wanglab/gogpt-training-data huggingface dataset:
Protein: BEL1-like homeodomain protein 10 (BEL1-like protein 10) (Q9FXG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription repressor OFP4
- Transcription repressor OFP2
- Transcription repressor OFP1
- Protein KNATM
- Transcription repressor OFP5
- At2g35290
Sequence:
MAVYYTSNVGCYQQEPIFLNHQQQNQQASSSSAAASFTVTGGDTVRNEMVFIPPTTTGDVVTGNGTVSSSDLSFHDGQGLSLSLGTQISVAPFHFHQYQLGFTSQNPSISVKETSPFHVDEMSVKSKEMILLGQSDPSSGYAGNGGNGFYNNYRYNETSGGFMSSVLRSRYLKPAQNLLDEVVSVKKELNQMGKKKMKVNDFNSGSKEIEGGGGELSSDSNGKSIELSTIEREELQNKKNKLLTMVDEVDKRYNQYYHQMEALASSFEIVAGLGSAKPYTSVALNRISRHFRALRDAIKEQIQIVREKLGEKGGESLDEQQGERIPRLRYLDQRLRQQRALHQQLGMVRPAWRPQRGLPENSVSVLRAWLFEHFLHPYPKESEKIMLAKQTGLSKNQVANWFINARVRLWKPMIEEMYKEEFGDESELLISKSSQEPNSTNQEDSSSQQQQQQENNNNSNLAYSSADTTNIVFSSETKPDRVLGNDNDPQQQQINRSSDYDTLMNYHGFGVDDYRYISGSNQQESRFSNSHHLHDFVV
Protein: rRNA 2'-O-methyltransferase fibrillarin (Histone-glutamine methyltransferase) (Q7ZTZ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Bystin-like.
- PWP2 small subunit processome component.
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit DKC1
- WD repeat domain 46.
- U3 small nucleolar RNA-interacting protein 2
- H/ACA ribonucleoprotein complex subunit 2-like protein
- WD repeat domain 36
- Nucleolar protein 6
- Nucleolar protein 56
Sequence:
MRPGFSPRGGGGRGGFGGRGRGGGDRGGRGGFRGGRGGFGGGFKSPGGEGGFRGRGGGRGTPRGRGGGRGGGRGGFRGGAKVTVEPHRHEGVFICRGKEDALVTKNMVIGESVYGEKRINVEEGETKIEYRAWNPFRSKLAAAILGGIDQIHIKPGVKVMYLGAASGTTVSHVSDIVGPEGLVYAVEFSHRSGRDLLNVAKKRTNIIPIIEDARHPHKYRMLVGMVDVIFADVAQPDQTRIVALNAHNFLKNGGHFVISIKANCIDSTAAPEAVFASEVKKMSAENMKPQEQLTLEPYERDHAVVVGIYRPPPKGKK
Protein: Ferredoxin-thioredoxin reductase, catalytic chain (FTR-C) (EC 1.8.7.2) (Ferredoxin-thioredoxin reductase subunit B) (FTR-B) (Q55389)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Interaction partners:
- Ferredoxin-thioredoxin reductase, variable chain
- Ferredoxin-1
- Photosystem II reaction center Psb28 protein
- Methionine aminopeptidase C
- Slr1699 protein
- Sll1390 protein
- Ycf53-like protein
- Fibrillin
- Photosystem II extrinsic protein O
- Photosystem I reaction center subunit IV
Sequence:
MTSSDTQNNKTLAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYEDKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQDIPMETLEEVKASMA
Protein: Flagellar basal-body rod protein FlgC (Putative proximal rod protein) (P0ABX2)
Organism: Escherichia coli (strain K12)
Subcellular location: Bacterial flagellum basal body.
