wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein SHOOT GRAVITROPISM 5 (Protein indeterminate-domain 15) (AtIDD15) (F4IPE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in inflorescence stems gravitropism, probably by regulating starch accumulation in amyloplasts of graviperceptive cells. Required for stem circumnutation movements. Regulates lateral organ morphogenesis and gravitropic responses. Acts cooperatively with IDD16 to control silique and branche orientation. Involved in the establishment of auxin gradients through the regulation of auxin biosynthesis and transport.
Subcellular location: Nucleus {ECO:0000269|PubMed:16813575}.
Interaction partners:
- Protein LOW PSII ACCUMULATION 1
- Protein TILLER ANGLE CONTROL 1
- Protein LAZY 1
- Protein SHOOT GRAVITROPISM 6
- Syntaxin-22
- Probable indole-3-pyruvate monooxygenase YUCCA5
- Uncharacterized protein
Sequence:
MRTDQVMLSNKNTNTCCVVSSSSSDPFLSSSENGVTTTNTSTQKRKRRPAGTPDPDAEVVSLSPRTLLESDRYICEICNQGFQRDQNLQMHRRRHKVPWKLLKRDNNIEVKKRVYVCPEPTCLHHNPCHALGDLVGIKKHFRRKHSNHKQWVCERCSKGYAVQSDYKAHLKTCGTRGHSCDCGRVFSRVESFIEHQDNCSARRVHREPPRPPQTAVTVPACSSRTASTVSTPSSETNYGGTVAVTTPQPLEGRPIHQRISSSILTNSSNNLNLELQLLPLSSNQNPNQENQQQKVKEPSHHHNHNHDTTNLNLSIAPSSSYQHYNNFDRIKEIMASEQIMKIAMKEKAYAEEAKREAKRQREIAENEFANAKKIRQKAQAELERAKFLKEQSMKKISSTIMQVTCQTCKGQFQAVAVPAATADETSLVVSYMSSANTDGELENGF
Protein: T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (Chaperonin CCT1) (P28769)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit zeta 1
- TCP-1/cpn60 chaperonin family protein
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit zeta 2
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit theta
- ATP binding protein
Sequence:
MSISAQNPDISGDRQSGQDVRTQNVMACQAVSNIVKTSLGPVGLDKMLVDDIGDVTITNDGATILRMLEVEHPAAKVLVELAELQDREVGDGTTSVVIVAAELLKRANDLVRNKIHPTSIISGYRLAMRESCKYIEEKLVTKVEKLGKVPLINCAKTSMSSKLISGDSDFFANLVVEAVLSVKMTNQRGEIKYPIKGINILKAHGQSARDSYLLNGYALNTGRAAQGMPLRVSPAKIACLDFNLQKTKMQLGVQVVVNDPRELEKIRQREADMTKERIEKLLKAGANVILTTKGIDDMALKYFVEAGAIAVRRVRKEDMRHVAKATGATLVTTFADMEGEETFDPAHLGSADEVVEERIADDDVILIKGTKTSSAVSLILRGANDYMLDEMERALHDALCIVKRTLESNTVVAGGGAVESALSVYLEHLATTLGSREQLAIAEFADALLIIPKVLAVNAAKDATELVAKLRAYHHTAQTKADKKHYSSMGLDLVNGTIRNNLEAGVIEPAMSKVKIIQFATEAAITILRIDDMIKLVKDESQGEE
Protein: Conserved protein TB16.3 (O53519)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator Rv0474
- Protein Rv2184c
- Conserved protein
- Probable conserved ATP-binding protein ABC transporter
- Uncharacterized protein Rv0502
- ATPase BagA
- Uncharacterized protein Rv0487
- Conserved protein
- 1-acylglycerol-3-phosphate O-acyltransferase
Sequence:
MADKTTQTIYIDADPGEVMKAIADIEAYPQWISEYKEVEILEADDEGYPKRARMLMDAAIFKDTLIMSYEWPEDRQSLSWTLESSSLLKSLEGTYRLAPKGSGTEVTYELAVDLAVPMIGMLKRKAERRLIDGALKDLKKRVEG
Protein: Paired box protein Pax-6 (Q66SS1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ
Protein: Lysine/arginine permease CAN1 (Basic amino acids permease CAN1) (A0A1D8PPI5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: High-affinity permease for basic amino acids arginine, lysine and histidine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10418152}; Multi-pass membrane protein {ECO:0000255}. Note=Degraded in the vacuole after internalization by endocytosis in a ubiquitin-dependent manner when expressed in S.cereviae (PubMed:10418152). {ECO:0000269|PubMed:10418152}.
