wanglab/gogpt-training-data huggingface dataset:
Protein: 5'-3' exoribonuclease XRND, putative (Q38AY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 5'-3' exoribonuclease 2
- 5'-3' exonuclease XRNC, putative
Sequence:
MGIAGFYLWLKRWYASCMEDVPQCVVEAASKSSPPPKEYMQSHKFDNLYLDLNGLVHPCCHDTSPLPEPESEEEMFERVFTQIDLVFKVVRPRKCLILCVDGVAPQSKMNQQRSRRFRAAEERAEGEVMSAKCADVLLEKGLPYPKVRERWDHNVITPSTPFMERLGLAIEWFVVKKVNEDPLWKKVAVVFSDAHVPGEGEHKIMQYIRGLRMQPGYDPDTSHVIYGMDADLISLGLSTHEKSVTILRNQLNETFNAAHGKFCYFSLVKFRECLKRDFDGIKEMSFERVVDDFIFLCFFVGNDFLPHVPLISIKTRGVELLLDHYVNEFASHSYLTDGGEVRFKALSSFLARFLNDYGSVLRDESSFGERAKERGRGNVAERVNKYQVELKKVLASVKRDKTNAQEVSDTAHKLMVSALKERVSFVGDKGSLGFTYHDEDYRDKYYQKKFGWDPEKRSKFEKRVKRCCAEYLRGTQWVMRYYTSGCPSWNWFYPYHYAPLLDDLARFTDSVDVEFERGTPRHPVVQLLAVLPRMSVGGLPVELHGAVLDPNSVFGPFYPDHVDVDYSEAIFAYQGVLRLPFIDCKEIEAACNTLVELQPDSGVTLLICNSGSKLSIMLEEYLGGVPKKKKRSSMKPIPTEVAAKFPIAGRVGYYRNEWKRDVQIVCPDAAIAEKTAHGGAIECNAARCYRYELDELAVYRPELLLKYGMDGPPKAVTAEEVSVGDVAAQPEETTNVKDSSPDAQYPETATVAGECSTRRKKRARVEVPPADPFNGSDDPPQKKPRLKKAAKKRGADRVIGR
Protein: Probable soluble pyridine nucleotide transhydrogenase (STH) (EC 1.6.1.1) (NAD(P)(+) transhydrogenase [B-specific]) (P9WHH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Multifunctional 2-oxoglutarate metabolism enzyme
- proton-translocating NAD
- NAD
- NAD
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Glutamine-dependent NAD
- NAD-dependent protein deacylase
- NAD-capped RNA hydrolase NudC
- NAD kinase
Sequence:
MREYDIVVIGSGPGGQKAAIASAKLGKSVAIVERGRMLGGVCVNTGTIPSKTLREAVLYLTGMNQRELYGASYRVKDRITPADLLARTQHVIGKEVDVVRNQLMRNRVDLIVGHGRFIDPHTILVEDQARREKTTVTGDYIIIATGTRPARPSGVEFDEERVLDSDGILDLKSLPSSMVVVGAGVIGIEYASMFAALGTKVTVVEKRDNMLDFCDPEVVEALKFHLRDLAVTFRFGEEVTAVDVGSAGTVTTLASGKQIPAETVMYSAGRQGQTDHLDLHNAGLEVQGRGRIFVDDRFQTKVDHIYAVGDVIGFPALAATSMEQGRLAAYHAFGEPTDGITELQPIGIYSIPEVSYVGATEVELTKSSIPYEVGVARYRELARGQIAGDSYGMLKLLVSTEDLKLLGVHIFGTSATEMVHIGQAVMGCGGSVEYLVDAVFNYPTFSEAYKNAALDVMNKMRALNQFRR
Protein: DNA primase large subunit PriL (Q9UWW1)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.
