wanglab/gogpt-training-data huggingface dataset:
Protein: Post-GPI attachment to proteins factor 3 (PER1-like domain-containing protein 1) (A2V7M9)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17314402}; Multi-pass membrane protein {ECO:0000269|PubMed:17314402}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17314402}; Multi-pass membrane protein {ECO:0000269|PubMed:17314402}. Note=Mainly localizes to Golgi apparatus.
Interaction partners:
Sequence:
MAERTARLLLLTVTVGLAWGSQGDREPVYRDCVLRCEERNCSGDALKHFRSLQPIYMSLAGWTCRDDCKYECMWITVGLYLQEGHRVPQFHGKWPFSRFLFIQEPASAVASLLNGLASLVMLCRYRASVPASSPMYHTCMAFAWVSLNAWFWSTVFHTRDTDLTEKMDYFCASAVILHSIYLCCVRTVGLQHPSVARAFGATLLLMLLLHTSYLSLVRFDYSYNMMANVAIGLVNLAWWLAWCLRNHRRLPHTRKCVAVVLLLQGLSLLELLDFPPLFWVLDAHAIWHISTIPVHVLFFRFLEDDSLYLLKESEAKFKLD
Protein: Serine protease gd (EC 3.4.21.-) (Protein gastrulation defective) (O62589)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo.
Subcellular location: Secreted {ECO:0000269|PubMed:9477324}.
Interaction partners:
- Serine protease snk
- Serine protease ea
- Phosphatidylinositol-specific phospholipase C X domain containing, isoform A
Sequence:
MRLHLAAILILCIEHVTKAVAQGMPISPCPKVFQYRFDGSEWFGLMAVRSPDGHQPLHIRVTLSMRGKPTTYTQNYLGEIELLTRGKFTHNAPVLYKIRFPKHHFPPKLLLMSANNHVICFGSGEHSIFMTQIQLEHIRKLSFIPDKKSSLLLDPEEEEVRKTDDKPPSTPHIQFKKKPFAQAPKEICGRIDRDLDFHLSQRTESLHVAIGEPKSSDGITSPVFVDDDEDDVLEHQFVDESEAEAIESDSADSLPSITRGSWPWLAAIYVNNLTSLDFQCGGSLVSARVVISSAHCFKLFNKRYTSNEVLVFLGRHNLKNWNEEGSLAAPVDGIYIHPDFNSQLSSYDADIAVIILKDEVRFNTFIRPACLWSGSSKTEYIVGERGIVIGWSFDRTNRTRDQKLSSELPGKKSTDASAPKVVKAPIVGNAECFRANAHFRSLSSNRTFCAGIQAEERDTHQSGASIYTGISGAGLFIRRNNRWMLRGTVSAALPAVETPDAESSHKLCCKNQYIIYADVAKFLDWITAFVI
Protein: CUB_2 domain-containing protein (O45142)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MCRRTLYALAFLICSVYADPRIIWLYNYDSGSTQNIVPVENGAKLHVASNDNVTLLQNIKIDAGLGAVSLDQVRSIADFKVSSNQLIITSTLDPPTSATLTGFIYVTTAAQANDNTFSVTTVDDLKTLSITSGKSTSVVLNTQFTTTHIRPFNAPDKTTYVTNVQQFGSTSLNFHYGYPNDTVITTNQFFENPQYIDNYDDNGEVANKTRVFFAHVEPIQVNLPYWYITADGPFNIYLDNIYINLNIHNTTSVNTTGAFVLTGVWQNPFVNFMTDPTRGGTTGLLLTTDLESDATILFSRPQSNFDLNFGKTNRMVHGQLLTDAMFNTLQINSTALYPGAMYCQYFVFTGDLLPVTSSVATNPPNPQTTPPVITTTKLASNLNLSSFILLVSSFLCLML
Protein: Protein CutA (Acetylcholinesterase-associated protein) (Brain acetylcholinesterase putative membrane anchor) (O60888)
Organism: Homo sapiens (Human)
Function: May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Copper homeostasis protein cutC homolog
- Filamin-binding LIM protein 1
Sequence:
MSGGRAPAVLLGGVASLLLSFVWMPALLPVASRLLLLPRVLLTMASGSPPTQPSPASDSGSGYVPGSVSAAFVTCPNEKVAKEIARAVVEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSSLVPALTDFVRSVHPYEVAEVIALPVEQGNFPYLQWVRQVTESVSDSITVLP
Protein: Calcium-transporting ATPase 1 (EC 7.2.2.10) (Golgi Ca(2+)-ATPase) (O59868)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transports calcium and manganese ions into the cell. Regulates cell morphogenesis through control of manganese and calcium homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15470240}; Multi-pass membrane protein {ECO:0000269|PubMed:15470240}.