Interaction partners:
- Phosphoribosylaminoimidazole carboxylase
- Orotidine 5'-phosphate decarboxylase
- 3-isopropylmalate dehydrogenase
- Imidazoleglycerol-phosphate dehydratase
- N-
- Plasma membrane ATPase
Sequence:
MPEDYEKYRMGSSNESHQKSVQPISSSISKSNKKTKHQTDFVQDSDIIEASSINDEFGEVKRDLKARHVSMIAIGGTIGTGLFISTGSLLHTTGPVMSLISFLFVTTICFSVTQSLGEMATYIPISGSFAQFVTRWVSKSCGAANGWLYWFSWAVTFGLELSVVGQVIQFWTDAVPLAAWISIFFVILTIFNFFPVKFYGEVEFWIASIKIIAVFGWIIYAFIMVCGAGKTGPVGFRYWRNGYAWGDGILVNNNGKYVAAFVSGLINSIFTFQGTELVAVTAGEASPRALRSAIRKVMFRILVFYVLCMLFMGLLVPYNDPKLTQDGGFTRNSPFLIAMENSGTKVLPHIFNAVIVTTIISAGNSNIYSGSRILYGLAQAGVAPKFFLRTNKGGVPFFAVAFTAAFGALGYLACSSQGNKAFTWLLNITATAGLISWGFISVSHIRFMKTLQRRGISRDTLPFKAFFMPFSAYYGMVVCFIVVLIQGFTVFWDFNASDFFTAYISVILFVVLWVGFHFFFYGFGKDSFKMSNILVPLDECDIDSGVRDINDAEFDIPPPKNAWDKFWAIVA
Protein: Protein spackle (P39230)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Inhibits viral DNA ejection into the host cytoplasm, thereby confering the infected host bacteria with immunity against secondary phage infection. Achieves superinfection exclusion by localizing to the periplasm and inhibiting the activity of tail-associated lysozyme, thereby preventing penetration by the tail tube of incoming phages.
Subcellular location: Host periplasm {ECO:0000255|HAMAP-Rule:MF_04159, ECO:0000269|PubMed:32987925}.
Interaction partners:
Sequence:
MKKFIFATIFALASCAAQPAMAGYDKDLCEWSMTADQTEVETQIEADIMNIVKRDRPEMKAEVQKQLKSGGVMQYNYVLYCDKNFNNKNIIAEVVGE
Protein: PRA1 family protein F4 (AtPRA1.F4) (Q9LIC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- RNA-binding
- PRA1 family protein A2
- PRA1 family protein H
- PRA1 family protein A3
- PRA1 family protein A1
- V-type proton ATPase subunit c''2
- Exocyst complex component SEC3B
- GDSL esterase/lipase At4g10955
- Aspartic proteinase A1
- Probable protein phosphatase 2C 22
Sequence:
MANNDEITTSSHASPAVNHESISRAKQRIKDGLATRRSWRVMFDLHSTGLPHGVSDVFSRIKTNLAYFRSNYAIVILNVIFFSLIWHPTSLIVFTGLVFLWIFLYFLRDVPLKVFRFQIDDRAVLIGLSVITIVLLLLTNATFNIVAALMAGAVLVLIHAVIRKTDDLFLDEEAATTETSGLTSHPSS