Interaction partners:
- DNA primase small subunit PriS
- Primase X domain-containing protein
- DNA polymerase 1
- Minichromosome maintenance protein MCM
- DNA primase DnaG
- DNA polymerase 3
- ORC1-type DNA replication protein 2
- DNA polymerase 2
- ORC1-type DNA replication protein 1
- ORC1-type DNA replication protein 3
Sequence:
MALDVKKYPFIKSLDDELKKYGGGITLTDLLLNSTTLIDQAKDRIQKTKSGDELPHYVSYNEPVLVFYTTLLSLAILNDVKLIRRYAYAEAKQFRSLLHTENEENLLEISKLLDLKINRCDPIKFYLEKKRRIIQKEFCVHFIDYLKYTKDLKEDWKLSGQILHKGYVYLDKNQLIGLIAESIKSKIVEMIRPLNLKEIPEKLKSLIERRGIIPPCIENILAKEKLNEEEIRTLITFYIDIGKGLSGIVSIMKKYNVSNVEDLYRKYRGDKGTRYIVYSCAKMKQLGLCVSSCNVKNPLQLYFLSNE
Protein: Long-chain acyl-protein thioester reductase (EC 1.2.1.50) (Acyl-CoA reductase) (P19841)
Organism: Photobacterium phosphoreum
Function: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
Interaction partners:
- Long-chain fatty acid--CoA ligase
- Acyl transferase
- Alkanal monooxygenase alpha chain
- Alkanal monooxygenase beta chain
- Glutamate synthase large subunit
- PTS sugar transporter
- Phosphate acetyltransferase
- Multifunctional fatty acid oxidation complex subunit alpha
- Multifunctional fatty acid oxidation complex subunit alpha
- Bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
Sequence:
MCNAEFKGDCMIKKIPMIIGGAERDTSEHEYRELTLNSYKVSIPIINQDDVEAIKSQSVENNLNINQIVNFLYTVGQKWKSENYSRRLTYIRDLVRFLGYSPEMAKLEANWISMILSSKSALYDIVETELGSRHIVDEWLPQGDCYVKAMPKGKSVHLLAGNVPLSGVTSIIRAILTKNECIIKTSSADPFTAIALASSFIDTDEHHPISRSMSVMYWSHNEDIAIPQQIMNCADVVVSWGGYDAIKWATEHTPVNVDILKFGPKKSIAIVDNPVDITASAIGVAHDICFYDQQACFSTQDIYYIGDNIDAFFDELVEQLNLYMDILPKGDQTFDEKASFSLIEKECQFAKYKVEKGDNQSWLLVKSPLGSFGNQPLARSAYIHHVSDISEITPYIENRITQTVTVTPWESSFKYRDVLASHGAERIVESGMNNIFRVGGAHDGMRPLQRLVKYISHERPYTYSTKDVAVKIEQTRYLEEDKFLVFVP
Protein: Putative transposase InsO for insertion sequence element IS911A (P75680)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MATLCHVFGVHRSSYKYWKNRPEKPDGRRAVLRSQVLELHGISHGSAGARSIATMATQRGYQMGRWLAGRLMKELGLVSCQQPTHRYKRGGHEHVAIPNHLERQFAVTEPNQVWCGDVTYSVPGVQGGHGCLNEPRVCLEY
Protein: Alternative transcription initiation factor, sigma-F (FliA) (O25676)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliN
- Bifunctional DNA-directed RNA polymerase subunit beta-beta'
- Flagellar basal body rod protein FlgB
- Flagellar hook-associated protein 1