Interaction partners:
- Calcium-transporting ATPase 2
- Vacuolar calcium ion transporter
- Transcriptional regulator prz1
- Calcium-channel protein cch1
- GDT1-like protein C186.05c
- Meiotically up-regulated gene 137 protein
- Uncharacterized protein C19C2.10
- Set1 complex component spp1
Sequence:
MSVQYDAFSVEQTCADLETDMYNGLSSLQEITRRNKVHGDNDLKVEDEENMVVQFLKQFVKDPLILLLFASSAISVTLGNIDDAISIALAIVIVVTVGFVQEYRSEQSLKALNNLVPHYCNVIRSGKTEHIVASKLVPGDLVILQIGDRVPADLRIVEATELEIDESNLTGENSPRKKSSEAISSNISLTERNNIAFMGTLVRHGHGRGIVVATGSDTEFGRVFLTMQQTEKPKTPLQNSMDDLGKQLSLISLIGIAVIVLVGFFQGKNWLEMLTIGVSLAVAAIPEGLPIIVTVTLALGVLRMSKKRAIIRRLPSVETLGSVNVICSDKTGTLTMNHMTVTKIYTCGMLAAFSLPESEHIELSVRRTVGIEKALLAAALCNNSKVHNKADSILDTTCPWAGFPVDVALIECSERFGLKDPRETYSRISEVSFSSERKYMSVAVQYNSSKMNFMKGATEQVLSSCAYFSDQDGVQHELTAEMKENIQRNEFEMAASGLRIIAVASGINTNKLVFHGLFGINDPPRPQVRESVQYLMTGGVRVIMITGDSVVTAISIARSLGMAIPSNDEEAIRNYALTGAQLDDLDSSSLRDAVSRVVVFARTTPQHKMKIVEALQSLGDVVAMTGDGVNDAPALKLADIGIAMGRQGTDVAKEAADMILTDDSFATILSAVEEGKGIFNNIKNFITFQLSTSVAALSLIAISSVFGFQNPLNAMQILWINILMDGPPAQSLGVESVDEDVMMKPPRPRNAPIISVQLLQRVLLSAFIIVTVTIVVFRVQMQDGNVTARDTTMTFTCFVFFDMFNALACRSETKSVFKLGIFSNRMFNIAVGGSLIGQALVVYASPFQRIFQTEAIGLKDVLILLACTSSVLWVDEIRKWYRRRKGLVRTKSNYLLRNV
Protein: Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (P09124)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10658653}.
Interaction partners:
- Enolase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Probable fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Central glycolytic genes regulator
- Pyruvate kinase
- Glucose-6-phosphate 1-dehydrogenase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Transketolase
Sequence:
MAVKVGINGFGRIGRNVFRAALNNPEVEVVAVNDLTDANMLAHLLQYDSVHGKLDAEVSVDGNNLVVNGKTIEVSAERDPAKLSWGKQGVEIVVESTGFFTKRADAAKHLEAGAKKVIISAPANEEDITIVMGVNEDKYDAANHDVISNASCTTNCLAPFAKVLNDKFGIKRGMMTTVHSYTNDQQILDLPHKDYRRARAAAENIIPTSTGAAKAVSLVLPELKGKLNGGAMRVPTPNVSLVDLVAELNQEVTAEEVNAALKEAAEGDLKGILGYSEEPLVSGDYNGNKNSSTIDALSTMVMEGSMVKVISWYDNESGYSNRVVDLAAYIAKKGL
Protein: Chitinase-like protein Idgf1 (Imaginal disk growth factor protein 1) (Q8MM24)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex.