Protein: Glycine--tRNA ligase (EC 6.1.1.14) (Glycyl-tRNA synthetase) (GlyRS) (P56206)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the attachment of glycine to tRNA(Gly).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MPASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNRITKKRYRLDHLLKEQPEEVLKRLYRAMEVEEENLHALVQAMMQAPERAGGAMTAAGVLDPASGEPGDWTPPRYFNMMFKTYVGPVEDEASLAYLRPETAQGIFVNFKNVLDATSRKLPFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPEELAHYAKATVDILYRFPHGLEELEGIANRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW
Protein: Probable leucine-rich repeat receptor-like protein kinase At5g49770 (EC 2.7.11.1) (Q9LT96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- At5g60630
- Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone:MOK16
- Late embryogenesis abundant
- Probable long-chain-alcohol O-fatty-acyltransferase 6
- 60S ribosomal L18a-like protein
- KIB1-4 beta-propeller domain-containing protein
- Beta-glucosidase 15
- Probable cysteine protease RD21C
- ACT domain-containing protein ACR7
- F25P12.91 protein
Sequence:
MKMSSRIGLFKLLILLFFQIYSVYAFTDGSDFTALQALKNEWDTLSKSWKSSDPCGTEWVGITCNNDNRVVSISLTNRNLKGKLPTEISTLSELQTLDLTGNPELSGPLPANIGNLRKLTFLSLMGCAFNGPIPDSIGNLEQLTRLSLNLNKFSGTIPASMGRLSKLYWFDIADNQLEGKLPVSDGASLPGLDMLLQTGHFHFGNNKLSGEIPEKLFSSEMTLLHVLFDGNQFTGSIPESLGLVQNLTVLRLDRNRLSGDIPSSLNNLTNLQELHLSDNKFTGSLPNLTSLTSLYTLDVSNNPLALSPVPSWIPFLNSLSTLRLEDIQLDGPVPTSLFSPLQLQTVSLKHNLINTTLDLGTNYSKQLDFVDLRDNFITGYKSPANNPVNVMLADNQVCQDPANQLSGYCNAVQPNSTFSTLTKCGNHCGKGKEPNQGCHCVYPLTGVFTLRSPSFSGFSNNSNFLKFGESLMTFFKNGKYPVDSVAMRNISENPTDYHLLINLLIFPSGRDRFNQTEMDSINSAFTIQDYKPPPRFGPYIFVADQYKTFSDLEDSKTVSMKVIIGVVVGVVVLLLLLALAGIYALRQKKRAQRATDQMNPFAKWDAGKNEMDAPQLMGTKAFTFEELSKCTNNFSDANDVGGGGYGQVYKGTLPNGQVIAIKRAQQGSMQGAFEFKTEIELLSRVHHKNVVKLLGFCFDQKEQMLVYEYIPNGSLRDGLSGKNGVKLDWTRRLKIALGSGKGLAYLHELADPPIIHRDVKSNNILLDEHLTAKVADFGLSKLVGDPEKAHVTTQVKGTMGYLDPEYYMTNQLTEKSDVYGFGVVMLELLTGKSPIDRGSYVVKEVKKKMDKSRNLYDLQELLDTTIIQNSGNLKGFEKYVDVALQCVEPEGVNRPTMSEVVQELESILRLVGLNPNADSATYEEASGDPYGRDSFEYTGVFPTPKP
Protein: FH1/FH2 domain-containing protein 3 (Formactin-2) (Formin homolog overexpressed in spleen 2) (hFHOS2) (Q2V2M9)
Organism: Homo sapiens (Human)
Function: Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21149568}. Note=Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, myofibril, sarcomere, Z line. Note=Threonine phosphorylation in isoform 4-specific sequence TDTDEEEEVE is required for targeting to myofibrils in cardiomyocytes.