- Flagellar basal-body rod protein FlgC
- Flagellar hook-associated protein 2
- DNA-directed RNA polymerase subunit alpha
- Flagellar motor switch protein FliG
- Flagellar protein FliL
Sequence:
MILMMENRMPKGIQKTETSEKNIEKVLNAYDKQQHHHQDDLAIQYLPAVRAMAFRLKERLPSSIDFNDLVSIGTEELIKLARRYESALNDSFWGYAKTRVNGAMLDYLRSLDVISRSSRKLIKSIDIEITKHLNEHGKEPSDAYLAQTLGENIEKIKEAKTASDIYALVPIDEQFNAIEQDEITKKIEAEELLEHVQKALNQMSEREQILIQLYYFEELNLSEIKEILGITESRISQIIKEVIKKVRKSLGVDHG
Protein: ORF31 (E5LBV4)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MKSVASPLCQFHGVFCLYQCRQCLAYHVCDGGAECVLLHTPESVICELTGNCMLGNIQEGQFLGPVPYRTLDNQVDRDAYHGMLACLKRDIVRYLQTWPDTTVIVQEIALGDGVTDTISAIIDETFGECLPVLGEAQGGYALVCSMYLHVIVSIYSTKTVYNSMLFKCTKNKKYDCIAKRVRTKWMRMLSTKDT
Protein: IP10846p (IP10946p) (IP11146p) (Q4V4D1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- MIP03875p
Sequence:
MSSPLLVTQQSQDASLPTWVEKKELEALVKQISEFRKIESLRWKWETQLAEPALCVHIQVLVADNKKRQVSYLIKSPETVPVGLKLPRTGDFSTERHMFEVVLPALEELYQNSDRIVHFGPPVIQAKLKSSHIYGDYILNKGYSVANGLKGLSVTAMEGVLSKLAAYHAGTAAYIAKTPGKIRELPKLRENSKSDEETAELKSLYQLRFHESLRSNDARQYEDKVKSFQKYVKSGTEILDSKTSFNVILNGSCWPNNLLLQVDAFGNVKDTLFSGFHTAQYGPAVYDLFSSLLTAPAEKSSRFDGYVKFYHDQLIENLNLLKFLGKKPSLTDLQLDLLKYGHWAFETATEILPIVLSDFGNNDIEELFRNPVFGEQIRELLPWMENRGYFEED
Protein: Myelin protein P0 isoform X1 (Myelin protein zero) (A0A2R8QN30)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLSVLALTSVVLLGIASQSTALVVNTDSEKHALVGSDVRLSCSFFSWQWTSPEVSFTWHYRPDGAKDAISIFHYGGGEAYPANKGPFQNRLEFVGNPSRRDGSILIKNLDFGDNGTFTCDAKNPPDIGGHPSTIRLLVFEKVPVQAGVITGSIIGVVLGLLILVVAIYYLMRFLVARRVFSLSMSKHGKKGKGKEGSQQKQASAVTDPAKLKAAASEKKKQESRREKK
Protein: Keratin-associated protein 19-8 (Q3LI54)
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:
Sequence:
MSYYRSYYGGLGYGYGGFGGWGYGYGCGYGSFRRLGYGCGYGGYGFSCCRPLYYGGYGFSAFY
Protein: Hydrophobic protein LTI6A (Low temperature-induced protein 6A) (Q8H5T6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MADSTATCIDIILAIILPPLGVFFKFGCGIEFWICLLLTFFGYLPGIIYAVWVITK
Protein: Octylphenol 4-monooxygenase (A7YJX0)
Organism: Sphingomonas sp. PWE1
Interaction partners:
Sequence:
MENEMTTEPGDRASQFDVAIVGCGPVGALLANLLKQYGHKVAVLEREPDIFYAPRGMGFDDESTRIMQSAGILDRLKAEGHIYQADLELIDRSGKRLGGFDRRSVGEDLLSGLHGHRHLTLFHQPSLEATLREEFATGENAATAYFNHEVTGITDQGDRVELNCKDRATDEEHSLIAKYVVGCDGARSTVRKTMNVPRIDLKYTQKYLVVDAIVDDPVYFRTMIPQGGYILLDGKEAGVLAKGLHGHVRFDFLQHSETIGQELKTDEDYQKAARDLIRSRGFDPENFRVIRSVSYTFHAGMPSKWRVGRLMVAGDAAHLTPPWSGQGLNMGVRDAANLSFKLNLALRGKSSDRILDTYDEERRPQSLETIQAAVDMGIRMQNTSPLQIGLRNLAYALSRKSKFVNRLLFKNWIRKPSYKSGLLGLQHRLSGGPMFQPWVETAEGKRVRMDDLIGLNFALISTDSPTGPEVRQFVSELGGVVLKLDCDFFDPSETVCKWYDEHRINAVLLRPDRVIYDAGRDGQALCRSLLAELRK
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q8SXB2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLSWRSDVNSRQDRYEVHYQRNGTREERTMATNETSLTIHYLHPGSGYEVKVHAISHGVRSEPHSYFQAVFPKPPQNLTLQTVHTNLVVLHWQAPEGSDFSEYVVRYRTDASPWQRISGLHENEARIKDMHYGERYLVQVNTVSFGVESPHPLELNVTMPPQPVSNVVPLVDSRNLTLEWPRPDGHVDFYTLKWWPTDEEDRVEFKNVTQLEDLSSPSVRIPIEDLSPGRQYRFEVQASSNGIRSGTTHLSTRTMPLIQSDVFIANAGHEQGQDETITLSYTPTPADSTRFDIYRFSMGDPTIKDKEKLANDTERKLSFSGLTPGKLYNVTVWTVSGGVASLPVQRLYRLHPLPISDLKAIQVAAREITLHWTAPAGEYTDFELQYLSADEEAPQLLQNVTKNTEITLQGLRPYHNYTFTVVVRSGSIQGTDFADVSVSTLMRSSAPISASYQTLTAPPGKVDYFQPSDVQPGEVTFEWSLEPAEQHGPIDYFRITCQNADDAADVSSYEFPVNATQGKIDGLVPGNHYIFRIQAKSALGYGAEREHIQTMPILAPPVPEPSVTPLEVSRTSSTIEISFRQGYFSNAHGMVRSYTIIIAEDVGKNASGLEMPSWQDVQAYTVWLPYQAIEPYNPFLTSNGSRKSSLEAEHFTIGTANCDKHQAGYCNGPLRAGTTYRIKIRAFTDEDKFTDTVYSSPITTERSDTVIVAATVSAVLLVAMVLVVVYCQHRCQLIRRASKLARMQDELAALPEGYITPNRPVHVKDFSEHYRIMSADSDFRFSEEFEELKHVGRDQACSFANLPCNRPKNRFTNILPYDHSRFKLQPVDDDDGSDYINANYMPGHNSPREFIVTQGPLHSTREEFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPVDRVAMFYGDIKVQLIIDTHYHDWSISEFMVSRNCESRIMRHFHFTTWPDFGVPEPPQSLVRFVRAFRDVIGTDMRPIIVHCSAGVGRSGTFIALDRILQHIHKSDYVDIFGIVFAMRKERVFMVQTETAVCVHPSVSAGGAGGQGAPAGRFARAARQRWLRSFINITC
Protein: Calmodulin-binding transcription activator 2 (AtCAMTA2) (AtER66) (Ethylene-induced calmodulin-binding protein c) (EICBP.c) (Signal-responsive protein 4) (AtSR4) (Q6NPP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in freezing tolerance in association with CAMTA1 and CAMTA3. Contributes together with CAMTA1 and CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2. Involved together with CAMTA3 and CAMTA4 in the positive regulation of a general stress response. Involved in tolerance to aluminum. Binds to the promoter of ALMT1 transporter and contributes to the positive regulation of aluminum-induced expression of ALMT1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767, ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:28351986}.