Subcellular location: Secreted {ECO:0000269|PubMed:9847235}. Note=Secreted in hemolymph. It is probably transported to target tissues via hemolymph.
Interaction partners:
Sequence:
MRFQLFYILGLLSVTSLTHAASNLICYYDSNSYLRQGLAKMHTNELDLALQFCTHLVYGYAGLKSGTLELFSLNVDLDMFYYKDITALRQKFPQLKILLSVGGDRDVDEAHPNKYVELLEANRTAQQNFIDSSMILLKRNGFDGLDLAFQLPRNKPRKVHGSLGSYWKSFKKLFTGDFVVDPQAEEHKSQFTDLVGNIKNAFRSANLMLSLTVLPNVNSTWYFDVPKLHPQFDYINLAAFDFLTPLRNPEEADFTAPIFFQDEQNRLPHLNVEFQINYWLQNHCPGQKLNLGIASYGRAWKLSKGSGLSGAPIVHETCGVAPGGIQIQSAEGLLSWPEICSKLSQNASAQYRGELAPLRKVTDLTQKYGNYALRPADDNGDFGVWLSFDDPDFAGIKAVYAKGKGLGGIALFDLSYDDFRGLCTGQKYPILRSIKYFMG
Protein: AT24447p (Rho guanine nucleotide exchange factor 3, isoform B) (Q8IRJ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRIDKILVVSRGKASSVEVAALRYIAASIATATLDSQSSQQIKAVSSPTLSEPCLEEQPQKGTESTDVANTGSSAGSGGLGVLQKFKRTLNNFNNKNQLHISPLSPAAVAPMITTTTASDPGSEAGDTSSGKYRFGPLIWRSSKERRKTKYNRRDKCNSGDSGIQIELEQDEQYSRATMAVSRQDEPRAFALTNGSCGVALSKMRAIRRTNSAKASSILGPFIVKTKIAKHLNIGESDKAERKAPESLPTRSLSQPNGLESYGMGRPDLEDSDSDSVASNEEAISFYPTTYAEVLYNFTAGGPQELGLERGMLIEILRKEVGPWWFGRIKKEETNLVEDILGPELGWFPKEFVRIIHCPETDNFFIAHRAAADEAAAEEATARAEEGSVPVPVAAFAEDTDVTVTTDQSNVTLIVIESPPTPSAPSVDFVAQPDHSTIIRRSAVRELLDTEVNYVKLLAAICDGYLPAMSKRIDIFSPNSIRLIFSNITAIYKFQRKFLEALRRGIEQNQVAKVFLKMHKGFLCYSTYCNAYPRALIELETYDRVKDARTILENCRESQNLAELPLSAHLLAPVQRICRYPLHLNEIIKSALEKGAKEGNDTDGAKSAGKTTDYEQLDVTELDIPDSQDTVNLALEAMRGITEAVNEGKRHSETIARHQASFQNFKGPPLHLHSARFFLQVDATRQKQNLWNSSYTLFLFDNQLVYCKRDIIKRSHFIYKGRIFLDRCRVVNVRDGKMFGHTIKNSLRIYSESRDKWYDFSFRSANRKHRFLSTLALERQFGGKALYVSEMTGFEYNYEERPGDYSDQSDYDAQDFELATGVTSGESSLPESPAKSTSRLCETLPKKSQSRDGISSAENSQIVTTTSTGSLGRRHFGNWFRKPKSANCTPSQSPTHKPSFDADATLTEARVAAMELAEAAAALVPTDSSSA
Protein: Apolipoprotein B receptor (Apolipoprotein B-100 receptor) (Apolipoprotein B48 receptor) (apoB-48R) (Q8VBT6)
Organism: Mus musculus (Mouse)
Function: Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Binds monocyte-macrophage membrane. Thought to be anchored in the membrane through an interaction with an integral membrane protein (By similarity). {ECO:0000250}.