Interaction partners:
- Flagellar hook-associated protein 1
- Basal-body rod modification protein FlgD
- Flagellar motor switch protein FliM
- Flagellar L-ring protein
- Flagellar motor switch protein FliG
- Flagellar basal body rod protein FlgB
- Flagellar motor switch protein FliN
- Flagellar basal-body rod protein FlgF
- Flagellar M-ring protein
- Flagellar hook protein FlgE
Sequence:
MALLNIFDIAGSALTAQSQRLNVAASNLANADSVTGPDGQPYRAKQVVFQVNAAPGAATGGVKVADVIESQAPDKLVYEPGNPLADAKGYVKMPNVDVVGEMVNTMSASRSYQANVEVLNTVKSMMLKTLTLGQ
Protein: Glutamate NMDA receptor subunit variant NR2-a (Glutamate NMDA receptor subunit variant NR2-b) (NMDA receptor 2, isoform A) (NMDA receptor 2, isoform B) (NMDA receptor 2, isoform D) (NMDA receptor subunit 2-1c) (NMDA receptor subunit 2-1d) (NMDA receptor subunit 2-1e) (NMDA receptor subunit 2-1f) (Q8MM14)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
Sequence:
MMNNEQFGHSTASAQYFLQLAGYLGIPVISWNADNSGLERRASQSTLQLQLAPSIEHQSAAMLSILERYKWHQFSVVTSQIAGHDDFVQAVRERVAEMQEHFKFTILNSIVVTRTSDLMELVNSEARVMLLYATQTEAITILRAAEEMKLTGENYVWVVSQSVIEKKDAHSQFPVGMLGVHFDTSSAALMNEISNAIKIYSYGVEAYLTDPANRDRRLTTQSLSCEDEGRGRWDNGEIFFKYLRNVSIEGDLNKPNIEFTADGDLRSAELKIMNLRPSANNKNLVWEEIGVWKSWETQKLDIRDIAWPGNSHAPPQGVPEKFHLKITFLEEAPYINLSPADPVSGKCLMDRGVLCRVAADHEMAADIDVGQAHRNESFYQCCSGFCIDLLEKFAEELGFTYELVRVEDGKWGTLENGKWNGLIADLVNRKTDMVLTSLMINTEREAVVDFSEPFMETGIAIVVAKRTGIISPTAFLEPFDTASWMLVGIVAIQAATFMIFLFEWLSPSGYDMKLYLQNTNVTPYRFSLFRTYWLVWAVLFQAAVHVDSPRGFTSRFMTNVWALFAVVFLAIYTANLAAFMITREEFHEFSGLNDSRLVHPFSHKPSFKFGTIPYSHTDSTIHKYFNVMHNYMRQYNKTSVADGVAAVLNGNLDSFIYDGTVLDYLVAQDEDCRLMTVGSWYAMTGYGLAFSRNSKYVQMFNKRLLEFRANGDLERLRRYWMTGTCRPGKQEHKSSDPLALEQFLSAFLLLMAGILLAALLLLLEHVYFKYIRKRLAKKDGGHCCALISLSMGKSLTFRGAVFEATEILKKHRCNDPICDTHLWKVKHELDMSRLRVRQLEKVMDKHGIKAPQLRLASSSDLLNHHHLKERPPLLGNLSLAASAQDLYRWSYKTEIAEMETVL
Protein: P-type ATPase (Q54Q77)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Probable copper chaperone for superoxide dismutase
- Copper transport protein ATOX1 homolog
- Natural resistance-associated macrophage protein 2 homolog
Sequence:
MGDYIQLEVLDKKVEEFPDGASIPKEKKAIFSVQGMTCSSCVGIIESFVSNVEGVISIQVALLQETAEVKFNPLILSEDDIVEQISMVGFEAKHLVQAENNTIVLNIGGMTCSSCVGIIENYVSNVDGVIECRVNLAMETARVVYDPDLTGVRDIIRNIEDVGFTAQIPSQNFDDTKNIQKEEAEKLKKNLIFSTFFTVPVFLIGMVLHKISFFNFLYTNNILHGISYADSIMLCLTTPVQFLVGKRFYVNGYKSLKHGGANMDVLVALGTSCAYFYSLMVLLMDYTSEDGGSTVGMKTFFDTSASLITFILLGKYLEVIAKGKTSEAIKKLMGLQATKALLLTIDQNEGGGGGGGSDNKTTTTILEEREIDIDLVQRGDYLKVLPGSKVPTDGIVVSGLSHIDESIITGESLPVSKKSGDKLIGGTLNQKGVLVMKATRIGGETSLSQIIKLVEKAQTERAPIQSLADKVSGYFVPSVITLGLLTFIVWLIAGSSGVASDYIKASNSSVFQFALRNAISVIVIACPCALGLATPTAVMVGTGIGAQNGILIKGGSHLETAHKISAIIFDKTGTLTTGKPIVSNVNIFGNLNNNNNGNNNSGKINKKTFFQMVASAEAASEHPLAGAIVNYAFEVCDVQSTTPPLSFESITGSGIRATLAPNNIEIMIGNLKWIKSEGISYDPTLTISPDRSINNNHHHNDDDDDDEGTLSHIEDQVRRLESDGNTVVYVVIDRQLMGYIAISDQLKPEAHATITELNKMGICTWMVTGDNPRTANAIAQQVGIDQVFAEVLPSNKSKKVMELKKMGHTVAMIGDGINDSPALAEADVGIAIGAGTDIAIEAADIVLVKSDLRDVITAISLSKTTFNRIRFNYLWATLYNILGIPLAAGLLIPFGISIPPMMAGLAMAFSSISVVLSSLHLKTYQKPDIPIHSRTTEETRQRIHKEQSQLFKKNKIIFESSPTISSKSNNKIEKLSLLSDHDNIV
Protein: phospholipase D (EC 3.1.4.4) (Q6NR18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
Sequence:
MADAGTVGGALPPYALTNSDEEHGSGEEDASEENSNNEEGEGVFRDCTDEAVVEHHNRCLPEFQFSLVDSEYDETLAFPDSVTILSNVGDKPVLVERKETDDDEEEFDDEENNSVVLRHEIPFTSIYGPSVKFNSFQRKVFIPGREIHVRIVDTERSVTTHLLNPNLYTIELTHGPFKWTIKRRYKHFNSLHQQLSFFRTSLNIPFPSRSHKEKRTTLKATAREMADESTLKDLPSHTKVKQTSTPLRAEGRSSKIAGSNANNAMAMISPNHSSILAGLTPRRIQKKRKKKKKRKLPRFPNRPESLVTVENLSVRIKQLEDYLYNLLNISLYRSHHETLNFVEVSNVSFVPGMGIKGKEGVILKRTGSTRPGQAGCNFFGCFQKNCCVRCNYFCSDVVCGTWRNRWFFVKETCFGYIRPTDGSIRAVILFDQGFDVSTGIYQTGMRKGLQVLTNNRHIVLKCWTRRKCKEWMQYLKNTANSYARDFTLPNPHMSFAPMRANTHATWYVDGAQYMSAVADGLEAALEEIYIADWWLSPEIYMKRPALDGDYWRLDKILLRKAEQGVRVFVLLYKEVEMALGINSYYSKSTLAKHENIKVMRHPDHARGGILLWAHHEKIVVIDQTYAFMGGIDLCYGRWDDHHHRLTDLGSISTSSFSGSTRRTPSLYFTKDDTDSAFGSRKSSRNAHYDTSAKERPPSPPPDEPNTSIELKLLSLVIDCLYRLRSFRVRVKLPQNRESL
Protein: Keratin-associated protein 26-1 (Q6PEX3)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 27-1
- Keratin-associated protein 25-1
- Keratin-associated protein 22-1
- Keratin-associated protein 8-1
- Keratin-associated protein 20-1
- Keratin-associated protein 6-1
- Keratin-associated protein 6-3
- Keratin-associated protein 15-1
- Keratin-associated protein 20-2
- Keratin-associated protein 6-2
Sequence:
MSCPNYCSGNSNSGSLRTSRHIPLTSIDLCPTSVSCGDVLYLPTSSQDHTWVTDNCQETCGEPTSCQPVHCETGNLETSCGSSTAYYVPRPCQGSSFLPASFFSSSCLPVSCRPQRYVSSGCRPLRPLLNSYQPIGDCVPNAYRPQFCLSKSCQPQNLLTSGCQPSSCLAYRPQSLHVVSSSLRPLGPLFSGCQPLTHVFSTCRPSCSGL
Protein: Importin subunit alpha (Q6P6T9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSTNENANSTAARLNRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKHGAIDPLLALLAVPDLSSLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQSHENESVYKASLNLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF
Protein: IQ motif containing GTPase activating protein 3 (A0A0A6YXJ2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEPCAAGRARTAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEVCLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNINFWLSAVAHIGLPSIFLPETTDIYDKKNMPRVIYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELGNIASELAKYGLQLPAFSKIGGILANEFSADEAAVHAAILAINDAVERGVVEDTLVTLQNPNALLGNLREPLAAVYQELLALAKMEKAANARNHDDGQEQDIYESCLTQAEIQGHINLANVQGALEVVDDALERQNPGALLEALHDPVLALQGVRGTFADWYLEQLTSDREQKSQELGLVRLLEKEEIQAGVAVANEKGDEEQTMLQAVWRINKAIRRGVAADTVKELMCPEAQLPRVYPFASAFYQQELALLQKQQQGELGQEELFVAVEMLSAVVLINRALEAGDVCAFWDNLVNPATGLAQVEEENAQRYFDALVKVQQFQGTHRGILSWNDLQAAVSQVNEQVQEETDQVLAISLINEALDQGCPEKTLSALLLPAAGLEDVSLHVAPRYHLLLVAAKRQKARVTGDPGAVLWLEEIRQGVARANEDTSTAQRSKQRGTLQGGAPHAILP
Protein: Cdc16-prov protein (Cell division cycle 16 L homeolog) (Q6DFI7)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- Anaphase-promoting complex subunit 1
- TPR_REGION domain-containing protein.
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 27 homolog
- Cell division cycle protein 20 homolog
- Cyclosome subunit 8
- Anaphase-promoting complex subunit 13
- Uncharacterized protein.
- Uncharacterized protein.
Sequence:
MNLDRLRKRVRQYIEQQQYQSALFWADKVASLSHEEPQDIYWLAQCLYLTAQYHRASHALRSRKLDKVHEACRYLAARCHYAAKEYQQALDILDMEEPINKKLFEKSLKEDLKEPSGEWQMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKFDVYCFEAFDLLTAHHMLTAQEEKELLDSLPLSKKCSEDQELLRFLYENKLKKYNKPSETLIPESADGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHANCLPVHIGTLVELNKANELFYLSHKLVDLYPNNPVSWFAVGCYYLMVGHKNEHARRYLSKATALERSYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGDWKTAEKWFLDALEKIRVIGDEVTVDKWEPLLNNLGHVLRKLKKYDEALEYHRQALVLIPQNASTYSAIGYIHSLMGNFESAIDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSDAYIGTEIKDKLRCYDFDVHTMKTLKNIISPPWEEREFDFERQSLDESGIMALETSNLLPKSSDTRSPIEEALEIEMNESDMMLETSMSDHST
Protein: Esterase EstP (EC 3.1.1.1) (Autotransporter esterase EstP) (Palmitoyl-CoA hydrolase) (EC 3.1.2.2) (Q88QS0)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Esterase that catalyzes the hydrolysis of p-nitrophenyl esters of acyl chain lengths C4-C10 and Tween detergents. Has also a pronounced thioesterase activity towards palmitoyl-coenzyme A.