Interaction partners:
- Aluminum-activated malate transporter 1
- Zinc finger CCCH domain-containing protein 16
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 1
- Dehydration-responsive element-binding protein 1C
- IQ domain-containing protein IQM6
- Calmodulin-binding protein 60 G
- Dehydration-responsive element-binding protein 1B
Sequence:
MADRGSFGFAPRLDIKQLLSEAQHRWLRPAEICEILRNHQKFHIASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLHCYYAHGEDNENFQRRCYWMLEQDLMHIVFVHYLEVKGNRMSTSGTKENHSNSLSGTGSVNVDSTATRSSILSPLCEDADSGDSRQASSSLQQNPEPQTVVPQIMHHQNASTINSYNTTSVLGNRDGWTSAHGNRVKGSNSQRSGDVPAWDASFENSLARYQNLPYNAPLTQTQPSTFGLIPMEGKTEKGSLLTSEHLRNPLQSQVNWQTPVQESVPLQKWPMDSHSGMTDATDLALFGQGAHENFGTFSSLLGSQDQQSSSFQAPFTNNEAAYIPKLGPEDLIYEASANQTLPLRKALLKKEDSLKKVDSFSRWVSKELGEMEDLQMQSSSGGIAWTSVECENAAAGSSLSPSLSEDQRFTMIDFWPKWTQTDSEVEVMVIGTFLLSPQEVTSYSWSCMFGEVEVPADILVDGVLCCHAPPHEVGRVPFYITCSDRFSCSEVREFDFLPGSTRKLNATDIYGANTIETSLHLRFENLLALRCSVQEHHIFENVGEKRRKISKIMLLKDEKEPPLPGTIEKDLTELEAKERLIREEFEDKLYLWLIHKVTEEGKGPNILDEDGQGVLHLAAALGYDWAIKPILAAGVSINFRDANGWSALHWAAFSGREDTVAVLVSLGADAGALADPSPEHPLGKTAADLAYGNGHRGISGFLAESSLTSYLEKLTVDAKENSSADSSGAKAVLTVAERTATPMSYGDVPETLSMKDSLTAVLNATQAADRLHQVFRMQSFQRKQLSELGGDNKFDISDELAVSFAAAKTKKSGHSSGAVHAAAVQIQKKYRGWKKRKEFLLIRQRIVKIQAHVRGHQVRKQYRAIIWSVGLLEKIILRWRRKGSGLRGFKRDTISKPTEPVCPAPQEDDYDFLKEGRKQTEERLQKALTRVKSMAQYPEARAQYRRLLTVVEGFRENEASSSSALKNNTEEAANYNEEDDLIDIDSLLDDDTFMSLAFE
Protein: CBM1 domain-containing protein (A8NRB3)
Organism: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata)
Interaction partners:
- G2/M phase checkpoint control protein Sum2
Sequence:
MLGLPWVFLSLLAVSANAGRIVWDGSFNNYTTPADFDRWSWANQVGTYQWYIKGSGPTSRYLNLDPSYKNPAITSELRGLKVTIDTTATWNSQMMRTELIPQTNANLGQGNLFYHFSIKRTNTNAPDPTLEHQVMFFESHFTELKYGVGSNPSNLGWYAGGTERWSTPFTADTWFNFAYDIDFTAKTVGLWASTNGNPLVKVVQNVPANTFTDSRDFHVGVLRIVNRNPPEDWYVSGVYIEEGPITTQIGDGSSPGPEPPVVTNPPPVTTPPVVTPPPPVTTTTPSGPLQTKYGQCGGNGYTGPTNCVEGTTCVAVSPPYYYQCQ
Protein: Epithelial sodium channel subunit beta (Beta-ENaC) (ENaC subunit beta) (ENaCB) (Epithelial Na(+) channel subunit beta) (Amiloride-sensitive sodium channel subunit beta) (Beta-NaCH) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB) (P51168)
Organism: Homo sapiens (Human)
Function: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:18174164, ECO:0000269|PubMed:7762608}; Multi-pass membrane protein {ECO:0000269|PubMed:30251954, ECO:0000269|PubMed:32729833}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein {ECO:0000269|PubMed:30251954, ECO:0000269|PubMed:32729833}.