Interaction partners:
- Apolipoprotein B-100
- Apolipoprotein A-V
Sequence:
MDFLRLRLPGLHQALRGALDSFSAFVSYLVGDTVPTVERQTQAAEELGEVTEGKVVGEEAQEVLEGLRSGQSEGVEAPEETRRCQEGSLAGEQTWGWRADSSARPQAERQDTGSWKAAEDARGQEPSVPLKPEAEPGTHRDRSSNTAQEIWEHGEEEASSGEPLRTCEQKEEEEEVVRAAESGMAEGVESQPTWHSEPGGNAGTEGQHVTEDSKEIDWVAKDMVAEIEWFGAKGIDKEEERMVPMRDGERARAQGTQCPGAESEDQAMLSREAWTVSDREGADSLGVQGTEYGSDPGDNFPGTTGRVWVLEEADKGDQQDEVDEKREAEVRFPIQTLEAERTGEMTEGHIAEEEAMGEQETEGSFEDEERQDLAIRDNGVSLEEEVRAEESSREKRNSWATEPTLVLDTEAKDEPDWEDSPEVSTEELFVGERSEAAQMTPEVLRVKVTEGQDPELVRHSQALTKQLEEGQKGQEETSGAPDLSPERVLSLKEYPGPVGFAGPELEAWGNWSRGVDRRNSQEVKADAEAGKEQTATEQAVEIRAEGGQEAQQPEVFGSGGEEALTSVALNPELEGSQGAEAGTEESVEESKPTENEAAEEEAVVPWEADGTCRKRRLEEVTLSLQDSEDTETSYLAEEIIVGIRAVDTEEGPKWEAGLAPETELGKAWCSEGRGEAGRGTELEETTEKQSGQEVGLVGSAEKVSGYDIQEIDGTEEGEQAEMETSVMAEDIRGTDGVTLGSQAERAEGSITPMETEGLLRDQMLLEEEAGGGQSREQKVHNSEGEIQTLDDSSDQEGQQTHQIPTVAVPGPLESAEATAGAPGDVHSNWNEALLPGSRLDVSVPRSRVLLSRSSSRRRSRPSFHRISVPEPQCDPPSPQPQAERPVPEQSSLQLEETPELSATKPEGTPVPARRKMLGRGFGFAHPGMMQELQARLSQPKPQ
Protein: X-ray repair cross-complementing protein 5 (EC 3.6.4.-) (A0A0R4IB13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
Interaction partners:
- DNA helicase
- DNA-dependent protein kinase catalytic subunit
- DNA ligase
- WRN RecQ-like helicase.
- Non-homologous end-joining factor 1
- Double-strand break repair protein
- DNA repair protein RAD52 homolog
- Protein artemis
- Zgc:165656.