Subcellular location: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Acyl-CoA thioesterase I/protease I/lysophospholipase L1
- Thioesterase
- Carboxylesterase
Sequence:
MRKAPLLRFTLASLALACSQALAGPSPYSTLIVFGDSLADAGQFPDLVGGTPGARFTNRDADGNFAPVSPMILGGRLGVAPGDLNPSTSVGIQPDGNNWAVGGYTTQQILDSITTTSETVIPPGNPNAGLVLRERPGYLANGLRADPNALYYLTGGGNDFLQGLVNSPADAVAAGARLAASAQALQQGGARYIMVWLLPDLGQTPNFSGTPQQNPLSLLSAAFNQSLISQLGQIDAQIIPLNIPLLLSEALASPSQFGLASDQNLVGTCYSGDSCVENPVYGINGTTPDPTKLLFNDSVHPTIAGQQLIADYAYSILAAPWELTLLPEMAHASLRAHQDELRNQWQTPWQAVGQWQAFVASGAQDLDFDGQHSAASGDGRGYNLTVGGSYRLNDAWRLGLAGGANRQKLEAGEQDSDYKLNSYMASAFAQYRQDRWWADAALTAGHLDYSDLKRTFALGVNDRSEKGDTDGEAWAMSGRLGYNLAADTSNWQLAPFISADYARVKVDGYDEKSGRSTALGFDDQERTSRRLGVGLLGSVQVLPSTRLFAEVAQEHEFEDDEQDVTMHLTSLPANDFTLTGYTPHSDLTRASLGVSHELVAGVHLRGNYNWRKSDELTQQGISVGVSVDF
Protein: ATP synthase subunit alpha, mitochondrial (P07251)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}. Note=Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit H
- ATP synthase subunit 5, mitochondrial
- ATP synthase protein 8
- ATP synthase subunit d
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit J, mitochondrial
Sequence:
MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF
Protein: Apoptosis-stimulating of p53 protein 2 (Bcl2-binding protein) (Bbp) (Renal carcinoma antigen NY-REN-51) (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2) (Q13625)
Organism: Homo sapiens (Human)
Function: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of NAE1 to conjugate NEDD8 to CUL1, and thereby decreases NAE1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42.
Subcellular location: Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.
Interaction partners:
- Cellular tumor antigen p53
- Apoptosis regulator Bcl-2
- Transcriptional coactivator YAP1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Tumor protein p73
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Ras association domain-containing protein 8
- Hypoxia-inducible factor 1-alpha inhibitor
- WW domain-containing transcription regulator protein 1
Sequence:
MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLKQQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQTKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQSSEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIPSVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPHFSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEVVSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPEGPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA
Protein: Os08g0141300 protein (cDNA clone:001-014-D04, full insert sequence) (Q6YZ10)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MPLWGTGSSAASAAAEGSAAGGDGAARSSSGGAAVIRSLLPTRRRLRLDPPSKLFFPYEPGKQVRSAVKIKNISKSHVAFKFQTTAPKSCFMRPPGGILAPGESIIATVFKFVEHPENNEKPLDQKCKVKFKIVSLKVKGPMEYVPELFDEQKNQVAVEQILRVVFLDAERQTPQMDKLKRQLAEAEAALEARKKPPEDTGPRIVGEGLVIDEWKERRERYLARQQIEGVDSA
Protein: Uncharacterized protein (Q38F97)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tetrapyrrole methylase domain-containing protein
Sequence:
MSLRSTIQTHFTVPTRHHSTRQRSFSGMFSAPASTTAGAPTPIRRFPLNNTQAEPSLGSPCELDFQKGALTGDCVCADRQLEWLRRNLVKSEKRDFHGMSKVKMPEGNPSWPRYHFPLRSCSYIYDPPNESKLAFITPENYCKLCCEPVELPIRHCAWWDHVTRMAGLRLTAIYPRRWDPSALMQELWAGKFPVRFMNTERPHPYLRPSHDGPSWSDLRQCYVFEREAVVRRGELRAILHILSTDVSGGRRVLRESLVLSPDGSYAANVGERTFRAFISRHITPLLPPMGPEPTTRLQQRCWGRKNLEAMFDLLGVEALQRLSGVEEVAVTKNEKATVMRQIVYELTTVLSECDARELSASNEHANEGAHSVKIAKDETHMQVRLLVELALQRLSHELIHLHMMLLIERVWNAYANLGYPGEEAFEESTFC
Protein: Protein FimF (P08189)
Organism: Escherichia coli (strain K12)
Function: Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
Subcellular location: Fimbrium.