Interaction partners:
- Epithelial sodium channel subunit alpha
- Epithelial sodium channel subunit gamma
- E3 ubiquitin-protein ligase NEDD4-like
- E3 ubiquitin-protein ligase NEDD4
- Epithelial sodium channel subunit delta
- Sodium channel protein type 4 subunit alpha
- Serine/threonine-protein kinase Sgk1
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-4
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MHVKKYLLKGLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIICEGPKKKAMWFLLTLLFAALVCWQWGIFIRTYLSWEVSVSLSVGFKTMDFPAVTICNASPFKYSKIKHLLKDLDELMEAVLERILAPELSHANATRNLNFSIWNHTPLVLIDERNPHHPMVLDLFGDNHNGLTSSSASEKICNAHGCKMAMRLCSLNRTQCTFRNFTSATQALTEWYILQATNIFAQVPQQELVEMSYPGEQMILACLFGAEPCNYRNFTSIFYPHYGNCYIFNWGMTEKALPSANPGTEFGLKLILDIGQEDYVPFLASTAGVRLMLHEQRSYPFIRDEGIYAMSGTETSIGVLVDKLQRMGEPYSPCTVNGSEVPVQNFYSDYNTTYSIQACLRSCFQDHMIRNCNCGHYLYPLPRGEKYCNNRDFPDWAHCYSDLQMSVAQRETCIGMCKESCNDTQYKMTISMADWPSEASEDWIFHVLSQERDQSTNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEFGEIIIDFVWITIIKLVALAKSLRQRRAQASYAGPPPTVAELVEAHTNFGFQPDTAPRSPNTGPYPSEQALPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
Protein: Interphotoreceptor retinoid binding protein (Q52P71)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MRTYFFLFSVLIVCSISAEEIFQPTLVLDMAKVLLDNYCYPENLVGMQEAIEQAIKSGEILDISDPKMLANVLTAGVQGALNDPRLVISYEPSLHAAPKQEAETYPTREQLLSLIEHVVIYDKLEGNVGYLRIDYIIGQEVVEKVGAFLVDKVWKTLINTSALVIDLRYSTGGQISGIPFIISYLHEADKMLHVETVYNRPSNTTTEIWTLPKVLGERYSKDKDVIVLISHHTTGVAEDVAYILKHMNRAITLGEKTAGGSLDIQKLRIGPSNFYMMVPVSRSVSPLSGGGQSWEVSGVMPCVASEAEQALKKSLDILAVRRAVPGTLSRLTDILKDYYSLVERVPVLLRHLTTSDFSSVQSAEDLATKLNTEMQTLSEDPRLLVRTMMPGEAAAPPAEMPIAMAANLPDNEQLLHALVDTVFKVSVLPGNVGYMRFDEFADASVLVKLGPYIVKKVWEPLQNTENLIMDLRYNPGGPSSSAVPMLISYFQDPTAGPVHLFTTYDRRTNHTQEHNSQAELLAQPYGAQRGIYVLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTCTFPLVQPEQGITRGLTITVPVITFIDNHGESWMGGGVVPDAIVLAEDALEKAEEVLTFHRKMGILLESTGQLLEAHYAIPEVAEKASVMLSTKRVQGGYRSAVDFETLASQLTSDLQEASGDHRLHVFHSHVEPTPEEQLPNMIPSPEELSYIIEALFKIEVLPGNLGYLRFDMMAEAETVKAIGPQLVQMVWNKLVDTDAMIIDMRYNTGGYSTAVPILCSYFFEPEPRQHLYTVFDRSTSRSTEVWTLPKVTGKRYGSLKDIYILTSHMSGSAAEAFTRSMKDLHRATVIGEPTVGGSLSVGIYRVGNSSLYRSIPSQVVLSPVTGKVWSVSGAEPHITIQASEALAAAKHIASLRTQVPQIVQTVGKLVAENYAFVDIGTDIASNLTKSVNKENYKRINSEKELARKLTAILQALSDDEHLKILYIPEHAKDSIPGILPKQIPSPEVFEDLIKFSFHTNVFENNIGYLRFDMFGDCELLTQVSDLLVEHVWKKIVHTDALIIDMRYNIGGYTNSIPILCSYFFDEGHQVLLDKVYDRPSDSVKEIWTQPQLRGERYGSQKGLIILTSAVTAGAAEEFVFIMKRLGRALIIGEQTSGGSHSPQTYQVDDTNFYIIIPTARSVISAESASWEGKGVPPHMETPAVTALIKAKEVLSAHLHSSR
Protein: Calsyntenin-2 (Q8VDA1)
Organism: Rattus norvegicus (Rat)
Function: May modulate calcium-mediated postsynaptic signals.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ER65}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000250|UniProtKB:Q9ER65}.