- non-specific serine/threonine protein kinase
Sequence:
MARAAKSALVLCMDVGFSMSNSGPGQEPPFEQAKKVIQKFVQRQVFAENKDEIGLVLFGTDGTKNPLANDGQYENITVHRHLMIPDFELLEEIERELQPGGQQADWLDALVVCMDLLQNETMGKKYDRLNIALLTDLNIQTSEDQLDIIIQNLKKAGITLQFFLPFPVDVEDEAGGGGDAAGPSAPPSRPGKGLSRQQTQGLEMVKHIMSSLEDEDGLEEVYTFSDALEKLSIFKRIERRPMAWPCQLTIGSSLSIRIVGYKAVTEEKVKKSWTIVDAQSHQRDDVKRETVYCLNDDDETEVQKDDTIQGYRYGSDIVPFSKVDEEQMKYKHDGKCFSVLGFTKQELIPRHQFMGSQVVKVFAPRDDEHAAVALSSLIRALDGLKMAAIVRYAYDRRSNPQVGAAFPCIKKKYECLLYVQLPYMEDLRQFTFPMLENNKKFMPSGSQLSAVDALIDSMMLMEKDENGESVEIFKVNHIPNPQFQRLFQCLHHRGVNPDDPLPPVDPWLKRVLERPQAVSARCQAPLRDVKTSFPLKVVVKKKEQKTSADVFGSSADEPDAKKVKVNEETEFNLAEITEGNITSVGSVNPARDFCTLIRQKTVSFDQACQQLTHRIEQLLGNRSTEYYTKSIACIQAFRDQSVLSGNAELFNSYLQSLKRSIADRSLQDFWNLLAQDALTLISKDEVEASTISKQEANQFLSFEQKQEVEVAPAQDDTGDVDDLLDMM
Protein: Homeobox protein DLX-4 (Beta protein 1) (Homeobox protein DLX-7) (Homeobox protein DLX-8) (Q92988)
Organism: Homo sapiens (Human)
Function: May play a role in determining the production of hemoglobin S. May act as a repressor. During embryonic development, plays a role in palatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:25954033}.
Interaction partners:
Sequence:
MTSLPCPLPGRDASKAVFPDLAPVPSVAAAYPLGLSPTTAASPNLSYSRPYGHLLSYPYTEPANPGDSYLSCQQPAALSQPLCGPAEHPQELEADSEKPRLSPEPSERRPQAPAKKLRKPRTIYSSLQLQHLNQRFQHTQYLALPERAQLAAQLGLTQTQVKIWFQNKRSKYKKLLKQNSGGQEGDFPGRTFSVSPCSPPLPSLWDLPKAGTLPTSGYGNSFGAWYQHHSSDVLASPQMM
Protein: Snaclec CHH-B subunit alpha (P81508)
Organism: Crotalus horridus (Timber rattlesnake)
Function: Binds to the subunit GPIbalpha (GP1BA) of the platelet GPIb/V/IX receptor system. It inhibits ristocetin- and vWF-induced platelet aggregation in platelet-rich plasma by inhibiting the binding of vWF to GPIbalpha.
Subcellular location: Secreted {ECO:0000269|PubMed:8823201}.
Interaction partners:
Sequence:
DLECPSGWSSYDRYCYKPFKQEMTWADAERFCSEQAKGRHLLSVETALEASFVDNVLYANKEYLTRYIWIGLRVQNKGQPCSSIYSENLVDPFDCFMVSRDTRLREWFKVDCEQQHSFICKFTRPRR
Protein: Protein SPOROCYTELESS (Protein NOZZLE) (Transcription factor SPL) (O81836)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator of sporocyte development. Acts as an adapter-like transcriptional repressor recruiting TPL/TPR corepressors to inhibit TCP transcription factors. Required for nucellus and embryo sac development. Plays a central role in patterning both the proximal-distal and the adaxial-abaxial axes during ovule development. Involved in establishing the prospective chalaza of the ovule and in controlling the cell number and the length of the funiculus, and is required for the development of the integuments. Required, with BEL1, for cytokinin-induced PIN1 expression in ovules. Involved in controlling stamen identity. May also regulate the morphology of lateral organs by repressing auxin production.
Subcellular location: Nucleus {ECO:0000269|PubMed:10465788}.
