytokeratin endo B) (Keratin D) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) (P05784)
Organism: Mus musculus (Mouse)
Function: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
Interaction partners:
- Keratin, type II cytoskeletal 8
- Tumor necrosis factor receptor superfamily member 1B
- Keratin, type I cytoskeletal 19
- Cadherin-1
- Desmoplakin
- Epithelial cell adhesion molecule
- Glyceraldehyde-3-phosphate dehydrogenase
- Catenin beta-1
- Epidermal growth factor receptor
Sequence:
MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLNDRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDVEARYKAQMEQLNGVLLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFSLNDALDSSNSMQTVQKTTTRKIVDGRVVSETNDTRVLRH
Protein: Ferredoxin-2, chloroplastic (Ferredoxin II) (Fd II) (O80429)
Organism: Zea mays (Maize)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Occupies a key position both for transferring the photoreducing power to Fd-NADP(+) oxidoreductase (FNR), hence the formation of NADPH, and for mediating the cyclic electron flow around photosystem I (PSI).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9952443}.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Ferredoxin--NADP reductase, chloroplastic
- Lipoyl synthase, chloroplastic
- DNA binding protein
- PGR5
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit IV A
- Ferredoxin--NADP reductase, chloroplastic
Sequence:
MAATALSMSILRAPPPCFSSPLRLRVAVAKPLAAPMRRQLLRAQATYNVKLITPEGEVELQVPDDVYILDFAEEEGIDLPFSCRAGSCSSCAGKVVSGSVDQSDQSFLNDNQVADGWVLTCAAYPTSDVVIETHKEDDLL
Protein: Bifunctional protein gal10 [Includes: UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase); Aldose 1-epimerase (EC 5.1.3.3) (Galactose mutarotase)] (Q9HDU3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).
Interaction partners:
- Galactose-1-phosphate uridylyltransferase
- Galactokinase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Alpha-galactosidase mel1
- Hexokinase-2
- Hexokinase-1
- UDP-glucose 4-epimerase uge1
- Uncharacterized protein PB2B2.11
Sequence:
MAVQDEYILVTGGAGYIGSHTVIELINHGYKVIIVDNLCNSCYDAVARVEFIVRKSIKFFKLDLRDKEGLAQIFDTFKIKGVIHFAALKAVGESMKLPLEYYDNNICGTITLLNVMREHRVKTVVFSSSATVYGDATRFDNMIPIPESCPNDPTNPYGKTKYAIENIIKDLHTSDNTWRGAILRYFNPIGAHPSGLLGEDPLGIPNNLLPFLAQVAIGRREKLLVFGDDYDSHDGTPIRDYIHVVDLAKGHIAALNYLNKINNSEGMYREWNLGTGKGSSVFDIYHAFCKEVGKDLPYEVVGRRTGDVLNLTASPNRANSELKWKAELSITDACRDLWKWTIENPFGFQIDNYKWKLFNTLGIMDYKNRLHTICFQDLEVSIANYGALVQAVRYKGRNLVNGFNDFSRYKLKENPFFGATIGRFANRIANGQFEVDGHLYTLCKNENNKTTLHGGNNGFDKQFFLGPIARQYEDYNTLEFILVDKDGNNGFPSDLETLVKYTIKNNSLEIEYKSVIPEYSKLNVTAVNLTNHSYWNLASPNKTIDGTIIKSTTNVYLKVNSETSLPTGDIVEWQNDITKPTKLDPNISFDNCFIVDREASKFCLDTRKYSLKNIVEVIHPSVPVKLVVSTTEPAFQLYTGDGNDICEFQSRSGFCVETGRFINALNNEKWSKQVILRKGEVYGARSKFSLYAQDLEENKHFLDSASYNSGEYY
Protein: Probable metal-nicotianamine transporter YSL6 (Protein YELLOW STRIPE LIKE 6) (AtYSL6) (Q6R3K6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the transport of nicotianamine-chelated metals.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Oligopeptide transporter 9
- Oligopeptide transporter 8
- Oligopeptide transporter 6
- Oligopeptide transporter 4
- Oligopeptide transporter 7
- Oligopeptide transporter 2
- Oligopeptide transporter 1
- Oligopeptide transporter 5
- Oligopeptide transporter 3
- Vacuolar iron transporter 1
Sequence:
MGTEIPRSAEISEALLPPESEKTVTATEEHVPEWKEQITIRGLTVSALLGTLFCIITHKLNLTVGIIPSLNVAAGLLGFFFVKSWTGFLSKLGFTVKPFTKQENTVIQTCVVACYGLAFSGGFGSYLIAMDEKTYKLIGADYPGNHAEDVINPGLWWMIGFLFVVSFLGLFSLVPLRKVMVLDYKLTYPSGTATAMLINSFHTNTGAELAGNQVKCLGKYLSLSLIWSCFKWFFSGIGDACGFDNFPTLGLTLFKNTFYFDFSPTYIGCGLICPHIVNCSVLLGAIISWGILWPFVSQHAGDWYPADLGSNDFKGLYGYKVFIAIAIILGDGLYNLVKIIAVTVKELCSSRSRRLNLPIVTDGVDDSEASEILLVKKKRDEVFLKDRIPLEFAIAGYVGLAAISTATIPIIFPPLKWYFVLCSYFIAPALAFCNSYGTGLTDWSLASTYGKIGLFIIASVVGSDGGVIAGLAACGVMMSIVSTAADLMQDFKTGYLTLSSAKSMFVSQLVGTAMGCVIAPLTFWLFWTAFDIGDPNGPYKAPYAVIFREMAILGIEGFAELPKHCLALCYGFFIAALIVNLLRDITPPKISQFIPIPMAMAVPFYIGAYFAIDMFVGTVILFVWERINRKDAEDFAGAVASGLICGDGIWTIPSAILSILRINPPICMYFGPSSAR
Protein: H/ACA ribonucleoprotein complex subunit 3 (Nucleolar protein 10) (Nucleolar protein family A member 3) (snoRNP protein NOP10) (Q6DRH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit DKC1
- H/ACA ribonucleoprotein complex subunit 1
- H/ACA ribonucleoprotein complex subunit 2-like protein
- WD repeat-containing, antisense to TP53.