Interaction partners:
Sequence:
MLPGRLCLVPLLLALGVGSGGGSGDGGDSRRRRLLAAKVNKHKPWIETSYHGVITENNDTVILDPTIVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEYTFIIQAYDCGAGPQEAAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAIVTEGKIYDSILQVEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQRQYEILVTAYDCGQKPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPGIHLETCDGAVSSLQVTAELQTNYIGKGCDRETYSEKSLQKLCGASSGIIDLLPSPSAATNWTAGLLVDSSEMIFKFDGRQGAKIPDGIVPKNLTDQFTITMWMKHGPSPGVRAEKETILCNSDKTEMNRHHYALYVHNCRLVFLLRKDFDQADTFRPAEFHWKLDQICDKEWHYYVINVEFPVVTLYMDGATYEPYLVTNDWPIHPSHIAMQLTVGACWQGGEVAKPRFAQFFHGSLASLTIRPGKMESQKVISCLQACKEGLDINSLESLGRGIKYHFNPSQSILVMEGDDIGNINQALQKVSYINSRQFPTAGVRRLRLSSKVQCFGEDVCISIPDVDAYIMVLQAIEPQITLQGTERFWRPAAQFESARGVTLFPDIKIISTFAKTEASGDLRATGTAPKSAVLEEMLHNLDFCDILVLGGDLDPRQECLELNHSELHQRHLDATNSTAGYSIYGVGSMSRYEQVLHHLRYRNWHPTSLETRRFQIKCSELNGRYTSNEFNLEVSVLHEVRVSDTEHVNHLIVQPPFLQSVYHPETRSSIQRSSVVPSIATVVIIISVCMLVFVVAMGVYRVRIAHQHFIQETEAAKEAEMDWDDSALTITVNPMEKHEGPGHGEDETEGEEEEEAEEGMSSSSSGSDDSEEEEEEGMGRVRHGQSGTSSQRPERSTWNTAGVINIWK
Protein: GEO04452p1 (Under-developed, isoform A) (Under-developed, isoform B) (A1Z7A5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD41005p
- TATA box-binding protein-associated factor RNA polymerase I subunit B
Sequence:
MKTKDEKPSPLKTAPRKIKGENFPARRIPANVLKRTLEIATSPEDGFWVNQNPSCAPPASNEFYFSVRRSTAYEKLRLARDCLMQRDYKNLAKILASNHMGETLLQRASFQIFTEYSKVLQKCPKFYTKMEQLRVEPTPPTRPTDEDIALDDSLNAILS
Protein: Secreted frizzled-related sequence protein 4 (FRP-4) (sFRP-4) (Q9Z1N6)
Organism: Mus musculus (Mouse)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP4 plays a role in bone morphogenesis. May also act as a regulator of adult uterine morphology and function. May also increase apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling (By similarity). Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6FHJ7}.