Interaction partners:
- Desmin
Sequence:
MATLACRVQFLDDTDPFNSTNFPEPSRPPLFTFREDLALGTQLAGVHRLLQAPHKLDDCTLQLSHNGAYLDLEATLAEQRDELEGFQDDAGRGKKHSIILRTQLSVRVHACIEKLYNSSGRDLRRALFSLKQIFQDDKDLVHEFVVAEGLTCLIKVGAEADQNYQNYILRALGQIMLYVDGMNGVINRNETIQWLYTLIGSKFRLVVKTALKLLLVFVEYSESNAPLLIQAVTAVDTKRGVKPWSNIMEILEEKDGVDTELLVYAMTLVNKTLSGLPDQDTFYDVVDCLEELGIAAVSQRHLNKKGTDLDLVEQLNIYEVALRHEDGDETTEPPPSGCRDRRRASVCSSGGGEHRGLDRRRSRRHSVQSIKSTLSAPTSPCSQSAPSFKPNQVRDLREKYSNFGNNSYHSSRPSSGSSVPTTPTSSVSPPQEARLERSSPSGLLTSSFRQHQESLAAERERRRQEREERLQRIEREERNKFRYKYLEQLAAEEHEKELRSRSVSRGRADLSLDLTSPAAPACLAPLSHSPSSSDSQEALTVSASSPGTPHHPQASAGDPEPESEAEPEAEAGAGQVADEAGQDIASAHEGAETEVEQALEQEPEERASLSEKERQNEGVNERDNCSASSVSSSSSTLEREEKEDKLSRDRTTGLWPAGVQDAGVNGQCGDILTNKRFMLDMLYAHNRKSPDDEEKGDGEAGRTQQEAEAVASLATRISTLQANSQTQDESVRRVDVGCLDNRGSVKAFAEKFNSGDLGRGSISPDAEPNDKVPETAPVQPKTESDYIWDQLMANPRELRIQDMDFTDLGEEDDIDVLDVDLGHREAPGPPPPPPPTFLGLPPPPPPPLLDSIPPPPVPGNLLVPPPPVFNAPQGLGWSQVPRGQPTFTKKKKTIRLFWNEVRPFDWPCKNNRRCREFLWSKLEPIKVDTSRLEHLFESKSKELSVSKKTAADGKRQEIIVLDSKRSNAINIGLTVLPPPRTIKIAILNFDEYALNKEGIEKILTMIPTDEEKQKIQEAQLANPEIPLGSAEQFLLTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGTNAKAFELSYLEKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAKHEMKPVLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPYAIREVNINKFCRIISEFALEYRTTRERVLQQKQKRANHRERNKTRGKMITDSGKFSGSSPAPPSQPQGLSYAEDAAEHENMKAVLKTSSPSVEDATPALGVRTRSRASRGSTSSWTMGTDDSPNVTDDAADEIMDRIVKSATQVPSQRVVPRERKRSRANRKSLRRTLKSGLTPEEARALGLVGTSELQL
Protein: Scavenger receptor acting in neural tissue and majority of rhodopsin is absent, isoform A (Scavenger receptor acting in neural tissue and majority of rhodopsin is absent, isoform C) (Q9VM10)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Carotenoid isomerooxygenase
- Neither inactivation nor afterpotential protein G
- GEO08194p1
Sequence:
MPTQNSAMWGQKSNRKLIIGIFGFCLGLFGILCGMFWVDLFDWIMHKEMALAPDTRVYENWKSPPIDLSLDIYLYNWTNPEDFGNLSTKPILEQVGPYRFIERPDKVDIHWHPENASVTYRRRSLFYFDAAGSNGSLDDEITTLNAVALSAAATAKYWPPVKRSLVDVGLKMYGAEMSVQKSIDELLFTGYNDAMIDVAMAMPIFGDEVKVPFDKFGWFYTRNGSADLTGVFNVFTGADQLAKLGQMHSWNYQENTGFFDSYCGMTNGSAGEFQPQHLKPGDSVGLFTPDMCRTIPLDYVETVDIEGLEGYKFSGGPRSVDNGTQYPENLCFCGGQCVPSGVMNISSCRFGSPVFMSYPHFFNADPYYPDQVEGLSPNQKDHEFYMVVQPSTGIPLEVAARFQVNMLVEPIQGISLYTGIPRIFFPLVWFEQKVRITPDMADQLKVLPIVMLSGHIFAGICLIVGITLLCWTPVQILLASCRNRRYDLRTKTKTNGQYKSRSQFSSAEELKSKASTLVCEKSVKGSPDSSPLLEKGRKPTIIKSQTGESVATASTAISDNKQD
Protein: Uncharacterized protein (Q38AJ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar GTP-binding protein 1
- 60S ribosomal protein L24, putative