- Telomerase reverse transcriptase
- Nucleolar protein 56
- Nucleolar protein 58
- rRNA 2'-O-methyltransferase fibrillarin
- NHP2-like protein 1
- H/ACA ribonucleoprotein complex non-core subunit NAF1
Sequence:
MFLQFYLNENGERVYTLKKVDPSGQPTSSAHPARFSPDDKFSRHRVTIKKRFGLLLTQQPRPVL
Protein: Prostaglandin reductase 1 (PRG-1) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (Dithiolethione-inducible gene 1 protein) (D3T-inducible gene 1 protein) (DIG-1) (Leukotriene B4 12-hydroxydehydrogenase) (NAD(P)H-dependent alkenal/one oxidoreductase) (EC 1.3.1.74) (Q9EQZ5)
Organism: Cavia porcellus (Guinea pig)
Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX). Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha (By similarity). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11733004}.
Interaction partners:
Sequence:
MVKAKSWTLKKHFQGKPTQSDFELKTVELPPLKNGEVLLEALFLSVDPYMRIASKRLKEGAVMMGQQVARVVESKNSAFPAGSIVLAQSGWTTHFISDGKGLEKLLTEWPDKLPLSLALGTIGMPGLTAYFGLLEVCGVKGGETVLVSAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKIAYLKQIGFDAAFNYKTVNSLEEALKKASPDGYDCYFDNVGGEFLNTVLSQMKDFGKIAICGAISVYNRMDQLPPGPSPESIIYKQLRIEGFIVYRWQGDVREKALRDLMKWVLEGKIQYHEHVTKGFENMPAAFIEMLNGANLGKAVVTA
Protein: P granule abnormality protein 2 (P34266)
Organism: Caenorhabditis elegans
Function: Transient component of P-granule which is involved in germline development.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:15238518}. Note=Localizes to P granules only during postembryonic development. {ECO:0000269|PubMed:15238518}.
Interaction partners:
- Tyrosine-protein phosphatase domain-containing protein
- Exostosin domain-containing protein
- Uncharacterized protein C40H1.2
- PPM-type phosphatase domain-containing protein
- F-box domain-containing protein
Sequence:
MKPCKREIVDFDGIRTHFFPNLALYTCYNEELIAHHSENANRFTSYVFGAVEDSPTEQEILEILFPENANPEAISTGMDACLALGENFLSHYKSFNARLNRQNHSHDLLDAVQEFDEKKILAISRKSRLRKSADSKILTILVNILLSENQEEKFMEICELCSLDLDFDAFVLIKILQLENEENAEEVQIIRENVVDQILEQKPFLAHLLKNGPEKIDEITKLLSVPIIGSSSNQINQLITKICDSSEISDTAVEEHYHQNFKLMNILVRTMIVDRFDLTIDALEQIPVEIKNRMFPGIRIRVLQDTLHFLHQLFKVFLNESQKFDNLAPQSFAKAIKNVWVRHAIIGILDSLKFSLNKDVFNQLVPLIPGSQVSNDVISGKVENAISCAIWIVKTFGTEGSRDSIEKLPWFDSSVELTELINSIEIAVTSVEVEDQTVNFRKIPQKDWLDGNLQKALKTEPTSEKFGISNSLKIKDENQRNQIRGFKDNSKEPNAKVSARFGSKFQRVDSSTKRRLFGGVGVGEPRNCRGFL