Interaction partners:
- Type 1 fimbrin D-mannose specific adhesin
- Protein FimG
- Chaperone protein FimC
- Outer membrane usher protein FimD
- Uncharacterized fimbrial-like protein SfmH
- Probable fimbrial chaperone SfmC
- Type-1 fimbrial protein, A chain
- Probable autotransporter YfaL
- Uncharacterized fimbrial-like protein SfmA
- Fimbrin-like protein FimI
Sequence:
MRNKPFYLLCAFLWLAVSHALAADSTITIRGYVRDNGCSVAAESTNFTVDLMENAAKQFNNIGATTPVVPFRILLSPCGNAVSAVKVGFTGVADSHNANLLALENTVSAASGLGIQLLNEQQNQIPLNAPSSALSWTTLTPGKPNTLNFYARLMATQVPVTAGHINATATFTLEYQ
Protein: Solute carrier organic anion transporter family member 1B2 (Liver-specific organic anion transporter 1) (rLST-1) (Sodium-independent organic anion-transporting polypeptide 4) (OATP-4) (Solute carrier family 21 member 10) (Q9QZX8)
Organism: Rattus norvegicus (Rat)
Function: Mediates the Na(+)-independent uptake of organic anions such as taurochlate, bromosulfophthalein and steroid conjugates (estrone 3-sulfate, 17-beta-glucuronosyl estradiol, dehydroepiandrosterone sulfate). Also transports prostaglandin E2 and L-thyroxine (T4). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions.
Subcellular location: Basolateral cell membrane; Multi-pass membrane protein. Note=Confined to the basolateral plasma membrane of hepatocytes.
Interaction partners:
- Hepatic sodium/bile acid cotransporter
- Bile salt export pump
- Leukocyte cell-derived chemotaxin-2
- ATP-binding cassette sub-family C member 2
- Cytochrome P450 7A1
- Cytochrome P450 family 8 subfamily B member 1
- Solute carrier family 22 member 7
- Long-chain fatty acid transport protein 5
- Cytochrome P450 3A1
- Histidine-rich glycoprotein
Sequence:
MDHTQQSRKAAEAQPSRSKQTRFCDGFKLFLAALSFSYICKALGGVVMKSSITQIERRFDIPSSISGLIDGGFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGSILTALPHFFMGYYKYAKENDIGSLGNSTLTCFINQMTSPTGPSPEIVEKGCEKGLKSHMWIYVLMGNMLRGIGETPIVPLGISYLDDFAKEGHTSMHLGTLHTIAMIGPILGFIMSSVFAKIYVDVGYVDLNSVRITPNDARWVGAWWLSFIVNGLLCITSSIPFFFLPKIPKRSQEERKNSVSLHAPKTDEEKKHMTNLTKQEEQDPSNMTGFLRSLRSILTNEIYVIFLILTLLQVSGFIGSFTYLFKFIEQQFGRTASQANFLLGIITIPTMATAMFLGGYIVKKFKLTSVGIAKFVFFTSSVAYAFQFLYFPLLCENKPFAGLTLTYDGMNPVDSHIDVPLSYCNSDCSCDKNQWEPICGENGVTYISPCLAGCKSFRGDKKPNNTEFYDCSCISNSGNNSAHLGECPRYKCKTNYYFYIILQVTVSFFTAMGSPSLILILMKSVQPELKSLAMGFHSLIIRALGGILAPIYYGAFIDRTCIKWSVTSCGKRGACRLYNSRLFGFSYLGLNLALKTPPLFLYVVLIYFTKRKYKRNDNKTLENGRQFTDEGNPDSVNKNGYYCVPYDEQSNETPL
Protein: Probable carboxylesterase 4, mitochondrial (AtCXE4) (EC 3.1.1.1) (Q9FX93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylesterase acting on esters with varying acyl chain length.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25732537}.