Interaction partners:
- Transcription factor MYB35
- Transcription factor DYT1
- Leucine-rich repeat receptor protein kinase EMS1
- Axial regulator YABBY 4
- Short-chain dehydrogenase reductase ATA1
- Pentatricopeptide repeat-containing protein At4g38150
- Protein TAPETUM DETERMINANT 1
- Protein WUSCHEL
- Transcription factor MYB80
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 13
Sequence:
MATSLFFMSTDQNSVGNPNDLLRNTRLVVNSSGEIRTETLKSRGRKPGSKTGQQKQKKPTLRGMGVAKLERQRIEEEKKQLAAATVGDTSSVASISNNATRLPVPVDPGVVLQGFPSSLGSNRIYCGGVGSGQVMIDPVISPWGFVETSSTTHELSSISNPQMFNASSNNRCDTCFKKKRLDGDQNNVVRSNGGGFSKYTMIPPPMNGYDQYLLQSDHHQRSQGFLYDHRIARAASVSASSTTINPYFNEATNHTGPMEEFGSYMEGNPRNGSGGVKEYEFFPGKYGERVSVVAKTSSLVGDCSPNTIDLSLKL
Protein: ATP synthase F(0) complex subunit g, mitochondrial (ATPase subunit g) (ATP synthase membrane subunit g) (Q6PDU7)
Organism: Rattus norvegicus (Rat)
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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase subunit ATP5MPL, mitochondrial
- ATP synthase F
Sequence:
MAKFIRNLADKAPSMVAAAVTYSKPRLATFWHYARVELVPPTLGEIPTAIQSMKSIIHSAQTGNFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV
Protein: DNA damage response protein Mdb1 (BRCT domain protein Mdb1) (Midzone and DNA break-localizing protein 1) (O14079)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in DNA damage response (DDR) mediated through its interaction with phosphorylated H2A proteins hta1 and hta2 which mark the discrete foci of DNA damage.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Chromosome {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}. Note=Associated with chromatin. Relocalizes to discrete nuclear foci at DNA double strand breaks (DSBs) following DNA damage by the HO endonuclease and ionizing radiation (IR). Focus formation requires interaction with phosphorylated hta1 and hta2. During mitosis, localizes to spindles and concentrates at spindle midzones at late mitosis. Localization to spindle midzones requires ase1, but does not require phosphorylated hta1 nor hta2 (PubMed:24806815). Localizes to spindle midzones in anaphase (PubMed:26160178). {ECO:0000269|PubMed:24806815, ECO:0000269|PubMed:26160178}.
Interaction partners:
- S-M checkpoint control protein rad4
- DNA repair protein crb2
- Serine/threonine-protein kinase tel1
- DNA repair and telomere maintenance protein nbs1
- Histone H2A-alpha
- Histone H2A-beta
- Uncharacterized protein C13G7.11
- BRCT-containing protein 1
Sequence:
MEIQFGNQRCRMVNSGGFLATDGSHLKEMETDDVLVEFLNIEHQLFIRNIRAIVKIADTTVLPSASDKKLLYYVFDETRVRINDTPVIFSKLEEDNANVNEGSKMGVMTVPNTPQKPNLQQQKFEAINANEDQIDYSSNLEQNYNSLIRQGSDQVIPLSRFASEKSALELEKELFSERIPESQSAAEPVLKVENSENDLDEKLVLDGQHVEGDHSSDTEEEVVSEDQKQLNKTDDESTFIESHQIYIQGETKSPSSVSQSLSGDPSLKPAEVFDRKQSAEINSPIEKDVNPQQNISDSSIKNNSIHSDEVNPEVRPDLTPSNENEESKRSAPEIALKEKESTSQDESNREAEEAPISTNYSFPSSSLEDQPDKNVQSSAVENKNKHTNLVTSSFNLTKPMKSFIRRNGLRVQESVTDETDFVILGSPPLRRTHKFLLATSLGIPLVSSQYLTDCIKSGKVLDFRSYKYKDEEAEAKWGFRLDDIHRRTCFNGKRLYITKAIRDSMVGDSIHGLYSILETSGAEIVGDIKRAQEKDTIILAQPDNDQEGRNMSATGLNVYKIELVALSILRDRIDFDEFLIDYDADSPTKVIGKRNVSKASRTGQGRKRSSRSSWNKPSAKEQRT
Protein: Cilia- and flagella-associated protein 43 (WD repeat-containing protein 96) (Q8NDM7)
Organism: Homo sapiens (Human)
Function: Flagellar protein involved in sperm flagellum axoneme organization and function (By similarity). Involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract (By similarity).