- Nucleolar GTP-binding protein 2
- Ribosome production factor 2 homolog
- KRR1 small subunit processome component
- 60S ribosomal export protein NMD3
- Ribosome biogenesis regulatory protein
- Ribosome assembly factor mrt4
Sequence:
MAGKGNAKVVVTHPKSRKVRQLQRQSRREKRISEQKGKRNAKAALEAARFFWFREQCLALGRTKLAFSREEAQVLTEQYLKRNDEEIVALKSMRNPTAGRIKILEAMKTSEADDFNSSKGIVIPDITNSDNLEILTSIWDGRADTAGVVRRVGLTRTGVSPAAPAVTELEGKLLTIDEVRERSIDFTSRKARKFQTMKRVQSVKKTPTAEDVWLRSKKRGVDLQAKRLRQGREAVLKTRRAN
Protein: Mortality factor 4-like protein 2 (Q5JXX2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSRKQGSQPRGQQSAEEENFKKPTRSNMQRSKMRGASSGKKTAGPQQKNLEPALPGRWGGRSAENPPSGSVRKTRKNKQKTPGNGDGGSTSEAPQPPRKKRARADPTVESEEAFKNRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAILEEYANCKKSQGNVDNKEY
Protein: Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) (Hepatitis C virus NS5A-transactivated protein 13) (HCV NS5A-transactivated protein 13) (Nucleolar 130 kDa protein) (Nucleolar phosphoprotein p130) (Q14978)
Organism: Homo sapiens (Human)
Function: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:7657714}. Cytoplasm {ECO:0000269|PubMed:7657714}. Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. {ECO:0000269|PubMed:7657714}.
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit DKC1
- Nucleolar protein 56
- Nucleolar protein 58
- Coilin
- DNA-directed RNA polymerase I subunit RPA1
- Ribosomal L1 domain-containing protein 1
- H/ACA ribonucleoprotein complex subunit 1
- H/ACA ribonucleoprotein complex subunit 2
- CCAAT/enhancer-binding protein zeta
Sequence:
MADAGIRRVVPSDLYPLVLGFLRDNQLSEVANKFAKATGATQQDANASSLLDIYSFWLKSAKVPERKLQANGPVAKKAKKKASSSDSEDSSEEEEEVQGPPAKKAAVPAKRVGLPPGKAAAKASESSSSEESSDDDDEEDQKKQPVQKGVKPQAKAAKAPPKKAKSSDSDSDSSSEDEPPKNQKPKITPVTVKAQTKAPPKPARAAPKIANGKAASSSSSSSSSSSSDDSEEEKAAATPKKTVPKKQVVAKAPVKAATTPTRKSSSSEDSSSDEEEEQKKPMKNKPGPYSSVPPPSAPPPKKSLGTQPPKKAVEKQQPVESSEDSSDESDSSSEEEKKPPTKAVVSKATTKPPPAKKAAESSSDSSDSDSSEDDEAPSKPAGTTKNSSNKPAVTTKSPAVKPAAAPKQPVGGGQKLLTRKADSSSSEEESSSSEEEKTKKMVATTKPKATAKAALSLPAKQAPQGSRDSSSDSDSSSSEEEEEKTSKSAVKKKPQKVAGGAAPSKPASAKKGKAESSNSSSSDDSSEEEEEKLKGKGSPRPQAPKANGTSALTAQNGKAAKNSEEEEEEKKKAAVVVSKSGSLKKRKQNEAAKEAETPQAKKIKLQTPNTFPKRKKGEKRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSIKFDSE
Protein: Zcf29p (A0A1D8PRB7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Chromatin structure-remodeling complex protein RSC58
- RFX-type winged-helix domain-containing protein
- Bromo domain-containing protein
- Arp9p
- Uncharacterized protein
- Chromatin structure-remodeling complex subunit SFH1