Interaction partners:
Sequence:
MLRRITCSSSLASPSLFLRFFRQLPRSYSSPTTIAVSGRNIRRLSTPTTLRCICSHSSSEIISEHPPFVRVYKDGRIERLSGTETVPASLNPRNDVVSKDVVYSPGHNLSVRLFLPHKSTQLAAGNKLPLLIYFHGGAWINESPFSPIYHNFLTEVVKSANCLAVSVQYRRAPEDPVPAAYEDTWSAIQWIFSHSCGSGEEDWINKYADFERVFLAGDSAGGNISHHMAMRAGKEKLKPRIKGTVIVHPAIWGKDPVDEHDVQDREIRDGVAEVWEKIVSPNSVDGADDPWFNVVGSGSNFSGMGCDKVLVEVAGKDVFWRQGLAYAAKLKKSGWKGEVEVIEEEDEEHCFHLLNPSSENAPSFMKRFVEFITG
Protein: Methionyl-tRNA formyltransferase, mitochondrial (MtFMT) (EC 2.1.2.9) (P32785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Formylates methionyl-tRNA in mitochondria and the cytoplasm. Responsible for the formylation of the 8 N-terminally formylated (Nt-formylated) mitochondrial matrix proteins that are encoded by mitochondrial DNA. Nt-formylated proteins in the cytoplasm are strongly up-regulated in stationary phase or upon starvation for specific amino acids (His or Lys) and are targeted for degradation by a PSH1 E3 ubiquitin ligase-mediated fMet/N-end rule pathway. Increased Nt-formylation of cytosolic proteins appears to be important for adaptation to these stresses. Stationary phase-degraded Nt-formylated proteins include histone H3-like centromeric protein CSE4, Mediator complex subunit 3 (PGD1) and small ribosomal subunit protein uS8-A (RPS22A).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:30409808}. Mitochondrion matrix {ECO:0000269|PubMed:30409808}. Cytoplasm {ECO:0000269|PubMed:30409808}. Note=In exponentially growing cells, more than 97% of FMT1 is present in mitochondria. In stationary phase, about 35% of FMT1 becomes localized to the cytosol in a GCN2-dependent manner. {ECO:0000269|PubMed:30409808}.
Interaction partners:
- C-1-tetrahydrofolate synthase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- C-1-tetrahydrofolate synthase, cytoplasmic
- Phosphoribosylglycinamide formyltransferase
- Dihydrofolate reductase
- Aminomethyltransferase, mitochondrial
- Translation initiation factor IF-2, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
Sequence:
MVKMRRITPTRLLFTCRYISNNASPPVQPLNVLFFGSDTFSNFSLQALNELRQNNGSCGIVDNIQVVTRSPKWCGRQKSILKYPPIFDMAEKLQLPRPITCDTKQEMLALSKLTPSRQGNPENDGSGAPFNAIIAVSFGKLIPGDLIRAVPLALNVHPSLLPRHKGSAPIQRALLEGDTYTGVTIQTLHPDRFDHGAIVAQTEPLAIATMLSKGRVNDSTADFNSEGLPRRTAILMDQLGALGAQLLGQTLRERLYLPQNRVQAPTAYKPSYAHRITTEDKRIHWARDSAAELLNKLETLGPLHAFKEATAARKDAQNSVLKRILFHECKVMRDARLDNGSKPGMFKYDDIKDCILVTCRGNLLLCVSRLQFEGFAVERAGQFMARLRKRCGALSEKLVFL