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JAF2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E9Q7R9}.
Interaction partners:
- Tetratricopeptide repeat protein 29
- Cilia- and flagella-associated protein 251
- Cilia- and flagella-associated protein 69
- Glutamine-rich protein 2
- Dynein axonemal heavy chain 1
- Cilia- and flagella-associated protein 70
- Cilia- and flagella-associated protein 91
- Coiled-coil domain-containing protein 39
- Tetratricopeptide repeat protein 21A
- Sperm flagellar protein 2
Sequence:
MAQGRERDEGPHSAGGASLSVRWVQGFPKQNVHFVNDNTICYPCGNYVIFINIETKKKTVLQCSNGIVGVMATNIPCEVVAFSDRKLKPLIYVYSFPGLTRRTKLKGNILLDYTLLSFSYCGTYLASYSSLPEFELALWNWESSIILCKKSQPGMDVNQMSFNPMNWRQLCLSSPSTVSVWTIERSNQEHCFRARSVKLPLEDGSFFNETDVVFPQSLPKDLIYGPVLPLSAIAGLVGKEAETFRPKDDLYPLLHPTMHCWTPTSDLYIGCEEGHLLMINGDTLQVTVLNKIEEESPLDRRNFISPVTLVYQKEGVLASGIDGFVYSFIIKDRSYMIEDFLEIERPVEHMTFSPNYTVLLIQTDKGSVYIYTFGKEPTLNKVLDACDGKFQAIDFITPGTQYFMTLTYSGEICVWWLEDCACVSKIYLNTLATVLACCPSSLSAAVGTEDGSVYFISVYDKESPQVVHKAFLSESSVQHVVYDQQGIFLLVGTAEGKVFIINANSSSSFQIIGFTEVAKDILQISTVSLLETDIVEVMVLSSLPEAGRSRLEMFTLPTLLPQVSTTFADERGRLKDEIIHKYLYELEHALSSAVLGFQSNQIYGFCSQVPYICSYLLPEEEHTGIYILKPYKKVQSRQYGPGLLYLSSHGLWLITIAKCGILCIRDVYTLETFAWCRSHSHQGHGIQSMRISMDGQNILVNGRDDGTLVYLKWKRFGGHLASEILDYYQKLLISLSSAMDKENHYLSTTPKVSVDLGSDSEHTKQKASTDLSQDELVLTDVKKEIPWIQQKSQEAIKKEVNLFSKKRKEIKQGIKSLSKTILNMMEENDKLENIAKLDQQEFGLDLEELERLHDESQEEVAKMIKDVEMHNLAKSYLAELIKEECWNSMAVKGRALKCFHIPCVVENFPMKARTVEELKELERVLQQKKIEAECLKLRKEIVEAQSGVKLIKQRHEEDDEEEEEEDKTVKYSNLPNYLLGSLSTDFGVDTSLLSSQLELHSREEKINQIILLKDIIYKVKTVFNNEFDAAYKQKEFEIARVKERNVRIREIILDLELEEAVWQPEFEDCEKPERTLVVQDEEITAHKHIKPWHKAKELIVNHEKEHWLLIQDASTRLRALMDMMGGVLEVKKEDILRMVIPQPAFMAKPDAVWTEEERKQFKDYEKKVKELNEERDKYRKSLEAELKKLQNSIQESTQAFDEHLKRLFERRVKAEMVTNQEELKISNLAFSLLLDEELSSREKFLNNYLTRKQHEKSQTSEAVRKSREDLDVCKEHYDNLLAEDKVMDRSFKKEFSEIPGHQVDILYKLFKRRPRISKQKTHSETTSVVPFGELPGSGKLNKDAFAQLMKAMDELDNISNMPEGLDPLVWNHFCMTRRAKVENEQKVKQKAADLLEMATFLQKRVEEEEKVQQEIERVFHELILLQEEKVRFQLNLTIQILLKQGQVELENFQLVLEYSDAILINKNIIEDLNSVIRTQGQKKVASMMESKDVHKRILQIEWEHKKMEMEREDLNQKAWDIQMLFFSRDRQKYLNEPNYEALISIQIGIMEQTIAVLDKMHKKNVENCKKLLKKLGKFSNQKDIANYALSCNLREELVAVSERKDICNAMGSKLTCEKIVKERYENMMQQQKLTNISKQQAEQISILQTEVERLRMKTFPALVQM