- Cdr11p
Sequence:
MGQKRNRISKVCDFCKRRKVKCDLGNPCSMCVKYKKSPCVYSEQPTEAPKSKQRKPRVVKSEITNNNDTSSGVASNGSSNSGYTNSSASTAVSIPSSMTYANSYAIESNNNNSTGVSINNSQSCPTLFQSATTVGGGSAIVHNELSFLKEKLKSLEDSILSKQDTSQGNNNAVISSSCSPNDSVHSQKPYFIPSLTNTPIDSTSLLGINPVASDTETINFYRGYNGTTDKEPLQKRNHGPLSWIALTKSDNAMRTLWAHIHIVKEQIRARMLAISDNAPQVDKEFTEKAIYDEGQDNLRPFRDAVEKDPKKPPTPATVTHLKNNSQSQMSLNQKAMCLGLSFYRGGLDQELELVEKIRLVLPKQEIIWLLFKRFFTHLYTALPILDEVVLKEELQKLIGPEDYSQSRVGVKIEKKLDFAYLGILLLVLRLSYVSLFSYDLSINENYFTTDDPSPKAQQTKYLLNNPINIDVVSVAQECFNQFNIMRNCNMTLMQLALLTRIYHQVAPEDGDGIDGGDSQIFTGMLVQMAYSLGLHRDPDNVPDSSKDQKLNNLGRKIWYMVLVQDFSNAMSSGSMLCVNVDSFDTKIPFYVPGNENVIDVEVEKIACSCFPNLESTYNPLCELLNMILRVKGEVKMIDLSKKMKLMENHFKDKYRHFTSPSEDSRNSMPATLKKKIFFSGNLFMVSIYMHIFNYYESKQNVELSFFYLKKMFVTTIFETMPYFTEYVTNTNDVFNSGSDIIAIPGYESVAHKSLIVIAAIYLRLMYRIRMFKIRYDHNTRMNSDAIEDEEYKAHFNKLIKCSDLLIECREIFRCGLAKLSNRYYYAWRVTKAQNFIGSMITDKFFESYKPKCVHNGYSTEMITELIYILESTLDRVREMKKLRKLHQKQMKNQSHSKQVLQKSHYHQSYQSQPQQQSQSQQQPQSQYRSQSHSWNGTGANPQYSYGDQNSLGERNPSLDQTSMASNTSSDVDINDYKTNDEIDSIWLQMMNLKNQDTIGTPGNTQFGGGGSGNWTTSFQADQSNMTFPQVSNNPAGGNVANVSLGQGSELASGSNDMGHVNYTNNAGGPGTNSLFNPLPNLPNTLIDMNNLFENVPLDELFKDFS
Protein: Magnesium transporter MRS2-2 (Magnesium Transporter 9) (AtMGT9) (Q9FLG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity magnesium transporter that mediates the influx of magnesium. Plays a crucial role in male gametophyte development and male fertility.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Magnesium/proton exchanger
- Putative non-specific lipid-transfer protein 14
- WAT1-related protein At5g45370
Sequence:
MAQNGYLVPADPSAVVTVKKKTPQASWALIDATGQSEPLDVDKYEIMHRVQIHARDLRILDPNLSYPSTILGRERAIVLNLEHIKAIITSEEVLLRDPSDENVIPVVEELRRRLPVGNASHNGGQGDGKEIAGAQNDGDTGDEDESPFEFRALEVALEAICSFLAARTAELETAAYPALDELTSKISSRNLDRVRKLKSAMTRLTARVQKVRDELEQLLDDDDDMADLYLSRKLSSASSPISSIGEPNWYTTSPTIGSKISRASRASLATVHGDENDVEELEMLLEAYFMQIDSTLNRLTTLREYIDDTEDYINIQLDNHRNQLIQLELVLSSGTVCLSMYSLVAGIFGMNIPYTWNDGHGYMFKYVVGLTGTLCVVVFVIIMSYARYKGLVGS
Protein: Cytochrome c oxidase subunit 6C (Cytochrome c oxidase polypeptide VIc) (P09669)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit NDUFA4
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 8A, mitochondrial
Sequence:
MAPEVLPKPRMRGLLARRLRNHMAVAFVLSLGVAALYKFRVADQRKKAYADFYRNYDVMKDFEEMRKAGIFQSVK
Protein: Folate synthesis bifunctional protein, mitochondrial [Includes: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK); Dihydropteroate synthase (DHPS) (EC 2.5.1.15)] (O04862)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9118956}.