Interaction partners:
- Protein Wnt-3a
- Protein Wnt-2
- Protein Wnt-4
- Proto-oncogene Wnt-1
- Proto-oncogene Wnt-3
- Protein Wnt-5b
- Protein Wnt-16
- Protein Wnt-5a
- Protein Wnt-2b
- Protein Wnt-10b
Sequence:
MLRSILVALCLWLRLALGVRGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIKPCKSVCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDLPEDVKWIDITPDMMVQERSFDADCKRLSPDRCKCKKVKPTLATYLSKNYSYVIHAKIKAVQRSGCNEVTTVVDVKEIFKSLSPIPRTQVPLITNSSCQCPHILPHQDVLIMCYEWRSRMMLLENCLVEKWRDQLSRRSIQWEERLQEQQRTIQDKKQIASRTSRTSRSNPPKSKGRPPAPKPASPKKNIKARSAPKKSNLKKSAS
Protein: Myeloid leukemia factor 1 (Hematopoietic lineage switch 7) (Myelodysplasia-myeloid leukemia factor 1) (Q9QWV4)
Organism: Mus musculus (Mouse)
Function: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10523300}. Nucleus {ECO:0000269|PubMed:10523300}. Cell projection, cilium {ECO:0000269|PubMed:27914912}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27914912}. Note=Shuttles between the cytoplasm and nucleus. {ECO:0000269|PubMed:17008314}.
Interaction partners:
- 14-3-3 protein epsilon
- Centromere protein U
Sequence:
MFRMLSSSFEDDPFFADSFLAHRESMRNMMRSFSEPLGRDLLSISDGRGRTHNRRERDDGEDSLTHADVNPFQTMDRMMANMRSGIQELQRNFGQLSMDPNGHSFCSSSVMTYSKVGDEPPKVFQASTQTRRAPGGVKETRKAMRDSDSGLERMAVGHHIHDRGHVIRKSKNNKTGDEEVNQEFINMNESDAHAFDDEWQNEVLKYKSIGRSGNTGMRSVGHEHPGSRELKRREKIHRNSAIESGRRSNVFVDKLNVKGSPVKITKK
Protein: Uncharacterized protein YbjX (P75829)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MVKSTPCITIDFMNMSQLTERTFTPSESLSSLSLFLSLARGQCRPGKFWHRRSFRQKFLLRSLIMPRLSVEWMNELSHWPNLNVLLTRQPRLPVRLHRPYLAANLSRKQLLEALRYHYALLRECMSAEEFSLYLNTPGLQLAKLEGKNGEQFTLELTMMISMDKEGDSTILFRNSEGIPLAEITFTLCEYQGKRTMFIGGLQGAKWEIPHQEIQNATKACHGLFPKRLVMEAACLFAQRLQVEQIIAVSNETHIYRSLRYRDKEGKIHADYNAFWESVGGVCDAERHYRLPAQIARKEIAEIASKKRAEYRRRYEMLDAIQPQMATMFRG
Protein: Ribokinase (RK) (EC 2.7.1.15) (Q8R1Q9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03215}.
Interaction partners:
- Ribose-5-phosphate isomerase
- ribose-phosphate diphosphokinase
- Transketolase
- Transketolase-like protein 2
- Transketolase-like protein 1
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Deoxyribose-phosphate aldolase
- Ribose-phosphate pyrophosphokinase 1
- Phosphopentomutase
Sequence:
MAACGEPGRPWQEEEAAAVVVVGSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVPKHIPTEAVKAVDTTGAGDSFVGALAFYLAYYPNLSLEEMLKRSNFIAAVSVQATGTQSSYPYKKDLPLALF
Protein: Calmodulin (Q8I4W8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Myosin-A
- Myosin J, putative
- Sphingomyelin phosphodiesterase
- Myosin essential light chain ELC
- non-specific serine/threonine protein kinase
- Glideosome-associated protein 45
Sequence:
MKQECNVCYFNLPDPESTLGPYDNELNYFTWGPGFEYEPEPQRKPLSIEESFENSEESEESVADIQQLEEKVDESDVRIYFNEKSSGGKISIDNASYNARKLGLAPSSIDEKKIKELYGDNLTYEQYLEYLSICVHDKDNVEELIKMFAHFDNNCTGYLTKSQMKNILTTWGDALTDQEAIDALNAFSSEDNIDYKLFCEDILQ