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (A0A1D8PJV4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MSKDKKQVDPLKSFIAGGTAGAVEGIITYPFEFAKTRLQLISKSSTASRNPLVLIYNVAKTQGVSSLYVGCPAFVVGNTLKASVRFLGFDSIKNLLSDKNGKLSGPRGVIAGLGAGLLESVVAVTPFEAIKTALIDDKQSIKPKYQNGVISGSFKLVRDMGFKGIYAGVVPVSLRQAANQAVRLGSYNAMKTMIQQASGQKPNEPLSGTTTFAVGALAGIITVYTTMPIDTVKTRMQALGADKLYSSTLNCFVKIFKDEGLLTFWKGATPRLGRLVLSGGIVFLCYEKIMILLN
Protein: Small ribosomal subunit protein uS11m (28S ribosomal protein S11, mitochondrial) (MRP-S11) (S11mt) (Cervical cancer proto-oncogene 2 protein) (HCC-2) (P82912)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS10m
Sequence:
MQAVRNAGSRFLRSWTWPQTAGRVVARTPAGTICTGARQLQDAAAKQKVEQNAAPSHTKFSIYPPIPGEESSLRWAGKKFEEIPIAHIKASHNNTQIQVVSASNEPLAFASCGTEGFRNAKKGTGIAAQTAGIAAAARAKQKGVIHIRVVVKGLGPGRLSAMHGLIMGGLEVISITDNTPIPHNGCRPRKARKL
Protein: Uncharacterized protein Rv0894 (P9WKP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Transcriptional regulatory protein MoaR1
- Transcriptional regulatory protein EmbR
- Uncharacterized protein Rv0891c
- Putative diacyglycerol O-acyltransferase Rv0895
- Uncharacterized protein Rv1359
- Probable transcriptional regulatory protein
- Transcriptional regulatory protein TcrA
- site-specific DNA-methyltransferase
- Putative mycofactocin biosynthesis transcriptional regulator MftR
- Possible transcriptional regulatory protein
Sequence:
MPSRATVQEFSDSYPFCHNGFRPIMMPKIVSVQHSTRRHLTSFVGRKAELNDVRRLLSDKRLVTLTGPDGMGKSRLALQIGAQIAHEFTYGRWDCDLATVTDRDCVSISMLNALGLPVQPGLSAIDTLVGVINDARVLLVLDHCEHLLDACAAIIDSLLRSCPRLTILTTSTEAIGLAGELTWRVPPLSLTNDAIELFVDRARRVRSDFAINADTAVTVGEICRRLDGVPLAIELAAARTDTLSPVEILAGLNDRFRLVAGAAGNAVRPEQTLCATVQWSHALLSGPERALLHRLAVFAGGFDLDGAQAVGANDEDFEGYQTLGRFAELVDKAFVVVENNRGRAGYRLLYSVRQYALEKLSESGEADAVLARYRKHLKQPNQVVRAGSGGVRY
Protein: Thioredoxin domain containing 9 (F8WCJ3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEADASVDMFSKVLEHQLLQTTKLVEEHLDSEIQKLDQMDEDELERLKEKRLQALRKAQQQKQEWLSKGHGEYREIPSERDFFQEVKESENVVCHFYRDSTFSVAYLGVRSFSSVMLFSFSS