Interaction partners:
Sequence:
MSILKCLGVRGNQLCAARNYLKVLGFSSFHTAPNSSIEIQTQDEEVVIALGSNVGDRLHNFKEALKLMRKSGIHITRHASLYETAPAYVTDQPRFLNSAVRADTKLGPHELLAALKRIEKDMGRTDGIRYGPRPIDLDILFYGKFKVRSDILTVPHERIWERPFVMAPLMDLLGTAIDSDTVASWHSFSGHSGGLNALWEKLGGESLIGEEGMYRVMPVANGLLDWSRRTLVMGILNLTPDSFSDGGNFQSVKSAVSQARLMISEGADIIDIGAQSTRPMASRISAEEELGRLIPVLEAVMSIPEVEGKLISVDTFYSEVALEAVRKGAHIINDVSAGKLDASMFKVMAELDVPYVAMHMRGDPSTMQDSENLKYDNVCKDISSELYSRVREAEISGIPAWRIIMDPGIGFSKKTEDNLAALTGIPDIREEISKRSLAISHAPILIGPSRKRFLGEICSRPSAVDRDPATIASVTAGVLCGANIVRVHNVKDNLDAVKLCDAILKQKSSPIKFKQ
Protein: Maturation protein A2 (MP) (A2 protein) (Q8LTE2)
Organism: Escherichia virus Qbeta (Bacteriophage Q-beta)
Function: Induces host cell lysis. Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis. May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome.
Subcellular location: Virion {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. Note=A single copy of the maturation protein is present in the virion. {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}.
Interaction partners:
Sequence:
MPKLPRGLRFGADNEILNDFQELWFPDLFIESSDTHPWYTLKGRVLNAHLDDRLPNVGGRQVRRTPHRVTVPIASSGLRPVTTVQYDPAALSFLLNARVDWDFGNGDSANLVINDFLFRTFAPKEFDFSNSLVPRYTQAFSAFNAKYGTMIGEGLETIKYLGLLLRRLREGYRAVKRGDLRALRRVIQSYHNGKWKPATAGNLWLEFRYGLMPLFYDIRDVMLDWQNRHDKIQRLLRFSVGHGEDYVVEFDNLYPAVAYFKLKGEITLERRHRHGISYANREGYAVFDNGSLRPVSDWKELATAFINPHEVAWELTPYSFVVDWFLNVGDILAQQGQLYHNIDIVDGFDRRDIRLKSFTIKGERNGRPVNVSASLSAVDLFYSRLHTSNLPFATLDLDTTFSSFKHVLDSIFLLTQRVKR
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (A0A0A0MR03)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM
Protein: Histidine biosynthesis trifunctional protein [Includes: Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphohydrolase (EC 3.6.1.31); Histidinol dehydrogenase (HDH) (EC 1.1.1.23)] (P00815)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- ATP phosphoribosyltransferase
- 1-
- Imidazole glycerol phosphate synthase hisHF
- Histidinol-phosphate aminotransferase
- Imidazoleglycerol-phosphate dehydratase
- L-2-aminoadipate reductase
- Histidinol-phosphatase
- Tryptophan synthase
- Polynucleotide 3'-phosphatase
- Phosphoserine phosphatase
Sequence:
MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGKFSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFSQDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDLGRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGEFKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAADLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLDVVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVLNAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKVGLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIVLAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVRKCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCGDYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGHRNAVKIRMSKLGLIPKDFQ